Results 11 to 20 of about 226,086 (342)
Calnexin cycle – structural features of the ER chaperone system
The FEBS Journal, 2020 The endoplasmic reticulum (ER) is the major folding compartment for secreted and membrane proteins and is the site of a specific chaperone system, the calnexin cycle, for folding N‐glycosylated proteins.
G. Kozlov, K. Gehring
semanticscholar +1 more source
Post-translational modifications of Hsp90 and translating the chaperone code
Journal of Biological Chemistry, 2020 Cells have a remarkable ability to synthesize large amounts of protein in a very short period of time. Under these conditions, many hydrophobic surfaces on proteins may be transiently exposed, and the likelihood of deleterious interactions is quite high.
Sarah J Backe +4 more
semanticscholar +1 more source
Post-translational modifications of Hsp70 family proteins: Expanding the chaperone code
Journal of Biological Chemistry, 2020 Cells must be able to cope with the challenge of folding newly synthesized proteins and refolding those that have become misfolded in the context of a crowded cytosol. One such coping mechanism that has appeared during evolution is the expression of well-
Nitika +3 more
semanticscholar +1 more source
Chaperone-mediated autophagy is involved in the execution of ferroptosis
Proceedings of the National Academy of Sciences of the United States of America, 2019 Significance This study reveals a common regulatory mechanism mediated by HSP90 that is shared by necroptosis and ferroptosis, two necrotic cell death mechanisms that have previously had no known mechanistic connections.
Zheming Wu +8 more
semanticscholar +1 more source
Life, 2020 DnaK3, a highly conserved cyanobacterial chaperone of the Hsp70 family, binds to cyanobacterial thylakoid membranes, and an involvement of DnaK3 in the biogenesis of thylakoid membranes has been suggested. As shown here, light triggers synthesis of DnaK3
Adrien Thurotte +4 more
doaj +1 more source
Frontiers in Microbiology, 2019 Helicobacter pylori is the etiologic agent in a variety of gastroduodenal diseases. As its key pathogenic factors, both urease and Hsp60 play important roles in the pathogenesis of H. pylori.
Huilin Zhao +9 more
doaj +1 more source
Pharmaceuticals, 2020 Mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) gene decrease the structural stability and function of the CFTR protein, resulting in cystic fibrosis. Recently, the effect of CFTR-targeting combination therapy has dramatically
Ryosuke Fukuda, Tsukasa Okiyoneda
doaj +1 more source
Dynamic Activity of Histone H3-Specific Chaperone Complexes in Oncogenesis
Frontiers in Oncology, 2022 Canonical histone H3.1 and variant H3.3 deposit at different sites of the chromatin via distinct histone chaperones. Histone H3.1 relies on chaperone CAF-1 to mediate replication-dependent nucleosome assembly during S-phase, while H3.3 variant is ...
Ting Wen, Qiao Yi Chen
doaj +1 more source
Chaperone-assisted translocation [PDF]
Physical Biology, 2004 24 pages, 3 figures, LaTeX (IOP class file)
Ambjørnsson, T, Metzler, R
openaire +3 more sources
The heat‐shock protein/chaperone network and multiple stress resistance
Plant Biotechnology Journal, 2017 Summary Crop yield has been greatly enhanced during the last century. However, most elite cultivars are adapted to temperate climates and are not well suited to more stressful conditions.
Pierre Jacob, H. Hirt, A. Bendahmane
semanticscholar +1 more source