Biological Heterogeneity of the Peptide-binding Motif of the 70-kDa Heat Shock Protein by Surface Plasmon Resonance Analysis-Reference-Cited by-同舟云学术

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Biological Heterogeneity of the Peptide-binding Motif of the 70-kDa Heat Shock Protein by Surface Plasmon Resonance Analysis

Published:2007-09 Issue:37 Volume:282 Page:26956-26962
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Maeda Hideki,Sahara Hiroeki,Mori Yoko,Torigo Toshihiko,Kamiguchi Kenjiro,Tamura Yutaka,Tamura Yasuaki,Hirata Kouichi,Sato Noriyuki

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference39 articles.

1. The Hsp70 and Hsp60 Chaperone Machines

2. Peptide-binding specificity of the molecular chaperone BiP

3. Binding Sites for Hsp70 Molecular Chaperones in Natural Proteins

4. Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP

5. The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE.

Cited by 21 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Electrostatics Drive the Molecular Chaperone BiP to Preferentially Bind Oligomerized States of a Client Protein;Journal of Molecular Biology;2022-07

2. Electrostatics cause the molecular chaperone BiP to preferentially bind oligomerized states of a client protein;2021-10-11

3. Electrostatics Drive the Molecular Chaperone BiP to Preferentially Bind Oligomerized States of a Client Protein;SSRN Electronic Journal;2021

4. Selective Binding of HSC70 and its Co-Chaperones to Structural Hotspots on CFTR;Scientific Reports;2020-03-06

5. A Bipartite Interaction between Hsp70 and CHIP Regulates Ubiquitination of Chaperoned Client Proteins;Structure;2015-03

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