Peptide-binding specificity of the molecular chaperone BiP
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Heterozygous yeast deletion collection screens reveal essential targets of Hsp90Regulation of AKT phosphorylation at Ser473 and Thr308 by endoplasmic reticulum stress modulates substrate specificity in a severity dependent mannerThe crystal structure of the fab fragment of the monoclonal antibody MAK33. Implications for folding and interaction with the chaperone bipLysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysisThe dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates.Mitochondrial Hsp70 Ssc1: role in protein folding.Binding of BiP to the processing enzyme lymphoma proprotein convertase prevents aggregation, but slows down maturationEffect of constitutive 70-kDa heat shock protein polymerization on its interaction with protein substrateStructural features of the precursor to mitochondrial aspartate aminotransferase responsible for binding to hsp70Modification of two distinct COOH-terminal domains is required for murine p53 activation by bacterial Hsp70ER chaperones in mammalian development and human diseasesMultiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulumSingle domain intrabodies against WASP inhibit TCR-induced immune responses in transgenic mice T cells.Mutagenesis of the Regulatory Subunit (RIIbeta) of cAMP-dependent Protein Kinase IIbeta Reveals Hydrophobic Amino Acids That Are Essential for RIIbeta Dimerization and/or Anchoring RIIbeta to the CytoskeletonNew Concepts in Alpha-1 Antitrypsin Deficiency Disease Mechanisms.Single Prolonged Stress induces ATF6 alpha-dependent Endoplasmic reticulum stress and the apoptotic process in medial Frontal Cortex neurons.HLA class I binding motifs derived from random peptide libraries differ at the COOH terminus from those of eluted peptides.Intracellular transport and secretion of salivary proteins.Analysis of ER resident proteins in Saccharomyces cerevisiae: implementation of H/KDEL retrieval sequences.Molecular chaperone Hsp110 rescues a vesicle transport defect produced by an ALS-associated mutant SOD1 protein in squid axoplasm.Polypeptide binding properties of the chaperone calreticulin.Analysis of Qa-1(b) peptide binding specificity and the capacity of CD94/NKG2A to discriminate between Qa-1-peptide complexesThe conserved helix C region in the superfamily of interferon-gamma /interleukin-10-related cytokines corresponds to a high-affinity binding site for the HSP70 chaperone DnaK.Activation and expression of proteins during synchronous germination of aerial spores of Streptomyces granaticolor.BiP clustering facilitates protein folding in the endoplasmic reticulumThe molecular chaperone DnaJ is required for the degradation of a soluble abnormal protein in Escherichia coli.Divergent Hsc70 binding properties of mitochondrial and cytosolic aspartate aminotransferase. Implications for their segregation to different cellular compartments.Kinetic analysis of the mechanism and specificity of protein-disulfide isomerase using fluorescence-quenched peptides.Affinity-based screening of combinatorial libraries using automated, serial-column chromatography.Biological heterogeneity of the peptide-binding motif of the 70-kDa heat shock protein by surface plasmon resonance analysis.Unfolded protein response and cell death after depletion of brefeldin A-inhibited guanine nucleotide-exchange protein GBF1The endoplasmic reticulum protein folding factory and its chaperones: new targets for drug discovery?A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch.Molecular basis for interactions of the DnaK chaperone with substrates.Mitochondrial protein import: molecular basis of the ATP-dependent interaction of MtHsp70 with Tim44.Glycoprotein folding in the endoplasmic reticulum.Molecular chaperones--cellular machines for protein folding.Misfolded proteins induce aggregation of the lectin Yos9.Defective protein folding and aggregation as the basis of neurodegenerative diseases: the darker aspect of proteins.Expression of insulin in yeast: the importance of molecular adaptation for secretion and conversion.
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Peptide-binding specificity of the molecular chaperone BiP
description
article publié dans la revue scientifique Nature
@fr
scientific article published in Nature
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в Nature в жовтні 1991
@uk
name
Peptide-binding specificity of the molecular chaperone BiP
@en
Peptide-binding specificity of the molecular chaperone BiP
@nl
type
label
Peptide-binding specificity of the molecular chaperone BiP
@en
Peptide-binding specificity of the molecular chaperone BiP
@nl
prefLabel
Peptide-binding specificity of the molecular chaperone BiP
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Peptide-binding specificity of the molecular chaperone BiP
@nl
P2093
P356
P1433
P1476
Peptide-binding specificity of the molecular chaperone BiP
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P2093
P2888
P304
P356
10.1038/353726A0
P407
P577
1991-10-01T00:00:00Z
P6179
1032320714