Results 101 to 110 of about 20,108 (219)
Structure and conformational cycle of a bacteriophage-encoded chaperonin.
PLoS ONE, 2020 Chaperonins are ubiquitous molecular chaperones found in all domains of life. They form ring-shaped complexes that assist in the folding of substrate proteins in an ATP-dependent reaction cycle.
Andreas Bracher +5 more
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Chaperonin-mediated Protein Folding [PDF]
Journal of Biological Chemistry, 2011 We have been studying chaperonins these past twenty years through an initial discovery of an action in protein folding, analysis of structure, and elucidation of mechanism. Some of the highlights of these studies were presented recently upon sharing the honor of the 2013 Herbert Tabor Award with my early collaborator, Ulrich Hartl, at the annual ...
openaire +3 more sources
Chemical synthesis of 10 kDa chaperonin Biological activity suggests chaperonins do not require other molecular chaperones [PDF]
, 1991 Molecular chaperones are required for the correct folding and assembly of certain other polypeptides. It is not known whether molecular chaperones themselves require other chaperones to become functional.
R.John Ellis +11 more
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Chaperonin facilitates protein folding by avoiding polypeptide collapse [PDF]
, 2017 Chaperonins assist folding of many cellular proteins, including essential proteins for cell viability. However, it remains unclear how chaperonin-assisted folding is different from spontaneous folding.
Fumihiro Motojima +2 more
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Heat shock proteins and oral diseases
SRM Journal of Research in Dental Sciences, 2012 Heat shock proteins (HSPs) are substances expressed in response to elevated temperatures or other cellular stress. They are highly conserved proteins inhabiting nearly all subcellular compartments and are found in all organisms and all cell types. When a
G Suresh Babu +3 more
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The essential role of CCT2 in the regulation of aggrephagy
Frontiers in Aging NeuroscienceProtein aggregation, a defining characteristic of numerous human diseases, poses a significant challenge to cellular health. Autophagy, an essential cellular recycling process, specifically targets and degrades these harmful protein aggregates through a ...
Jie Luo, Ze-Sen Feng, Ji-Xin Tang
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Versatile platform for nanotechnology based on circular permutations of chaperonin protein [PDF]
, 2010 The present invention provides chaperonin polypeptides which are modified to include N-terminal and C-terminal ends that are relocated from the central pore region to various different positions in the polypeptide which are located on the exterior of the
Trent, Jonathan D. +5 more
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Interaction of β-lactoglobulin with chaperonin GroEL [PDF]
, 2002 Sakai, Kazuko, Hoshino, Masaru and Goto, Yuji "Interaction of β-lactoglobulin with chaperonin GroEL", Proceedings of the Indian National Science Academy, 68, 4A, 341-347, Indian National Science Academy ...
Sakai, Kazuko +2 more
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