Results 61 to 70 of about 5,379 (199)
Small, EarlyView.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
GroEL actively stimulates folding of the endogenous substrate protein PepQ
Nature Communications, 2017 In the prevailing model for assisted protein folding, chaperonins act passively by preventing protein aggregation. Here, the authors use single-molecule fluorescence measurements and cryo-electron microscopy and show that theE.
Jeremy Weaver +5 more
doaj +1 more source
A comprehensive analysis of prefoldins and their implication in cancer
iScience, 2021 Summary: Prefoldins (PFDNs) are evolutionary conserved co-chaperones, initially discovered in archaea but universally present in eukaryotes. PFDNs are prevalently organized into hetero-hexameric complexes.
Irene Herranz-Montoya +2 more
doaj +1 more source
Gut microbiota dysbiosis and Long COVID susceptibility in chronic kidney disease
VIEW, EarlyView.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
VIEW, EarlyView.Rare‐earth ions act as multifunctional modifiers in perovskite solar cells by improving charge transport, suppressing oxygen vacancies, passivating defects, promoting grain growth, and enabling redox‐mediated stabilization. In addition, RE‐doped layers can expand spectral utilization through upconversion and downconversion, thereby enhancing light ...
Jiaqi Meng +9 more
wiley +1 more source
Mechanisms involved in the functional divergence of duplicated GroEL chaperonins in Myxococcus xanthus DK1622. [PDF]
PLoS Genetics, 2013 The gene encoding the GroEL chaperonin is duplicated in nearly 30% of bacterial genomes; and although duplicated groEL genes have been comprehensively determined to have distinct physiological functions in different species, the mechanisms involved have ...
Yan Wang +9 more
doaj +1 more source
Mechanisms of a Mycobacterium tuberculosis Active Peptide
Pharmaceutics, 2023 Multidrug-resistant tuberculosis (MDR) continues to pose a threat to public health. Previously, we identified a cationic host defense peptide with activity against Mycobacterium tuberculosis in vivo and with a bactericidal effect against MDR M ...
Komal Umashankar Rao +7 more
doaj +1 more source
Brain Pathology, EarlyView.Omics‐driven drug repositioning reveals pyroxamide as a neuroprotective HDAC1 inhibitor in Parkinson's disease models. Abstract Parkinson's disease (PD) is the second most common neurodegenerative disorder mainly characterized by the degeneration of dopaminergic neurons originating in the substantia nigra (SN) pars compacta and projecting to other ...
Paz Cartas‐Cejudo +7 more
wiley +1 more source
cpnDB: A Chaperonin Sequence Database [PDF]
Genome Research, 2004 Type I chaperonins are molecular chaperones present in virtually all bacteria, some archaea and the plastids and mitochondria of eukaryotes. Sequences of cpn60 genes, encoding 60-kDa chaperonin protein subunits (CPN60, also known as GroEL or HSP60), are useful for phylogenetic studies and as targets for detection and identification of organisms ...
Hill, Janet +4 more
openaire +2 more sources
Structural Studies Of The Human Hsp60 And Bacteriophage Phiel Chaperonins [PDF]
, 2023 Chaperonins are large protein complexes responsible for the refolding of misfoldedsubstrate. Many mechanisms of the folding process have not been completely elucidated.
von Salzen, Daniel Han
core +1 more source