Reactivation of Aggregated Proteins by the ClpB/DnaK Bi‐Chaperone System-Reference-Cited by-同舟云学术

Reactivation of Aggregated Proteins by the ClpB/DnaK Bi‐Chaperone System

Published:2016-02 Issue:1 Volume:83 Page:
ISSN:1934-3655
Container-title:Current Protocols in Protein Science
language:en
Short-container-title:Current Protocols in Protein Science

Author:

Zolkiewski Michal¹,Chesnokova Liudmila S.²,Witt Stephan N.³

Affiliation:

1. Department of Biochemistry and Molecular Biophysics, Kansas State University Manhattan Kansas

2. Department of Microbiology and Immunology, Louisiana State University Health Sciences Center Shreveport Louisiana

3. Department of Biochemistry and Molecular Biology and Department of Pharmacology, Toxicology and Neuroscience, Louisiana State University Health Sciences Center Shreveport Louisiana

Publisher

Wiley

Subject

Biochemistry,General Medicine,Structural Biology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/0471140864.ps2810s83

Reference53 articles.

1. Structure and Activity of ClpB from Escherichia coli

2. The Amino-terminal Domain of ClpB Supports Binding to Strongly Aggregated Proteins

3. The molecular chaperone Hsp104—A molecular machine for protein disaggregation

4. Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone.

5. Molecular Chaperones and Protein Quality Control

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