Substrate Discrimination by ClpB and Hsp104-Reference-Cited by-同舟云学术

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Substrate Discrimination by ClpB and Hsp104

Published:2017-05-29 Issue: Volume:4 Page:
ISSN:2296-889X
Container-title:Frontiers in Molecular Biosciences
language:
Short-container-title:Front. Mol. Biosci.

Author:

Johnston Danielle M.,Miot Marika,Hoskins Joel R.,Wickner Sue,Doyle Shannon M.

Funder

National Institutes of Health

Publisher

Frontiers Media SA

Subject

Biochemistry, Genetics and Molecular Biology (miscellaneous),Molecular Biology,Biochemistry

Reference67 articles.

1. ClpXP, an ATP-powered unfolding and protein-degradation machine;Baker;Biochim. Biophys. Acta,2012

2. Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides;Bosl;J. Biol. Chem.,2005

3. Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients;DeSantis;Cell,2012

4. Modeling AAA+ ring complexes from monomeric structures;Diemand;J. Struct. Biol.,2006

5. Protein rescue from aggregates by powerful molecular chaperone machines;Doyle;Nat. Rev. Mol. Cell Biol.,2013

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1. Probing Single Chaperone Substrates;Biophysics of Molecular Chaperones;2023-11-01

2. Membrane protein chaperone and sodium chloride modulate the kinetics and morphology of amyloid beta aggregation;The FEBS Journal;2023-10-11

3. Characterization and Degradation Pathways of Microbacterium resistens MZT7, A Novel 17β-Estradiol-Degrading Bacterium;International Journal of Environmental Research and Public Health;2022-09-05

4. Hsp104 N‐terminal domain interaction with substrates plays a regulatory role in protein disaggregation;The FEBS Journal;2022-03-30

5. Amyloid conformation-dependent disaggregation in a reconstituted yeast prion system;Nature Chemical Biology;2022-02-17

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