Chaperone Activity of a Chimeric GroEL Protein That Can Exist in a Single or Double Ring Form
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference38 articles.
1. The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
2. The Hsp70 and Hsp60 Chaperone Machines
3. Structural aspects of GroEl function
4. The ins and outs of a molecular chaperone machine
5. The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
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2. New GroEL-like chaperonin of bacteriophage OBP Pseudomonas fluorescens suppresses thermal protein aggregation in an ATP-dependent manner;Biochemical Journal;2016-07-28
3. Allosteric Mechanisms in Chaperonin Machines;Chemical Reviews;2016-01-04
4. The unusual mycobacterial chaperonins: evidence forin vivooligomerization and specialization of function;Molecular Microbiology;2012-07-26
5. Comparative Biochemical Characterization of Two GroEL Homologs from the CyanobacteriumSynechococcus elongatusPCC 7942;Bioscience, Biotechnology, and Biochemistry;2010-11-23
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