In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum. - Wikidata - wikimedia - TriplyDB

In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum.

In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum.

http://www.wikidata.org/entity/Q34447105

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Coupling endoplasmic reticulum stress to the cell death program: role of the ER chaperone GRP78 A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions ATPase activity of a yeast secretory glycoprotein allows ER exit during inactivation of COPII components Sec24p and Sec13p.Co- and Post-Translational Protein Folding in the ER UPR-induced resistance to etoposide is downstream of PERK and independent of changes in topoisomerase IIα levels Cloning and characterization of a novel GRP78-binding protein in the rat brain ERdj4 protein is a soluble endoplasmic reticulum (ER) DnaJ family protein that interacts with ER-associated degradation machinery Transcriptional and post-transcriptional regulation of proangiogenic factors by the unfolded protein response.Probing for membrane domains in the endoplasmic reticulum: retention and degradation of unassembled MHC class I molecules.Identification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by ER stress.Sil1, a nucleotide exchange factor for BiP, is not required for antibody assembly or secretion GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development.Antigen retrieval to improve the immunocytochemistry detection of sigma-1 receptors and ER chaperones.Misfolded proteins, endoplasmic reticulum stress and neurodegeneration.Hsp70 promotes epithelial sodium channel functional expression by increasing its association with coat complex II and its exit from endoplasmic reticulum.Proteomic assessment shows that many endoplasmic reticulum (ER)-resident proteins are targeted by N(epsilon)-lysine acetylation in the lumen of the organelle and predicts broad biological impact.Physiological modulation of BiP activity by trans-protomer engagement of the interdomain linker Dimerization-dependent folding underlies assembly control of the clonotypic αβT cell receptor chains The in vivo association of BiP with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP.Dominant-interfering Hsc70 mutants disrupt multiple stages of the clathrin-coated vesicle cycle in vivo.BiP mutants that are unable to interact with endoplasmic reticulum DnaJ proteins provide insights into interdomain interactions in BiP.Bacteria- and host-derived mechanisms to control intestinal epithelial cell homeostasis: implications for chronic inflammation.Tissue-specific expression of dominant negative mutant Drosophila HSC70 causes developmental defects and lethality.In vitro reconstitution of microtubule plus end-directed, GTPgammaS-sensitive motility of Golgi membranes Hsc70 negatively regulates epithelial sodium channel trafficking at multiple sites in epithelial cells.Central ceramide-induced hypothalamic lipotoxicity and ER stress regulate energy balance The large Hsp70 Grp170 binds to unfolded protein substrates in vivo with a regulation distinct from conventional Hsp70s.Endoplasmic reticulum (ER) stress and hypoxia response pathways interact to potentiate hypoxia-inducible factor 1 (HIF-1) transcriptional activity on targets like vascular endothelial growth factor (VEGF)Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutants.Endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins and mutant P23H rhodopsin in photoreceptor cells.Glucose-regulated proteins in cancer: molecular mechanisms and therapeutic potential A soluble secretory reporter system in Trypanosoma brucei. Studies on endoplasmic reticulum targeting.Herp coordinates compartmentalization and recruitment of HRD1 and misfolded proteins for ERAD.BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly.Transcriptional and post-transcriptional regulation of transmembrane protein 132A.The unfolded protein response regulator GRP78/BiP is required for endoplasmic reticulum integrity and stress-induced autophagy in mammalian cells.The Role of BiP Retrieval by the KDEL Receptor in the Early Secretory Pathway and its Effect on Protein Quality Control and Neurodegeneration.Protein processing: a role in the pathophysiology of genetic disease.ERdj3, a luminal ER DnaJ homologue, binds directly to unfolded proteins in the mammalian ER: identification of critical residues.

P2860

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P2860

In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum.

http://www.wikidata.org/entity/Q34447105

description

1995 nî lūn-bûn

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1995 թուականի Մարտին հրատարակուած գիտական յօդուած

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1995 թվականի մարտին հրատարակված գիտական հոդված

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1995年の論文

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In vivo expression of mammalia ...... of the endoplasmic reticulum.

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In vivo expression of mammalia ...... of the endoplasmic reticulum.

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In vivo expression of mammalia ...... of the endoplasmic reticulum.

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In vivo expression of mammalia ...... of the endoplasmic reticulum.

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In vivo expression of mammalia ...... of the endoplasmic reticulum.

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In vivo expression of mammalia ...... of the endoplasmic reticulum.

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In vivo expression of mammalia ...... of the endoplasmic reticulum.

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In vivo expression of mammalia ...... of the endoplasmic reticulum.

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In vivo expression of mammalia ...... of the endoplasmic reticulum.

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Molecular Biology of the Cell

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In vivo expression of mammalia ...... of the endoplasmic reticulum.

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B Lawson

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J R Gaut

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J Y Wei

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K G Murti

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P2860

ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase

Use of peptide tagging to detect proteins expressed from cloned genes: deletion mapping functional domains of Drosophila hsp 70

Regulating the retention of T-cell receptor alpha chain variants within the endoplasmic reticulum: Ca(2+)-dependent association with BiP

Genetics of somatic mammalian cells. III. Long-term cultivation of euploid cells from human and animal subjects

Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment

Threonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysis

Site-directed mutagenesis by overlap extension using the polymerase chain reaction

KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene.

"Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate--polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A

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endoplasmic reticulum

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