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Author Details

Timothy O Street
Brandeis University
2005
28
16
Andrej Sali (CM4AI)
PMIDPaper TitleJournal TitlePublished Year
37159299Mechanisms of Protein Quality Control in the Endoplasmic Reticulum by a Coordinated Hsp40-Hsp70-Hsp90 System.Annu Rev Biophys2023
35597552Electrostatics Drive the Molecular Chaperone BiP to Preferentially Bind Oligomerized States of a Client Protein.J Mol Biol2022
33811917The ER Chaperones BiP and Grp94 Regulate the Formation of Insulin-Like Growth Factor 2 (IGF2) Oligomers.J Mol Biol2021
31254414Multimapping confounds ribosome profiling analysis: A case-study of the Hsp90 molecular chaperone.Proteins2020
32812680Hsp90 chaperones have an energetic hot-spot for binding inhibitors.Protein Sci2020
30787103The endoplasmic reticulum (ER) chaperones BiP and Grp94 selectively associate when BiP is in the ADP conformation.J Biol Chem2019
31202885Conformational Cycling within the Closed State of Grp94, an Hsp90-Family Chaperone.J Mol Biol2019
28822683Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms.J Mol Biol2017
28383119Molecular mechanism of bacterial Hsp90 pH-dependent ATPase activity.Protein Sci2017
26797120Crowding Activates Heat Shock Protein 90.J Biol Chem2016
276675305'-N-ethylcarboxamidoadenosine is not a paralog-specific Hsp90 inhibitor.Protein Sci2016
25902543Two-sided block of a dual-topology F- channel.Proc Natl Acad Sci U S A2015
24726919Elucidating the mechanism of substrate recognition by the bacterial Hsp90 molecular chaperone.J Mol Biol2014
23260660Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.Mol Cell2013
22063096Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activity.J Mol Biol2012
21474071Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone.Mol Cell2011
21414251Conformational dynamics of the molecular chaperone Hsp90.Q Rev Biophys2011
19890989Osmolyte-induced conformational changes in the Hsp90 molecular chaperone.Protein Sci2010
19177351Predicting repeat protein folding kinetics from an experimentally determined folding energy landscape.Protein Sci2009
19427321pH-dependent conformational changes in bacterial Hsp90 reveal a Grp94-like conformation at pH 6 that is highly active in suppression of citrate synthase aggregation.J Mol Biol2009
17964936Protein folding and stability using denaturants.Methods Cell Biol2008
18434497Structures, basins, and energies: a deconstruction of the Protein Coil Library.Protein Sci2008
17360387Predicting coupling limits from an experimentally determined energy landscape.Proc Natl Acad Sci U S A2007
17656584Physical-chemical determinants of turn conformations in globular proteins.Protein Sci2007
16968772A molecular mechanism for osmolyte-induced protein stability.Proc Natl Acad Sci U S A2006
16781737The role of introns in repeat protein gene formation.J Mol Biol2006
15691652Are proteins made from a limited parts list?Trends Biochem Sci2005
16131666An improved experimental system for determining small folding entropy changes resulting from proline to alanine substitutions.Protein Sci2005
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Collaborators

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