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🏷️ Tags (8587 usages)
⚗️ Metals 2487
▸ Metals — Platinum (109)
apoptosis (297)Pt (214)pt (24)ferroptosis (22)oxaliplatin (21)cisplatin (21)pyroptosis (7)necroptosis (6)transcription (6)carboplatin (5)transcription factors (5)transcriptional regulation (5)platinum (4)lead optimization (3)transcription regulation (3)metabolic adaptation (3)pt(ii) complexes (2)transcriptional regulatory interactions (2)ferroptosis induction (2)transcription initiation (2)transcription-coupled repair (2)adaptive binding (2)cellular adaptation (2)post-transcriptional regulation (2)pt(dach)methionine (1)transcription-coupled nucleotide excision repair (tc-ner) (1)triptolide (1)molecular optimization (1)pt(dach)cl4 (1)innate apoptotic immunity (1)pta (1)oligopeptides (1)transcription-coupled ner (1)ferroptosis suppressor protein 1 (fsp1) (1)apoptotic cells (1)platinumbased (1)hptab (1)signaling-transcriptional mechanisms (1)oncogene transcription inhibition (1)pt2 (1)admet optimization (1)receptor (1)pten (1)platinum(ii) (1)chain-of-thought prompt engineering (1)tetrapeptides (1)apoptotic function (1)adaptive immune response (1)gpt-2 (1)platinum drugs (1)ptii complex (1)platinum complexes (1)transcriptomics (1)cell metabolism disruption (1)peptide (1)pt(s,s-dab) (1)pt(r,r-dab) (1)pt3(hptab) (1)estrogen receptor (1)transcriptional addiction (1)transcription stress (1)septicemia (1)optical spectroscopies (1)receptors (1)selective serotonin reuptake inhibitors (ssri) (1)transcription-coupled nucleotide excision repair (1)pt(r,r-dach) (1)chiroptical response (1)diplatinum helicate (1)cyclometalated 1,3-bis(8-quinolyl) phenyl chloroplatinum(ii) (1)transcriptional activity (1)pt1 (1)disrupting a base pair (1)platinum-containing drugs (1)gpt-4 (1)transcriptional stalling (1)transcription inhibition (1)apoptotic (1)eukaryotic transcription (1)base pairing disruption (1)apoptosis-related disorders (1)coordination chemistry is not relevant, but bioinorganic and medicinal chemistry are related concepts (1)chatgpt (1)apoptosis induction (1)platinum(ii)-based (1)transcriptional activation (1)platinum-based compounds (1)inhibition of transcription factors (1)molecular descriptors (1)pt(dach)oxalato (1)polypeptide chains (1)pt(dach)cl2 (1)glp-1 receptor agonists (1)chiroptical applications (1)pt(s,s-dach) (1)cell-penetrating peptides (1)cysteine uptake (1)therapeutic optimization (1)shape description methods (1)transcription blockage (1)antiferroptotic (1)rna transcription (1)electronic absorption (1)cellular adaptation to hypoxia (1)ferroptosis suppressor protein 1 (1)apoptosis evasion (1)phosphopeptide-based kinome analysis (1)anti-apoptotic (1)gpt (1)
▸ Metals — Cobalt (185)
coordination-chemistry (102)Co (64)coordination chemistry (55)colorectal cancer (19)computational biology (7)spectroscopy (7)computational chemistry (6)computational modeling (6)pharmacology (6)co (5)pharmacovigilance (5)cryo-electron microscopy (4)glucose (4)colon cancer (4)metal complexes (4)glycolysis (4)oncology (4)pharmacokinetics (4)conformational change (3)glycocalyx (3)oncometabolite (3)complex i (3)oncosis (3)oncogenesis (2)polypharmacology (2)in-silico (2)plant secondary metabolites (2)computational approaches (2)in silico (2)convolutional neural networks (2)complex iii (2)natural compounds (2)pharmacodynamics (2)mitochondrial complex i (2)aerobic glycolysis (2)oncogene (2)covid-19 (2)microviscosity (1)pharmacometabolomics (1)complex formation (1)redox control (1)fatty alcohols (1)influence on physicochemical properties (1)fluorescence recovery after photobleaching (1)convolutional neural network (1)conditional lethality (1)picolinic acid (1)sars-cov-1 (1)metabolic control (1)pharmacological inhibition (1)pharmacokinetic (1)therapeutic controversy (1)multicolor emission (1)co2 fixation (1)protein complex (1)oncogenes (1)recombination (1)confocal microscopy (1)metal-ligand cooperation (1)cell surface recognition (1)sarcoma (1)network pharmacology (1)covalent interaction (1)escherichia coli (1)cobalamin (1)reversible compartmentalization (1)oncogene promoter regions (1)cellular compartments (1)coulometric karl fischer apparatus (1)combinatorial treatment (1)heme-containing enzymes (1)coimmunoprecipitation assay (1)glycosphingolipids (1)comorbidities (1)glycolytic activity (1)computational metabolomics (1)conformational isomerization (1)constitutive induction (1)confocal imaging (1)alcoholic hepatitis (1)knowledge discovery (1)oncogenic mutation (1)cobaltocene (1)coordination (1)computational approach (1)inorganic compounds (1)toxicology (1)conformational stability (1)connectivity mapping (1)mitochondrial uncoupling protein 2 (1)pharmacokinetic analyses (1)membrane permeability comparison (1)computer models (1)pathological conditions (1)dna condensation (1)4-octyl-itaconate (4-oi) (1)glucose dependence (1)cockayne's syndrome (1)atomic force microscope (1)complex diseases (1)dna conformational distortion (1)computational prediction (1)health economics (1)viscometry (1)conformational transitions (1)anticoagulant (1)glycome (1)oncogenic pathways (1)mitochondrial quality control (1)spin-orbit coupling (1)cytosolic ca21 concentration (1)cobamide (1)glycobiology (1)coimmunoprecipitation (1)dual protein expansion microscopy (1)brightfield microscopy (1)complexes (1)fluorescence recovery after photobleaching (frap) (1)glucose deprivation resistance (1)physicochemical properties (1)cell-like compartments (1)expansion microscopy (1)anticoagulants (1)ascorbic acid (1)oncogenic signaling (1)collective intelligence (1)cordycepin (1)genetic encoding (1)co2 (1)coupled-cluster computations (1)atp-competitive inhibitors (1)non-covalent interaction (1)computational methods (1)conformational states (1)conformational transition (1)electronic health records (1)sars-cov-2 (1)computational models (1)pharmacodynamic (1)text encoder (1)social cognition (1)sensory nerve conduction velocity (1)covalent binding (1)oncogene-mediated cellular transformation (1)fluorescence microscopy (1)glycolysis pathway (1)electronic conductometry (1)conformational landscapes (1)inductively coupled plasma mass spectrometry (1)itaconate (1)co(terpy)2+ (1)nmr spectroscopy (1)computational analysis (1)inductively coupled plasma mass spectrometer (1)coenzyme q10 (1)cell communication (1)colony formation assay (1)physico-chemical mechanisms (1)recognition (1)glycolytic enzymes (1)systems pharmacology (1)atomic force microscopy (1)computational methodologies (1)oncogenic (1)click expansion microscopy (1)glycosylation (1)n-(2-picolyl)salicylimine (1)ewing sarcoma (1)computational study (1)anticoagulation (1)confocal laser scanning microscopy (1)immuno-oncology (1)genome conformation profiling (1)somatic comorbidities (1)uv-vis spectroscopy (1)in silico analysis (1)co-immunoprecipitation (1)caco-2 cell monolayers (1)scoping review (1)conformational switch (1)damage recognition (1)entity recognition (1)energy conversion (1)noncovalent interactions (1)computer analysis (1)
▸ Metals — Iron (60)
▸ Metals — Ruthenium (86)
Ru (41)drug discovery (27)drug-delivery (23)drug resistance (11)prodrug (9)drug-drug interactions (9)drugs (7)adverse drug reactions (7)structural biology (7)drug repurposing (6)drug delivery (5)drug (5)drug development (5)g-quadruplex dna (4)ru (4)protein structure (3)drug interactions (3)structural analysis (3)drug screening (3)drug-target interaction prediction (3)g-quadruplex (3)drug design (3)drug repositioning (2)metallodrugs (2)structural data (2)drug-target interaction (2)serum (1)structure-based virtual screening (1)recruitment (1)hexammineruthenium(iii) (1)drug testing (1)spectrum diagrams (1)drug therapy (1)drug safety monitoring (1)drug sensitivity and resistance testing (1)drug safety assessment (1)structure (1)structural insights (1)adverse drug reaction detection (1)drug sensitization (1)drug target (1)truncations (1)drug-drug interaction prediction (1)protein structure-function relationship (1)pyruvate (1)drug-drug interaction identification (1)phenotypic drug screening (1)spontaneous adverse drug reaction reports (1)structural basis (1)antiviral drug discovery (1)drug tolerance (1)green rust (1)structural modeling (1)small-molecule drugs (1)structural methods (1)drug-nutrient interactions (1)adverse drug events (1)computational drug discovery (1)metal-based drugs (1)structural rearrangement (1)protein structure analysis (1)virus (1)small-molecule oral drugs (1)targeted drug delivery (1)adverse drug reaction (1)chemical drugs (1)doxorubicin (1)drug resistance reduction (1)drug-likeness (1)drug interaction prediction (1)drug target identification (1)macromolecular structure determination (1)resorufin (1)drug interaction analysis (1)drug combinations (1)non-steroidal anti-inflammatory drugs (nsaids) (1)structural bioinformatics (1)structure prediction (1)drug response (1)drug interaction screening (1)ruthenium(ii)-based (1)drug detection (1)structure-function analysis (1)metal-based drug (1)protocellular structures (1)drug interaction identification (1)
▸ Metals — Copper (63)
▸ Metals — Gold (19)
▸ Metals — Iridium (29)
▸ Metals — Others (17)
▸ Metals — Palladium (13)
▸ Metals — Zinc (5)
▸ Metals — Other (17)
🔬 Methods 1116
▸ Methods — Other experimental (213)
synthesis (244)ML (51)docking (23)natural language processing (12)in vitro (7)in vivo (6)morphological profiling (4)literature search (4)benchmarking (4)network analysis (4)image-based profiling (3)biochemical analysis (3)text analysis (3)bibliometric analysis (3)api (2)incites (2)vosviewer (2)experimental (2)theoretical studies (2)high-throughput screening (2)sequence analysis (2)information extraction (2)pubmed (2)cck-8 assay (2)statistics (2)lectin array (2)statistical approach (2)literature review (2)genetic (2)icite (2)lectin microarray (2)semantic search (2)data visualization (1)in vivo studies (1)target-based approaches (1)permeability measurement (1)gene expression profile (1)patch clamp (1)cnns (1)knockout mouse studies (1)cpg island methylator phenotype (1)in vitro models (1)immunoblot (1)bret2 (1)preclinical models (1)graph theory (1)gnns (1)passive rheology (1)nonequilibrium sensitivity analysis (1)ex vivo (1)multilayer network integration (1)inhibition assay (1)go analysis (1)experimental data analysis (1)caspase activity (1)nct (1)esm (1)web of science (1)gene expression microarray (1)uv light exposure (1)text2sql (1)decision-making (1)short tandem repeat profiling (1)in-vitro (1)analytical determination methods (1)perturbation (1)immunospecific antibodies (1)overexpression (1)mechanistic analysis (1)nuclease digestion (1)enzymatic reaction (1)excision assay (1)nuclear magnetic resonance (not explicitly mentioned but implied through study of variants) (1)pampa assay (1)experimental studies (1)null models (1)binding studies (1)clinical analysis (1)semi-supervised learning (1)efficacy analyses (1)supervised learning (1)electric field application (1)mouse model (1)estimates (1)isothermal calorimetry (1)rational design (1)learning to rank (1)gene expression analysis (1)fluorometry (1)octanol-aqueous shake-flask method (1)polypharmacy regimens (1)predictive models (1)xr-seq (1)graph learning (1)human studies (1)in vivo lung perfusion (1)merip-seq (1)uv-detection (1)atp hydrolysis (1)clinical methods (1)data processing (1)glovebox-bound apparatus (1)hoechst 33,258 staining (1)mutational analyses (1)semantic retrieval (1)solid-phase microextraction (1)immunization (1)pathscan array (1)quantitative phase behavior (1)natural bond orbital (nbo) analysis (1)ai (1)immunological analysis (1)cellular assays (1)synthetic biology tools (1)nanotherapeutic approaches (1)splicing regulation profiling (1)genome-wide screening (1)loss-of-function screens (1)histochemical staining (1)resazurin reduction assay (1)stopped-flow ph jump experiments (1)protein language model (1)experimental validation (1)matrix factorization (1)giao method (1)multi-head attention mechanism (1)rnns (1)phase ii trial (1)calorimetry (1)high throughput screening (1)trp emission (1)self-supervised learning (1)chemocentric approach (1)graph-based learning (1)tcga analysis (1)theoretical framework (1)machine-learning algorithms (1)ablation experiments (1)boolean logic (1)guanidine hydrochloride denaturation (1)ic50 index (1)statistical analysis (1)quantification (1)ensemble learning (1)in vitro study (1)relation search (1)relation extraction (1)image segmentation (1)genetic studies (1)genome-wide analysis (1)knockdown (1)ccsd(t) (1)biochemical characterization (1)performance evaluation (1)nbo 3.1 (1)rocplotter (1)mitoplast preparation (1)cryoem (1)entity annotation (1)modeling (1)systems engineering (1)database analysis (1)radiation exposure (1)prognostic tools (1)mouse models (1)nuclear magnetic resonance (1)proximity ligation assays (1)mp2(fc)/6–311 +  + (2d,2p) (1)personalized treatments (1)ncbi e-utilities (1)gradient boosting machines (1)kegg analysis (1)genetic algorithm (1)algorithms (1)experimental design (1)system-level/network analyses (1)visualized analysis (1)aimall (1)radiotherapy (1)laboratory methods (1)displacement assay (1)electrophoretic retardation measurements (1)seahorse platform (1)normoxia (1)mixture modeling (1)high-throughput (1)experimental methods (1)slot blot (1)magnetic tweezers (1)thermal denaturation (1)global genome ner (1)genetic profiling (1)mutation analysis (1)algorithm development (1)modelling (1)cell migration assay (1)methylome profiling (1)biochemical studies (1)patch clamping (1)umbrella review (1)zotero (1)immunoblotting (1)statistical methods (1)cellular models (1)miclip (1)fluorometric assay (1)enzymatic assays (1)genetic analysis (1)photophysical (1)biomedical information retrieval (1)logistic regression (1)in-vivo (1)mutational status analysis (1)
