Principles of protein folding in the cellular environment.
about
Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53.Expressional patterns of chaperones in ten human tumor cell lines.Macromolecule-assisted de novo protein foldingChemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosisMultiple chaperonins in bacteria--novel functions and non-canonical behaviorsThe alpha and beta subunit of the nascent polypeptide-associated complex have distinct functionsDomain structure of the HSC70 cochaperone, HIPThe 'sequential allosteric ring' mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulinIts substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone.Influence of trehalose on the molecular chaperone activity of p26, a small heat shock/alpha-crystallin proteinThe relationship between third-codon position nucleotide content, codon bias, mRNA secondary structure and gene expression in the drosophilid alcohol dehydrogenase genes Adh and AdhrHeat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar speciesThe ordered and compartment-specfific autoproteolytic removal of the furin intramolecular chaperone is required for enzyme activation.Online Hydrogen-Deuterium Exchange Traveling Wave Ion Mobility Mass Spectrometry (HDX-IM-MS): a Systematic EvaluationPreferential binding effects on protein structure and dynamics revealed by coarse-grained Monte Carlo simulation.Perspectives in biological physics: the nDDB project for a neutron Dynamics Data Bank for biological macromolecules.Dissection of the ATP-binding domain of the chaperone hsc70 for interaction with the cofactor Hap46.BiP clustering facilitates protein folding in the endoplasmic reticulumProtein solubility and folding enhancement by interaction with RNARegulation of inducible nitric oxide synthase by rapid cellular turnover and cotranslational down-regulation by dimerization inhibitors.Crowding activates ClpB and enhances its association with DnaK for efficient protein aggregate reactivation.Lipid-assisted protein folding.Signal peptide-chaperone interactions on the twin-arginine protein transport pathway.Stress signaling and the shaping of the mammary tissue in development and cancer.Molecular chaperones in the kidney: distribution, putative roles, and regulation.Strategies for manipulating the p53 pathway in the treatment of human cancer.Cell-to-cell movement and assembly of a plant closterovirus: roles for the capsid proteins and Hsp70 homologFolding nuclei in proteins.The stress of protein misfolding: from single cells to multicellular organismsThe unfolding action of GroEL on a protein substrateProtein folding: a perspective for biology, medicine and biotechnology.Hsp70 interactions with the p53 tumour suppressor protein.Surfactant copolymers prevent aggregation of heat denatured lysozyme.Proteomic analysis of acidic chaperones, and stress proteins in extreme halophile Halobacterium NRC-1: a comparative proteomic approach to study heat shock response.Allostery and cooperativity revisited.The unfolding story of the Escherichia coli Hsp70 DnaK: is DnaK a holdase or an unfoldase?A GTP-driven motor moves proteins across the outer envelope of chloroplasts.Protein folding in the post-genomic era.Chaperoning roles of macromolecules interacting with proteins in vivo.Chaperonin 60 unfolds its secrets of cellular communication
P2860
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P2860
Principles of protein folding in the cellular environment.
description
1999 nî lūn-bûn
@nan
1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
name
Principles of protein folding in the cellular environment.
@ast
Principles of protein folding in the cellular environment.
@en
Principles of protein folding in the cellular environment.
@nl
type
label
Principles of protein folding in the cellular environment.
@ast
Principles of protein folding in the cellular environment.
@en
Principles of protein folding in the cellular environment.
@nl
prefLabel
Principles of protein folding in the cellular environment.
@ast
Principles of protein folding in the cellular environment.
@en
Principles of protein folding in the cellular environment.
@nl
P1476
Principles of protein folding in the cellular environment.
@en
P2093
P304
P356
10.1016/S0959-440X(99)80013-X
P577
1999-02-01T00:00:00Z