👤 B. Vladimir

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3
Articles
3
Name variants
Also published as: Gevorgyan, Vladimir, Gorshkov, Vladimir
articles

Targeting lipid–protein interaction to treat Syk-mediated acute myeloid leukemia - Nature Chemical Biology

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
đź“„ PDF DOI: 10.1038/s41589-022-01150-z
amino-acid

Role of AMPK in Regulation of Oxaliplatin-Resistant Human Colorectal Cancer

Y. Park, P. Xu, D.M. Parkin +324 more · 2022 · Biomedicines · MDPI · added 2026-04-20
Y. Park, P. Xu, D.M. Parkin, F. Bray, J. Ferlay, P. Pisani, N. Andre, W. Schmiegel, B. Gustavsson, G. Carlsson, D. Machover, N. Petrelli, A. Roth, H. Schmoll, K. Tveit, F. Gibson, G. Housman, S. Byler, S. Heerboth, K. Lapinska, M. Longacre, N. Snyder, S. Sarkar, L. Bao, S. Hazari, S. Mehra, D. Kaushal, K. Moroz, S. Dash, Z. Yuan, X. Shi, Y. Qi, T. Jia, X. Yuan, Y. Zou, C. Liu, H. Yu, Y. Yuan, X. He, A.K. Pandurangan, D. Chao, W. Jiao, C. Yin, N. Jianyun, C. Ceshi, A. Guerrero-Zotano, I.A. Mayer, C.L. Arteaga, C. Han, G. Xing, M. Zhang, M. Zhong, Z. Han, C. He, X. Liu, Z. Zou, T. Tao, H. Li, X. Zhu, D.D. Sarbassov, S.M. Ali, D.M. Sabatini, D. Heras-Sandoval, J.M. Pérez-Rojas, J. Hernández-Damián, J. Pedraza-Chaverri, J. Roper, M.P. Richardson, W.V. Wang, L.G. Richard, W. Chen, E.M. Coffee, M.J. Sinnamon, L. Lee, P. Chen, R.T. Bronson, Y. Kondo, T. Kanzawa, R. Sawaya, S. Kondo, W. Li, Y. Zhou, J. Yang, H. Zhang, P. Zheng, Z. Wang, N. Wang, P. Liu, X. Xie, D. Zhang, W. Wang, X. Sun, D. Xu, C. Wang, Q. Zhang, H. Wang, W. Luo, Y. Chen, H. Chen, Z. Cao, Y. Yang, S. Yu, Y. Li, J. Huang, L. Xiong, S. Lei, C. Peng, M.G. Vander Heiden, L.C. Cantley, C.B. Thompson, D.H. Suh, M.A. Kim, H. Kim, M. Kim, H.S. Kim, H.H. Chung, Y. Kim, Y.S. Song, J. Peng, Y. Cui, S. Xu, X. Wu, Y. Huang, W. Zhou, S. Wang, Z. Fu, H. Xie, G. Wang, Y. Yu, Y.Z. Wang, P.H. Yin, K. Xu, H. Bleiberg, P. Perego, J. Robert, W. Lian, M. Li, R.N. Seetharam, A. Sood, S. Goel, E. Martinez-Balibrea, A. Martínez-Cardús, A. Ginés, V. Ruiz de Porras, C. Moutinho, L. Layos, J.L. Manzano, C. Bugés, S. Bystrup, M. Esteller, P. Noordhuis, A.C. Laan, K. Van de Born, R.J. Honeywell, G.J. Peters, W. Sun, Y. Ge, J. Cui, B. Liu, W. Lu, M. Ma, Q. Yan, W. He, Y. Hu, L. Xia, W. Hou, J. Chai, H. Guo, J. Yu, S.H. Bae, J.H. Park, H.G. Choi, S.H. Kim, H.Y. Yoo, S.Y. Park, S.Y. Chang, G. Meyer, A. Czompa, C. Reboul, E. Stepania, A. Czegledi, I. Bak, G. Balla, J. Balla, A. Tosaki, I. Lekli, W. Cao, J. Li, K. Yang, D. Cao, I. Tanida, T. Ueno, E. Kominami, J.M. Woynarowski, S. Faivre, M.C. Herzig, B. Arnett, W.G. Chapman, A.V. Trevino, E. Raymond, S.G. Chaney, A. Vaisman, M. Varchenko, R. Teng, J. Zhou, B. Seifer, J. Shen, L. Wang, H.R. Kang, C.K. Jeon, S. Lim, J.I. Barrasa, A. Santiago-Gómez, N. Olmo, M.A. Lizarbe, J. Turnay, A. Derjuga, C. Richard, M. Crosato, P.S. Wright, L. Chalifour, J. Valdez, A. Barraso, H.A. Crissman, W. Nishioka, E.M. Bradbury, Q. Shi, S. Li, L. Jin, H. Lai, Y. Wu, Z. Cai, M. Zhu, Q. Li, C.W. Yao, K.A. Kang, M.J. Piao, Y.S. Ryu, P.M.D.J. Fernando, M.C. Oh, J.E. Park, K. Shilnikova, S.