Results 161 to 170 of about 19,683 (209)
`Mix-it-up': accessible time-resolved cryo-EM on the millisecond timescale. [PDF]
IUCrJAlexandrescu L, Lessin W, Lander GC.
europepmc +1 more source
Analysis of peptides and proteins in their binding to GroEL [PDF]
Journal of Peptide Science, 2010 AbstractThe GroEL–GroES is an essential molecular chaperon system that assists protein folding in cell. Binding of various substrate proteins to GroEL is one of the key aspects in GroEL‐assisted protein folding. Small peptides may mimic segments of the substrate proteins in contact with GroEL and allow detailed structural analysis of the interactions ...
Yali, Li +3 more
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GroEL/ES inhibitors as potential antibiotics [PDF]
Bioorganic and Medicinal Chemistry Letters, 2016 We recently reported results from a high-throughput screening effort that identified 235 inhibitors of the Escherichia coli GroEL/ES chaperonin system [Bioorg. Med. Chem. Lett.2014, 24, 786]. As the GroEL/ES chaperonin system is essential for growth under all conditions, we reasoned that targeting GroEL/ES with small molecule inhibitors could be a ...
Steven M Johnson +2 more
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Lactobacillus stress protein GroEL prevents colonic inflammation [PDF]
Journal of Gastroenterology, 2021 International audienceBACKGROUND: We previously showed that supernatants of Lactobacillus biofilms induced an anti-inflammatory response by affecting the secretion of macrophage-derived cytokines, which was abrogated upon immunodepletion of the stress ...
François Hermetet +2 more
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Functional Differences between E. coli and ESKAPE Pathogen GroES/GroEL.
MBio, 2021 As the GroES/GroEL chaperonin system is the only bacterial chaperone that is essential under all conditions, we have been interested in the development of GroES/GroEL inhibitors as potential antibiotics. Using Escherichia coli GroES/GroEL as a surrogate,
Steven M Johnson +2 more
exaly +2 more sources
GroEL Ring Separation and Exchange in the Chaperonin Reaction
Cell, 2018 The bacterial chaperonin GroEL and its cofactor, GroES, form a nano-cage for a single molecule of substrate protein (SP) to fold in isolation. GroEL and GroES undergo an ATP-regulated interaction cycle to close and open the folding cage.
Manajit Hayer-Hartl +2 more
exaly +2 more sources
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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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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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