Results 51 to 60 of about 21,272 (221)
Functional screening identified PcSyn14890, a cyanobacteria‐specific protein that enhances growth and stress resistance in E. coli and Synechocystis PCC6803. Although we expected it to function as a molecular chaperone, it was unable to protect against thermal aggregation of GAPDH.
Akiyo Yamada +7 more
wiley +1 more source
Protein nanoreactors and native enzymes for controlled/living radical polymerization [PDF]
The present PhD thesis entitled ‚Protein Nanoreactors and Native Enzymes for Controlled/Living Radical Polymerization‘ began with the hypothesis that protein-catalyst conjugates are able to beneficially influence controlled/living radical polymerization,
Renggli, Kasper
core +1 more source
Chaperonin containing tailless complex polypeptide 1 (CCT) is a molecular chaperone protein that consists of eight completely different subunits and assists in the folding of newly synthesized peptides.
Sheng Xu +8 more
doaj +1 more source
Heat Shock Protein 60 (HSP60) detection by QCM Biosensor and Antibody Covered Gold Nanoparticles
Heat Shock Protein 60 (HSP60) is a 60 kDa weighting chaperonin that is an evolutionary conserved protein occurring in a wide number of organisms. It can serve as a plasma or blood serum biomarker of serious pathologies including cancer.
Miroslav Pohanka
doaj +1 more source
ABSTRACT Genetic modifiers of Duchenne muscular dystrophy (DMD) that alter disease severity or response to therapy have been reported using natural history or registry data sets of older corticosteroid‐treated patients. We tested associations of genetic modifiers on motor function outcomes in young (4 to < 7 years) steroid naïve clinical trial ...
Utkarsh J. Dang +16 more
wiley +1 more source
Chaperonins are universally conserved proteins that nonspecifically facilitate the folding of a wide spectrum of proteins. While bacterial GroEL is functionally promiscuous with various co-chaperonin partners, its human homologue, Hsp60 functions ...
Richardson A +3 more
core +1 more source
A photoreversible 1D protein assembly has been developed by utilizing symmetry matching between StrepTactin and photoswitchable Dronpa145N. The light‐induced modulation of oligomerization allows for precise control over protein connectivity and valency.
Jangwon Bae, Yongwon Jung
wiley +1 more source
Evolvability of Chaperonin Substrate Proteins [PDF]
Molecular chaperones ensure that their substrate proteins reach the functional native state, and prevent their aggregation. Recently, an additional function was proposed for molecular chaperones: they serve as buffers (_capacitors_) for evolution by ...
Tobias Maier +7 more
core
Chaperonin-co-chaperonin interactions measured by SPR.
Association and dissociation patterns of 10 µM of the indicated chaperonin to immobilized (A) GroES (∼ 600 Relative Units-RU) or (B) mHsp10 (∼ 800 RU) in the presence of 2 mM ATP.
Galit Levy-Rimler (115146) +8 more
core +1 more source
Gut microbiota dysbiosis and Long COVID susceptibility in chronic kidney disease
This study investigated gut microbiota dysbiosis and its association with Long COVID susceptibility in 224 hemodialysis patients. We found that 35.3% of patients developed Long COVID, characterized by neurological symptoms and elevated inflammatory markers, accompanied by significant gut microbiota alterations including enriched proinflammatory taxa ...
Meiling Jin +5 more
wiley +1 more source