▸ Methods — Computational (31)
▸ Methods — Crystallography / Structure (4)
▸ Methods — Cell biology (21)
▸ Methods — Spectroscopy (19)
▸ Methods — Genomics / Omics (25)
▸ Methods — Mass spec / Chromatography (6)
▸ Methods — Clinical / Epidemiology (8)
▸ Methods — Electrochemistry (5)
▸ Methods — Other (1)
🎯 Targets 980
▸ Targets — Mitochondria (15)
▸ Targets — Other (157)
protein (58)enzyme (19)heme (11)gene expression (10)nucleus (9)genome (5)cardiolipin (5)enzymes (5)are (4)nucleolus (4)genetic variants (4)tfiih (4)lipids (4)signal transduction (4)cytoplasm (4)cellular metabolism (4)cell metabolism (3)cell surface (3)ribosome (3)metalloproteins (3)cells (3)cell (3)fumarate hydratase (2)dihydroorotate dehydrogenase (2)ubiquinone (2)stress response (2)tubulin (2)cytosol (2)polysulfides (2)cytochrome c oxidase (2)xpb (2)aif (2)genes (2)ribosome biogenesis (2)chromophore (1)none (1)substrates (1)clinical notes (1)acsl4 (1)protein phosphatase 2a (1)dpscs (1)albumin (1)tissues (1)trxr (1)substrate (1)platelet aggregation (1)tbk1 (1)metabolic phenotype (1)lab results (1)intracellular ph (1)sqr (1)cellular biochemistry (1)target (1)healthy cells (1)sting (1)gene targets (1)variants (1)three-way junction (1)heme-oxygenase1 (1)ddr1 (1)cajal bodies (1)target genes (1)upr (1)mif (1)heme a3 (1)nucleic acids (1)intracellular substrates (1)hydrogen sulfide (h2s) (1)mt1-mmp (1)gene (1)plasma proteins (1)adenine (1)metabolic signatures (1)nuclear foci (1)mscs (1)caspase cascade (1)p65 (1)dna synthesis (1)ddb2 (1)nuclear factor (1)hmga2 (1)ecm (1)diseases (1)spliceosomal proteins (1)neurons (1)smn protein (1)nadh/nad(p)h (1)rtk clusters (1)reactive species (1)metal (1)translation initiation (1)ligand (1)lipid droplet (1)metabolic enzymes (1)pkcd (1)protein kinases (1)peripheral nervous system (1)stem cells (1)cellular targets (1)metalloenzyme (1)chemical reactions (1)4ebp1 (1)procaspase 3 (1)ump synthase (1)rbx1 (1)literature-based evidence (1)ras (1)metabolic biomarkers (1)guanine (1)metal centers (1)ccr7 (1)cytochrome p450 2e1 (1)cell nucleus (1)lung tissue (1)ph (1)stress granules (1)erythrocytes (1)hexokinase 2 (1)nucleic acid (1)nitrogen species (1)four-way junction (1)nucleolar protein (1)p21 (1)mek1/2 (1)membrane potential (1)polysulfides (h2sn) (1)mek (1)annexin v (1)atp production (1)actin (1)traf5 (1)tme (1)cytoskeleton (1)proteoforms (1)cell cycle (1)p47phox (1)metabolome (1)cellular (1)aldoa (1)oxidants (1)zbp1 (1)cellular machines (1)atp (1)actin filaments (1)disease network (1)lipid damage (1)focal adhesions (1)p97 (1)protein sequence (1)xpc (1)whole cell (1)p38 (1)plectin (1)plasmids (1)propidium iodide (1)nadph oxidase 1 (nox1) (1)hdac enzymes (1)
▸ Targets — Nucleic acids (44)
▸ Targets — Membrane / Transport (15)
▸ Targets — Enzymes / Kinases (18)
▸ Targets — Transcription factors (5)
🦠 Diseases 880
▸ Diseases — Cancer (69)
▸ Diseases — Other (41)
▸ Diseases — Neurodegenerative (18)
▸ Diseases — Inflammatory / Immune (6)
▸ Diseases — Metabolic (5)
▸ Diseases — Cardiovascular (6)
▸ Diseases — Hepatic / Renal (8)
⚙️ Mechanisms 800
▸ Mechanisms — ROS / Redox (65)
▸ Mechanisms — Other (96)
cell cycle arrest (16)enzyme inhibition (12)phosphorylation (5)gene expression regulation (5)cell cycle regulation (4)persulfidation (3)detoxification (3)ligand dissociation (2)sequence variants (2)mechanism of action (2)resistance (2)inactivation (2)invasion inhibition (1)er stress responses (1)hormesis (1)invasiveness (1)epithelial-to-mesenchymal transition inhibition (1)oxygen-dependent metabolism (1)aquation (1)paracellular permeability (1)translation efficiency (1)denaturation (1)sequestration (1)oxidative post-translational modification (1)lipid metabolism (1)duplex unwinding (1)unfolded protein response (1)antioxidation (1)calcium regulation (1)radical formation (1)oxidative damage (1)splicing regulation (1)cell growth arrest (1)protein destabilization (1)multivalent interactions (1)protein phosphatase 2a modulation (1)protein dislocation (1)cell growth suppression (1)proteotoxic stress (1)protein rearrangements (1)p21 translation inhibition (1)gg-ner (1)pseudohypoxia (1)hypoxic response (1)electron shuttle (1)low-barrier hydrogen bond (1)kinase inhibition (1)synthetic lethality (1)stress responses (1)mutagenesis (1)subcellular relocalization (1)weak interactions (1)proton ejection (1)metabolic fuel selection (1)posttranslational modification (1)regulatory interactions (1)proton pumps (1)genetic regulation (1)protein unfolding (1)nucleolar homeostasis (1)ligand switch (1)ribosomopathies (1)oxidation-reduction (1)induced fit (1)localization (1)genetic mutation (1)mode of action (1)nucleolar stress response (1)cell killing capacity (1)ligand exchange (1)bond breaking (1)kinase activation (1)modulation (1)diadduct formation (1)cytoskeleton modulation (1)radical-mediated reaction (1)electron self-exchange (1)protein shuttling (1)pore formation (1)cellular metabolism regulation (1)nuclear export processes (1)ion selectivity (1)cell survival suppression (1)stabilization (1)cell damage (1)mitochondrial bioenergetics (1)gene therapy (1)cytochrome p450 2e1 inhibition (1)oxidative metabolic phenotype (1)phosphorylation regulation (1)aggregation (1)downregulation (1)glutamate exchange (1)acidosis (1)dysregulated gene expression (1)glycan expression (1)
▸ Mechanisms — Signaling (51)
▸ Mechanisms — Immune modulation (21)
▸ Mechanisms — DNA damage / Repair (5)
▸ Mechanisms — Epigenetic (18)
▸ Mechanisms — Cell death (7)
▸ Mechanisms — Protein interaction (14)
▸ Mechanisms — Metabolic rewiring (8)
🔗 Ligands 659
▸ Ligands — N-donor (25)
▸ Ligands — Heterocyclic (9)
▸ Ligands — C-donor / NHC (4)
▸ Ligands — S-donor (14)
▸ Ligands — O-donor (7)
▸ Ligands — Other (8)
▸ Ligands — P-donor (2)
▸ Ligands — Peptide / Protein (4)
▸ Ligands — Macrocyclic (3)
▸ Ligands — Polydentate (5)
🧠 Concepts 612
▸ Concepts — Other biomedical (178)
medicinal chemistry (122)photoactivated (27)cell biology (13)chemotherapy (11)metabolism (10)biochemistry (9)artificial intelligence (7)large language models (7)systems biology (6)information retrieval (5)precision medicine (5)gene regulation (5)data mining (5)chemoprevention (4)cheminformatics (4)therapeutic target (4)mitophagy (4)immunology (4)genetics (4)biomedical research (3)large language model (3)biomedical literature (3)hydrogen bonding (3)post-translational modifications (3)chemotherapy resistance (3)variant interpretation (3)immunometabolism (3)physiology (2)clinical practice (2)evidence extraction (2)biotransformation (2)metabolic regulation (2)physiological relevance (2)chemical biology (2)cell cycle progression (2)immunomodulation (2)biophysics (2)protein modification (2)biopharmaceutics (2)immunity (2)in vitro modeling (2)post-translational modification (2)targeted therapy (2)predictive modeling (2)therapy resistance (2)desiccant efficiency (1)multimodal data integration (1)stereochemistry (1)variant evaluation (1)epithelial-mesenchymal transition (1)metalloprotein (1)genetic screening (1)self-assembly (1)personalized therapy (1)protein function prediction (1)cellular mechanisms (1)protein targeting (1)evidence-based medicine (1)photophysics (1)protein modifications (1)translational research (1)paracellular transport (1)helicase mechanism (1)chemiosmosis (1)polarizability (1)nonequilibrium (1)genotype characterization (1)nuclear shape (1)nutrient dependency (1)metabolic engineering (1)interactome (1)therapies (1)probing (1)multiscale analysis (1)reactive species interactome (1)tissue-specific (1)pharmaceutics (1)knowledge extraction (1)metabolic activities (1)protein function (1)chemical ontology (1)proton delocalization (1)permeability (1)biomarkers (1)prediction tool (1)mechanisms of action (1)protein-ligand binding affinity prediction (1)short hydrogen bonds (1)chemical language models (1)biomedical informatics (1)organelle function (1)microbiome (1)pathogenesis (1)mechanistic framework (1)biosignatures (1)cellular stress response (1)ion-selective electrodes (1)multimodal fusion (1)gasotransmitter (1)carbon metabolism (1)bioengineering (1)ion association (1)enzyme mechanism (1)symmetry breaking (1)micropolarity (1)genome stability (1)scaffold (1)global health (1)clinical implications (1)cellular neurobiology (1)mesh indexing (1)llm (1)therapeutic strategy (1)ner (1)dissipative behavior (1)enzymology (1)pretrained model (1)longevity (1)profiling approaches (1)multimodal information integration (1)therapeutic implications (1)astrobiology (1)protein sequence analysis (1)selective degradation (1)mechanical properties (1)biomedical literature search (1)metabolism regulation (1)extracellular vesicles (1)protein chemistry (1)foundation model (1)data science (1)low-barrier hydrogen bonds (1)variant detection (1)synthetic biology (1)therapeutic innovation (1)therapeutic targeting (1)metabolic dependencies (1)protein data bank (1)cellular biology (1)phenotypic screening (1)immunoengineering (1)database (1)thermochemistry (1)therapeutic approaches (1)medical subject heading (1)network biology (1)inorganic chemistry (1)immunoregulation (1)ageing (1)protein interaction networks (1)hormone mimics (1)therapeutics (1)chemotherapy efficacy (1)metabolite-mediated regulation (1)regulatory landscape (1)chemical informatics (1)mental well-being (1)personalized medicine (1)cell plasticity (1)protein science (1)metabolic therapy (1)cell polarity (1)bioavailability (1)biomedicine (1)cellular stress (1)network medicine (1)energy transduction (1)boron helices (1)nucleolar biology (1)sialic acid (1)organic solvent drying (1)phenotypic analysis (1)in vivo perfusion (1)polypharmacy (1)hyperglycemia (1)phenotypic screens (1)mechanobiology (1)nuclear organization (1)
▸ Concepts — Bioinorganic (7)
▸ Concepts — Thermodynamics / Kinetics (10)
▸ Concepts — Evolution / Origin of life (9)
▸ Concepts — Nanomedicine / Delivery (2)
▸ Concepts — Cancer biology (1)
📦 Other 583
▸ Other (169)
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309 articles with selected tags
Vanha N Pham, Christopher J Chang · 2023 · Angewandte Chemie · Wiley · added 2026-04-20
Transition metal chemistry is essential to life, where metal binding to DNA, RNA, and proteins underpins all facets of the central dogma of biology. In this context, metals in proteins are typically s Show more
