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Peter Tsvetkov, Ph.D. - Publications

Affiliations: 
2010 Weizmann Institute of Science, Rehovot, Israel 
Area:
Physiology Biology, Oncology, Aging
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31 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2023 Dreishpoon MB, Bick NR, Petrova B, Warui DM, Cameron A, Booker SJ, Kanarek N, Golub TR, Tsvetkov P. FDX1 regulates cellular protein lipoylation through direct binding to LIAS. The Journal of Biological Chemistry. 105046. PMID 37453661 DOI: 10.1016/j.jbc.2023.105046  0.319
2023 Dreishpoon MB, Bick NR, Petrova B, Warui DM, Cameron A, Booker SJ, Kanarek N, Golub TR, Tsvetkov P. FDX1 regulates cellular protein lipoylation through direct binding to LIAS. Biorxiv : the Preprint Server For Biology. PMID 36778498 DOI: 10.1101/2023.02.03.526472  0.302
2021 Tsvetkov P, Adler J, Strobelt R, Adamovich Y, Asher G, Reuven N, Shaul Y. NQO1 Binds and Supports SIRT1 Function. Frontiers in Pharmacology. 12: 671929. PMID 34234670 DOI: 10.3389/fphar.2021.671929  0.58
2020 Tsvetkov P, Myers N, Adler J, Shaul Y. Degradation of Intrinsically Disordered Proteins by the NADH 26S Proteasome. Biomolecules. 10. PMID 33297334 DOI: 10.3390/biom10121642  0.589
2020 Tsvetkov P, Eisen TJ, Heinrich SU, Brune Z, Hallacli E, Newby GA, Kayatekin C, Pincus D, Lindquist S. Persistent Activation of mRNA Translation by Transient Hsp90 Inhibition. Cell Reports. 32: 108001. PMID 32783929 DOI: 10.1016/J.Celrep.2020.108001  0.374
2020 Graindorge A, Pinheiro I, Nawrocka A, Mallory AC, Tsvetkov P, Gil N, Carolis C, Buchholz F, Ulitsky I, Heard E, Taipale M, Shkumatava A. Author Correction: In-cell identification and measurement of RNA-protein interactions. Nature Communications. 11: 3498. PMID 32641823 DOI: 10.1038/S41467-020-17282-6  0.314
2019 Tsvetkov P, Detappe A, Cai K, Keys HR, Brune Z, Ying W, Thiru P, Reidy M, Kugener G, Rossen J, Kocak M, Kory N, Tsherniak A, Santagata S, Whitesell L, et al. Mitochondrial metabolism promotes adaptation to proteotoxic stress. Nature Chemical Biology. PMID 31133756 DOI: 10.1038/S41589-019-0291-9  0.349
2018 Tsvetkov P, Adler J, Myers N, Biran A, Reuven N, Shaul Y. Oncogenic addiction to high 26S proteasome level. Cell Death & Disease. 9: 773. PMID 29991718 DOI: 10.1038/S41419-018-0806-4  0.594
2017 Newby GA, Kiriakov S, Hallacli E, Kayatekin C, Tsvetkov P, Mancuso CP, Bonner JM, Hesse WR, Chakrabortee S, Manogaran AL, Liebman SW, Lindquist S, Khalil AS. A Genetic Tool to Track Protein Aggregates and Control Prion Inheritance. Cell. PMID 29056345 DOI: 10.1016/J.Cell.2017.09.041  0.351
2017 Tsvetkov P, Sokol E, Jin D, Gupta P, Santagata S, Whitesell L, Lindquist S. Abstract A28: Targeting the epigenetic state regulating cancer cell vulnerability to proteasome inhibition Clinical Cancer Research. 23. DOI: 10.1158/1557-3265.Pmccavuln16-A28  0.351
2016 Tsvetkov P, Sokol E, Jin D, Brune Z, Thiru P, Ghandi M, Garraway LA, Gupta PB, Santagata S, Whitesell L, Lindquist S. Suppression of 19S proteasome subunits marks emergence of an altered cell state in diverse cancers. Proceedings of the National Academy of Sciences of the United States of America. PMID 28028240 DOI: 10.1073/Pnas.1619067114  0.367
2015 Tsvetkov P, Mendillo ML, Zhao J, Carette JE, Merrill PH, Cikes D, Varadarajan M, van Diemen FR, Penninger JM, Goldberg AL, Brummelkamp TR, Santagata S, Lindquist S. Compromising the 19S proteasome complex protects cells from reduced flux through the proteasome. Elife. 4. PMID 26327695 DOI: 10.7554/Elife.08467  0.453
2015 Tsvetkov P, Mendillo ML, Zhao J, Carette JE, Merrill PH, Cikes D, Varadarajan M, Diemen FRv, Penninger JM, Goldberg AL, Brummelkamp TR, Santagata S, Lindquist S. Author response: Compromising the 19S proteasome complex protects cells from reduced flux through the proteasome Elife. DOI: 10.7554/Elife.08467.021  0.312
2014 Tsvetkov P, Myers N, Eliav R, Adamovich Y, Hagai T, Adler J, Navon A, Shaul Y. NADH Binds and stabilizes the 26S proteasomes independent of ATP Journal of Biological Chemistry. 289: 11272-11281. PMID 24596095 DOI: 10.1074/Jbc.M113.537175  0.625
