Protasevich II - Search Results

1

Structures of a minimal human CFTR first nucleotide-binding domain as a monomer, head-to-tail homodimer, and pathogenic mutant.

Atwell S, Brouillette CG, Conners K, Emtage S, Gheyi T, Guggino WB, Hendle J, Hunt JF, Lewis HA, Lu F, Protasevich II, Rodgers LA, Romero R, Wasserman SR, Weber PC, Wetmore D, Zhang FF, Zhao X. Atwell S, et al. Among authors: protasevich ii. Protein Eng Des Sel. 2010 May;23(5):375-84. doi: 10.1093/protein/gzq004. Epub 2010 Feb 11. Protein Eng Des Sel. 2010. PMID: 20150177

2

Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1.

Protasevich I, Yang Z, Wang C, Atwell S, Zhao X, Emtage S, Wetmore D, Hunt JF, Brouillette CG. Protasevich I, et al. Protein Sci. 2010 Oct;19(10):1917-31. doi: 10.1002/pro.479. Protein Sci. 2010. PMID: 20687133 Free PMC article.

3

Integrated biophysical studies implicate partial unfolding of NBD1 of CFTR in the molecular pathogenesis of F508del cystic fibrosis.

Wang C, Protasevich I, Yang Z, Seehausen D, Skalak T, Zhao X, Atwell S, Spencer Emtage J, Wetmore DR, Brouillette CG, Hunt JF. Wang C, et al. Protein Sci. 2010 Oct;19(10):1932-47. doi: 10.1002/pro.480. Protein Sci. 2010. PMID: 20687163 Free PMC article.

4

Conformational changes relevant to channel activity and folding within the first nucleotide binding domain of the cystic fibrosis transmembrane conductance regulator.

Hudson RP, Chong PA, Protasevich II, Vernon R, Noy E, Bihler H, An JL, Kalid O, Sela-Culang I, Mense M, Senderowitz H, Brouillette CG, Forman-Kay JD. Hudson RP, et al. Among authors: protasevich ii. J Biol Chem. 2012 Aug 17;287(34):28480-94. doi: 10.1074/jbc.M112.371138. Epub 2012 Jun 21. J Biol Chem. 2012. PMID: 22722932 Free PMC article.

5

Structural adaptation of an interacting non-native C-terminal helical extension revealed in the crystal structure of NAD+ synthetase from Bacillus anthracis.

McDonald HM, Pruett PS, Deivanayagam C, Protasevich II, Carson WM, DeLucas LJ, Brouillette WJ, Brouillette CG. McDonald HM, et al. Among authors: protasevich ii. Acta Crystallogr D Biol Crystallogr. 2007 Aug;63(Pt 8):891-905. doi: 10.1107/S0907444907029769. Epub 2007 Jul 17. Acta Crystallogr D Biol Crystallogr. 2007. PMID: 17642516

6

Role of inhibitor aliphatic chain in the thermodynamics of inhibitor binding to Escherichia coli enoyl-ACP reductase and the Phe203Leu mutant: a proposed mechanism for drug resistance.

Protasevich II, Brouillette CG, Snow ME, Dunham S, Rubin JR, Gogliotti R, Siegel K. Protasevich II, et al. Biochemistry. 2004 Oct 26;43(42):13380-9. doi: 10.1021/bi0492509. Biochemistry. 2004. PMID: 15491144

7

Deletion of DnaK's lid strengthens binding to the nucleotide exchange factor, GrpE: a kinetic and thermodynamic analysis.

Chesnokova LS, Slepenkov SV, Protasevich II, Sehorn MG, Brouillette CG, Witt SN. Chesnokova LS, et al. Among authors: protasevich ii. Biochemistry. 2003 Aug 5;42(30):9028-40. doi: 10.1021/bi0346493. Biochemistry. 2003. PMID: 12885236

8

Förster resonance energy transfer measurements are consistent with a helical bundle model for lipid-free apolipoprotein A-I.

Brouillette CG, Dong WJ, Yang ZW, Ray MJ, Protasevich II, Cheung HC, Engler JA. Brouillette CG, et al. Among authors: protasevich ii. Biochemistry. 2005 Dec 20;44(50):16413-25. doi: 10.1021/bi051018v. Biochemistry. 2005. PMID: 16342934

9

A gene optimization strategy that enhances production of fully functional P-glycoprotein in Pichia pastoris.

Bai J, Swartz DJ, Protasevich II, Brouillette CG, Harrell PM, Hildebrandt E, Gasser B, Mattanovich D, Ward A, Chang G, Urbatsch IL. Bai J, et al. Among authors: protasevich ii. PLoS One. 2011;6(8):e22577. doi: 10.1371/journal.pone.0022577. Epub 2011 Aug 3. PLoS One. 2011. PMID: 21826197 Free PMC article.

10

Conformation and thermal denaturation of apocalmodulin: role of electrostatic mutations.

Protasevich I, Ranjbar B, Lobachov V, Makarov A, Gilli R, Briand C, Lafitte D, Haiech J. Protasevich I, et al. Biochemistry. 1997 Feb 25;36(8):2017-24. doi: 10.1021/bi962538g. Biochemistry. 1997. PMID: 9047299

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