Results 91 to 100 of about 21,272 (221)
Physiological Reports, Volume 14, Issue 19, October 2026.We examined the vastus lateralis (VL) muscle proteomic signature in younger and older males before and after a 10–12‐week resistance training period. Despite similar training volumes between age groups, VL hypertrophy (determined via ultrasound) was dampened in older individuals, and this coincided with an attenuated proteome plasticity response.
Dustyn T. Lewis +16 more
wiley +1 more source
Reversible interaction of beta-actin along the channel of the TCP-1 cytoplasmic chaperonin [PDF]
, 1994 The cytoplasm of eukaryotes contains a heteromeric toroidal chaperonin assembled from the t-complex TCP-1 and several other related polypeptides. The structure of the TCP-1 cytoplasmic chaperonin and that of the binary complex formed between this ...
Valpuesta, J.M. +5 more
core +1 more source
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
doaj +1 more source
Crystal Structure of Chaperonin GroEL from Xanthomonas oryzae pv. oryzae
Crystals, 2019 Xanthomonas oryzae pv. oryzae (Xoo) is a plant pathogen that causes bacterial blight of rice, with outbreaks occurring in most rice-growing countries. Thus far, there is no effective pesticide against bacterial blight.
Huyen-Thi Tran +6 more
doaj +1 more source
Functional role of Chaperonin protein complexes
, 2000 The chaperonins are high-molecular weight protein complexes present in all living cells; they are thought to participate in the folding or refolding of cellular proteins and may also have a function in RNA metabolism.
Giordano R +3 more
core +1 more source
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
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
doaj +1 more source
Single-molecule spectroscopy of protein folding in a chaperonin cage [PDF]
, 2010 Molecular chaperones are known to be essential for avoiding protein aggregation in vivo, but it is still unclear how they affect protein folding mechanisms.
Nettels, D +17 more
core +1 more source
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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