2013 Adamovich Y, Shlomai A, Tsvetkov P, Umansky KB, Reuven N, Estall JL, Spiegelman BM, Shaul Y. The protein level of PGC-1α, a key metabolic regulator, is controlled by NADH-NQO1. Molecular and Cellular Biology. 33: 2603-13. PMID 23648480 DOI: 10.1128/Mcb.01672-12  0.711
2012 Moscovitz O, Tsvetkov P, Hazan N, Michaelevski I, Keisar H, Ben-Nissan G, Shaul Y, Sharon M. A mutually inhibitory feedback loop between the 20S proteasome and its regulator, NQO1. Molecular Cell. 47: 76-86. PMID 22793692 DOI: 10.1016/J.Molcel.2012.05.049  0.684
2012 Tsvetkov P, Shaul Y. Determination of IUP based on susceptibility for degradation by default. Methods in Molecular Biology (Clifton, N.J.). 895: 3-18. PMID 22760308 DOI: 10.1007/978-1-61779-927-3_1  0.623
2012 Tsvetkov P, Myers N, Moscovitz O, Sharon M, Prilusky J, Shaul Y. Thermo-resistant intrinsically disordered proteins are efficient 20S proteasome substrates. Molecular Biosystems. 8: 368-73. PMID 22027891 DOI: 10.1039/C1Mb05283G  0.592
2011 Wiggins CM, Tsvetkov P, Johnson M, Joyce CL, Lamb CA, Bryant NJ, Komander D, Shaul Y, Cook SJ. BIM(EL), an intrinsically disordered protein, is degraded by 20S proteasomes in the absence of poly-ubiquitylation. Journal of Cell Science. 124: 969-77. PMID 21378313 DOI: 10.1242/Jcs.058438  0.653
2011 Tsvetkov P, Adamovich Y, Elliott E, Shaul Y. E3 ligase STUB1/CHIP regulates NAD(P)H:quinone oxidoreductase 1 (NQO1) accumulation in aged brain, a process impaired in certain Alzheimer disease patients. The Journal of Biological Chemistry. 286: 8839-45. PMID 21220432 DOI: 10.1074/Jbc.M110.193276  0.613
2010 Tsvetkov P, Reuven N, Shaul Y. Ubiquitin-independent p53 proteasomal degradation. Cell Death and Differentiation. 17: 103-8. PMID 19557012 DOI: 10.1038/Cdd.2009.67  0.608
2010 Shaul Y, Tsvetkov P, Reuven N. IDPs and Protein Degradation in the Cell Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation. 1-36. DOI: 10.1002/9780470602614.ch1  0.632
2009 Tsvetkov P, Reuven N, Shaul Y. The nanny model for IDPs. Nature Chemical Biology. 5: 778-81. PMID 19841623 DOI: 10.1038/Nchembio.233  0.608
2009 Tsvetkov P, Reuven N, Prives C, Shaul Y. Susceptibility of p53 unstructured N terminus to 20 S proteasomal degradation programs the stress response. The Journal of Biological Chemistry. 284: 26234-42. PMID 19617345 DOI: 10.1074/Jbc.M109.040493  0.613
2008 Tsvetkov P, Asher G, Paz A, Reuven N, Sussman JL, Silman I, Shaul Y. Operational definition of intrinsically unstructured protein sequences based on susceptibility to the 20S proteasome Proteins: Structure, Function and Genetics. 70: 1357-1366. PMID 17879262 DOI: 10.1002/Prot.21614  0.61
2007 Elliott E, Tsvetkov P, Ginzburg I. BAG-1 associates with Hsc70.Tau complex and regulates the proteasomal degradation of Tau protein. The Journal of Biological Chemistry. 282: 37276-84. PMID 17954934 DOI: 10.1074/Jbc.M706379200  0.419
2006 Asher G, Dym O, Tsvetkov P, Adler J, Shaul Y. The crystal structure of NAD(P)H quinone oxidoreductase 1 in complex with its potent inhibitor dicoumarol. Biochemistry. 45: 6372-8. PMID 16700548 DOI: 10.1021/Bi0600087  0.618
2005 Tsvetkov P, Asher G, Reiss V, Shaul Y, Sachs L, Lotem J. Inhibition of NAD(P)H:quinone oxidoreductase 1 activity and induction of p53 degradation by the natural phenolic compound curcumin. Proceedings of the National Academy of Sciences of the United States of America. 102: 5535-40. PMID 15809436 DOI: 10.1073/Pnas.0501828102  0.613
2005 Asher G, Bercovich Z, Tsvetkov P, Shaul Y, Kahana C. 20S proteasomal degradation of ornithine decarboxylase is regulated by NQO1. Molecular Cell. 17: 645-55. PMID 15749015 DOI: 10.1016/J.Molcel.2005.01.020  0.669
2005 Asher G, Tsvetkov P, Kahana C, Shaul Y. A mechanism of ubiquitin-independent proteasomal degradation of the tumor suppressors p53 and p73. Genes & Development. 19: 316-21. PMID 15687255 DOI: 10.1101/Gad.319905  0.643
2003 Asher G, Lotem J, Tsvetkov P, Reiss V, Sachs L, Shaul Y. P53 hot-spot mutants are resistant to ubiquitin-independent degradation by increased binding to NAD(P)H:quinone oxidoreductase 1. Proceedings of the National Academy of Sciences of the United States of America. 100: 15065-70. PMID 14634213 DOI: 10.1073/Pnas.2436329100  0.627
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