đŸ‘€ KW Daniel

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9
Articles
9
Name variants
Also published as: AG Daniel, Carrizo, Daniel, L. Daniel, Laurianne Daniel, M.C. Daniel, Santhanaraj Daniel, Sheeba Daniel, Whitaker, Daniel
articles
Singh, Jyoti, Thoma, Benjamin, Whitaker, Daniel +3 more · 2025 · Nature Publishing Group · Nature · added 2026-04-20
Aminoacyl-thiols reacting selectively with RNA diols over amine nucleophiles and demonstration of chemically controlled formation of peptidyl-RNA in water at neutral pH suggest an important role for t Show more
Aminoacyl-thiols reacting selectively with RNA diols over amine nucleophiles and demonstration of chemically controlled formation of peptidyl-RNA in water at neutral pH suggest an important role for thiol cofactors before the evolution of enzymes. Show less
📄 PDF DOI: 10.1038/s41586-025-09388-y
synthesis
Zorzano, Maria-Paz, Basapathi Raghavendra, Jyothi, Carrizo, Daniel +4 more · 2025 · Nature Publishing Group · Nature · added 2026-04-20
Taxonomically identifiable DNA can be recovered from terrestrial rocks containing as little as 182 ppm of total organic carbon after exposure to radiation equivalent to 136 million years on Mars, sugg Show more
Taxonomically identifiable DNA can be recovered from terrestrial rocks containing as little as 182 ppm of total organic carbon after exposure to radiation equivalent to 136 million years on Mars, suggesting that biosignatures could remain detectable. Show less
📄 PDF DOI: 10.1038/s43247-025-02809-w
biosignatures dna dna extraction organic carbon radiation exposure
S. Hangan, J. Lodge, A. Odani +529 more · 2024 · Molecules · MDPI · added 2026-04-20
S. Hangan, J. Lodge, A. Odani, T. Yamaguchi, I. Persson, N. Hadjiliadis, E. Sletten, S.A. Mehrdad, A. Cucchiarini, J.L. Mergny, S.K. Noureini, S. Muthaiah, A. Bhatia, M. Kannan, A.N. Srivastva, M. Stankovic, J. Kljun, N.L.J. Stevanovic, J. Lazic, S.S. Bogojevic, S. Vojnovic, M. Zlatar, J. Nikodinovic-Runic, I. Turel, M.I. Djuran, I. Aleksic, A. Veselinovic, B.D. Glisic, H. Alshater, A.I. Al-Sulami, S.A. Aly, E.M. Abdalla, M.A. Sakr, S.S. Hassan, S. de la Mata Moratilla, S. Casado Angulo, N. GĂłmez-Casanova, J.L. Copa-Patiño, I. Heredero-Bermejo, F.J. de la Mata, S. GarcĂ­a-Gallego, A. Hangan, A. Turza, R.L. Lucaciu, B. Sevastre, E. Pall, L.S. Oprean, G. Borodi, D. Rusu, A. Stănilă, I.O. Marian, C.O. Marian, M. Rusu, R. Lucaciu, T.J. Hubin, P.N. Amoyaw, K.D. Roewe, N.C. Simpson, R.D. Maples, T.N. Carder Freeman, A.N. Cain, J.G. Le, S.J. Archibald, S.I. Khan, E. Bortolamiol, F. Visentin, T. Scattolin, I. Kostova, A.C. Hangan, L. Dican, E. PĂĄll, R.L. Stan, S. Gheorghe-Cetean, A. Tsoupras, S. Pafli, C. Stylianoudakis, K. Ladomenou, C.A. Demopoulos, A. Philippopoulos, J. Wlodarczyk, J. Krajewska, L. Szeleszczuk, P. Szalwinska, A. Gurba, S. Lipiec, P. Taciak, R. Szczepaniak, I. Mlynarzuk-Bialy, J. Fichna, C. Abate, F. Carnamucio, O. Giuffre, C. Foti, C. Chuong, C.M. DuChane, E.M. Webb, P. Rai, J.M. Marano, C.M. Bernier, J.S. Merola, J. Weger-Lucarelli, L. Oprean, P. Kumar, S. Gorai, M.K. Santra, B. Mondal, D. Manna, M. Sirajuddin, S. Ali, A. Badshah, J.D. Watson, F.H.C. Crick, B. Maddox, P.J. Kennelly, K.M. Botham, O. McGuinness, V.W. Rodwell, P.A. Weil, R.A. Harvey, D.R. Ferrier, J.M. Berg, J.L. Tymoczko, G.J. Gatto, L. Stryer, J.A. Cowan, P. Yakovchuk, E. Protozanova, M.D. Frank-Kamenetskii, M.J. Hannon, I. Bertini, H.B. Gray, S.J. Lippard, J.S. Valentine, Z. Shakked, G. Guerstein-Guzikevich, M. Eisenstein, F. Frolow, D. Rabinovich, J.C. Garcia-Ramos, R. Galindo-Murillo, F. Cortez-Guzman, L. Ruiz-Azuara, S. Neidle, M. HĂ€gerlöf, P. Papsai, C.S. Chow, S.K.C. Elmroth, J. François, N.T. Thuong, C. HĂ©lĂšne, J.L. Huppert, T.A. Brooks, S. Kendrick, L. Hurley, X. Li, Y. Peng, J. Ren, X. Qu, Y. Akiyama, S.M. Hecht, L.H. Hurley, J. Zhou, C. Wei, G. Jia, X. Wang, Z. Feng, C. Li, A. Mukherjee, K.M. Vasquez, E. Marian, L.G. Vicas, J. Tunde, M. Muresan, Z. Diaconeasa, C. Ionescu, R.G. Pearson, G. Barone, A. Terenzi, A. Lauria, A.M. Almerico, J.M. Leal, N. Busto, B. Garcia, J. Vinje, J.A. Parkinson, P.J. Sadler, T. Brown, A.A. Almaqwashi, T. Paramanathan, I. Rouzina, M.C. Williams, F.R. Keene, J.A. Smith, J.G. Collins, A. Rilak, R. Masnikosa, I. Bratsos, E. Alessio, S.K. Srivastava, T.C. Johnstone, K. Suntharalingam, S. Cetean, T. Ciuleanu, D.C. Leucuta, C. Cainap, A.M. Constantin, I. Cazacu, S. Cainap, A. Gherman, Y. He, Y. Ding, D. Wang, W. Zhang, W. Chen, X. Liu, W. Qin, X. Qian, H. Chen, Z. Guo, E. StefĂ no, F. De Castro, A. Ciccarese, A. Muscella, S. Marsigliante, M. Benedetti, F.P. Fanizzi, P.M. Takahara, A.C. Rosenzweig, C.A. Frederick, M. Demeunynck, C. Bailly, W.D. Wilson, K. Nakamoto, M. Tsuboi, G.D. Strahan, B.M. Zeglis, V.C. Pierre, J.K. Barton, C. Shobha Devi, B. Thulasiram, R.R. Aerva, P. Nagababu, T. Biver, F. Secco, M. Venturini, C.E. Maciel-Flores, J.A. Lozano-Alvarez, E.Y. BiviĂĄn-Castro, F. Jia, S. Wang, Y. Man, B. Liu, P. Modrich, A. Erxleben, E. Dumont, A. Monari, D.L. Morris, G.S. Khan, A. Shah, D. Zia-ur-Rehman, B.J. Pages, D.L. Ang, E.P. Wright, J.R. Aldrich-Wright, S.M. Nelson, L.R. Ferguson, W.A. Denny, L. Winkler, F. Cortes-Guzman, T.E. Cheatham, O. Sarpataki, N.K. Olah, M. Taulescu, I. Marcus, C. Cătoi, M.M. GonzĂĄlez-Ballesteros, L. SĂĄnchez-SĂĄnchez, A. Espinoza-GuillĂ©n, J. Espinal-EnrĂ­quez, C. MejĂ­a, E. HernĂĄndez-Lemus, P.H. von Hippel, A.H. Marcus, S. Komeda, T. Moulaei, K. Kruger Woods, M. Chikuma, N.P. Farrell, L.D. Williams, T. Jany, A. Moreth, C. Gruschka, A. Sischka, A. Spiering, M. Dieding, Y. Wang, S. Haji Samo, A. Stammler, H. Bögge, S. Li, B. Yuan, J. Zhang, L. Yue, H. Hou, J. Hu, S. Chen, B.R. Kirthan, M.C. Prabhakara, H.S. Bhojya Naik, P.H.A. Nayak, E.I. Naik, U. Saha, S. Chatterjee, M. Dolai, G.S. Kumar, A.M. Abu-Dief, N.H. Alotaibi, E.S. Al-Farraj, H.A. Qasem, S. Alzahrani, M.K. Mahfouz, A. Abdou, B. Kurt, H. Temel, M. Atlan, S. Kaya, H.A. Kiwaan, A.S. El-Mowafy, A.A. El-Bindary, S. Baskaran, M.N. Krishnan, M. Arumugham, R. Kumar, N. Kumar, R. Kaushal, P. Awasthi, A. Kellett, Z. Molphy, C. Slator, V. McKee, V.G. Vaidyanathan, B.U. Nair, R. Vijayalakshmi, P. Karacan, O. Okay, S. Phukan, S. Mitra, S. Nafisi, A.A. Saboury, N. Keramat, J.F. Neault, H.A. Tajmir-Riahi, P. Sathyadevi, P. Krishnamoorthy, R.R. Butorac, A.H. Cowley, N.S.P. Bhuvanesh, N. Dharmaraj, F. Arjmand, S. Parveen, M. Afzal, M. Shahid, J.B. Lepecq, C. Paoletti, J.L. Garcia-Gimenez, M. Gonzalez-Alvarez, M. Liu-Gonzalez, B. Macias, J. Borras, G. Alzuet, M. Aslanoglu, M. Zaheer, R. Qureshi, Z. Akhter, M.F. Nazar, M. Ngoepe, H. Clayton, P. Mucha, P. Hikisz, K. GwoĆșdziƄski, U. Krajewska, A. Leniart, E. Budzisz, E.F. Garman, J.R. Helliwell, E.P. Mitchell, A.N. Boynton, K.M. Boyle, M.J. Waring, S. Da Vela, D.I. Svergun, L.A. Feigin, P.P.P. Kumar, D.K. Lim, T.H. Jensen, M. Bech, O. Bunk, M. Thomsen, A. Menzel, A. Bouchet, G. Le Duc, R. Feidenhans, F. Pfeiffer, S. Sidhu, G. Falzon, S.A. Hart, J.G. Fox, R.A. Lewis, K.K.W. Siu, D.A. Jacques, J. Trewhella, N. Allec, M. Choi, N. Yesupriya, B. Szychowski, M.R. White, M.G. Kann, E.D. Garcin, M.C. Daniel, A. Badano, Y. Qu, J.B. Mangrum, A. Hegmans, S.J. Berners-Price, L. Ronconi, X. Filip, C. Tripon, C. Morari, C. Filip, T. Urathamakul, D.J. Waller, J.L. Beck, S.F. Ralph, X. Fan, J. Wang, X. Zhang, Z. Yang, J.C. Zhang, L. Zhao, H. Peng, J. Lei, H.W. Wang, J.L. Rubinstein, X. Benjin, L. Ling, A. Punjani, D.J. Fleet, M.A. Brubaker, A. Goldstein, Y. Soroka, M. FruĆĄic-Zlotkin, I. Popov, R. Kohen, M. Havrdova, K. Polakova, J. Skopalik, M. Vujtek, A. Mokdad, M. Homolkova, J. Tucek, J. Nebesarova, R. Zboril, M. Malatesta, M.R. RodrĂ­guez, M.J. Lavecchia, B.Z. ParajĂłn-Costa, A.C. GonzĂĄlez-BarĂł, M.R. GonzĂĄlez-BarĂł, E. CattĂĄneo, A.N. Alaghaz, S. Aldulmani, A. Yadav, K. Poonia, R. Ștefan, K.R. Fox, M.V. Villa, R. Lapresa, J. Hernandez-Gil, F. Sanz, J.B. Chaires, M. Mudasir, E.T. Wahyuni, D.H. Tjahjono, N. Yoshioka, H. Inoue, P. Jaividhya, R. Dhivya, M.A. Akbarsha, M. Palaniandavar, N. Raman, R. Jeyamurugan, A. Sakthivel, L. Mitu, A. Prisecaru, R.G. Kipping, E.J. Peterson, J.L. GarcĂ­a-GimĂ©nez, J. HernĂĄndez-Gil, A. MartĂ­nez-RuĂ­z, A. Castiñeiras, M. Liu-GonzĂĄles, F.V. PallardĂł, J. BorrĂĄs, G. Alzuet Piña, M. Swathi, D.S. Shankar, S. Daravath, N. Ganji, P.V.A. Lakshmi, R. Shivaraj, A. PĂ©rez, F.J. Luque, M. Orozco, N.M. Henriksen, D.R. Davis, D.A. Case, T.E.I. Cheatham, T. Darden, H. Gohlke, R. Luo, K.M. Merz, A. Onufriev, C. Simmerling, B. Wang, R.J. Woods, M.B. Peters, Y. Yang, L. FĂŒsti-MolnĂĄr, M.N. Weaver, M. Sahadevan, M. Sundaram, K. Subramanian Show less
DNA structure has many potential places where endogenous compounds and xenobiotics can bind. Therefore, xenobiotics bind along the sites of the nucleic acid with the aim of changing its structure, its Show more
DNA structure has many potential places where endogenous compounds and xenobiotics can bind. Therefore, xenobiotics bind along the sites of the nucleic acid with the aim of changing its structure, its genetic message, and, implicitly, its functions. Currently, there are several mechanisms known to be involved in DNA binding. These mechanisms are covalent and non-covalent interactions. The covalent interaction or metal base coordination is an irreversible binding and it is represented by an intra-/interstrand cross-link. The non-covalent interaction is generally a reversible binding and it is represented by intercalation between DNA base pairs, insertion, major and/or minor groove binding, and electrostatic interactions with the sugar phosphate DNA backbone. In the present review, we focus on the types of DNA–metal complex interactions (including some representative examples) and on presenting the methods currently used to study them. Show less
