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GroES Protein

Known as: GroES Stress Protein 
A chaperonin 10 heat-shock protein isolated from bacterial sources.
National Institutes of Health

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Broader (2)

Chaperonin 10GroE protein, E coli

Papers overview

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2017
2017
Formation of the chaperonin complex studied by 2D NMR spectroscopy
We studied the interaction between GroES and a single-ring mutant (SR1) of GroEL by the NMR titration of 15N-labeled GroES with… 
2009
2009
بیان همزمان ترکیب چاپرونهایGroEL / GroES / Dnak / Dnaj / GrpEوGroEL / GroES با فاکتور رشد فیبرو بلاستی بازی انسانی در باکتری اشرشیاکلی به منظور کاهش پروتئینهای نامحلول نوترکیب
2007
2007
Structural stability of covalently linked GroES heptamer: advantages in the formation of oligomeric structure.
2004
2004
Initial peptide mass fingerprinting analysis of proteins obtained by lysis of Coxiella burnetii cells.
Whereas the complete genome of Coxiella burnetii (C.b.), the etiological agent of Q-fever, has recently been published (Seshadri… 
2003
2003
Interaction of GroEL and GroEL/GroES complexes with a nonnative subtilisin variant: a small-angle neutron scattering study.
2003
2003
Phylogenetic reconstruction of Gram-positive organisms based on comparative sequence analysis of molecular chaperones from the ruminal microorganism Ruminococcus flavefaciens FD-1.
2001
2001
Chaperonins as Potential Gene Regulatory Factors
A previous study (Govezensky, D., Greener, T., and Zamir, A. (1991) J. Bacteriol. 20, 6339-6346) indicated that the chaperonin… 
Highly Cited
1998
Highly Cited
1998
Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings.
The ATPase cycle of GroE chaperonins has been examined by transient kinetics to dissect partial reactions in complexes where… 
1997
1997
Role of chaperonins in protein folding. A new model of the GroEL/GroES complex architecture.
  • M. Basharov
  • Biochemistry. Biokhimiia
  • 1997
  • Corpus ID: 33627289
Polypeptide chain folds to native protein under physiological conditions. At least in vivo, in addition to physiological… 
1995
1995
Bovine adrenodoxin--a mitochondrial iron-sulphur protein--binds to chaperonin GroEL.
The interaction of bovine adrenodoxin with the chaperonin GroEL was investigated using sucrose density centrifugation and… 
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