Chaperone activity and structure of monomeric polypeptide binding domains of GroEL - Wikidata - awgldk - TriplyDB

Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

http://www.wikidata.org/entity/Q27734289

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Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperone Identification and characterization of a novel thioredoxin-related transmembrane protein of the endoplasmic reticulum Nucleotide-dependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludis NMR solution structure of the human prion protein A structural model for GroEL-polypeptide recognition ERp57 is a multifunctional thiol-disulfide oxidoreductase Chaperonins Single amino acid substitutions on the surface of Escherichia coli maltose-binding protein can have a profound impact on the solubility of fusion proteins Heat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar species Design 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 folding Self-assembly of the chaperonin GroEL nanocage induced at submicellar detergent The substrate binding domain of DnaK facilitates slow protein refolding Structure-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 calmodulin Structural insight into the cooperation of chloroplast chaperonin subunits.Dissecting intrinsic chaperonin activity Refolding chromatography with immobilized mini-chaperones The allosteric mechanism of the chaperonin GroEL: a dynamic analysis.In vivo activities of GroEL minichaperones GroEL-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 Folding The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding

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Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

http://www.wikidata.org/entity/Q27734289

description

1996 nî lūn-bûn

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1996 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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1996 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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1996年の論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年论文

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Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

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Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

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Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

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Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

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Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

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Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

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Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

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Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

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Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

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PNAS.93.26.15024

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

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P2093

A M Buckle

http://www.w3.org/2001/XMLSchema#string

A R Fersht

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C M Johnson

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F J Corrales

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R Golbik

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R Zahn

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S Perrett

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P2860

Improved methods for building protein models in electron density maps and the location of errors in these models

PROCHECK: a program to check the stereochemical quality of protein structures

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution

Raster3D Version 2.0. A program for photorealistic molecular graphics

Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

Detection, delineation, measurement and display of cavities in macromolecular structures

Residues in chaperonin GroEL required for polypeptide binding and release

AMoRe: an automated package for molecular replacement

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scholarly article

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2366063

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10.1073/PNAS.93.26.15024

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26

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93

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235614017

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8986757

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molecular chaperones

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26349

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