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Mechanism of substrate recognition by the chaperonin GroEL
Biochemistry and Cell Biology, 2001The bacterial chaperonin GroEL functions with its cofactor GroES in assisting the folding of a wide range of proteins in an ATP-dependent manner. GroELGroES constitute one of the main chaperone systems in the Escherichia coli cytoplasm. The chaperonin facilitates protein folding by enclosing substrate proteins in a cage defined by the GroEL cylinder ...
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The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex
Nature, 1997Zhaohui Xu, A. Horwich, P. Sigler
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Functional Differences between E. coli and ESKAPE Pathogen GroES/GroEL
MBio, 2021Steven M Johnson +2 more
exaly
The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
Nature, 1994K. Braig +6 more
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Tannerella forsythia GroEL induces inflammatory bone resorption and synergizes with interleukin‐17
Molecular Oral Microbiology, 2017Y-J Jung +5 more
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The formation of symmetrical GroEL-GroES complexes in the presence of ATP
FEBS Letters, 1994OSCAR Llorca, JOSÉ Valpuesta
exaly
Annealing function of GroEL: structural and bioinformatic analysis
Biophysical Chemistry, 2002Dave Thirumalai +2 more
exaly