-Y. Na, S.U. Jeong, Y. Zhao, X. Hu, Y. Liu, S. Dong, Z. Wen, S. Zhang, Q. Huang, M. Shi, V.G.A. Arciuch, M.A. Russo, K.S. Kang, A.D. Cristofano, L. Vucicevic, M. Misirkic, J. Kristina, U. Vilimanovich, E. Sudar, E. Isenovic, M. Prica, L. Harhaji-Trajkovic, T. Kravic-Stevovic, B. Vladimir, S. Lee, W. Yang, D.K. Kim, M. Shin, K.U. Choi, D.S. Suh, Y.H. Kim, T.-H. Hwang, J.H. Kim, C. Wu, Y. Chao, S. Shiah, W. Lin, M. Mouradian, K.D. Kikawa, B.P. Dranka, S.M. Komas, B. Kalyanaraman, R.S. Pardini, F. Gharibpoor, S.K. Zonouzi, S. Razi, H. Rezaei, Z. Yao, F. Xie, Z. Liang, W. Xu, H. Zhou, L.-H. Qu, D. Catanzaro, D. Gabbia, V. Cocetta, M. Biagi, E. Ragazzi, M. Montopoli, M. Carrara, X. Cao, L. Fang, S. Gibbs, Z. Dai, P. Wen, X. Zheng, W. Sadee, D. Sun, E.E. Mendoza, M.G. Pocceschi, X. Kong, D.B. Leeper, J. Caro, K.H. Limesand, R. Burd, E. Domenech, C. Maestre, L. Esteban-Martínez, D. Partida, R. Pascual, G. Fernandez-Miranda, E. Seco, R. Campos-Olivas, M. Perez, D. Megias Show less
Oxaliplatin is a platinum analog that can interfere with DNA replication and transcription. Continuous exposure to oxaliplatin results in chemoresistance; however, this mechanism is not well known. In Show more
Oxaliplatin is a platinum analog that can interfere with DNA replication and transcription. Continuous exposure to oxaliplatin results in chemoresistance; however, this mechanism is not well known. In this study, oxaliplatin-resistant (OR) colorectal cancer (CRC) cells of HCT116, HT29, SW480 and SW620 were established by gradually increasing the drug concentration to 2.5 μM. The inhibitory concentrations of cell growth by 50% (IC 50 ) of oxaliplatin were 4.40–12.7-fold significantly higher in OR CRC cells as compared to their respective parental (PT) CRC cells. Phospho-Akt and phospho-mammalian target of rapamycin (mTOR) decreased in PT CRC cells but was overexpressed in OR CRC cells in response to oxaliplatin. In addition, an oxaliplatin-mediated decrease in phospho-AMP-activated protein kinase (AMPK) in PT CRC cells induced autophagy. Contrastingly, an increased phospho-AMPK in OR CRC cells was accompanied by a decrease in LC3B, further inducing the activity of glycolytic enzymes, such as glucose transporter 1 (GLUT1), 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 (PFKFB3) and phosphofructokinase 1 (PFK1), to mediate cell survival. Inhibition of AMPK in OR CRC cells induced autophagy through inactivation of Akt/mTOR pathway and a decrease in GLUT1, PFKFB3, and PFK1. Collectively, targeting AMPK may provide solutions to overcome chemoresistance in OR CRC cells and restore chemosensitivity to anticancer drugs. Show less
đź“„ PDF DOI: 10.3390/biomedicines10112690
Pt amino-acid anticancer

PRMT5 methylome profiling uncovers a direct link to splicing regulation in acute myeloid leukemia - Nature Structural & Molecular Biology

Radzisheuskaya, Aliaksandra, Shliaha, Pavel V., Grinev, Vasily +7 more · 2019 · Nature Publishing Group · Nature · added 2026-04-20
The arginine methyltransferase PRMT5 modifies the splicing regulator SRSF1 and affects acute myeloid leukemia cell survival by modulating SRSF1 function.
đź“„ PDF DOI: 10.1038/s41594-019-0313-z
acute myeloid leukemia bioinorganic regulation cancer cell survival mass spectrometry methylome profiling prmt5 protein