Transition metal chemistry is essential to life, where metal binding to DNA, RNA, and proteins underpins all facets of the central dogma of biology. In this context, metals in proteins are typically studied as static active site cofactors. However, the emergence of transition metal signaling, where mobile metal pools can transiently bind to biological targets beyond active sites, is expanding this conventional view of bioinorganic chemistry. This Minireview focuses on the concept of metalloallostery, using copper as a canonical example of how metals can regulate protein function by binding to remote allosteric sites (e.g., exosites). We summarize advances in and prospects for the field, including imaging dynamic transition metal signaling pools, allosteric inhibition or activation of protein targets by metal binding, and metal-dependent signaling pathways that underlie nutrient vulnerabilities in diseases spanning obesity, fatty liver disease, cancer, and neurodegeneration. Show less
📄 PDF DOI: 10.1002/anie.202213644
Cu amino-acid imaging
Segal E, Nissenbaum J, Peretz M +6 more · 2023 · Cell Proliferation · Blackwell Publishing · added 2026-04-20
Anticancer drugs are at the frontline of cancer therapy. However, innate resistance to these drugs occurs in one-third to one-half of patients, exposing them to the side effects of these drugs with no Show more
Anticancer drugs are at the frontline of cancer therapy. However, innate resistance to these drugs occurs in one-third to one-half of patients, exposing them to the side effects of these drugs with no meaningful benefit. To identify the genes and pathways that confer resistance to such therapies, we performed a genome-wide screen in haploid human embryonic stem cells (hESCs). These cells possess the advantage of having only one copy of each gene, harbour a normal karyotype, and lack any underlying point mutations. We initially show a close correlation between the potency of anticancer drugs in cancer cell lines to those in hESCs. We then exposed a genome-wide loss-of-function library of mutations in all protein-coding genes to 10 selected anticancer drugs, which represent five different mechanisms of drug therapies. The genetic screening enabled us to identify genes and pathways which can confer resistance to these drugs, demonstrating several common pathways. We validated a few of the resistance-conferring genes, demonstrating a significant shift in the effective drug concentrations to indicate a drug-specific effect to these genes. Strikingly, the p53 signalling pathway seems to induce resistance to a large array of anticancer drugs. The data shows dramatic effects of loss of p53 on resistance to many but not all drugs, calling for clinical evaluation of mutations in this gene prior to anticancer therapy. Show less
📄 PDF DOI: 10.1111/cpr.13475
amino-acid anticancer
Woo Jae Jeong, Jaehee Lee, Hyunuk Eom +1 more · 2023 · Accounts of Chemical Research · ACS Publications · added 2026-04-20
no PDF DOI: 10.1021/acs.accounts.3c00336
amino-acid
2023 · Current Opinion in Chemical Biology · Elsevier · added 2026-04-20
no PDF DOI: 10.1016/j.cbpa.2022.102257
amino-acid
Q. Dan, X. Dan, R. Jiang +1557 more · 2023 · Advanced Science · Wiley · added 2026-04-20
Q. Dan, X. Dan, R. Jiang, Z. Wang, D. Dai, L. Sun, A. Caschera, L. Lazzara, D. Piergallini, B. Ricci, A. Tuscano, F. Vanzulli, D. R. Czeyda‐Pommersheim, J. R. Martin, B. Costello, J. Kalb, N. Wallyn, S. Anton, T. F. Akram, S. N. Vandamme, M. A. Gandhi, J. G. Brown, D. A. Wong, C. B. Aguirre, N. Sirlin, E. Naseri, F. Ajorlou, Y. Asghari, N. Pilehvar‐Soltanahmadi, P. Tsapis, I. Dey, N. Blakey, V. T. C. Stone, X. Tsang, T. T. W. Li, G. S. Wong, K. D. Filonov, L.‐M. Piatkevich, J. Ting, K. Zhang, V. V. Kim, L. Verkhusha, A. R. Truong, P. Ferre‐D'Amare, P. J. Charalampaki, A. Proskynitopoulos, M. Heimann, A. J. Nakamura, M. G. Sinnamon, Y. Neuwirth, S. M. Song, S. Schultz, X. Liu, C. M. Xu, G. C. Sehgal, T. Karakousis, M. von Knorring, A. Mogensen, S. V. Upadhyay, D. Dalvi, A. Maresca, M. Lakshmanan, A. Abedi, A. Bar‐Zion, G. J. Farhadi, J. O. Lu, D. Szablowski, S. Wu, M. G. Yoo, N. Shapiro, S. von Knebel Doeberitz, L. Maksimovic, D. Loi, A. Paech, G. J. Lakshmanan, A. Lu, S. P. Farhadi, M. Nety, A. Kunth, D. Lee‐Gosselin, R. W. Maresca, M. Bourdeau, J. Yin, C. Yan, D. Witte, F. S. Malounda, L. Foster, M. G. Schroder, M. G. Shapiro, R. M. Shapiro, L. J. Ramirez, G. Sperling, J. Sun, A. Sun, D. V. Pines, V. S. Schaffer, H. Bajaj, M. W. Kang, S. Kang, H. S. Kashiwagi, V. H. Choi, A. E. Roberts, A. J. Frias, C. C. Fordham, N. Hacherl, K. Patel, B. Jones, M. Myers, J. Abraham, M. Gendreau, A. B. Ormo, K. Cubitt, L. A. Kallio, R. Y. Gross, S. J. Tsien, J. Remington, F. Wiedenmann, G. U. Oswald, N. C. Nienhaus, G. H. Shaner, M. W. Patterson, R. N. Davidson, M. W. Day, N. C. Davidson, R. E. Shaner, P. A. Campbell, B. N. G. Steinbach, A. E. Giepmans, R. Y. Palmer, M. M. Tsien, O. V. Karasev, K. A. Stepanenko, K. K. Rumyantsev, V. V. Turoverov, K. Verkhusha, C. Vintersten, M. Monetti, P. Z. Gertsenstein, L. Zhang, S. Laszlo, A. Biechele, A. Nagy, S. Amsterdam, N. Lin, T. Hopkins, A. Matsumoto, K. Suetsugu, M. Hasegawa, Y. Nakamura, H. Shibata, T. Aoki, H. Kunisada, M. Tsurumi, M. Shimizu, R. M. Bouvet, Q. T. Hoffman, E. S. Nguyen, T. A. Olson, T. Aguilera, M. Jiang, L. G. Scadeng, R. Y. Ellies, M. Tsien, B. Zhao, H. Li, F. Zhang, N. C. Zhang, J. C. Rockwell, S. H. Lagarias, S. J. Bhoo, J. Davis, B. Walker, R. D. Karniol, S. J. Vierstra, A. V. Davis, R. D. Vener, L. Vierstra, P. A. O'Brien, K. Hosick, D. E. John, T. D. Stec, X. Hinds, A. Shu, M. Z. Royant, T. A. Lin, V. Aguilera, P. A. Lev‐Ram, R. Y. Steinbach, K. D. Tsien, F. V. Piatkevich, V. V. Subach, D. M. Verkhusha, V. V. Shcherbakova, M. Shcherbakova, A. V. Baloban, M. Emelyanov, P. Brenowitz, V. V. Guo, R. Verkhusha, Y. Liu, K. Xu, Z. Xu, S. K. Dai, R. Donnelly, S. P. H. Cabrera, J. R. Mao, B. Christin, W. Wu, J. J. Guo, J. S. Bravo‐Cordero, J. E. Condeelis, L. Segall, D. M. Hodgson, O. V. Shcherbakova, K. K. Stepanenko, V. V. Baloban, J. S. Verkhusha, K. Y. Paige, S. R. Wu, E. V. Jaffrey, P. J. Dolgosheina, R. L. Unrau, M. D. Strack, S. R. Disney, K. D. Jaffrey, M. C. Warner, W. Chen, R. L. Song, A. Strack, S. R. Thorn, A. R. Jaffrey, A. Ferre‐D'Amare, E. Autour, M. Westhof, G. S. Ryckelynck, J. D. Filonov, N. Moon, S. R. Svensen, A. Jaffrey, S. C. Y. Autour, A. D. Jeng, A. Cawte, A. Abdolahzadeh, S. S. S. Galli, D. Panchapakesan, M. Rueda, P. J. Ryckelynck, A. Unrau, M. Arora, A. Sunbul, W. Jaeschke, G. S. Song, H. Filonov, M. Kim, X. Hirsch, J. D. Li, S. R. Moon, M. Jaffrey, J. I. Jaeschke, M. N. Traylor, A. C. Pernik, S. K. Sternisha, K. G. McBrayer, Y. Abdullah, Y. Harada, T. Murayama, E. Takamatsu, H. Otsuji, S. Tanaka, F. Broekx, S. Weyns, W. De Vleeschouwer, S. Stummer, S. Stocker, H. Wagner, C. Stepp, C. Fritsch, A. E. Goetz, R. Goetz, H. J. Kiefmann, W. Reulen, U. Stummer, T. Pichlmeier, O. D. Meinel, F. Wiestler, H. J. Zanella, A. L.‐G. S. Reulen, A. P. K. K. K. Group, R. Mudiyanselage, M. A. Wu, K. Leon‐Duque, M. Ren, J. You, J. Vachtenheim, E. Borovansky, I. Dimitrow, A. Riemann, M. J. Ehlers, J. Koehler, P. Norgauer, K. Elsner, M. Koenig, S. Kaatz, F. Seidenari, C. Arginelli, P. M. W. Dunsby, K. French, C. Koenig, C. Magnoni, G. Talbot, J. Ponti, P. Staley, A. K. Grogan, H. Samadi, M. S. Cui, X. Cohen, E. I. Yang, E. V. Galanzha, P. M. Shashkov, J. Y. Spring, V. P. Suen, E. I. Zharov, V. P. Galanzha, Z. Zharov, W. Habli, R. AlChamaa, H. Saab, M. L. Kadara, Y. Khraiche, F. Sun, Z. Ding, R. Chen, C. Zhang, Y. Li, Y. Xu, R. Zhang, X. Ni, G. Li, Y. Yang, P. J. Sun, B. Stang, X. Fan, X. Yang, S. Li, H. Lv, J. Zhang, L. Li, B. Wang, X. Qu, R. Peng, D. Zhang, D. Sheng, Y. Wang, K. Yao, Z. Yang, L. Wang, Y. Deng, S. Chen, M. Sirsi, L. Borden, S. V. Abou‐Elkacem, J. K. Bachawal, F. Willmann, F. Pfeifer, S. Pfeifer, P. DasSarma, A. Arora, A. Lakshmanan, A. Nety, R. W. Lee‐Gosselin, D. Bourdeau, M. G. Maresca, A. Shapiro, A. E. Oren, D. Walsby, J. M. Lee‐Gosselin, Y.‐L. Melis, R. W. Ni, D. M. Bourdeau, M. G. Kochmann, J. O. Shapiro, A. Szablowski, M. G. Bar‐Zion, P. W. Shapiro, A. Goodwill, M. Neogy, F. S. Yin, D. V. Foster, S. M. Schaffer, L. Conolly, J. Xie, T. Song, F. Jiang, R. C. Yan, M. T. Hurt, M. Buss, K. Duan, M. Y. Wong, D. P. You, M. B. Sawyer, P. Swift, P. Dutka, D. R. Barturen‐Larrea, Z. Mittelstein, M. H. Jin, R. Farhadi, M. G. Deshpande, G. H. Farhadi, D. P. Ho, R. W. Sawyer, M. G. Bourdeau, D. Shapiro, T. Maresca, A. Payen, B. Lee‐Gosselin, D. Ling, C. Malounda, M. Demene, M. G. Tanter, Z. Lakshmanan, S. P. Jin, D. P. Nety, A. Sawyer, M. B. Malounda, D. Swift, T. Hao, F. Ai, X. Goerner, V. M. Hu, M. Runge, K. M. Tweedle, A. H. Ward, R. S. Aletras, L. Balaban, T. J. Schroeder, C. Lowery, D. E. Hilty, A. Wemmer, J. J. Pines, J. Neil, A. M. Badaut, A. Fukuda, K. G. Jullienne, Y. Petry, V. S. Jasanoff, E. Lelyveld, F. H. Brustad, A. Arnold, S. M. Jasanoff, J. M. Cohen, J. G. Rifkind, E. Mohanty, P. C. M. Nagababu, S. M. van Zijl, J. A. Eleff, J. M. E. Ulatowski, A. M. Oja, R. J. Ulug, R. A. Traystman, K. Kauppinen, P. Uludag, J. P. B. Blinder, S. P. O'Connor, J. C. Robinson, H. Waterton, G. Kroll, T. Zaharchuk, J. J. Christen, M. Heit, B. Iv, G. Jacobi, S. Bongartz, A.‐C. Partovi, M. Schulte, A. B. Aschwanden, M. G. Lumsden, M. Davies, G. P. Loebe, S. Noon, J. K. Karimi, D. Lyo, R. W. Staub, D. Huegli, M. G. Bilecen, G. G. Shapiro, P. A. Westmeyer, J. O. Romero, B. Szablowski, A. Kuester, C. R. Shah, R. Otey, F. H. Langer, A. Jasanoff, L. X. Hai, T. Cai, V. S. Lee, A. Lelyveld, T. Jasanoff, L. X. Lee, V. S. Cai, A. Hai, H. Jasanoff, B. Gunshin, U. V. Mackenzie, Y. Berger, M. F. Gunshin, W. F. Romero, S. Boron, J. L. Nussberger, M. A. Gollan, B. B. Hediger, K. U. Bartelle, G. A. Szulc, J. J. Suero‐Abreu, D. H. Rodriguez, C. M. Turnbull, S. A. Lewis, R. Graves, H. F. Hernandez, T. E. Valdovinos, W. Barnhart, M. E. Cai, R. J. Meyerand, M. Nickles, P. M. Suzuki, P. Harrison, A. Arosio, J. R. Yevenes, J. Harris, Y. Marles‐Wright, R. N. Gossuin, P. Muller, L. Gillis, A. E. Bartel, Y. Z. Deans, L. M. Wadghiri, X. Bernas, B. K. Yu, D. H. Rutt, X. Turnbull, J. He, B. Cai, Y. Zhong, A. V. Qin, H. Naumova, V. Reinecke, J. Yarnykh, C. Deem, C. E. Yuan, M. Murry, V. Campan, G. D. Lionetti, F. Aquaro, M. Forini, L. Matteucci, F. Vannucci, C. Chiuppesi, M. Di Cristofano, M. Faggioni, L. Maioli, E. Barile, M. Messina, A. Lombardi, M. Pucci, F. A. Pistello, B. Recchia, E. T. Iordanova, C. Ahrens, J. Song, C. Wang, S. Mo, X. Mu, X. Jiang, Z. Zhong, G. Zhao, Y. Zhou, F. Zhuo, L. Chen, T. Kong, J. Lu, T. Yang, X. Yu, K. Shi, H. S. Li, J. Kim, J. H. Woo, H. J. Lee, Y. Joo, H. Choi, W. K. Kim, S. J. Moon, K. Kim, C. M. Bernau, A. M. Lewis, M. S. Petelinsek, D. J. Reagan, V. B. Niles, E. Mattis, M. Meyerand, C. N. Suzuki, M. Svendsen, H. Wang, F. He, Y. Gao, S. C. Guo, L. J. Beeman, J. F. Mandarino, K. M. Georges, P. C. Bennett, J. M. Ulatowski, F. Kauppinen, C. Mickoleit, S. Jorke, D. S. Geimer, J. P. Maier, J. Muller, C. Demut, D. Grafe, J. H. Schuler, J. Clement, E. C. H. Liu, R. C. Cheng, S.‐H. Long, L. Yang, P.‐H. Wang, J. Cheng, D. Yang, H. Wu, A. W. S. Mao, S. M. Chan, D. Pereira, S. R. Moss, P. Williams, A. Murray, B. Taylor, X. Todorich, B. Zhang, W. E. Slagle‐Webb, J. R. Seaman, T. T. Connor, D. H. Li, C. D. C. Chung, S. V. Allen, F. M. Torti, J. G. Torti, C. Y. Cyster, F. M. Chen, E. C. Brodsky, M. C. Niemi, W. E. Nakamura, M. R. Seaman, P. S. Daws, T. B. Patrick, M. I. Rodrigues, S. K. Kettunen, A. A. Lyons, K. M. Neves, R. Brindle, R. Blakemore, D. Uebe, S. Schueler, M. Meriaux, B. Boucher, Y. Marty, S. Lalatonne, L. Preveral, C. T. Motte, F. Lefevre, F. Geffroy, M. Lethimonnier, D. Pean, G. Garcia, D. Adryanczyk‐Perrier, N. Pignol, T. Ginet, S. Orlando, E. Mannucci, G. Fantechi, S. Conti, A. Tambalo, C. Busato, L. Innocenti, R. Ghin, P. Bassi, F. Arosio, C. Orsini, M. Sangregorio, M. F. Corti, P. Casula, A. Marzola, A. Lascialfari, P. Sbarbati, M. D. Tartaj, S. Morales, T. Veintemillas‐Verdaguer, C. J. Gonzalez‐Carreno, K. Serna, C. Grunberg, B. M. Wawer, D. Tebo, Z. Schuler, X. Xiang, J. Yang, W. Xu, Z. Lai, J. Hu, L. Tian, Q. Geng, E. Fang, M. Erdal, Y. Demirbilek, O. Yeh, L. Akbal, D. Ruff, A. Bozkurt, Y. Cabuk, B. Senel, O. Gumuskaya, S. Algin, S. Colak, E. B. Esener, M. Denkbas, F. Boucher, S. Geffroy, E. Bellanger, G. Selingue, M. Adryanczyk‐Perrier, C. T. Pean, D. Lefevre, S. Ginet, D. E. Meriaux, R. Goldhawk, A. Rohani, N. Sengupta, F. S. Gelman, K. M. Prato, A. C. Jones, M. D. Pollard, B. Pagel, G. Wu, M. Warnock, C. Zaiss, M. Lin, Z. Chen, L. Zhou, D. Mu, R. Nanz, G. Tuura, Y. Delso, Y. Jia, K. Chen, Y. Geng, Y. Cheng, J. Li, H. Qiu, R. Huang, R. P. R. Krishnamoorthy, P. Nanga, H. Bagga, R. Hariharan, S. Reddy, M. Chen, Y. Jiang, B. Yuan, Z.