📄 PDF DOI: 10.3390/molecules29184361
DNA-binding coordination-chemistry review
Santhiya S, Arul Mary S, Sheeba Daniel · 2024 · Chemical Physics Impact · Elsevier · added 2026-05-01
📄 PDF DOI: 10.1016/j.chphi.2023.100424
Biometal
S. Arul Mary, Sheeba Daniel, P. Sakthivel · 2024 · Inorganic Chemistry Communications · Elsevier · added 2026-05-01
📄 PDF DOI: 10.1016/j.inoche.2024.113339
Biometal
K.M. Okuda, L.S. Churchman, R.D. Chapman +252 more · 2022 · Nucleic acids research · Oxford University Press · added 2026-04-20
K.M. Okuda, L.S. Churchman, R.D. Chapman, M. Heidemann, C. Hintermair, D. Eick, E. Compe, J.M. Egly, P. Di Lello, L.M. Miller Jenkins, C. Mas, C. Langlois, E. Malitskaya, A. Fradet-Turcotte, J. Archambault, P. Legault, J.G. Omichinski, M. Okuda, A. Tanaka, M. Satoh, S. Mizuta, M. Takazawa, Y. Ohkuma, Y. Nishimura, L.M. Jenkins, T.N. Jones, B.D. Nguyen, T. Hara, H. Yamaguchi, J.D. Dikeakos, E. Appella, M. Lussier-Price, S. Soni, T. Morse, G. Arseneault, J. Lafrance-Vanasse, J.J. Bieker, K. Araki, K. Ohtani, K. Potempa, M.S. Kobor, P.R. Chabot, L. Raiola, L. Cappadocia, M. Kinoshita, E. Kakumu, K. Sugasawa, Y. Nakazawa, C. Guo, T. Ogi, V. Gervais, V. Lamour, A. Jawhari, F. Frindel, E. Wasielewski, S. Dubaele, J.C. Thierry, B. Kieffer, A. Poterszman, H.T. Chen, Y. He, C. Yan, J. Fang, C. Inouye, R. Tjian, I. Ivanov, E. Nogales, B.J. Greber, T.H.D. Nguyen, P.V. Afonine, P.D. Adams, D.B. Toso, J. Cavanagh, W.J. Fairbroher, A.G., III Palmer, N.J. Skelton, F. Delaglio, S. Grzesiek, G.W. Vuister, G. Zhu, J. Pfeifer, A. Bax, B.A. Johnson, R.A. Blevins, G. Cornilescu, A.T. BrĂŒnger, C.D. Schwieters, J.J. Kuszewski, N. Tjandra, G.M. Clore, J.P. Linge, M.A. Williams, C.A. Spronk, A.M. Bonvin, M. Nilges, R.A. Laskowski, J.A.C. Rullmann, M.W. MacArthur, R. Kaptein, J.M. Thornton, R. Koradi, M. Billeter, K. WĂŒthrich, T. Ekimoto, J. Kurita, M. Ikeguchi, S. Yamashita, A.R. Lehmann, C. McQuin, A. Goodman, V. Chernyshev, L. Kamentsky, B.A. Cimini, K.W. Karhohs, M. Doan, L. Ding, S.M. Rafelski, D. Thirstrup, P. Cramer, D.A. Bushnell, J. Fu, A.L. Gnatt, B. Maier-Davis, N.E. Thompson, R.R. Burgess, A.M. Edwards, P.R. David, R.D. Kornberg, F. del RĂ­o-Portilla, A. Gaskell, D. Gilbert, J.A. Ladias, G. Wagner, K. Kayukawa, Y. Makino, S. Yogosawa, T. Tamura, G.L. Christensen, C.D. Kelstrup, C. LyngsĂž, U. Sarwar, R. BĂžgebo, S.P. Sheikh, S. Gammeltoft, J.V. Olsen, J.L. Hansen, T. Dodd, J.A. Tainer, S.E. Tsutakawa, S.M. Vos, L. Farnung, M. Boehning, C. Wigge, A. Linden, H. Urlaub, E. Evans, J. Fellows, A. Coffer, R.D. Wood, A. Tapias, J. Auriol, D. Forget, J.H. Enzlin, O.D. SchĂ€rer, F. Coin, B. Coulombe, W.L. de