Timothy O. Street

发表

A molecular mechanism for osmolyte-induced protein stability

G. Rose, D. W. Bolen, Timothy O. Street, 2006, Proceedings of the National Academy of Sciences.

Are proteins made from a limited parts list?

G. Rose, H. Gong, Nicholas C. Fitzkee, 2005, Trends in biochemical sciences.

Protein folding and stability using denaturants.

D. Barrick, Timothy O. Street, N. Courtemanche, 2008, Methods in cell biology.

Conformational dynamics of the molecular chaperone Hsp90

David A Agard, D. Agard, Laura A Lavery, 2011, Quarterly Reviews of Biophysics.

Structures, basins, and energies: A deconstruction of the Protein Coil Library

George D Rose, Lauren L. Perskie, G. Rose, 2008, Protein science : a publication of the Protein Society.

Multimapping confounds ribosome profiling analysis: A case‐study of the Hsp90 molecular chaperone

J. Halpin, Timothy O. Street, Radhika Jangi, 2020, Proteins.

Erratum: A molecular mechanism for osmolyte-induced protein stability (Proceedings of the National Academy of Sciences of the United States of America (September 19, 2006) 38, 103 (13997-14002) DOI 10.1073/pnas.0606236103)

G. Rose, D. W. Bolen, Timothy O. Street, 2006 .

Osmolyte‐induced conformational changes in the Hsp90 molecular chaperone

D. Agard, D. W. Bolen, K. Krukenberg, 2009, Protein science : a publication of the Protein Society.

Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms.

J. Halpin, Timothy O. Street, 2017, Journal of molecular biology.

Electrostatics drive the molecular chaperone BiP to preferentially bind oligomerized states of a client protein.

Timothy O. Street, J. M. Kotler, Erin Deans, 2022, Journal of molecular biology.

Conformational Cycling within the Closed State of Grp94, an Hsp90-Family Chaperone.

J. Gelles, Ming Sun, Timothy O. Street, 2019, Journal of molecular biology.

5′‐N‐ethylcarboxamidoadenosine is not a paralog‐specific Hsp90 inhibitor

Timothy O. Street, Shanshan Liu, 2016, Protein science : a publication of the Protein Society.

The ER chaperones BiP and Grp94 regulate the formation of insulin-like growth factor 2 (IGF2) oligomers.

J. Halpin, Timothy O. Street, Yi Jin, 2021, Journal of molecular biology.

Crowding Activates Heat Shock Protein 90*

Ming Sun, J. Halpin, Timothy O. Street, 2016, The Journal of Biological Chemistry.

The ER chaperones BiP and Grp94 selectively associate when BiP is in the ADP

M. Sun, Timothy O. Street, J. M. Kotler, 2019 .

Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.

D. Agard, J. Hoskins, D. Masison, 2013, Molecular cell.

The role of introns in repeat protein gene formation.

George D Rose, Doug Barrick, G. Rose, 2006, Journal of molecular biology.

An improved experimental system for determining small folding entropy changes resulting from proline to alanine substitutions

Doug Barrick, D. Barrick, Timothy O. Street, 2005, Protein science : a publication of the Protein Society.

Predicting repeat protein folding kinetics from an experimentally determined folding energy landscape

Doug Barrick, D. Barrick, Timothy O. Street, 2008, Protein science : a publication of the Protein Society.

Physical‐chemical determinants of turn conformations in globular proteins

Lauren L. Perskie, G. Rose, Nicholas C. Fitzkee, 2007, Protein science : a publication of the Protein Society.

Molecular mechanism of bacterial Hsp90 pH‐dependent ATPase activity

Timothy O. Street, Yi Jin, Reyal S Hoxie, 2017, Protein science : a publication of the Protein Society.

The endoplasmic reticulum (ER) chaperones BiP and Grp94 selectively associate when BiP is in the ADP conformation

Ming Sun, Timothy O. Street, Shanshan Liu, 2019, The Journal of Biological Chemistry.

pH-dependent conformational changes in bacterial Hsp90 reveal a Grp94-like conformation at pH 6 that is highly active in suppression of citrate synthase aggregation.

D. Agard, K. Krukenberg, Timothy O. Street, 2009, Journal of molecular biology.

Elucidating the mechanism of substrate recognition by the bacterial Hsp90 molecular chaperone.

Massimiliano Bonomi, Andrej Sali, David A Agard, 2014, Journal of molecular biology.

Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activity.

D. Agard, Laura A Lavery, K. Verba, 2012, Journal of molecular biology.

Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone.

D. Agard, Laura A Lavery, Timothy O. Street, 2011, Molecular cell.

Two-sided block of a dual-topology F− channel

Daniel L Turman, Christopher Miller, R. Stockbridge, 2015, Proceedings of the National Academy of Sciences.

Electrostatics cause the molecular chaperone BiP to preferentially bind oligomerized states of a client protein

Wei Wei, Timothy O. Street, J. M. Kotler, 2021, bioRxiv.

Predicting coupling limits from an experimentally determined energy landscape

Doug Barrick, D. Barrick, Timothy O. Street, 2007, Proceedings of the National Academy of Sciences.

The endoplasmic reticulum chaperone BiP is a closure-accelerating cochaperone of Grp94

J. Gelles, Timothy O. Street, J. M. Kotler, 2022, Proceedings of the National Academy of Sciences.

The ER chaperones BiP and Grp94 regulate the formation of insulin-like growth factor 2 (IGF2) oligomers

J. Halpin, Timothy O. Street, Yi Jin, 2020, bioRxiv.

Hsp90 chaperones have an energetic hot‐spot for binding inhibitors

Timothy O. Street, Reyal S Hoxie, 2020, Protein science : a publication of the Protein Society.

Mechanisms of Protein Quality Control in the Endoplasmic Reticulum by a Coordinated Hsp40-Hsp70-Hsp90 System.

Timothy O. Street, J. M. Kotler, 2023, Annual review of biophysics.

Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms.

J. Halpin, Timothy O. Street, 2017, Journal of molecular biology.