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Molecular chaperones: guardians of the proteome in normal and disease statesWhat distinguishes GroEL substrates from other Escherichia coli proteins?Dynamic Complexes in the Chaperonin-Mediated Protein Folding CycleMultiple chaperonins in bacteria--novel functions and non-canonical behaviorsMycobacterium tuberculosis WhiB1 represses transcription of the essential chaperonin GroEL2A comprehensive analysis of the Omp85/TpsB protein superfamily structural diversity, taxonomic occurrence, and evolution.The chaperonin-60 universal target is a barcode for bacteria that enables de novo assembly of metagenomic sequence data.Activators of the glutamate-dependent acid resistance system alleviate deleterious effects of YidC depletion in Escherichia coli.Functional characterization of LotP from Liberibacter asiaticus.Myxococcus xanthus DK1622 Coordinates Expressions of the Duplicate groEL and Single groES Genes for Synergistic Functions of GroELs and GroESComplete genome sequence of Bradyrhizobium sp. S23321: insights into symbiosis evolution in soil oligotrophsCrystallization and preliminary X-ray crystallographic analysis of a GroEL1 fragment from Mycobacterium tuberculosis H37Rv.Characterization of the active bacterial community involved in natural attenuation processes in arsenic-rich creek sediments.A chaperonin subunit with unique structures is essential for folding of a specific substrate.GroEL actively stimulates folding of the endogenous substrate protein PepQComplete sequencing of the bla(NDM-1)-positive IncA/C plasmid from Escherichia coli ST38 isolate suggests a possible origin from plant pathogensThe C-terminal tails of the bacterial chaperonin GroEL stimulate protein folding by directly altering the conformation of a substrate proteinProteome-wide analysis of functional divergence in bacteria: exploring a host of ecological adaptations.Immunodetection of the recombinant GroEL by the Nanobody NbBruc02.Mechanisms involved in the functional divergence of duplicated GroEL chaperonins in Myxococcus xanthus DK1622.Coevolution analyses illuminate the dependencies between amino acid sites in the chaperonin system GroES-L.Synergistic roles of Helicobacter pylori methionine sulfoxide reductase and GroEL in repairing oxidant-damaged catalase.The Legionella pneumophila Chaperonin - An Unusual Multifunctional Protein in Unusual Locations.Bacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious diseaseThe effect of chaperonin buffering on protein evolutionApplication of meta-transcriptomics and -proteomics to analysis of in situ physiological state.Identification and distribution of high-abundance proteins in the octopus spring microbial mat community.Effects of a Mutation in the HSPE1 Gene Encoding the Mitochondrial Co-chaperonin HSP10 and Its Potential Association with a Neurological and Developmental Disorder.Prokaryotic Chaperonins as Experimental Models for Elucidating Structure-Function Abnormalities of Human Pathogenic Mutant Counterparts.Loss and gain of GroEL in the Mollicutes.The resilience and versatility of acidophiles that contribute to the bio-assisted extraction of metals from mineral sulphides.Biochemical and Genetic Analysis of the Chlamydia GroEL Chaperonins.The molecular anatomy of human Hsp60 and its similarity with that of bacterial orthologs and acetylcholine receptor reveal a potential pathogenetic role of anti-chaperonin immunity in myasthenia gravis.Response to temperature stress in rhizobia.Diversity in the origins of proteostasis networks--a driver for protein function in evolutionChaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions.The Mechanism and Function of Group II Chaperonins.Life Stage-specific Proteomes of Legionella pneumophila Reveal a Highly Differential Abundance of Virulence-associated Dot/Icm effectors.Novel chaperonins are prevalent in the virioplankton and demonstrate links to viral biology and ecologyNon-housekeeping, non-essential GroEL (chaperonin) has acquired novel structure and function beneficial under stress in cyanobacteria.
P2860
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P2860
description
article científic
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article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 07 April 2009
@en
vedecký článok
@sk
vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Multiple chaperonins in bacteria--why so many?
@en
Multiple chaperonins in bacteria--why so many?
@nl
type
label
Multiple chaperonins in bacteria--why so many?
@en
Multiple chaperonins in bacteria--why so many?
@nl
prefLabel
Multiple chaperonins in bacteria--why so many?
@en
Multiple chaperonins in bacteria--why so many?
@nl
P1476
Multiple chaperonins in bacteria--why so many?
@en
P304
P356
10.1111/J.1574-6976.2009.00178.X
P50
P577
2009-04-07T00:00:00Z