Molecular chaperones involved in protein degradation in the endoplasmic reticulum: quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum
about
Procaryotic expression of single-chain variable-fragment (scFv) antibodies: secretion in L-form cells of Proteus mirabilis leads to active product and overcomes the limitations of periplasmic expression in Escherichia coliERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substratesMutations in the human lambda5/14.1 gene result in B cell deficiency and agammaglobulinemiaOne step at a time: endoplasmic reticulum-associated degradationRegulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genesThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyDer1, a novel protein specifically required for endoplasmic reticulum degradation in yeastN-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast.A novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomesThe endoplasmic reticulum-associated degradation of the epithelial sodium channel requires a unique complement of molecular chaperones.Evasion of endoplasmic reticulum surveillance makes Wsc1p an obligate substrate of Golgi quality controlActive site residues of human beta-glucuronidase. Evidence for Glu(540) as the nucleophile and Glu(451) as the acid-base residue.Roles of heavy and light chains in IgM polymerization.Binding of free immunoglobulin light chains to VpreB3 inhibits their maturation and secretion in chicken B cells.Characterization of pancreatic ERj3p, a homolog of yeast DnaJ-like protein Scj1p.Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes.Antimyeloma Effects of the Heat Shock Protein 70 Molecular Chaperone Inhibitor MAL3-101Dependence of endoplasmic reticulum-associated degradation on the peptide binding domain and concentration of BiP.Delta F508 CFTR pool in the endoplasmic reticulum is increased by calnexin overexpression.The variable domain of nonassembled Ig light chains determines both their half-life and binding to the chaperone BiP.Members of the Hsp70 Family Recognize Distinct Types of Sequences to Execute ER Quality Control.Protein folding in the endoplasmic reticulum: lessons from the human chorionic gonadotropin beta subunitHsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast.Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER.Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae.Targeting PKC: a novel role for beta-catenin in ER stress and apoptotic signalingSubtilase cytotoxin cleaves newly synthesized BiP and blocks antibody secretion in B lymphocytes.Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutants.Endoplasmic reticulum-dependent redox reactions control endoplasmic reticulum-associated degradation and pathogen entry.Endoplasmic reticulum (ER)-associated degradation of misfolded N-linked glycoproteins is suppressed upon inhibition of ER mannosidase I.Dissociation from BiP and retrotranslocation of unassembled immunoglobulin light chains are tightly coupled to proteasome activity.BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly.Degradation of a short-lived glycoprotein from the lumen of the endoplasmic reticulum: the role of N-linked glycans and the unfolded protein response.HSPA5 Gene encoding Hsp70 chaperone BiP in the endoplasmic reticulum.Analysis of heterologous protein production in defined recombinant Aspergillus awamori strains.The role of BiP in endoplasmic reticulum-associated degradation of major histocompatibility complex class I heavy chain induced by cytomegalovirus proteins.Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells.Association of the thyrotropin receptor with calnexin, calreticulin and BiP. Efects on the maturation of the receptor.Pivotal role of calnexin and mannose trimming in regulating the endoplasmic reticulum-associated degradation of major histocompatibility complex class I heavy chain.Assembly of immunoglobulin light chains as a prerequisite for secretion. A model for oligomerization-dependent subunit folding.
P2860
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P2860
Molecular chaperones involved in protein degradation in the endoplasmic reticulum: quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum
description
1995 nî lūn-bûn
@nan
1995 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Molecular chaperones involved ...... d in the endoplasmic reticulum
@ast
Molecular chaperones involved ...... d in the endoplasmic reticulum
@en
Molecular chaperones involved ...... d in the endoplasmic reticulum
@nl
type
label
Molecular chaperones involved ...... d in the endoplasmic reticulum
@ast
Molecular chaperones involved ...... d in the endoplasmic reticulum
@en
Molecular chaperones involved ...... d in the endoplasmic reticulum
@nl
prefLabel
Molecular chaperones involved ...... d in the endoplasmic reticulum
@ast
Molecular chaperones involved ...... d in the endoplasmic reticulum
@en
Molecular chaperones involved ...... d in the endoplasmic reticulum
@nl
P2093
P2860
P921
P356
P1476
Molecular chaperones involved ...... d in the endoplasmic reticulum
@en
P2093
P2860
P304
P356
10.1073/PNAS.92.5.1764
P407
P577
1995-02-01T00:00:00Z