The Chaperonin TRiC/CCT Inhibitor HSF1A Protects Cells from Intoxication with Pertussis Toxin
ToxinsPertussis toxin (PT) is a bacterial AB5-toxin produced by Bordetella pertussis and a major molecular determinant of pertussis, also known as whooping cough, a highly contagious respiratory disease.
Jinfang Jia +4 more
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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
Chan, Suzanne L. +5 more
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Systematic interaction network filtering identifies CRMP1 as a novel suppressor of huntingtin misfolding and neurotoxicity [PDF]
, 2015 Assemblies of huntingtin (HTT) fragments with expanded polyglutamine (polyQ) tracts are a pathological hallmark of Huntington's disease (HD). The molecular mechanisms by which these structures are formed and cause neuronal dysfunction and toxicity are ...
Andrade-Navarro, Miguel A. +24 more
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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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Hsp70 in mitochondrial biogenesis [PDF]
, 1994 The family of hsp70 (70 kilodalton heat shock protein) molecular chaperones plays an essential and diverse role in cellular physiology, Hsp70 proteins appear to elicit their effects by interacting with polypeptides that present domains which exhibit non ...
A. Tzagoloff +53 more
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Overproduction of β-glucosidase in active form by anEscherichia colisystem coexpressing the chaperonin GroEL/ES [PDF]
, 1998 Sachiko Machida +5 more
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Protein folding tames chaos [PDF]
, 2013 Protein folding produces characteristic and functional three-dimensional structures from unfolded polypeptides or disordered coils. The emergence of extraordinary complexity in the protein folding process poses astonishing challenges to theoretical ...
Wei, Guo-Wei, Xia, Kelin
core
Expression of stress proteins and mitochondrial chaperonins in chronically stimulated skeletal muscle [PDF]
, 1995 Olga Ornatsky +2 more
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Cloning and expression of a new mammalian chaperonin gene from a multipotent hematopoietic progenitor clone [PDF]
, 1994 Xiaolei Xie, Ronald Palacios
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, 2020 The ATP-dependent Hsp70 chaperones (DnaK in E. coli) mediate protein folding in cooperation with J proteins and nucleotide exchange factors (E. coli DnaJ and GrpE, respectively). The Hsp70 system prevents protein aggregation and increases folding yields.
Balchin, D. +3 more
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