‐X. Zhang, C. Jiang, X. Ye, C. Yuan, S. Wang, J. Kuddannaya, D. R. Zhang, Z. Arifin, P. Han, G. Walczak, J. W. M. Liu, P. C. M. Bulte, N. N. van Zijl, G. Yadav, K. W. Y. Song, M. T. Chan, M. T. McMahon, A. A. McMahon, J. Y. Gilad, P. Z. Zhou, J. W. M. Sun, J. Y. van Zijl, J. F. Zhou, D. A. Payen, R. J. Wilson, P. C. M. Traystman, N. van Zijl, A. X. McVicar, D. F. Li, M. Goncalves, S. O. Bellyou, M. A. M. Meakin, R. Prado, A. Bartha, Y. Sakata, T. Fushimi, Y. Okada, T. Arakawa, S. Kunieda, A. Minamiguchi, N. Kido, S. Sakashita, K. Miyamoto, B. Togashi, K. Joo, Y. S. Han, S.‐K. Choi, S. S. Lee, J. H. Ahn, S.‐G. Chang, S. H. Kang, C. Zhou, C. Su, L. Liu, J. Zhao, J. Jiang, S. Zhang, W. Li, J. Zhu, Y. S. Wang, S. S. Choi, S.‐K. Ahn, J. H. Lee, S. Zhou, C. G. Jiang, Y. Eberhart, H.‐Y. Zhang, Z. Heo, L. Wen, H. Blair, M. Qin, A. Lim, J. D. Quinones‐Hinojosa, P. B. Weingart, M. G. Barker, J. Pomper, P. C. M. Laterra, J. O. van Zijl, J. Blakeley, H. Zhou, H. Yu, T. Lou, X. Zou, Z. Jiang, Y. Huang, C. Du, L. Jiang, J. Ma, W. Zhu, Q. He, J. Rui, Z. Zhou, S. Wen, H. Jiang, Y. Lu, Y. Feng, D.‐H. Heo, J. Lee, C. Wen, X. Su, M. Zhou, S.‐Y. Wang, M. Li, J.‐Y. Chen, D.‐T. Zhou, C. Peng, Y.‐M. Zhang, M. Dai, X. Wang, C.‐F. Hong, Q. Chang, B. Li, H. Ma, H.‐Y. Xiang, Y. Heo, D.‐H. Zhang, S. Lee, R. C. Leigh, P. C. M. Koehler, J. van Zijl, J. Wang, H.‐K. Zhou, K. Jeong, J. Han, Y. S. Zhao, X. Ahn, Y. Ma, Y. Bai, X. Lin, T. Hong, E. M. Ma, J. Haacke, J. Zhou, M. Wang, P. C. M. Zhou, G. W. J. van Zijl, Y. K. Harston, N. Tee, T. W. Blockley, S. Okell, G. Thandeswaran, F. Shaya, M. Sheerin, S. Cellerini, P. Payne, M. Jezzard, J. Chappell, A. Kennedy, J. Tietze, I. K. Blicher, L. Mikkelsen, M. K. Ostergaard, S. A. Strother, M. J. Smith, R. J. Donahue, T. F. Harris, L. M. Cloughesy, P. L. Liau, A. Nghiemphu, W. B. Lai, B. M. Pope, R. J. Ellingson, R. M. Liau, J. P. Prins, D. Antonios, W. H. Li, W. B. Yong, A. Pope, P. L. Lai, B. M. Nghiemphu, K. Ellingson, A. Cai, D. R. Singh, R. P. R. Roalf, M. Nanga, H. Haris, R. Gur, K. Reddy, M. Cai, A. Haris, F. Singh, J. H. Kogan, H. Greenberg, J. A. Hariharan, R. Detre, F. Reddy, A. Kogan, C. Singh, M. Debrosse, K. Haris, R. P. Cai, H. Elliott, K. A. Reddy, R. P. R. Davis, S. Nanga, S. H. Das, P. N. Chen, J. R. Hadar, T. H. Pollard, R. T. Lucas, B. Shinohara, H. Litt, M. A. Hariharan, J. A. Elliott, D. R. Reddy, P. E. Nanga, H. Rupert, M. Hariharan, M. E. Quarmley, E. Calkins, K. Dress, M. A. Prabhakaran, P. J. Elliott, R. C. Moberg, R. E. Gur, B. I. Reddy, K. P. Turetsky, A. N. O'Grady, B. D. Dula, L. M. Lyttle, B. N. Thompson, B. A. Conrad, L. J. Box, S. McKeithan, F. Pawate, B. A. Bagnato, P. Landman, S. A. Newhouse, M. Smith, K. Nath, R. Singh, F. Crescenzi, G. Kogan, S. Verma, H. Reddy, E. R. Hariharan, R. Melhem, P. Reddy, S. Bagga, R. Pickup, D. Crescenzi, A. Martinez, K. Borthakur, A. D'Aquilla, G. Singh, J. A. Verma, J. Detre, J. Reddy, L. Pepin, M.‐A. Francelle, L. Carrillo‐de Sauvage, P. de Longprez, K. Gipchtein, J. Cambon, E. Valette, J. Brouillet, W. Flament, R. R. Ling, G. Regatte, A. Navon, S. Jerschow, A. J. R. Glyn‐Jones, R. Palmer, A. J. Agricola, T. L. Price, H. Vincent, A. J. Weinans, Y. H. Carr, H.‐K. Yang, J.‐S. Jeong, S. Suh, R. Brinkhof, V. Nizak, J. J. Khlebnikov, D. W. J. Prompers, D. B. F. Klomp, X. Saris, N. N. Xu, L. Yadav, J. Knutsson, R. Hua, E. Kalyani, J. Hall, J. Laterra, R. Blakeley, M. Strowd, P. Pomper, K. W. Y. Barker, G. Chan, M. T. Liu, R. D. McMahon, P. C. M. Stevens, K.‐P. Weygand, A. S. R. Hwang, Y. Mohamed, C. D. Ding, S. Y. Fuller, S. J. Lai, J. Frank, K. W. Y. Zhou, Y. McMahon, G. Kato, Z. M. Bulte, D. Bhujwalla, P. C. M. Artemov, S. van Zijl, R. Walker‐Samuel, F. Ramasawmy, M. Torrealdea, V. Rega, S. P. Rajkumar, S. Johnson, M. Richardson, H. G. Goncalves, E. Parkes, D. L. Arstad, R. B. Thomas, M. F. Pedley, X. Lythgoe, P. C. M. Golay, C. K. van Zijl, J. Jones, C. R. Ren, A. D. Malloy, C. O. Sherry, J. Miller, E. Y. Cao, B. M. Chekmenev, A. D. Damon, J. C. Cherrington, G. L. Gore, A. J. W. Simegn, F. C. Van der Kouwe, E. M. Robertson, A. Meintjes, M. Alhamud, R. Wyss, K. Kaddurah‐Daouk, R.‐W. Cai, X. J. Tain, F. C. Zhou, A. M. Damen, H. Scotti, H. Hariharan, R. Poptani, H. Singh, W. Poptani, H. Lu, X. J. Hariharan, R. Zhou, Z. Reddy, Y. Nguyen, J. L. Chen, Z. Shaw, E. Dawkins, D. Marbyn, C. Li, R. P. R. DeBrosse, N. Nanga, K. Wilson, M. D'Aquilla, F. Hariharan, K. Yan, N. Wade, D. Sara, C. Worsley, E. Parris‐Skeete, R. McCormick, Z. Z. Xiao, L. Cunningham, K. L. Fishbein, D. R. Nathanson, V. A. Lynch, M. Stallings, M. J. Yudkoff, R. Falk, S. E. Reddy, X.‐Y. McCormack, F. Xie, E. C. Wang, J. Lin, D. F. Xu, J. C. Gochberg, Z. Gore, S. Zu, A. A. Meier, J. A. Gilad, C. Brandon, E. Qian, J. F. Gao, M. Abisambra, M. J. Vandsburger, P. C. M. Donahue, S. Donahue, C. R. Rane, M. K. Thompson, A. O. Strother, S. A. Scott, Z. Smith, F. Hu, X. Huang, X. Guo, S. Quan, X. Zhou, Z. Zhao, F. Wen, S. Huang, X. Lu, D. Hu, J. Zu, K. Zhou, Z. Yan, C. Fu, K. Yang, D.‐H. Jiang, H.‐Y. Lee, R. N. Zhang, J. E. Cole, J. Van Eyk, J. Zaiss, S. Windschuh, D. Goerke, J.‐E. Paech, S. Meissner, P. Burth, W. Kickingereder, M. Wick, H.‐P. Bendszus, M. E. Schlemmer, P. Ladd, A. Bachert, C. K. Radbruch, M. J. Jones, P. C. M. Schlosser, M. G. van Zijl, X. Pomper, J. Golay, J. O. Zhou, M. Hua, M. G. Laterra, P. C. M. Pomper, M. Zhu, L. Lim, A. Blair, S. A. Quinones‐Hinojosa, C. G. Messina, M. G. Eberhart, P. B. Laterra, P. C. M. Barker, A. N. Blakeley, S. Dula, L. M. Pawate, B. N. Dethrage, B. E. Conrad, R. L. Dewey, S. A. Barry, A. N. Smith, E. M. Dula, B. A. Asche, E. B. Landman, S. Welch, S. Pawate, J. C. Sriram, S. A. Gore, J. A. Smith, J. M. Wells, H. E. O'Callaghan, N. M. Holmes, R. A. Powell, B. Johnson, F. Siow, O. Torrealdea, S. Ismail, X. Walker‐Samuel, M. Golay, S. Rega, M. J. Modat, S. Cardoso, A. J. Ourselin, Z. Schwarz, T. K. Ahmed, M. J. Murray, E. C. O'Neill, N. Collins, M. F. Colgan, J. Lythgoe, C. van Zijl, A. Schleich, L. Mueller‐Lutz, J. Zimmermann, B. Boos, H.‐J. Schmitt, G. Wittsack, F. Antoch, M. Miese, Q. Kim, M.‐P. Chan, K. M. C. Anthony, D. Cheung, P.‐L. Samartzis, C. Khong, M. Mueller‐Lutz, B. Eichner, F. Schmitt, B. Matuschke, C. Bittersohl, H.‐J. Zilkens, C. Miese, F. Mueller‐Lutz, P. Matuschke, R. Sewerin, B. Sengewein, B. Schmitt, H.‐J. Ostendorf, K. Wittsack, G. Stanke, R. P. R. Haris, A. Nanga, K. Singh, F. Cai, H. Kogan, M. Kogan, C. Cai, H. Nanga, J. J. Reddy, T. Chung, J. H. Jin, S.‐G. Lee, E. Kim, M. Rerich, A. Zaiss, M. E. Korzowski, F. Bachert, R. B. Kogan, E. K. Stafford, G. E. Englund, H. Gold, R. Reddy, D. Bammer, P. W. Le Bihan, P. E. Schaefer, R. G. Grant, L. Gonzalez, M. Zhang, Z. Tang, J. Min, X. Lei, N. M. Henderson, K. de Souza, S. F. Thomas, V. A. Riches, S. A. Morgan, D. P. Sohaib, C. C. Dearnaley, N. J. Parker, V. van As, R. Granata, O. Fusco, B. Catalano, F. Guarino, F. Granata, A. Tatangelo, M. Avallone, R. Piccirillo, F. Palaia, A. Izzo, P. Petrillo, L. S. Agre, M. King, W. B. Yasui, O. P. Guggino, Y. Ottersen, A. Fujiyoshi, S. Engel, I. Nielsen, A. Direito, M. A. Madeira, G. Brito, G. Soveral, G.‐Y. Tang, H. Tomita, A. J. Dorward, E. Yool, A. R. Smith, T. J. Townsend, J. E. Price, A. S. Hardingham, A. J. Verkman, P.‐w. Smith, L. Phuan, M. O. Tradtrantip, J. A. Anderson, J. I. Hubbard, D. K. Szu, E. A. Binder, O. P. Nagelhus, M. C. Ottersen, A. S. Papadopoulos, C. Verkman, E. Iacovetta, R. Rudloff, M. Kirby, G. Xiao, B. Hu, Y. Desai, B. Hsu, J. G. Schneller, A. I. Hobbs, A. Mehta, S. Linninger, M. C. Saadoun, A. M. Papadopoulos, J. Fukuda, H. Badaut, C. Chu, H. Huang, J. Ding, Z. Dong, X. Gao, Q. Tang, C. Dong, J. Mai, T. Li, T. Wang, Y.‐L. Lu, J. Lan, T. Zhao, S. Ma, Y.‐L. Li, X. Lan, J.‐C. Wang, X.‐C. Lou, B. Ma, V. Zhang, F. Gradinaru, J. Ramakrishnan, R. Mattis, I. Prakash, I. Diester, K. R. Goshen, K. Thompson, Y.‐W. Deisseroth, P. Shieh, P. Minguez, J. J. Bork, D. L. Auburger, G. Guilbride, B. Kramer, E. Bukau, J. N. Natan, S. A. Wells, J. A. Teichmann, A. Marsh, H. C. Mukherjee, P. Davis, G. J. Ramesh, M. G. Lu, Y. Shapiro, B. W. Wang, E. J. Roose, V. Palovcak, I. J. Carnevale, J. P. F. Dmochowski, K. Werner, Y. Mishra, P. Huang, S. Vetschera, A. Glasl, K. Chmyrov, V. Richter, A. C. Ntziachristos, P. Stiel, K. Vetschera, J. P. Mishra, A. Fuenzalida‐Werner, V. Chmyrov, K. Stiel, K. Ono, K. Fuma, M. Tabata, H. S. Sawada, H. R. Kim, S. H. Cho, J. S. Choi, W. K. Woo, Y. Moon, H. S. Choi, K.‐W. Kim, K.‐M. Cho, Y. J. Lee, S.‐J. Yi, H. J. Eun, S. H. Woo, T.‐K. Choi, C. Whangbo, D.‐Y. Choi, W. K. Noh, S. Moon, R. Cheng, Y. Mi, G. Xu, J. Jin, Y. Zhang, F. Chen, C. Liu, D. Jiang, E. M. Wu, B. Haacke, H. Cohen, G. Dafni, A. Meir, M. Harmelin, M.‐R. Neeman, A. Lisy, C. Hartung, D. Lang, W. Schueler, J. R. Richter, W. A. Reichenbach, I. Kaiser, A. Hilger, Y. Bar‐Shir, K. W. Y. Liang, A. A. Chan, J. W. M. Gilad, D. I. Bulte, A. Piraner, H. C. Farhadi, D. Davis, D. Wu, J. O. Maresca, M. G. Szablowski, G. Farhadi, M. Ho, B. Kunth, A. Ling, R. W. Lu, L. Bourdeau, M. G. Schroeder, G. J. Shapiro, A. Farhadi, M. G. Mukherjee, J. O. Farhadi, S. R. Lee‐Gosselin, A. Barnes, R. W. Lakshmanan, M. Shapiro, E. Bekiesinska‐Figatowska, K. Sawicka, O. Zak, J. Szczygielski, L. Stritzker, M. Kirscher, N. C. Scadeng, S. Deliolanis, P. Morscher, K. Symvoulidis, Q. Schaefer, M. Buckel, U. Hess, W. G. Donat, V. Bradley, A. A. Ntziachristos, T. Szalay, A. Repenko, A. Rix, J. Nedilko, A. Rose, R. Hermann, S. Vinokur, R. Moli, M. Cao‐Milan, G. Mayer, A. von Plessen, L. Fery, W. De Laporte, D. N. Lederle, A. J. C. Chigrin, J. E. Kuehne, Z. Lemaster, A. Wang, F. Hariri, Y. Hu, C. V. Huang, R. Barback, N. C. Cochran, J. V. Gianneschi, R. J. Jokerst, A. E. Paproski, K. Forbrich, M. M. Wachowicz, R. J. Hitt, A. Zemp, F. Farhadi, G. G. Sigmund, M. G. Westmeyer Show less
Abstract Imaging contrast agents are widely investigated in preclinical and clinical studies, among which biogenic imaging contrast agents (BICAs) are developing rapidly and playing an increasingly i Show more
Abstract Imaging contrast agents are widely investigated in preclinical and clinical studies, among which biogenic imaging contrast agents (BICAs) are developing rapidly and playing an increasingly important role in biomedical research ranging from subcellular level to individual level. The unique properties of BICAs, including expression by cells as reporters and specific genetic modification, facilitate various in vitro and in vivo studies, such as quantification of gene expression, observation of protein interactions, visualization of cellular proliferation, monitoring of metabolism, and detection of dysfunctions. Furthermore, in human body, BICAs are remarkably helpful for disease diagnosis when the dysregulation of these agents occurs and can be detected through imaging techniques. There are various BICAs matched with a set of imaging techniques, including fluorescent proteins for fluorescence imaging, gas vesicles for ultrasound imaging, and ferritin for magnetic resonance imaging. In addition, bimodal and multimodal imaging can be realized through combining the functions of different BICAs, which helps overcome the limitations of monomodal imaging. In this review, the focus is on the properties, mechanisms, applications, and future directions of BICAs. Show less
📄 PDF DOI: 10.1002/advs.202207090
Fe amino-acid imaging review
Joseph M Hendricks, Cody E Doubravsky, Eddie Wehri +10 more · 2023 · Cell chemical biology · Elsevier · added 2026-04-20
Ferroptosis is a regulated form of cell death associated with the iron-dependent accumulation of phospholipid hydroperoxides. Inducing ferroptosis is a promising approach to treat therapy-resistant ca Show more
