Stability of 20S Proteasome Configurations: Preopening the Axial Gate-Reference-Cited by-同舟云学术

Stability of 20S Proteasome Configurations: Preopening the Axial Gate

Published:2023-05-24 Issue:21 Volume:14 Page:5014-5017
ISSN:1948-7185
Container-title:The Journal of Physical Chemistry Letters
language:en
Short-container-title:J. Phys. Chem. Lett.

Author:

Henderson Lucas W.¹,Sharon Edie M.¹,Gautam Amit K. S.²,Anthony Adam J.¹,Jarrold Martin F.¹^ORCID,Russell David H.³^ORCID,Matouschek Andreas²^ORCID,Clemmer David E.¹^ORCID

Affiliation:

1. Department of Chemistry, Indiana University, Bloomington, Indiana 47401, United States

2. Department of Molecular Biosciences, University of Texas, Austin, Texas 78712, United States

3. Department of Chemistry, Texas A&M University, College Station, Texas 77843, United States

Funder

Welch Foundation

National Institutes of Health

National Science Foundation

Publisher

American Chemical Society (ACS)

Subject

General Materials Science,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpclett.3c01040

Reference25 articles.

1. The proteasome: Overview of structure and functions

2. Mechanisms of substrate recognition by the 26S proteasome

3. The proteasome 19S cap and its ubiquitin receptors provide a versatile recognition platform for substrates

4. Structure of the human 26S proteasome at a resolution of 3.9 Å

5. The 20S as a stand-alone proteasome in cells can degrade the ubiquitin tag

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