Pletnev AA - Search Results

1

Correction: Cysteine modification reveals an allosteric inhibitory site on the CAL PDZ domain.

Zhao Y, Cushing PR, Smithson DC, Pellegrini M, Pletnev AA, Al-Ayyoubi S, Grassetti AV, Gerber SA, Guy RK, Madden DR. Zhao Y, et al. Among authors: pletnev aa. Biosci Rep. 2018 Jul 6;38(4):BSR20180231_COR. doi: 10.1042/BSR20180231_COR. Print 2018 Aug 31. Biosci Rep. 2018. PMID: 29871975 Free PMC article. No abstract available.

2

Cysteine modifiers suggest an allosteric inhibitory site on the CAL PDZ domain.

Zhao Y, Cushing PR, Smithson DC, Pellegrini M, Pletnev AA, Al-Ayyoubi S, Grassetti AV, Gerber SA, Guy RK, Madden DR. Zhao Y, et al. Among authors: pletnev aa. Biosci Rep. 2018 Jul 6;38(4):BSR20180231. doi: 10.1042/BSR20180231. Print 2018 Aug 31. Biosci Rep. 2018. PMID: 29472314 Free PMC article.

3

Quantitative phosphoproteomics identifies substrates and functional modules of Aurora and Polo-like kinase activities in mitotic cells.

Kettenbach AN, Schweppe DK, Faherty BK, Pechenick D, Pletnev AA, Gerber SA. Kettenbach AN, et al. Among authors: pletnev aa. Sci Signal. 2011 Jun 28;4(179):rs5. doi: 10.1126/scisignal.2001497. Sci Signal. 2011. PMID: 21712546 Free PMC article.

4

Multiple BH3 mimetics antagonize antiapoptotic MCL1 protein by inducing the endoplasmic reticulum stress response and up-regulating BH3-only protein NOXA.

Albershardt TC, Salerni BL, Soderquist RS, Bates DJ, Pletnev AA, Kisselev AF, Eastman A. Albershardt TC, et al. Among authors: pletnev aa. J Biol Chem. 2011 Jul 15;286(28):24882-95. doi: 10.1074/jbc.M111.255828. Epub 2011 May 31. J Biol Chem. 2011. PMID: 21628457 Free PMC article.

5

Specific cell-permeable inhibitor of proteasome trypsin-like sites selectively sensitizes myeloma cells to bortezomib and carfilzomib.

Mirabella AC, Pletnev AA, Downey SL, Florea BI, Shabaneh TB, Britton M, Verdoes M, Filippov DV, Overkleeft HS, Kisselev AF. Mirabella AC, et al. Among authors: pletnev aa. Chem Biol. 2011 May 27;18(5):608-18. doi: 10.1016/j.chembiol.2011.02.015. Chem Biol. 2011. PMID: 21609842 Free PMC article.

6

Selective inhibitor of proteasome's caspase-like sites sensitizes cells to specific inhibition of chymotrypsin-like sites.

Britton M, Lucas MM, Downey SL, Screen M, Pletnev AA, Verdoes M, Tokhunts RA, Amir O, Goddard AL, Pelphrey PM, Wright DL, Overkleeft HS, Kisselev AF. Britton M, et al. Among authors: pletnev aa. Chem Biol. 2009 Dec 24;16(12):1278-89. doi: 10.1016/j.chembiol.2009.11.015. Chem Biol. 2009. PMID: 20064438 Free PMC article.

7

The putative BH3 mimetic S1 sensitizes leukemia to ABT-737 by increasing reactive oxygen species, inducing endoplasmic reticulum stress, and upregulating the BH3-only protein NOXA.

Soderquist R, Pletnev AA, Danilov AV, Eastman A. Soderquist R, et al. Among authors: pletnev aa. Apoptosis. 2014 Jan;19(1):201-9. doi: 10.1007/s10495-013-0910-y. Apoptosis. 2014. PMID: 24072590 Free PMC article.

8

Inhibition of endoglin-GIPC interaction inhibits pancreatic cancer cell growth.

Pal K, Pletnev AA, Dutta SK, Wang E, Zhao R, Baral A, Yadav VK, Aggarwal S, Krishnaswamy S, Alkharfy KM, Chowdhury S, Spaller MR, Mukhopadhyay D. Pal K, et al. Among authors: pletnev aa. Mol Cancer Ther. 2014 Oct;13(10):2264-75. doi: 10.1158/1535-7163.MCT-14-0291. Epub 2014 Aug 14. Mol Cancer Ther. 2014. PMID: 25125675 Free PMC article.

9

A small fluorophore reporter of protein conformation and redox state.

Pound GJ, Pletnev AA, Fang X, Pletneva EV. Pound GJ, et al. Among authors: pletnev aa. Chem Commun (Camb). 2011 May 28;47(20):5714-6. doi: 10.1039/c1cc10896d. Epub 2011 Apr 12. Chem Commun (Camb). 2011. PMID: 21487611

10

Nature of pharmacophore influences active site specificity of proteasome inhibitors.

Screen M, Britton M, Downey SL, Verdoes M, Voges MJ, Blom AE, Geurink PP, Risseeuw MD, Florea BI, van der Linden WA, Pletnev AA, Overkleeft HS, Kisselev AF. Screen M, et al. Among authors: pletnev aa. J Biol Chem. 2010 Dec 17;285(51):40125-34. doi: 10.1074/jbc.M110.160606. Epub 2010 Oct 11. J Biol Chem. 2010. PMID: 20937826 Free PMC article.

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