Ferroptosis is a regulated form of cell death associated with the iron-dependent accumulation of phospholipid hydroperoxides. Inducing ferroptosis is a promising approach to treat therapy-resistant cancer. Ferroptosis suppressor protein 1 (FSP1) promotes ferroptosis resistance in cancer by generating the antioxidant form of coenzyme Q10 (CoQ). Despite the important role of FSP1, few molecular tools exist that target the CoQ-FSP1 pathway. Through a series of chemical screens, we identify several structurally diverse FSP1 inhibitors. The most potent of these compounds, ferroptosis sensitizer 1 (FSEN1), is an uncompetitive inhibitor that acts selectively through on-target inhibition of FSP1 to sensitize cancer cells to ferroptosis. Furthermore, a synthetic lethality screen reveals that FSEN1 synergizes with endoperoxide-containing ferroptosis inducers, including dihydroartemisinin, to trigger ferroptosis. These results provide new tools that catalyze the exploration of FSP1 as a therapeutic target and highlight the value of combinatorial therapeutic regimes targeting FSP1 and additional ferroptosis defense pathways. Show less
📄 PDF DOI: 10.1016/j.chembiol.2023.04.007
Fe amino-acid
Pham, Hoang Quoc Hai , Tao, Xiaoqun , Yang, Yanzhong · 2023 · Frontiers · Frontiers · added 2026-04-20
Arginine methylation is a prevalent post-translational modification (PTM) found in all eukaryotic systems. It involves the addition of a methyl group to the guanidino nitrogen atoms of arginine residu Show more
Arginine methylation is a prevalent post-translational modification (PTM) found in all eukaryotic systems. It involves the addition of a methyl group to the guanidino nitrogen atoms of arginine residues within proteins, and this process is catalyzed by a family of enzymes called protein arginine methyltransferases (PRMTs). In mammals, there exist nine PRMTs (PRMT1-9) that catalyze three distinct types of arginine methylation: monomethylarginine (MMA), asymmetric dimethylarginine (ADMA) and symmetric dimethylarginine (SDMA). These modifications play critical roles in numerous fundamental cellular processes, including transcription, RNA metabolism, genome maintenance, and signaling transduction. Aberrations in protein arginine methylation have been implicated in various human diseases, such as neurodevelopmental disorders and cancer. This review offers a general overview of arginine methylation, covering its deposition, its impact on protein function, and the diverse regulatory mechanisms involved. We specifically focus on an in-depth view of the role of arginine methylation in transcription and the epigenetic regulation of gene expression. Readers are directed towards additional reviews that encompass other aspects of arginine methylation biology. Show less
📄 PDF DOI: 10.3389/freae.2023.1245832
amino-acid review
Lee J, Roh JL · 2023 · Antioxidants · MDPI · added 2026-04-20
Ferroptosis, a recently identified form of regulated cell death characterized by the iron-dependent accumulation of lethal lipid peroxidation, has gained increasing attention in cancer therapy. Ferrop Show more
Ferroptosis, a recently identified form of regulated cell death characterized by the iron-dependent accumulation of lethal lipid peroxidation, has gained increasing attention in cancer therapy. Ferroptosis suppressor protein 1 (FSP1), an NAD(P)H-ubiquinone oxidoreductase that reduces ubiquinone to ubiquinol, has emerged as a critical player in the regulation of ferroptosis. FSP1 operates independently of the canonical system xc-/glutathione peroxidase 4 pathway, making it a promising target for inducing ferroptosis in cancer cells and overcoming ferroptosis resistance. This review provides a comprehensive overview of FSP1 and ferroptosis, emphasizing the importance of FSP1 modulation and its potential as a therapeutic target in cancer treatment. We also discuss recent progress in developing FSP1 inhibitors and their implications for cancer therapy. Despite the challenges associated with targeting FSP1, advances in this field may provide a strong foundation for developing innovative and effective treatments for cancer and other diseases. Show less
📄 PDF DOI: 10.3390/antiox12061218
Fe amino-acid review
Nakamura T, Hipp C, Santos Dias Mourão A +10 more · 2023 · Nature · Nature · added 2026-04-20
Ferroptosis is evolving as a highly promising approach to combat difficult-to-treat tumour entities including therapy-refractory and dedifferentiating cancers1-3. Recently, ferroptosis suppressor prot Show more
Ferroptosis is evolving as a highly promising approach to combat difficult-to-treat tumour entities including therapy-refractory and dedifferentiating cancers1-3. Recently, ferroptosis suppressor protein-1 (FSP1), along with extramitochondrial ubiquinone or exogenous vitamin K and NAD(P)H/H+ as an electron donor, has been identified as the second ferroptosis-suppressing system, which efficiently prevents lipid peroxidation independently of the cyst(e)ine-glutathione (GSH)-glutathione peroxidase 4 (GPX4) axis4-6. To develop FSP1 inhibitors as next-generation therapeutic ferroptosis inducers, here we performed a small molecule library screen and identified the compound class of 3-phenylquinazolinones (represented by icFSP1) as potent FSP1 inhibitors. We show that icFSP1, unlike iFSP1, the first described on-target FSP1 inhibitor5, does not competitively inhibit FSP1 enzyme activity, but instead triggers subcellular relocalization of FSP1 from the membrane and FSP1 condensation before ferroptosis induction, in synergism with GPX4 inhibition. icFSP1-induced FSP1 condensates show droplet-like properties consistent with phase separation, an emerging and widespread mechanism to modulate biological activity7. N-terminal myristoylation, distinct amino acid residues and intrinsically disordered, low-complexity regions in FSP1 were identified to be essential for FSP1-dependent phase separation in cells and in vitro. We further demonstrate that icFSP1 impairs tumour growth and induces FSP1 condensates in tumours in vivo. Hence, our results suggest that icFSP1 exhibits a unique mechanism of action and synergizes with ferroptosis-inducing agents to potentiate the ferroptotic cell death response, thus providing a rationale for targeting FSP1-dependent phase separation as an efficient anti-cancer therapy. Show less
📄 PDF DOI: 10.1038/s41586-023-06255-6
Fe amino-acid
Jacob, Prince, Lindelöf, Hillevi, Rustad, Cecilie F. +17 more · 2023 · Nature Publishing Group · Nature · added 2026-04-20
Spondyloepimetaphyseal dysplasia with severe short stature, RPL13-related (SEMD-RPL13), MIM#618728), is a rare autosomal dominant disorder characterized by short stature and skeletal changes such as m Show more
Spondyloepimetaphyseal dysplasia with severe short stature, RPL13-related (SEMD-RPL13), MIM#618728), is a rare autosomal dominant disorder characterized by short stature and skeletal changes such as mild spondylar and epimetaphyseal dysplasia affecting primarily the lower limbs. The genetic cause was first reported in 2019 by Le Caignec et al., and six disease-causing variants in the gene coding for a ribosomal protein, RPL13 (NM₀₀₀₉₇₇.3) have been identified to date. This study presents clinical and radiographic data from 12 affected individuals aged 2–64 years from seven unrelated families, showing highly variable manifestations. The affected individuals showed a range from mild to severe short stature, retaining the same radiographic pattern of spondylar- and epi-metaphyseal dysplasia, but with varying severity of the hip and knee deformities. Two new missense variants, c.548 G>A, p.(Arg183His) and c.569 G>T, p.(Arg190Leu), and a previously known splice variant c.477+1G>A were identified, confirming mutational clustering in a highly specific RNA binding motif. Structural analysis and interpretation of the variants’ impact on the protein suggests that disruption of extra-ribosomal functions of the protein through binding of mRNA may play a role in the skeletal phenotype of SEMD-RPL13. In addition, we present gonadal and somatic mosaicism for the condition. Show less
📄 PDF DOI: 10.1038/s41525-023-00380-x
amino-acid
Parvanendhu Pradeep, Krishnankutty Chandrika Sivakumar, Easwaran Sreekumar · 2023 · Microbiology spectrum · added 2026-04-20
Chikungunya virus (CHIKV) hijacks host cell machinery to support its replication. Nucleophosmin 1 (NPM1/B23), a nucleolar phosphoprotein, is one of the host proteins known to restrict CHIKV infection; Show more
Chikungunya virus (CHIKV) hijacks host cell machinery to support its replication. Nucleophosmin 1 (NPM1/B23), a nucleolar phosphoprotein, is one of the host proteins known to restrict CHIKV infection; however, the mechanistic details of the antiviral role of NPM1 are not elucidated. It was seen in our experiments that the level of NPM1 expression affected the expression levels of interferon-stimulated genes (ISGs) that play antiviral roles in CHIKV infection, such as IRF1, IRF7, OAS3, and IFIT1, indicating that one of the antiviral mechanisms could be through modulation of interferon-mediated pathways. Our experiments also identified that for CHIKV restriction, NPM1 must move from the nucleus to the cytoplasm. A deletion of the nuclear export signal (NES), which confines NPM1 within the nucleus, abolishes its anti-CHIKV action. We observed that NPM1 binds CHIKV nonstructural protein 3 (nsP3) strongly via its macrodomain, thereby exerting a direct interaction with viral proteins to limit infection. Based on site-directed mutagenesis and coimmunoprecipitation studies, it was also observed that amino acid residues N24 and Y114 of the CHIKV nsP3 macrodomain, known to be involved in virus virulence, bind ADP-ribosylated NPM1 to inhibit infection. Overall, the results show a key role of NPM1 in CHIKV restriction and indicate it as a promising host target for developing antiviral strategies against CHIKV. IMPORTANCE Chikungunya, a recently reemerged mosquito-borne infection caused by a positive-sense, single-stranded RNA virus, has caused explosive epidemics in tropical regions. Unlike the classical symptoms of acute fever and debilitating arthralgia, incidences of neurological complications and mortality were reported. Currently there are no antivirals or commercial vaccines available against chikungunya. Like all viruses, CHIKV uses host cellular machinery for establishment of infection and successful replication. To counter this, the host cell activates several restriction factors and innate immune response mediators. Understanding these host-virus interactions helps to develop host-targeted antivirals against the disease. Here, we report the antiviral role of the multifunctional host protein NPM1 against CHIKV. The significant inhibitory effect of this protein against CHIKV involves its increased expression and movement from its natural location within the nucleus to the cytoplasm. There, it interacts with functional domains of key viral proteins. Our results support ongoing efforts toward development of host-directed antivirals against CHIKV and other alphaviruses. Show less
no PDF DOI: 10.1128/spectrum.05371-22
amino-acid
Shabutdinova OR, Dautov AR, Samkov AA +8 more · 2023 · Problemy endokrinologii · added 2026-04-20
Overweight and obesity are a worldwide common problem and are diagnosed with a body mass index (BMI) value in the range of 25.0-29.9 kg/m2 and ≥30.0 kg/m2, respectively. Obese patients are at h Show more
Overweight and obesity are a worldwide common problem and are diagnosed with a body mass index (BMI) value in the range of 25.0-29.9 kg/m2 and ≥30.0 kg/m2, respectively. Obese patients are at high risk of developing concomitant diseases, such as hypertension, type 2 diabetes mellitus (DM2), hyperlipidemia, stroke and even some types of cancer. In the Russian Federation in 2016, the proportion of overweight people was 62.0%, with obesity - 26.2%. The authors performed an electronic search in the PubMed information database. Two search elements were used: «Semaglutide» and «Obesity». The search included studies published from the date of foundation of the database to August 2022. The search was limited only to the results of clinical trials. The authors obtained 26 results, but only the studies of SUSTAIN, PIONEER (Peptide Innovation for Early Diabetes Treatment) and STEP were considered, since they were original, randomized, controlled clinical trials conducted before the approval of semaglutide for the treatment of DM2 and obesity. Show less