Laat, N.G. Jaspers, J.H. Hoeijmakers, H. SpĂ„hr, G. Calero, L. Minakhin, S. Bhagat, A. Brunning, E.A. Campbell, S.A. Darst, R.H. Ebright, K. Severinov, S. Nouraini, J.D. Friesen, D. Xu, S. Nelson, M. Lee, A. Ishiguro, Y. Nogi, K. Hisatake, M. Muramatsu, A. Ishihama, Q. Tan, M.H. Prysak, N.A. Woychik, J.F. Briand, F. Navarro, P. Rematier, C. Boschiero, S. Labarre, M. Werner, G.V. Shpakovski, P. Thuriaux, A.I. Garrido-Godino, M.C. GarcĂ­a-LĂłpez, V. Goler-Baron, M. Selitrennik, O. Barkai, G. Haimovich, R. Lotan, M. Choder, Z.R. Qiu, B. Schwer, S. Shuman, L. Daniel, E. Cerutti, L.M. Donnio, J. Nonnekens, C. Carrat, S. Zahova, P.O. Mari, G. Giglia-Mari, Y. Yang, J. Hu, C.P. Selby, W. Li, A. Yimit, Y. Jiang, A. Sancar, Y. van der Weegen, H. Golan-Berman, T.E.T. Mevissen, K. Apelt, R. GonzĂĄlez-Prieto, J. Goedhart, E.E. Heilbrun, A.C.O. Vertegaal, D. van den Heuvel, J.C. Walter, Y. Hara, Y. Oka, O. Komine, Y. Daigaku, M. Isono, M. Shimada, N. Deger, L.A. Lindsey-Boltz, C. Engel, S. Sainsbury, A.C. Cheung, D. Kostrewa, N.A. Hoffmann, A.J. Jakobi, M. Moreno-Morcillo, S. Glatt, J. Kosinski, W.J.H. Hagen, C. Sachse, C.W. MĂŒller Show less
Abstract In eukaryotes, three RNA polymerases (RNAPs) play essential roles in the synthesis of various types of RNA: namely, RNAPI for rRNA; RNAPII for mRNA and most snRNAs; and RNAPIII for tRNA and Show more
Abstract In eukaryotes, three RNA polymerases (RNAPs) play essential roles in the synthesis of various types of RNA: namely, RNAPI for rRNA; RNAPII for mRNA and most snRNAs; and RNAPIII for tRNA and other small RNAs. All three RNAPs possess a short flexible tail derived from their common subunit RPB6. However, the function of this shared N-terminal tail (NTT) is not clear. Here we show that NTT interacts with the PH domain (PH-D) of the p62 subunit of the general transcription/repair factor TFIIH, and present the structures of RPB6 unbound and bound to PH-D by nuclear magnetic resonance (NMR). Using available cryo-EM structures, we modelled the activated elongation complex of RNAPII bound to TFIIH. We also provide evidence that the recruitment of TFIIH to transcription sites through the p62–RPB6 interaction is a common mechanism for transcription-coupled nucleotide excision repair (TC-NER) of RNAPI- and RNAPII-transcribed genes. Moreover, point mutations in the RPB6 NTT cause a significant reduction in transcription of RNAPI-, RNAPII- and RNAPIII-transcribed genes. These and other results show that the p62–RPB6 interaction plays multiple roles in transcription, TC-NER, and cell proliferation, suggesting that TFIIH is engaged in all RNAP systems. Show less
📄 PDF DOI: 10.1093/nar/gkab612
NMR synthesis
Jayanthi Eswaran, Anusuya Mariappan, Nagaveni Arumugham +5 more · 2022 · Journal of Molecular Structure · Elsevier · added 2026-05-01
📄 PDF DOI: 10.1016/j.molstruc.2022.133929
Biometal
Laurianne Daniel, Elena Cerutti, Lise-Marie Donnio +5 more · 2018 · Proceedings of the National Academy of Sciences · National Academy of Sciences · added 2026-04-20
Significance RNAP1 transcription, dedicated to ribosomal DNAs (rDNAs), is the first and rate-limiting step of ribosome biogenesis. rDNAs are grouped into several copies. This redundancy is important t Show more
