Results 11 to 20 of about 158,532 (263)
Pharmacological Research, 2012 Cells continuously turn over proteins through cycles of synthesis and degradation in order to maintain a functional proteome and to exert a tight control in the levels of regulatory proteins. Selective degradation of proteins was initially thought to be an exclusive function of the ubiquitin-proteasome system, however, over the years, the contribution ...
Susmita, Kaushik, Ana Maria, Cuervo
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Biomolecules, 2020 Scc4 is an unusual bi-functional protein from Chlamydia trachomatis (CT) that functions as a type III secretion system (T3SS) chaperone and an RNA polymerase (RNAP)-binding protein.
Thilini O. Ukwaththage +3 more
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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
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Chaperones in Neurodegeneration [PDF]
The Journal of Neuroscience, 2015 Cellular protein homeostasis (proteostasis) maintains the integrity of the proteome and includes protein synthesis, folding, oligomerization, and turnover; chaperone proteins assist with all of these processes. Neurons appear to be especially susceptible to failures in proteostasis, and this is now increasingly recognized as a major origin of ...
Lindberg, Iris +5 more
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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
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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
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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
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Enzymes as chaperones and chaperones as enzymes
FEBS Letters, 1998 Chaperones and foldases are two groups of accessory proteins which assist maturation of nascent peptides into functional proteins in cells. Protein disulfide isomerase, a foldase, and ATP‐dependent proteases, responsible for degradation of misfolded proteins in cells, both have intrinsic chaperone activities.
Wang, Chih-Chen, Tsou, Chen-Lu
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Molecules, 2020 For large-scale bioproduction, thermal stability is a crucial property for most industrial enzymes. A new method to improve both the thermal stability and activity of enzymes is of great significance.
Chunmeng Xu +5 more
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Frontiers in Cell and Developmental Biology, 2021 For fully differentiated, long lived cells the maintenance of protein homeostasis (proteostasis) becomes a crucial determinant of cellular function and viability.
Shenae L. Cafe +7 more
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