📄 PDF DOI: 10.14341/probl13197
amino-acid
Zhouyang Huang, Justin J. Wilson · 2023 · ChemMedChem · Wiley · added 2026-04-20
AbstractThe mitochondrial calcium uniporter (MCU) is a transmembrane protein that is responsible for mediating mitochondrial calcium (mCa2+) uptake. Given this critical function, the MCU has been impl Show more
AbstractThe mitochondrial calcium uniporter (MCU) is a transmembrane protein that is responsible for mediating mitochondrial calcium (mCa2+) uptake. Given this critical function, the MCU has been implicated as an important target for addressing various human diseases. As such, there has a been growing interest in developing small molecules that can inhibit this protein. To date, metal coordination complexes, particularly multinuclear ruthenium complexes, are the most widely investigated MCU inhibitors due to both their potent inhibitory activities as well as their longstanding use for this application. Recent efforts have expanded the metal‐based toolkit for MCU inhibition. This concept paper summarizes the development of new metal‐based inhibitors of the MCU and their structure‐activity relationships in the context of improving their potential for therapeutic use in managing human diseases related to mCa2+ dysregulation. Show less
no PDF DOI: 10.1002/cmdc.202300106
Ru amino-acid coordination-chemistry mitochondria
Domán A, Dóka É, Garai D +4 more · 2023 · Redox biology · Elsevier · added 2026-04-20
Reactive sulfur species (RSS) entail a diverse family of sulfur derivatives that have emerged as important effector molecules in H2S-mediated biological events. RSS (including H2S) can exert their bio Show more
Reactive sulfur species (RSS) entail a diverse family of sulfur derivatives that have emerged as important effector molecules in H2S-mediated biological events. RSS (including H2S) can exert their biological roles via widespread interactions with metalloproteins. Metalloproteins are essential components along the metabolic route of oxygen in the body, from the transport and storage of O2, through cellular respiration, to the maintenance of redox homeostasis by elimination of reactive oxygen species (ROS). Moreover, heme peroxidases contribute to immune defense by killing pathogens using oxygen-derived H2O2 as a precursor for stronger oxidants. Coordination and redox reactions with metal centers are primary means of RSS to alter fundamental cellular functions. In addition to RSS-mediated metalloprotein functions, the reduction of high-valent metal centers by RSS results in radical formation and opens the way for subsequent per- and polysulfide formation, which may have implications in cellular protection against oxidative stress and in redox signaling. Furthermore, recent findings pointed out the potential role of RSS as substrates for mitochondrial energy production and their cytoprotective capacity, with the involvement of metalloproteins. The current review summarizes the interactions of RSS with protein metal centers and their biological implications with special emphasis on mechanistic aspects, sulfide-mediated signaling, and pathophysiological consequences. A deeper understanding of the biological actions of reactive sulfur species on a molecular level is primordial in H2S-related drug development and the advancement of redox medicine. Show less
📄 PDF DOI: 10.1016/j.redox.2023.102617
ROS amino-acid mitochondria review
T. Narayan, A. Dutta, A. Agarwal +541 more · 2022 · iScience · Elsevier · added 2026-04-20
T. Narayan, A. Dutta, A. Agarwal, R.J. MacKenzie, R. Pippa, C.A. Eide, J. Oddo, J.W. Tyner, R. Sears, M.P. Vitek, M.D. Odero, D.J. Christensen, B.J. Druker, A. Ashkenazi, R.C. Pai, S. Fong, S. Leung, D.A. Lawrence, S.A. Marsters, C. Blackie, L. Chang, A.E. McMurtrey, A. Hebert, A. Bene, T.C. Chambers, I. Beuvink, A. Boulay, S. Fumagalli, F. Zilbermann, S. Ruetz, T. O'Reilly, F. Natt, J. Hall, H.A. Lane, G. Thomas, M. Bhat, N. Robichaud, L. Hulea, N. Sonenberg, J. Pelletier, I. Topisirovic, R. Briffa, S.P. Langdon, G. Grech, D.J. Harrison, B.A. Carneiro, W.S. El-Deiry, T.C. Chou, A.E. Collier, D.F. Spandau, R.C. Wek, I. Cristobal, R. Manso, R. Rincón, C. Caramés, C. Senin, A. Borrero, J. Martínez-Useros, M. Rodriguez, S. Zazo, O. Aguilera, R. Rincon, C. Carames, J. Madoz-Gurpide, F. Rojo, J. Garcia-Foncillas, R.M. De Palma, S.R. Parnham, Y. Li, J.J. Oaks, Y.K. Peterson, Z.M. Szulc, B.M. Roth, Y. Xing, B. Ogretmen, D. Deng, K. Shah, M.J. Fournier, L. Coudert, S. Mellaoui, P. Adjibade, C. Gareau, M.F. Côté, R.C. Gaudreault, R. Mazroui, A.M. Gaben, C. Saucier, M. Bedin, V. Barbu, J. Mester, C. Filion, D. Martel, Y. Labelle, A.G. Georgakilas, O.A. Martin, W.M. Bonner, M.J. Gerdes, C.J. Sevinsky, A. Sood, S. Adak, M.O. Bello, A. Bordwell, A. Can, A. Corwin, S. Dinn, R.J. Filkins, M. Gorospe, X. Wang, K.Z. Guyton, N.J. Holbrook, M.M. Gottesman, J.R. Graff, B.W. Konicek, J.H. Carter, E.G. Marcusson, R.S. Herbst, S.G. Eckhardt, R. Kurzrock, S. Ebbinghaus, P.J. O'Dwyer, M.S. Gordon, W. Novotny, M.A. Goldwasser, T.M. Tohnya, B.L. Lum, S.D. Heys, K.G. Park, M.A. McNurlan, A.G. Calder, V. Buchan, K. Blessing, O. Eremin, P.J. Garlick, B. Hoang, A. Benavides, Y. Shi, Y. Yang, P. Frost, J. Gera, A. Lichtenstein, A.N. Hobden, E. Cundliffe, N. Ikoma, K. Raghav, G. Chang, A. Ishitsuka, E. Fujine, Y. Mizutani, C. Tawada, H. Kanoh, Y. Banno, M. Seishima, S. Iwasaki, N.T. Ingolia, S.C. Jahn, P.E. Corsino, B.J. Davis, M.E. Law, P. Nørgaard, B.K. Law, V. Janssens, S. Longin, J. Goris, M.A. Jensen, V. Ferretti, R.L. Grossman, L.M. Staudt, Y.H. Jin, K.J. Yoo, Y.H. Lee, S.K. Lee, A. Kahvejian, Y.V. Svitkin, R. Sukarieh, M.N. M'Boutchou, S.K. Kelley, L.A. Harris, D. Xie, L. Deforge, K. Totpal, J. Bussiere, J.A. Fox, S.L. Kim, Y.C. Liu, Y.R. Park, S.Y. Seo, S.H. Kim, I.H. Kim, S.O. Lee, S.T. Lee, D.G. Kim, S.W. Kim, N.N. Kreis, F. Louwen, J. Yuan, M. Law, E. Forrester, A. Chytil, P. Corsino, G. Green, B. Davis, T. Rowe, B. Law, S.L. Lehman, G.J. Cerniglia, G.J. Johannes, J. Ye, S. Ryeom, C. Koumenis, S. Lek, J. Vargas-Medrano, E. Villanueva, B. Marcus, W. Godfrey, R.G. Perez, J. Lemke, S. von Karstedt, J. Zinngrebe, H. Walczak, D. Leonard, W. Huang, S. Izadmehr, C.M. O'Connor, D.D. Wiredja, Z. Wang, N. Zaware, Y. Chen, D.M. Schlatzer, J. Kiselar, V. Leung-Pineda, C.E. Ryan, H. Piwnica-Worms, L. Li, J. Wang, J.G. Li, Z. Wu, P. Ma, X.J. Lian, I.E. Gallouzi, H. Lin, X. Qiu, B. Zhang, J. Zhang, T.A. Lin, X. Kong, T.A.J. Haystead, A. Pause, G. Belsham, J.C. Lawrence, J. Lu, J.S. Kovach, F. Johnson, J. Chiang, R. Hodes, R. Lonser, Z. Zhuang, M. Mahyar-Roemer, K. Roemer, A. Maiuthed, C. Ninsontia, K. Erlenbach-Wuensch, B. Ndreshkjana, J.K. Muenzner, A. Caliskan, H. Ahmed P, A.P. Husayn, C. Chaotham, A. Hartmann, K. Malinowsky, U. Nitsche, K.P. Janssen, F.G. Bader, C. Spath, E. Drecoll, G. Keller, H. Hofler, S. Mazhar, S.E. Taylor, J. Sangodkar, G. Narla, K. McClinch, R.A. Avelar, D. Callejas, D. Wiredja, A. Perl, D.B. Kastrinsky, D. Schlatzer, M. Cooper, D.R. McIlwain, T. Berger, T.W. Mak, N. Melling, R. Simon, J.R. Izbicki, L.M. Terracciano, C. Bokemeyer, G. Sauter, A.H. Marx, J.R. Mills, Y. Hippo, F. Robert, S.M.H. Chen, A. Malina, C.J. Lin, U. Trojahn, H.G. Wendel, A. Charest, R.T. Bronson, C.S. Mitsiades, S.P. Treon, N. Mitsiades, Y. Shima, P. Richardson, R. Schlossman, T. Hideshima, K.C. Anderson, K. Morita, S. He, R.P. Nowak, M.W. Zimmerman, C. Fu, A.D. Durbin, M.W. Martel, N. Prutsch, N.S. Gray, S. Narayan, A.S. Jaiswal, R. Sharma, A. Nawab, L.V. Duckworth, M. Zajac-Kaye, T.J. George, J. Sharma, A.K. Sharma, R.A. Hromas, S. Ramisetti, A. Singh-Pillay, P. Singh, S. Amin, P. Palaiologos, D. Chrysikos, S. Theocharis, G. Kouraklis, G.J. Belsham, A.C. Gingras, O. Donzé, M.D. Ralff, P.G. Richardson, C. Eng, J. Kolesar, N.R. Rodrigues, A. Rowan, M.E. Smith, I.B. Kerr, W.F. Bodmer, J.V. Gannon, D.P. Lane, H.K. Roy, B.F. Olusola, D.L. Clemens, W.J. Karolski, A. Ratashak, H.T. Lynch, T.C. Smyrk, E. Rozengurt, H.P. Soares, J. Sinnet-Smith, P.P. Ruvolo, R. Tohme, E.K. Schmidt, G. Clavarino, M. Ceppi, P. Pierre, R.R. Sharma, T.S. Ravikumar, D. Raimo, W.L. Yang, R.L. Siegel, K.D. Miller, H.E. Fuchs, A. Jemal, J.C. Soria, Z. Márk, P. Zatloukal, B. Szima, I. Albert, E. Juhász, J.L. Pujol, J. Kozielski, N. Baker, D. Smethurst, W. Stöcklein, W. Piepersberg, A. Surov, P. Clauser, Y.W. Chang, L. Martincich, S.C. Partridge, J.Y. Kim, H.J. Meyer, A. Wienke, A. Suzuki, T. Ito, H. Kawano, M. Hayashida, Y. Hayasaki, Y. Tsutomi, K. Akahane, T. Nakano, M. Miura, K. Shiraki, T. Araki, S. Tahmasebi, T. Alain, V.K. Rajasekhar, J.P. Zhang, M. Prager-Khoutorsky, A. Khoutorsky, Y. Dogan, C.G. Gkogkas, E. Petroulakis, A. Sylvestre, A. Thorburn, K. Behbakht, H. Ford, H. Tian, E.K. Wittmack, T.J. Jorgensen, R. Tohmé, S. Gandhe, G. Tabaro, S. Vallabhaneni, A. Thomas, N. Vasireddi, N.S. Dhawan, A. Ma'ayan, N. Sharma, C. Vaklavas, S.W. Blume, W.E. Grizzle, K. Van der Jeught, H.C. Xu, Y.J. Li, X.B. Lu, G. Ji, A. Montinaro, R.E. Miller, K. Ariail, B. Gliniak, T.S. Griffith, M. Kubin, W. Chin, J. Jones, A. Woodward, T. Le, H. Wang, Y. Liu, J. Ding, Y. Huang, J. Liu, N. Liu, Y. Ao, Y. Hong, L. Wang, L. Zhang, M. Wang, E. Yaaghubi, A.F. Ghilardi, R.B. Ferreira, C.W. Chiang, O.A. Guryanova, D. Kopinke, C.D. Heldermon, S.S. Wang, E.D. Esplin, J.L. Li, L. Huang, A. Gazdar, J. Minna, G.A. Evans, X.W. Wang, Y.J. Zhang, J.S. Warmus, G.J. Dilley, A.I. Meyers, F. Wei, Y. Zhang, L. Geng, P. Zhang, G. Wang, R.H. Weiss, J. Westermarck, N. Wu, Z. Du, Y. Zhu, Y. Song, L. Pang, Z. Chen, J. Xu, P. Wang, H. Yang, J. Zhou, X. Li, W. Xue, C. Yu, Y. Tian, F. Zhu, J.Y. Zhou, W.Z. Wei, G.S. Wu, S.Q. Xu, P. Yaffee, A. Osipov, C. Tan, R. Tuli, A. Hendifar, L. Yong, Z. YuFeng, B. Guang, P.E. Young, C.M. Womeldorph, E.K. Johnson, J.A. Maykel, B. Brucher, A. Stojadinovic, I. Avital, A. Nissan, S.R. Steele, Y. Yu, S.S. Kanwar, B.B. Patel, J. Nautiyal, F.H. Sarkar, A.P. Majumdar, B. Fang, N. Fujita, T. Tsuruo, X. Zhou, W. Liu, X. Hu, A. Dorrance, R. Garzon, P.J. Houghton, C. Shen Show less
Summary The treatment of colorectal cancer (CRC) with FOLFOX shows some efficacy, but these tumors quickly develop resistance to this treatment. We have observed increased phosphorylation of AKT1/mTO Show more
Summary The treatment of colorectal cancer (CRC) with FOLFOX shows some efficacy, but these tumors quickly develop resistance to this treatment. We have observed increased phosphorylation of AKT1/mTOR/4EBP1 and levels of p21 in FOLFOX-resistant CRC cells. We have identified a small molecule, NSC49L, that stimulates protein phosphatase 2A (PP2A) activity, downregulates the AKT1/mTOR/4EBP1-axis, and inhibits p21 translation. We have provided evidence that NSC49L- and TRAIL-mediated sensitization is synergistically induced in p21-knockdown CRC cells, which is reversed in p21-overexpressing cells. p21 binds with procaspase 3 and prevents the activation of caspase 3. We have shown that TRAIL induces apoptosis through the activation of caspase 3 by NSC49L-mediated downregulation of p21 translation, and thereby cleavage of procaspase 3 into caspase 3. NSC49L does not affect global protein synthesis. These studies provide a mechanistic understanding of NSC49L as a PP2A agonist, and how its combination with TRAIL sensitizes FOLFOX-resistant CRC cells. Show less
📄 PDF DOI: 10.1016/j.isci.2022.104518
amino-acid synthesis
Raquel Nunes Palmeira, Marco Colnaghi, Stuart A Harrison +2 more · 2022 · Proceedings. Biological sciences · The Royal Society · added 2026-04-20
The universal core of metabolism could have emerged from thermodynamically favoured prebiotic pathways at the origin of life. Starting with H2 and CO2, the synthesis of amino acids and mixed fatty aci Show more
