Results 171 to 180 of about 21,316 (231)
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A biochemical screen for GroEL/GroES inhibitors
Bioorganic and Medicinal Chemistry Letters, 2014High-throughput screening of 700,000 small molecules has identified 235 inhibitors of the GroEL/GroES-mediated refolding cycle. Dose-response analysis of a subset of these hits revealed that 21 compounds are potent inhibitors of GroEL/GroES-mediated refolding (IC50
Steven M Johnson +2 more
exaly +3 more sources
The GroEL–GroES Chaperonin Machine: A Nano-Cage for Protein Folding
Trends in Biochemical Sciences, 2016Manajit Hayer-Hartl +2 more
exaly +2 more sources
The Journal of Periodontology, 2021
OBJECTIVE GroEL, a bacterial metabolite, is an important stimulator of inflammation. The aim of this study is to confirm the effect of the virulence factor GroEL on differentiation potential of periodontal ligament stem cells (PDLSCs) and the potential ...
L. Zhang +9 more
semanticscholar +1 more source
OBJECTIVE GroEL, a bacterial metabolite, is an important stimulator of inflammation. The aim of this study is to confirm the effect of the virulence factor GroEL on differentiation potential of periodontal ligament stem cells (PDLSCs) and the potential ...
L. Zhang +9 more
semanticscholar +1 more source
GroEL Ring Separation and Exchange in the Chaperonin Reaction
Cell, 2018 Manajit Hayer-Hartl +2 more
exaly +2 more sources
Efficient Catalysis of Protein Folding by GroEL/ES of the Obligate Chaperonin Substrate MetF.
Journal of Molecular Biology, 2020The cylindrical chaperonin GroEL and its cofactor GroES mediate ATP-dependent protein folding in E. coli by transiently encapsulating non-native substrate in a nano-cage formed by the GroEL ring cavity and the lid-shaped GroES.
Amit K. Singh +4 more
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Transmission Electron Microscopy of GroEL, GroES, and the Symmetrical GroEL/ES Complex
Journal of Structural Biology, 1994Two new 2-D crystal forms of the Escherichia coli chaperone GroEL (cpn60) 2 x 7-mer have been produced using the negative staining-carbon film (NS-CF) technique. These 2-D crystals, which contain the cylindrical GroEL in side-on and end-on orientations, both possess p21 symmetry, with two molecules in the respective unit cells. The crystallographically
J R, Harris, A, Plückthun, R, Zahn
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Folding of maltose binding protein outside of and in GroEL
Proceedings of the National Academy of Sciences of the United States of America, 2018Significance The GroEL/ES chaperonin is known to prevent protein aggregation during folding by passive containment within the central cavity. The possible role of more active intervention is controversial.
Zhong-Yuan Kan +2 more
exaly +2 more sources
Structure and Allostery of the Chaperonin GroEL
Journal of Molecular Biology, 2013Chaperonins are intricate allosteric machines formed of two back-to-back, stacked rings of subunits presenting end cavities lined with hydrophobic binding sites for nonnative polypeptides. Once bound, substrates are subjected to forceful, concerted movements that result in their ejection from the binding surface and simultaneous encapsulation inside a ...
Helen R, Saibil +3 more
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Fish and Shellfish Immunology, 2019
Fish nocardiosis is a chronic granulomatous bacterial disease mainly caused by three pathogenic bacteria, including Nocardia seriolae, N. asteroids and N. salmonicida.
Jianlin Chen +6 more
semanticscholar +1 more source
Fish nocardiosis is a chronic granulomatous bacterial disease mainly caused by three pathogenic bacteria, including Nocardia seriolae, N. asteroids and N. salmonicida.
Jianlin Chen +6 more
semanticscholar +1 more source