Results 61 to 70 of about 8,317 (219)
How Salmonella Works Under Osmotic and Desiccation Stresses
Comprehensive Reviews in Food Science and Food Safety, Volume 25, Issue 3, May 2026.ABSTRACT Salmonella remains one of the leading threats in foods with reduced water activity, where it can survive for long periods and cause outbreaks. Its persistence stems from a wide array of adaptive strategies shaped by the selective pressures imposed by low‐moisture foods.
Mayara Messias Oliveira +2 more
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
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
High salt-induced conversion of Escherichia coli GroEL into a fully functional thermophilic chaperonin [PDF]
, 2000 The GroE chaperonin system can adapt to and function at various environmental folding conditions. To examine chaperonin-assisted protein folding at high salt concentrations, we characterized Escherichia coli GroE chaperonin activity in 1.2 M ammonium ...
Kusmierczyk, Andrew R, Martin, Jörg
core +1 more source
Journal of Extracellular Vesicles, Volume 15, Issue 4, April 2026.ABSTRACT Clostridioides difficile (CD) is a leading cause of antibiotic‐associated diarrhoea in both hospitalized and non‐hospitalized patients. This study explores the role of extracellular vesicles (EVs) derived from Clostridioides difficile strain 630 (CD630‐EVs), which released spherical EVs during in vitro culture, in modulating pro‐inflammatory ...
Fangfang Fan +11 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
Natural supramolecular protein assemblies [PDF]
, 2016 Supramolecular protein assemblies are an emerging area within the chemical sciences, which combine the topological structures of the field of supramolecular chemistry and the state-of-the-art chemical biology approaches to unravel the formation and ...
Mecinović, Jasmin +3 more
core +2 more sources
Acetyl‐Phosphate Dependent Protein Acetylation in Neisseria gonorrhoeae
MicrobiologyOpen, Volume 15, Issue 2, April 2026.The role of acetyl‐phosphate‐dependent non‐enzymatic protein acetylation in Neisseria gonorrhoeae was investigated through the deletion of the phosphotransacetylase (pta) and the acetate kinase (ackA) genes, this led to a decrease and increase in protein acetylation, respectively.
Ernesto F. D. Parga +6 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
The Cpn10(1) co-chaperonin of A. thaliana functions only as a hetero-oligomer with Cpn20. [PDF]
PLoS ONE, 2014 The A. thaliana genome encodes five co-chaperonin homologs, three of which are destined to the chloroplast. Two of the proteins, Cpn10(2) and Cpn20, form functional homo-oligomers in vitro.
Anna Vitlin Gruber +3 more
doaj +1 more source