The universal core of metabolism could have emerged from thermodynamically favoured prebiotic pathways at the origin of life. Starting with H2 and CO2, the synthesis of amino acids and mixed fatty acids, which self-assemble into protocells, is favoured under warm anoxic conditions. Here, we address whether it is possible for protocells to evolve greater metabolic complexity, through positive feedbacks involving nucleotide catalysis. Using mathematical simulations to model metabolic heredity in protocells, based on branch points in protometabolic flux, we show that nucleotide catalysis can indeed promote protocell growth. This outcome only occurs when nucleotides directly catalyse CO2 fixation. Strong nucleotide catalysis of other pathways (e.g. fatty acids and amino acids) generally unbalances metabolism and slows down protocell growth, and when there is competition between catalytic functions cell growth collapses. Autocatalysis of nucleotide synthesis can promote growth but only if nucleotides also catalyse CO2 fixation; autocatalysis alone leads to the accumulation of nucleotides at the expense of CO2 fixation and protocell growth rate. Our findings offer a new framework for the emergence of greater metabolic complexity, in which nucleotides catalyse broad-spectrum processes such as CO2 fixation, hydrogenation and phosphorylation important to the emergence of genetic heredity at the origin of life. Show less
no PDF DOI: 10.1098/rspb.2022.1469
amino-acid catalysis synthesis
Linchong Sun, Huafeng Zhang, Ping Gao · 2022 · Protein & cell · Springer · added 2026-04-20
Metabolic rewiring and epigenetic remodeling, which are closely linked and reciprocally regulate each other, are among the well-known cancer hallmarks. Recent evidence suggests that many metabolites s Show more
Metabolic rewiring and epigenetic remodeling, which are closely linked and reciprocally regulate each other, are among the well-known cancer hallmarks. Recent evidence suggests that many metabolites serve as substrates or cofactors of chromatin-modifying enzymes as a consequence of the translocation or spatial regionalization of enzymes or metabolites. Various metabolic alterations and epigenetic modifications also reportedly drive immune escape or impede immunosurveillance within certain contexts, playing important roles in tumor progression. In this review, we focus on how metabolic reprogramming of tumor cells and immune cells reshapes epigenetic alterations, in particular the acetylation and methylation of histone proteins and DNA. We also discuss other eminent metabolic modifications such as, succinylation, hydroxybutyrylation, and lactylation, and update the current advances in metabolism- and epigenetic modification-based therapeutic prospects in cancer. Show less
📄 PDF DOI: 10.1007/s13238-021-00846-7
amino-acid review
Dai W, Zhang J, Li S +8 more · 2022 · Frontiers in immunology · Frontiers · added 2026-04-20
In recent years, protein arginine methyltransferases (PRMTs) have emerged as new members of a gene expression regulator family in eukaryotes, and are associated with cancer pathogenesis and progressio Show more
In recent years, protein arginine methyltransferases (PRMTs) have emerged as new members of a gene expression regulator family in eukaryotes, and are associated with cancer pathogenesis and progression. Cancer immunotherapy has significantly improved cancer treatment in terms of overall survival and quality of life. Protein arginine methylation is an epigenetic modification function not only in transcription, RNA processing, and signal transduction cascades, but also in many cancer-immunity cycle processes. Arginine methylation is involved in the activation of anti-cancer immunity and the regulation of immunotherapy efficacy. In this review, we summarize the most up-to-date information on regulatory molecular mechanisms and different underlying arginine methylation signaling pathways in innate and adaptive immune responses during cancer. We also outline the potential of PRMT-inhibitors as effective combinatorial treatments with immunotherapy. Show less
📄 PDF DOI: 10.3389/fimmu.2022.865964
amino-acid review
2022 · Molecular Cancer Therapeutics · added 2026-04-20
Abstract CCAAT/enhancer binding protein β (C/EBPβ) is a basic leucine zipper (bZIP) family transcription factor, which is upregulated or overactivate Show more
Abstract CCAAT/enhancer binding protein β (C/EBPβ) is a basic leucine zipper (bZIP) family transcription factor, which is upregulated or overactivated in many cancers, resulting in a gene expression profile that drives oncogenesis. C/EBPβ dimerization regulates binding to DNA at the canonical TTGCGCAA motif and subsequent transcriptional activity, suggesting that disruption of dimerization represents a powerful approach to inhibit this previously “undruggable” oncogenic target. Here we describe the mechanism of action and antitumor activity of ST101, a novel and selective peptide antagonist of C/EBPβ that is currently in clinical evaluation in patients with advanced solid tumors. ST101 binds the leucine zipper domain of C/EBPβ, preventing its dimerization and enhancing ubiquitin-proteasome dependent C/EBPβ degradation. ST101 exposure attenuates transcription of C/EBPβ target genes, including a significant decrease in expression of survival, transcription factors, and cell-cycle-related proteins. The result of ST101 exposure is potent, tumor-specific in vitro cytotoxic activity in cancer cell lines including glioblastoma, breast, melanoma, prostate, and lung cancer, whereas normal human immune and epithelial cells are not impacted. Further, in mouse xenograft models ST101 exposure results in potent tumor growth inhibition or regression, both as a single agent and in combination studies. These data provide the First Disclosure of ST101, and support continued clinical development of ST101 as a novel strategy for targeting C/EBPβ-dependent cancers. Show less
no PDF DOI: 10.1158/1535-7163.mct-21-0962
amino-acid anticancer
Isabel Kleinwächter, Bernadette Mohr, Aljoscha Joppe +4 more · 2022 · RSC Chemical Biology · Royal Society of Chemistry · added 2026-04-20
Cardiolipin, the mitochondria marker lipid, is crucially involved in stabilizing the inner mitochondrial membrane and is vital for the activity of mitochondrial proteins and protein complexes. Directl Show more
Cardiolipin, the mitochondria marker lipid, is crucially involved in stabilizing the inner mitochondrial membrane and is vital for the activity of mitochondrial proteins and protein complexes. Directly targeting cardiolipin by a chemical-biology approach and thereby altering the cellular concentration of "available" cardiolipin eventually allows to systematically study the dependence of cellular processes on cardiolipin availability. In the present study, physics-based coarse-grained free energy calculations allowed us to identify the physical and chemical properties indicative of cardiolipin selectivity and to apply these to screen a compound database for putative cardiolipin-binders. The membrane binding properties of the 22 most promising molecules identified in the in silico approach were screened in vitro, using model membrane systems finally resulting in the identification of a single molecule, CLiB (CardioLipin-Binder). CLiB clearly affects respiration of cardiolipin-containing intact bacterial cells as well as of isolated mitochondria. Thus, the structure and function of mitochondrial membranes and membrane proteins might be (indirectly) targeted and controlled by CLiB for basic research and, potentially, also for therapeutic purposes. Show less
📄 PDF DOI: 10.1039/d2cb00125j
amino-acid mitochondria
de Souza JG, Fernandes MAC, de Melo Barbosa R · 2022 · Pharmaceutics · MDPI · added 2026-04-20
Drug discovery (DD) is a time-consuming and expensive process. Thus, the industry employs strategies such as drug repositioning and drug repurposing, which allows the application of already approved d Show more
Drug discovery (DD) is a time-consuming and expensive process. Thus, the industry employs strategies such as drug repositioning and drug repurposing, which allows the application of already approved drugs to treat a different disease, as occurred in the first months of 2020, during the COVID-19 pandemic. The prediction of drug-target interactions is an essential part of the DD process because it can accelerate it and reduce the required costs. DTI prediction performed in silico have used approaches based on molecular docking simulations, including similarity-based and network- and graph-based ones. This paper presents MPS2IT-DTI, a DTI prediction model obtained from research conducted in the following steps: the definition of a new method for encoding molecule and protein sequences onto images; the definition of a deep-learning approach based on a convolutional neural network in order to create a new method for DTI prediction. Training results conducted with the Davis and KIBA datasets show that MPS2IT-DTI is viable compared to other state-of-the-art (SOTA) approaches in terms of performance and complexity of the neural network model. With the Davis dataset, we obtained 0.876 for the concordance index and 0.276 for the MSE; with the KIBA dataset, we obtained 0.836 and 0.226 for the concordance index and the MSE, respectively. Moreover, the MPS2IT-DTI model represents molecule and protein sequences as images, instead of treating them as an NLP task, and as such, does not employ an embedding layer, which is present in other models. Show less
📄 PDF DOI: 10.3390/pharmaceutics14030625
ML amino-acid docking
Ambre M Bertholet, Andrew M Natale, Paola Bisignano +10 more · 2022 · Nature · Nature · added 2026-04-20
Mitochondria generate heat due to H+ leak (IH) across their inner membrane1. IH results from the action of long-chain fatty acids on uncoupling protein 1 (UCP1) in brown fat2-6 and ADP/ATP carrier (AA Show more
Mitochondria generate heat due to H+ leak (IH) across their inner membrane1. IH results from the action of long-chain fatty acids on uncoupling protein 1 (UCP1) in brown fat2-6 and ADP/ATP carrier (AAC) in other tissues1,7-9, but the underlying mechanism is poorly understood. As evidence of pharmacological activators of IH through UCP1 and AAC is lacking, IH is induced by protonophores such as 2,4-dinitrophenol (DNP) and cyanide-4-(trifluoromethoxy) phenylhydrazone (FCCP)10,11. Although protonophores show potential in combating obesity, diabetes and fatty liver in animal models12-14, their clinical potential for treating human disease is limited due to indiscriminately increasing H+ conductance across all biological membranes10,11 and adverse side effects15. Here we report the direct measurement of IH induced by DNP, FCCP and other common protonophores and find that it is dependent on AAC and UCP1. Using molecular structures of AAC, we perform a computational analysis to determine the binding sites for protonophores and long-chain fatty acids, and find that they overlap with the putative ADP/ATP-binding site. We also develop a mathematical model that proposes a mechanism of uncoupler-dependent IH through AAC. Thus, common protonophoric uncouplers are synthetic activators of IH through AAC and UCP1, paving the way for the development of new and more specific activators of these two central mediators of mitochondrial bioenergetics. Show less
📄 PDF DOI: 10.1038/s41586-022-04747-5
amino-acid mitochondria
Ling Gao, Luyao Chen, Yu Peng +5 more · 2022 · Dalton Transactions · Royal Society of Chemistry · added 2026-04-20
In this work, three iridium(III) tetrazolato complexes have been designed and successfully synthesized. Beside photophysical properties, their performances in protein staining have been compre Show more
In this work, three iridium(III) tetrazolato complexes have been designed and successfully synthesized. Beside photophysical properties, their performances in protein staining have been comprehensively investigated in this work for the first time. Notably, these iridium(III) tetrazolato complexes with high quantum efficiency exhibited much better protein staining properties than the commercial agent Coomassie Brilliant Blue (CBB) under the same experimental conditions, which may pave the way to explore new efficient iridium-based protein staining agents both for commercial markets and academic research in the future. Show less
