Breaking barriers: transitioning from X-ray crystallography to cryo-EM for structural studies. [PDF]
Acta Crystallogr D Struct BiolThis article describes the transition of the Glass laboratory from X‐ray crystallography to single‐particle cryo‐electron microscopy (cryo‐EM) for structural studies of ATAD2B, a large AAA+ ATPase‐ and bromodomain‐containing protein involved in chromatin regulation.
Zafar H +4 more
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GroEL‐Mediated protein folding [PDF]
Protein Science, 1997 Abstract Architecture of GroEL and GroES and the reaction pathway Architecture of the chaperonins Reaction pathway of GroEL‐GroES‐mediated folding Polypeptide binding A parallel network of chaperones binding polypeptides in vivo Polypeptide binding in vitro Role of hydrophobicity in recognition Homologous proteins with differing recognition ...
W A, Fenton, A L, Horwich
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Symmetric GroEL‐GroES complexes can contain substrate simultaneously in both GroEL rings [PDF]
FEBS Letters, 1997 © 1997 Federation of European Biochemical Societies.
Llorca, Oscar +3 more
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Journal of the Formosan Medical Association, 2021 Background/Purpose: Porphyromonas gingivalis is an oral pathogen associated with periodontal diseases. P. gingivalis GroEL protein is a stimulator of inflammatory cytokines in macrophages. This study inspected effects of P.
Hsiu-Hui Lin +5 more
doaj +1 more source
Structural and Computational Study of the GroEL–Prion Protein Complex
Biomedicines, 2021 The molecular chaperone GroEL is designed to promote protein folding and prevent aggregation. However, the interaction between GroEL and the prion protein, PrPC, could lead to pathogenic transformation of the latter to the aggregation-prone PrPSc form ...
Aleksandra A. Mamchur +8 more
doaj +1 more source
Porphyromonas gingivalis GroEL induces osteoclastogenesis of periodontal ligament cells and enhances alveolar bone resorption in rats. [PDF]
PLoS ONE, 2014 Porphyromonas gingivalis is a major periodontal pathogen that contains a variety of virulence factors. The antibody titer to P. gingivalis GroEL, a homologue of HSP60, is significantly higher in periodontitis patients than in healthy control subjects ...
Feng-Yen Lin +9 more
doaj +1 more source
Cryo-EM map interpretation and protein model-building using iterative map segmentation. [PDF]
, 2020 A procedure for building protein chains into maps produced by single-particle electron cryo-microscopy (cryo-EM) is described. The procedure is similar to the way an experienced structural biologist might analyze a map, focusing first on secondary ...
Afonine PV +9 more
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Structural Plasticity and Noncovalent Substrate Binding in the GroEL Apical Domain. A study using electrospray ionization mass spectrometry and fluorescence binding studies [PDF]
, 2002 Advances in understanding how GroEL binds to non-native proteins are reported. Conformational flexibility in the GroEL apical domain, which could account for the variety of substrates that GroEL binds, is illustrated by comparison of several independent ...
Adams +62 more
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Borrelia burgdorferi Surface Exposed GroEL Is a Multifunctional Protein
Pathogens, 2021 The spirochete, Borrelia burgdorferi, has a large number of membrane proteins involved in a complex life cycle, that includes a tick vector and a vertebrate host.
Thomas Cafiero, Alvaro Toledo
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Ligands regulate GroEL thermostability
FEBS Letters, 1997 Escherichia coli heat‐shock proteins GroEL and GroES stimulate (in an ATP‐dependent manner) the folding of various proteins. In this study scanning microcalorimetry was applied to investigate GroEL thermostability in the presence of its ligands. Mg2+ and K+ ions stabilize while ADP destabilizes the GroEL molecule against the action of temperature ...
Surin, A.K +5 more
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