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ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

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JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

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Timothy O Street

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Journal of Molecular Biology|May 21, 2022

Electrostatics Drive the Molecular Chaperone BiP to Preferentially Bind Oligomerized States of a Client ProteinErin E Deans, Judy L M Kotler, Wei-Shao Wei, et al.

Proceedings of the National Academy of Sciences of the United States of America|April 23, 2015

Two-sided block of a dual-topology F- channelDaniel L Turman, Jacob T Nathanson, Randy B Stockbridge, et al.

Protein Science : a Publication of the Protein Society|November 6, 2009

Osmolyte-induced conformational changes in the Hsp90 molecular chaperoneTimothy O Street, Kristin A Krukenberg, Jörg Rosgen, et al.

Trends in Biochemical Sciences|February 5, 2005

Are proteins made from a limited parts list?Nicholas C Fitzkee, Patrick J Fleming, Haipeng Gong, et al.

Journal of Molecular Biology|April 3, 2021

The ER Chaperones BiP and Grp94 Regulate the Formation of Insulin-Like Growth Factor 2 (IGF2) OligomersYi Jin, Judy L M Kotler, Shiyu Wang, et al.

Journal of Molecular Biology|November 9, 2011

Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activityTimothy O Street, Laura A Lavery, Kliment A Verba, et al.

Proceedings of the National Academy of Sciences of the United States of America|January 26, 2022

The endoplasmic reticulum chaperone BiP is a closure-accelerating cochaperone of Grp94Bin Huang, Ming Sun, Reyal Hoxie, et al.

Journal of Molecular Biology|April 15, 2014

Elucidating the mechanism of substrate recognition by the bacterial Hsp90 molecular chaperoneTimothy O Street, Xiaohui Zeng, Riccardo Pellarin, et al.

Nature Communications|April 15, 2025

Mechanism of client loading from BiP to Grp94 and its disruption by select inhibitorsTara P Azam, Luna Han, Erin E Deans, et al.

Molecular Cell|December 25, 2012

Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeastOlivier Genest, Michael Reidy, Timothy O Street, et al.

Pageof 3

Search research articles

Showing results (21-30 of 30) with videos related to

Sort By:

Pageof 3

You have reached the last page of results.This site can display upto 30 results.

Journal of Molecular Biology|May 21, 2022

Electrostatics Drive the Molecular Chaperone BiP to Preferentially Bind Oligomerized States of a Client ProteinErin E Deans, Judy L M Kotler, Wei-Shao Wei, et al.

Proceedings of the National Academy of Sciences of the United States of America|April 23, 2015

Two-sided block of a dual-topology F- channelDaniel L Turman, Jacob T Nathanson, Randy B Stockbridge, et al.

Protein Science : a Publication of the Protein Society|November 6, 2009

Osmolyte-induced conformational changes in the Hsp90 molecular chaperoneTimothy O Street, Kristin A Krukenberg, Jörg Rosgen, et al.

Trends in Biochemical Sciences|February 5, 2005

Are proteins made from a limited parts list?Nicholas C Fitzkee, Patrick J Fleming, Haipeng Gong, et al.

Journal of Molecular Biology|April 3, 2021

The ER Chaperones BiP and Grp94 Regulate the Formation of Insulin-Like Growth Factor 2 (IGF2) OligomersYi Jin, Judy L M Kotler, Shiyu Wang, et al.

Journal of Molecular Biology|November 9, 2011

Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activityTimothy O Street, Laura A Lavery, Kliment A Verba, et al.

Proceedings of the National Academy of Sciences of the United States of America|January 26, 2022

The endoplasmic reticulum chaperone BiP is a closure-accelerating cochaperone of Grp94Bin Huang, Ming Sun, Reyal Hoxie, et al.

Journal of Molecular Biology|April 15, 2014

Elucidating the mechanism of substrate recognition by the bacterial Hsp90 molecular chaperoneTimothy O Street, Xiaohui Zeng, Riccardo Pellarin, et al.

Nature Communications|April 15, 2025

Mechanism of client loading from BiP to Grp94 and its disruption by select inhibitorsTara P Azam, Luna Han, Erin E Deans, et al.

Molecular Cell|December 25, 2012

Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeastOlivier Genest, Michael Reidy, Timothy O Street, et al.

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