📄 PDF DOI: 10.1039/D2DT02564G
Ir amino-acid synthesis tetrazole
Singaram, Indira, Sharma, Ashutosh, Pant, Shashank +12 more · 2022 · Nature Publishing Group · Nature · added 2026-04-20
A small molecule was developed that disrupted the lipid–SH2 domain interaction of the spleen tyrosine kinase (Syk), suppressed oncogenic activities in acute myeloid leukemia cell lines and was refract Show more
A small molecule was developed that disrupted the lipid–SH2 domain interaction of the spleen tyrosine kinase (Syk), suppressed oncogenic activities in acute myeloid leukemia cell lines and was refractory to drug resistance. Show less
📄 PDF DOI: 10.1038/s41589-022-01150-z
amino-acid
Zhang, Guangzhi, Wang, Jinyong, Zhao, Zhanran +7 more · 2022 · Nature Publishing Group · Nature · added 2026-04-20
Since the discovery of cell apoptosis, other gene-regulated cell deaths are gradually appreciated, including pyroptosis, ferroptosis, and necroptosis. Necroptosis is, so far, one of the best-character Show more
Since the discovery of cell apoptosis, other gene-regulated cell deaths are gradually appreciated, including pyroptosis, ferroptosis, and necroptosis. Necroptosis is, so far, one of the best-characterized regulated necrosis. In response to diverse stimuli (death receptor or toll-like receptor stimulation, pathogenic infection, or other factors), necroptosis is initiated and precisely regulated by the receptor-interacting protein kinase 3 (RIPK3) with the involvement of its partners (RIPK1, TRIF, DAI, or others), ultimately leading to the activation of its downstream substrate, mixed lineage kinase domain-like (MLKL). Necroptosis plays a significant role in the host’s defense against pathogenic infections. Although much has been recognized regarding modulatory mechanisms of necroptosis during pathogenic infection, the exact role of necroptosis at different stages of infectious diseases is still being unveiled, e.g., how and when pathogens utilize or evade necroptosis to facilitate their invasion and how hosts manipulate necroptosis to counteract these detrimental effects brought by pathogenic infections and further eliminate the encroaching pathogens. In this review, we summarize and discuss the recent progress in the role of necroptosis during a series of viral, bacterial, and parasitic infections with zoonotic potentials, aiming to provide references and directions for the prevention and control of infectious diseases of both human and animals. Show less
📄 PDF DOI: 10.1038/s41419-022-05066-3
Fe amino-acid review
Sven T Stripp, Benjamin R Duffus, Vincent Fourmond +7 more · 2022 · Chemical Reviews · ACS Publications · added 2026-04-20
Gases like H2, N2, CO2, and CO are increasingly recognized as critical feedstock in "green" energy conversion and as sources of nitrogen and carbon for the agricultural and chemical sectors. However, Show more
Gases like H2, N2, CO2, and CO are increasingly recognized as critical feedstock in "green" energy conversion and as sources of nitrogen and carbon for the agricultural and chemical sectors. However, the industrial transformation of N2, CO2, and CO and the production of H2 require significant energy input, which renders processes like steam reforming and the Haber-Bosch reaction economically and environmentally unviable. Nature, on the other hand, performs similar tasks efficiently at ambient temperature and pressure, exploiting gas-processing metalloenzymes (GPMs) that bind low-valent metal cofactors based on iron, nickel, molybdenum, tungsten, and sulfur. Such systems are studied to understand the biocatalytic principles of gas conversion including N2 fixation by nitrogenase and H2 production by hydrogenase as well as CO2 and CO conversion by formate dehydrogenase, carbon monoxide dehydrogenase, and nitrogenase. In this review, we emphasize the importance of the cofactor/protein interface, discussing how second and outer coordination sphere effects determine, modulate, and optimize the catalytic activity of GPMs. These may comprise ionic interactions in the second coordination sphere that shape the electron density distribution across the cofactor, hydrogen bonding changes, and allosteric effects. In the outer coordination sphere, proton transfer and electron transfer are discussed, alongside the role of hydrophobic substrate channels and protein structural changes. Combining the information gained from structural biology, enzyme kinetics, and various spectroscopic techniques, we aim toward a comprehensive understanding of catalysis beyond the first coordination sphere. Show less
no PDF DOI: 10.1021/acs.chemrev.1c00914
Co Fe Ni amino-acid catalysis review
Tania Gamberi, Giovanni Chiappetta, Tania Fiaschi +3 more · 2022 · Medicinal Research Reviews · Wiley · added 2026-04-20
AbstractAuranofin is an oral gold(I) compound, initially developed for the treatment of rheumatoid arthritis. Currently, Auranofin is under investigation for oncological application within a drug repu Show more
AbstractAuranofin is an oral gold(I) compound, initially developed for the treatment of rheumatoid arthritis. Currently, Auranofin is under investigation for oncological application within a drug repurposing plan due to the relevant antineoplastic activity observed both in vitro and in vivo tumor models. In this review, we analysed studies in which Auranofin was used as a single drug or in combination with other molecules to enhance their anticancer activity or to overcome chemoresistance. The analysis of different targets/pathways affected by this drug in different cancer types has allowed us to highlight several interesting targets and effects of Auranofin besides the already well‐known inhibition of thioredoxin reductase. Among these targets, inhibitory‐κB kinase, deubiquitinates, protein kinase C iota have been frequently suggested. To rationalize the effects of Auranofin by a system biology‐like approach, we exploited transcriptomic data obtained from a wide range of cell models, extrapolating the data deposited in the Connectivity Maps website and we attempted to provide a general conclusion and discussed the major points that need further investigation. Show less
no PDF DOI: 10.1002/med.21872
Au amino-acid anticancer review
Ulasov AV, Rosenkranz AA, Georgiev GP +1 more · 2022 · Life Sciences · Elsevier · added 2026-04-20
The Nrf2 transcription factor governs the expression of hundreds genes involved in cell defense against oxidative stress, the hallmark of numerous diseases such as neurodegenerative, cardiovascular, s Show more
The Nrf2 transcription factor governs the expression of hundreds genes involved in cell defense against oxidative stress, the hallmark of numerous diseases such as neurodegenerative, cardiovascular, some viral pathologies, diabetes and others. The main route for Nrf2 activity regulation is via interactions with the Keap1 protein. Under the normoxia the Keap1 binds the Nrf2 and targets it to the proteasomal degradation, while the Keap1 is regenerated. Upon oxidative stress the interactions between Nrf2 and Keap1 are interrupted and the Nrf2 activates the transcription of the protective genes. Currently, the Nrf2 system activation is considered as a powerful cytoprotective strategy for treatment of different pathologies, which pathogenesis relies on oxidative stress including viral diseases of pivotal importance such as COVID-19. The implementation of this strategy is accomplished mainly through the inactivation of the Keap1 "guardian" function. Two approaches are now developing: the Keap1 modification via electrophilic agents, which leads to the Nrf2 release, and direct interruption of the Nrf2:Keap1 protein-protein interactions (PPI). Because of theirs chemical structure, the Nrf2 electrophilic inducers could non-specifically interact with others cellular proteins leading to undesired effects. Whereas the non-electrophilic inhibitors of the Nrf2:Keap1 PPI could be more specific, thereby widening the therapeutic window. Show less
📄 PDF DOI: 10.1016/j.lfs.2021.120111
ROS amino-acid
Aina Calls, Abel Torres‐Espin, Marc Tormo +7 more · 2022 · Annals of Clinical and Translational Neurology · Wiley · added 2026-04-20
AbstractObjectivesPeripheral neuropathy is a relevant dose‐limiting adverse event that can affect up to 90% of oncologic patients with colorectal cancer receiving oxaliplatin treatment. The severity o Show more
AbstractObjectivesPeripheral neuropathy is a relevant dose‐limiting adverse event that can affect up to 90% of oncologic patients with colorectal cancer receiving oxaliplatin treatment. The severity of neurotoxicity often leads to dose reduction or even premature cessation of chemotherapy. Unfortunately, the limited knowledge about the molecular mechanisms related to oxaliplatin neurotoxicity leads to a lack of effective treatments to prevent the development of this clinical condition. In this context, the present work aimed to determine the exact molecular mechanisms involved in the development of oxaliplatin neurotoxicity in a murine model to try to find new therapeutical targets.MethodsBy single‐cell RNA sequencing (scRNA‐seq), we studied the transcriptomic profile of sensory neurons and satellite glial cells (SGC) of the Dorsal Root Ganglia (DRG) from a well‐characterized mouse model of oxaliplatin neurotoxicity.ResultsAnalysis of scRNA‐seq data pointed to modulation of inflammatory processes in response to oxaliplatin treatment. In this line, we observed increased levels of NF‐kB p65 protein, pro‐inflammatory cytokines, and immune cell infiltration in DRGs and peripheral nerves of oxaliplatin‐treated mice, which was accompanied by mechanical allodynia and decrease in sensory nerve amplitudes.InterpretationOur data show that, in addition to the well‐described DNA damage, oxaliplatin neurotoxicity is related to an exacerbated pro‐inflammatory response in DRG and peripheral nerves, and open new insights in the development of anti‐inflammatory strategies as a treatment for preventing peripheral neuropathy induced by oxaliplatin. Show less
no PDF DOI: 10.1002/acn3.51691
DNA-binding amino-acid
Jiho Yoo · 2022 · BMB reports · added 2026-04-20
Mitochondria are cellular organelles that perform various functions within cells. They are responsible for ATP production, cell-signal regulation, autophagy, and cell apoptosis. Because the mitochondr Show more
Mitochondria are cellular organelles that perform various functions within cells. They are responsible for ATP production, cell-signal regulation, autophagy, and cell apoptosis. Because the mitochondrial proteins that perform these functions need Ca2+ ions for their activity, mitochondria have ion channels to selectively uptake Ca2+ ions from the cytoplasm. The ion channel known to play the most important role in the Ca2+ uptake in mitochondria is the mitochondrial calcium uniporter (MCU) holo-complex located in the inner mitochondrial membrane (IMM). This ion channel complex exists in the form of a complex consisting of the pore-forming protein through which the Ca2+ ions are transported into the mitochondrial matrix, and the auxiliary protein involved in regulating the activity of the Ca2+ uptake by the MCU holo-complex. Studies of this MCU holocomplex have long been conducted, but we didn't know in detail how mitochondria uptake Ca2+ ions through this ion channel complex or how the activity of this ion channel complex is regulated. Recently, the protein structure of the MCU holo-complex was identified, enabling the mechanism of Ca2+ uptake and its regulation by the MCU holo-complex to be confirmed. In this review, I will introduce the mechanism of action of the MCU holo-complex at the molecular level based on the Cryo-EM structure of the MCU holo-complex to help understand how mitochondria uptake the necessary Ca2+ ions through the MCU holo-complex and how these Ca2+ uptake mechanisms are regulated. [BMB Reports 2022; 55(11): 528-534]. Show less
no PDF DOI: 10.5483/BMBRep.2022.55.11.134
amino-acid mitochondria review