Results 41 to 50 of about 4,302 (172)
A comprehensive analysis of prefoldins and their implication in cancer
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
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
cpnDB: A Chaperonin Sequence Database [PDF]
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
Chaperonins (CPNs) are ATP-dependent protein-folding machines. Here the authors present the open and closed crystal structures of a Group III CPN from the thermophilic bacterium Carboxydothermus hydrogenoformans, discuss its mechanism and structurally ...
Young Jun An +8 more
doaj +1 more source
Proteostasis of organelles in aging and disease
Cells rely on regulated proteostasis mechanisms to keep their internal compartments functioning properly. When these mechanisms fail, damaged proteins accumulate, disrupting organelles, such as the nucleus, mitochondria, endoplasmic reticulum, Golgi, and lysosomes, as well as membraneless organelles, such as stress granules, processing bodies, the ...
Yara Nabawi +5 more
wiley +1 more source
GroEL actively stimulates folding of the endogenous substrate protein PepQ
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
Mechanisms of a Mycobacterium tuberculosis Active Peptide
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
RNA‐seq and Batelli gland proteomics of fifth‐instar Mahanarva spectabilis nymphs reveal transcripts and proteins associated with xylem feeding, foam production and environmental interaction. Functional annotation identified genes involved in osmoregulation, detoxification, chemosensation and stress responses, while proteomic analysis confirmed ...
Monique da Silva Bonjour +8 more
wiley +1 more source
Mechanisms involved in the functional divergence of duplicated GroEL chaperonins in Myxococcus xanthus DK1622. [PDF]
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
Summary Experimental evolution under elevated temperatures has generated heat‐evolved (HE) strains of Symbiodiniaceae that enhance coral bleaching tolerance. However, the biomolecular mechanisms underlying this resilience remain poorly understood. We conducted a laboratory heat‐stress experiment and applied synchrotron‐based Fourier transform infrared (
Bede G. Johnston +5 more
wiley +1 more source