Significance RNAP1 transcription, dedicated to ribosomal DNAs (rDNAs), is the first and rate-limiting step of ribosome biogenesis. rDNAs are grouped into several copies. This redundancy is important to guarantee that at low damage levels one rDNA gene can be temporarily silenced without affecting overall ribosome biogenesis. Nevertheless, when DNA repair is defective or overloaded, several rDNAs could be damaged, disturbing the whole RNAP1 transcription process and later on modifying the ribosome content of cells. Therefore, it is of fundamental importance for the cell to maintain a functional RNAP1 transcription by repairing DNA lesions on rDNAs. In this work we identified, in mammals, the repair mechanism of rDNAs along with a specific behavior for RNAP1 after UV irradiation. Show less
no PDF DOI: 10.1073/pnas.1716581115
JP JeĆŸek, AGW Leslie, R Lutter +1993 more · 2018 · Antioxidants & redox signaling · added 2026-04-20
JP JeĆŸek, AGW Leslie, R Lutter, JE Walker, AE Adams, AM Carroll, PG Fallon, RK Porter, O Hanrahan, DN Nolan, HP Voorheis, P Fallon, OM Kelly, C Affourtit, MD Brand, M Jastroch, C Aguer, BD Piccolo, O Fiehn, SH Adams, ME Harper, L AlĂĄn, K SmolkovĂĄ, E KronusovĂĄ, J Ć antorovĂĄ, P JeĆŸek, EM Allister, CA Robson-Doucette, KJ Prentice, AB Hardy, S Sultan, HY Gaisano, D Kong, P Gilon, PL Herrera, BB Lowell, MB Wheeler, R Amat, G Solanes, M Giralt, F Villarroya, ZB Andrews, ZW Liu, N Walllingford, DM Erion, E Borok, JM Friedman, MH Tschöp, M Shanabrough, G Cline, GI Shulman, A Coppola, XB Gao, TL Horvath, S Diano, MA Aon, S Cortassa, E MarbĂĄn, B O'Rourke, H Aquila, TA Link, M Klingenberg, D Arsenijevic, H Onuma, C Pecqueur, S Raimbault, BS Manning, B Miroux, E Couplan, MC Alves-Guerra, M Goubern, R Surwit, F Bouillaud, D Richard, S Collins, D Ricquier, V Ayyasamy, KM Owens, MM Desouki, P Liang, A Bakin, K Thangaraj, DJ Buchsbaum, AF LoBuglio, KK Singh, V Azzu, EP Breen, N Parker, G Baffy, Z Derdak, SC Robson, Y Bai, X Bai, AV Medvedev, M Misukonis, JB Weinberg, W Cao, J Robidoux, LM Floering, KW Daniel, KA Ball, AW Nelson, DG Foster, RO Poyton, J Barlow, V Hirschberg Jensen, CJ Barnstable, R Reddy, H Li, W Basu Ball, S Kar, M Mukherjee, AG Chande, R Mukhopadhyaya, PK Das, JM Baughman, F Perocchi, HS Girgis, M Plovanich, CA Belcher-Timme, Y Sancak, XR Bao, L Strittmatter, O Goldberger, RL Bogorad, V Koteliansky, VK Mootha, V Beck, M JabĆŻrek, EE Pohl, T Demina, A Rupprecht, EL Bell, TA Klimova, J Eisenbart, CT Moraes, MP Murphy, GRS Budinger, NS Chandel, MJ Berardi, JJ Chou, WM Shih, SC Harrison, M Bertolotti, G Farinelli, M Galli, A Aiuti, R Sitia, J Blanc, B Esposito, S Rousset, P Gourdy, A Tedgui, Z Mallat, L Bleier, S Dröse, M Board, C Lopez, C van den Bos, R Callaghan, K Clarke, C Carr, AI Bondarenko, W Parichatikanond, CT Madreiter, R Rost, M Waldeck-Weiermair, R Malli, WF Graier, J BoreckĂœ, D Siemen, O Boss, S Samec, A Paoloni-Giacobino, C Rossier, A Dulloo, J Seydoux, P Muzzin, JP Giacobino, S Boudina, S Sena, BT O'Neill, P Tathireddy, ME Young, ED Abel, H Theobald, X Sheng, JJ Wright, XH