BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions - Test2 - elhamkhani - TriplyDB

BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions

BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions

http://www.wikidata.org/entity/Q26825679

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The nucleotide exchange factors of Hsp70 molecular chaperones How Polyomaviruses Exploit the ERAD Machinery to Cause Infection Co- and Post-Translational Protein Folding in the ER A bacterial toxin and a nonenveloped virus hijack ER-to-cytosol membrane translocation pathways to cause disease Secretion of the endoplasmic reticulum stress protein, GRP78, into the BALF is increased in cigarette smokers.Regulation of calreticulin-major histocompatibility complex (MHC) class I interactions by ATP.Dimerization-dependent folding underlies assembly control of the clonotypic αβT cell receptor chains The Grp170 nucleotide exchange factor executes a key role during ERAD of cellular misfolded clients.Opportunistic intruders: how viruses orchestrate ER functions to infect cells.Ritterostatin GN 1N , a Cephalostatin-Ritterazine Bis-steroidal Pyrazine Hybrid, Selectively Targets GRP78.Chaperone-Driven Degradation of a Misfolded Proinsulin Mutant in Parallel With Restoration of Wild-Type Insulin Secretion.Unfolded protein response in pollen development and heat stress tolerance.Modulation of Molecular Chaperones in Huntington's Disease and Other Polyglutamine Disorders.Mutations in INPP5K Cause a Form of Congenital Muscular Dystrophy Overlapping Marinesco-Sjögren Syndrome and Dystroglycanopathy.HSPA5 Gene encoding Hsp70 chaperone BiP in the endoplasmic reticulum.The Role of BiP Retrieval by the KDEL Receptor in the Early Secretory Pathway and its Effect on Protein Quality Control and Neurodegeneration.Division of Labor: ER-Resident BiP Co-Chaperones Match Substrates to Fates Based on Specific Binding Sequences.p53-mediated suppression of BiP triggers BIK-induced apoptosis during prolonged endoplasmic reticulum stress.A Conserved Cysteine within the ATPase Domain of the Endoplasmic Reticulum Chaperone BiP is Necessary for a Complete Complement of BiP Activities.Allosteric fine-tuning of the conformational equilibrium poises the chaperone BiP for post-translational regulation A Chaperone Complex Formed by HSP47, FKBP65, and BiP Modulates Telopeptide Lysyl Hydroxylation of Type I Procollagen.A J-Protein Co-chaperone Recruits BiP to Monomerize IRE1 and Repress the Unfolded Protein Response.AMPylation targets the rate-limiting step of BiP's ATPase cycle for its functional inactivation.Ratiometric sensing of BiP-client versus BiP levels by the unfolded protein response determines its signaling amplitude.Lysine trimethylation regulates 78-kDa glucose-regulated protein proteostasis during endoplasmic reticulum stress.Bap (Sil1) regulates the molecular chaperone BiP by coupling release of nucleotide and substrate.Endoplasmic reticulum proteins SDF2 and SDF2L1 act as components of the BiP chaperone cycle to prevent protein aggregation.Endoplasmic reticulum chaperone GRP78 mediates cigarette smoke-induced necroptosis and injury in bronchial epithelium.Single molecule force spectroscopy reveals the effect of BiP chaperone on protein folding.SIL1, the endoplasmic-reticulum-localized BiP co-chaperone, plays a crucial role in maintaining skeletal muscle proteostasis and physiology.Effect of the unfolded protein response on ER protein export: a potential new mechanism to relieve ER stress.Ethanol Induced Disordering of Pancreatic Acinar Cell Endoplasmic Reticulum: An ER Stress/Defective Unfolded Protein Response Model.Metabolic Reprogramming and the Recovery of Physiological Functionality in 3D Cultures in Micro-Bioreactors.

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BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions

http://www.wikidata.org/entity/Q26825679

description

2015 nî lūn-bûn

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2015 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2015 թվականի ապրիլին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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BiP and its nucleotide exchang ...... ction and biological functions

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BiP and its nucleotide exchang ...... ction and biological functions

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BiP and its nucleotide exchang ...... ction and biological functions

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BiP and its nucleotide exchang ...... ction and biological functions

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J.JMB.2015.02.011

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Journal of Molecular Biology

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BiP and its nucleotide exchang ...... ction and biological functions

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Julia Behnke

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Linda M Hendershot

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P2860

Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein

150-kDa oxygen-regulated protein (ORP150) functions as a novel molecular chaperone in MDCK cells

LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum

BiP-mediated closing of the Sec61 channel limits Ca2+ leakage from the ER

Grp78, Grp94, and Grp170 interact with alpha1-antitrypsin mutants that are retained in the endoplasmic reticulum

Cloning and expression of cDNA encoding the human 150 kDa oxygen-regulated protein, ORP150

Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3

A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.

ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates

150-kD oxygen-regulated protein is expressed in human atherosclerotic plaques and allows mononuclear phagocytes to withstand cellular stress on exposure to hypoxia and modified low density lipoprotein

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1589-1608

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scholarly article

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3843290

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10.1016/J.JMB.2015.02.011

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7

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427

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Matthias J Feige

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25698114

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4356644

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