Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions.
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Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced ActivityVersatile roles of the chaperonin GroEL in microorganism-insect interactionsDynamic Complexes in the Chaperonin-Mediated Protein Folding CycleMultiple chaperonins in bacteria--novel functions and non-canonical behaviorsA comprehensive analysis of the Omp85/TpsB protein superfamily structural diversity, taxonomic occurrence, and evolution.Functional characterization of LotP from Liberibacter asiaticus.Coevolution analyses illuminate the dependencies between amino acid sites in the chaperonin system GroES-L.Genome-scale identification and characterization of moonlighting proteins.Computational and experimental analysis of the secretome of Methylococcus capsulatus (Bath)Flagellin and GroEL mediates in vitro binding of an atypical enteropathogenic Escherichia coli to cellular fibronectinFolding of newly translated membrane protein CCR5 is assisted by the chaperonin GroEL-GroES.Skeletal muscle Heat shock protein 60 increases after endurance training and induces peroxisome proliferator-activated receptor gamma coactivator 1 α1 expression.Integration of two ancestral chaperone systems into one: the evolution of eukaryotic molecular chaperones in light of eukaryogenesis.Biochemical and Genetic Analysis of the Chlamydia GroEL Chaperonins.Non-proteolytic functions of microbial proteases increase pathological complexity.Novel chaperonins are prevalent in the virioplankton and demonstrate links to viral biology and ecologyThe human mitochondrial Hsp60 in the APO conformation forms a stable tetradecameric complex.Comparative proteomic analysis of Xanthomonas citri ssp. citri periplasmic proteins reveals changes in cellular envelope metabolism during in vitro pathogenicity induction.Structure-to-function relationships of bacterial translocator protein (TSPO): a focus on Pseudomonas.Chance and necessity in the genome evolution of endosymbiotic bacteria of insects.Do reciprocal interactions between cell stress proteins and cytokines create a new intra-/extra-cellular signalling nexus?Comparative genomic analysis of mollicutes with and without a chaperonin system.Toward Developing Chemical Modulators of Hsp60 as Potential Therapeutics.Single-Ring Intermediates Are Essential for Some Chaperonins.
P2860
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P2860
Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions.
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article científic
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article scientifique
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articol științific
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articolo scientifico
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artigo científico
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artigo científico
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artigo científico
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artikel ilmiah
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artículo científico
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name
Chaperonin 60: a paradoxical, ...... ltiple moonlighting functions.
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type
label
Chaperonin 60: a paradoxical, ...... ltiple moonlighting functions.
@en
prefLabel
Chaperonin 60: a paradoxical, ...... ltiple moonlighting functions.
@en
P2860
P356
P1433
P1476
Chaperonin 60: a paradoxical, ...... ultiple moonlighting functions
@en
P2093
Brian Henderson
Peter A Lund
P2860
P304
P356
10.1111/BRV.12037
P577
2013-03-29T00:00:00Z