Xia, S Aziz, JI Johnson, H Bugger, VG Zaha, TC Esteves, J Brandi, D Cecconi, M Cordani, M Torrens-Mas, R Pacchiana, E Dalla Pozza, G Butera, M Manfredi, E Marengo, J Oliver, P Roca, I Dando, M Donadelli, MO Breckwoldt, FMJ Pfister, PM Bradley, P Marinković, PR Williams, MS Brill, B Plomer, A Schmalz, DK St Clair, R Naumann, O Griesbeck, M SchwarzlĂ€nder, L Godinho, FM Bareyre, TP Dick, M Kerschensteiner, T Misgeld, W Pilgrim, KJ Clarke, C Yssel, M Farrell, J Zhou, PV Murphy, PS Brookes, JA Buckingham, A Vidal-Puig, AP Halestrap, TE Gunter, DG Nicholls, P Bernardi, JJ Lemasters, A Bugge, M SiersbĂŠk, MS Madsen, A Göndör, C Rougier, S Mandrup, C Guzman, C Zechner, M Palmeri, KS Russell, RR Russell, JA Cabrera, EA Ziemba, R Colbert, RF Kelly, M Kuskowski, EA Arriaga, W Sluiter, DJ Duncker, HB Ward, EO McFalls, V Calegari, CC Zoppi, L Rezende, L Silveira, E 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Abstract Significance: Mitochondria are the energetic, metabolic, redox, and information signaling centers of the cell. Substrate pressure, mitochondrial network dynamics, and cristae morphology Show more
Abstract Significance: Mitochondria are the energetic, metabolic, redox, and information signaling centers of the cell. Substrate pressure, mitochondrial network dynamics, and cristae morphology state are integrated by the protonmotive force Δ p or its potential component, Δ ι , which are attenuated by proton backflux into the matrix, termed uncoupling. The mitochondrial uncoupling proteins (UCP1–5) play an eminent role in the regulation of each of the mentioned aspects, being involved in numerous physiological events including redox signaling. Recent Advances: UCP2 structure, including purine nucleotide and fatty acid (FA) binding sites, strongly support the FA cycling mechanism: UCP2 expels FA anions, whereas uncoupling is achieved by the membrane backflux of protonated FA. Nascent FAs, cleaved by phospholipases, are preferential. The resulting Δ p dissipation decreases superoxide formation dependent on Δ p . UCP-mediated antioxidant protection and its impairment are expected to play a major role in cell physiology and pathology. Moreover, UCP2-mediated aspartate, oxaloacetate, and malate antiport with phosphate is expected to alter metabolism of cancer cells. Critical Issues: A wide range of UCP antioxidant effects and participations in redox signaling have been reported; however, mechanisms of UCP activation are still debated. Switching off/on the UCP2 protonophoretic function might serve as redox signaling either by employing/releasing the extra capacity of cell antioxidant systems or by directly increasing/decreasing mitochondrial superoxide sources. Rapid UCP2 degradation, FA levels, elevation of purine nucleotides, decreased Mg 2+ , or increased pyruvate accumulation may initiate UCP-mediated redox signaling. Future Directions: Issues such as UCP2 participation in glucose sensing, neuronal (synaptic) function, and immune cell activation should be elucidated. Antioxid. Redox Signal. 29, 667–714. Show less
📄 PDF DOI: 10.1089/ars.2017.7225
mitochondria