Results 201 to 210 of about 21,316 (231)
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Mechanism of substrate recognition by the chaperonin GroEL

Biochemistry and Cell Biology, 2001
The bacterial chaperonin GroEL functions with its cofactor GroES in assisting the folding of a wide range of proteins in an ATP-dependent manner. GroEL–GroES 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 ...
openaire   +2 more sources

Chaperonin-GroEL as a Smart Hydrophobic Drug Delivery and Tumor Targeting Molecular Machine for Tumor Therapy.

Nano letters (Print), 2018
Yi Yuan   +10 more
semanticscholar   +1 more source

Functional Differences between E. coli and ESKAPE Pathogen GroES/GroEL

MBio, 2021
Steven M Johnson   +2 more
exaly  

The crystal structure of the bacterial chaperonln GroEL at 2.8 Å

Nature, 1994
K. Braig   +6 more
semanticscholar   +1 more source

Tannerella forsythia GroEL induces inflammatory bone resorption and synergizes with interleukin‐17

Molecular Oral Microbiology, 2017
Y-J Jung   +5 more
semanticscholar   +1 more source

GroEL

2008
openaire   +1 more source

The formation of symmetrical GroEL-GroES complexes in the presence of ATP

FEBS Letters, 1994
OSCAR Llorca, JOSÉ Valpuesta
exaly  

Annealing function of GroEL: structural and bioinformatic analysis

Biophysical Chemistry, 2002
Dave Thirumalai   +2 more
exaly  

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