Chaperone activity and structure of monomeric polypeptide binding domains of GroEL
about
Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperoneIdentification and characterization of a novel thioredoxin-related transmembrane protein of the endoplasmic reticulumNucleotide-dependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludisNMR solution structure of the human prion proteinA structural model for GroEL-polypeptide recognitionERp57 is a multifunctional thiol-disulfide oxidoreductaseChaperoninsSingle amino acid substitutions on the surface of Escherichia coli maltose-binding protein can have a profound impact on the solubility of fusion proteinsHeat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar speciesDesign of highly stable functional GroEL minichaperones.Three-dimensional structure topology of the calreticulin P-domain based on NMR assignment.Minimal and optimal mechanisms for GroE-mediated protein foldingSelf-assembly of the chaperonin GroEL nanocage induced at submicellar detergentThe substrate binding domain of DnaK facilitates slow protein refoldingStructure-function analysis of the endoplasmic reticulum oxidoreductase TMX3 reveals interdomain stabilization of the N-terminal redox-active domain.Bacterial and yeast chaperones reduce both aggregate formation and cell death in mammalian cell models of Huntington's disease.The inner cavity of Escherichia coli DegP protein is not essential for molecular chaperone and proteolytic activity.Cloning and expression of the gene for a novel protein from Mycobacterium smegmatis with functional similarity to eukaryotic calmodulinStructural insight into the cooperation of chloroplast chaperonin subunits.Dissecting intrinsic chaperonin activityRefolding chromatography with immobilized mini-chaperonesThe allosteric mechanism of the chaperonin GroEL: a dynamic analysis.In vivo activities of GroEL minichaperonesGroEL-GroES-mediated protein folding requires an intact central cavity.Accelerated folding in the weak hydrophobic environment of a chaperonin cavity: creation of an alternate fast folding pathway.GroEL-assisted protein folding: does it occur within the chaperonin inner cavity?Protein refolding using chemical refolding additives.Isolation of a periplasmic molecular chaperone-like protein of Rhodobacter sphaeroides f. sp. denitrificans that is homologous to the dipeptide transport protein DppA of Escherichia coli.The interaction of Hsc70 protein with fibrillar α-Synuclein and its therapeutic potential in Parkinson's disease.Suppression of amyloid fibrils using the GroEL apical domain.Interaction of the N-terminal domain of Escherichia coli heat-shock protein ClpB and protein aggregates during chaperone activity.Binding of a burst-phase intermediate formed in the folding of denatured D-glyceraldehyde-3-phosphate dehydrogenase by chaperonin 60 and 8-anilino-1-naphthalenesulphonic acid.A minichaperone-based fusion system for producing insoluble proteins in soluble stable forms.The versatile mutational "repertoire" of Escherichia coli GroEL, a multidomain chaperonin nanomachine.Application of a chaperone-based refolding method to two- and three-dimensional off-lattice protein models.On the Role of Symmetrical and Asymmetrical Chaperonin Complexes in Assisted Protein FoldingThe oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding
P2860
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P2860
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL
description
1996 nî lūn-bûn
@nan
1996 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL
@ast
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL
@en
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL
@nl
type
label
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL
@ast
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL
@en
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL
@nl
prefLabel
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL
@ast
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL
@en
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL
@nl
P2093
P2860
P3181
P356
P1476
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL
@en
P2093
A M Buckle
A R Fersht
C M Johnson
F J Corrales
P2860
P304
P3181
P356
10.1073/PNAS.93.26.15024
P407
P577
1996-12-24T00:00:00Z