Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins. - Wikidata - wikimedia - TriplyDB

Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins.

Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins.

http://www.wikidata.org/entity/Q27931697

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Structure of the Ire1 autophosphorylation complex and implications for the unfolded protein response Saccharomyces cerevisiae Rot1 is an essential molecular chaperone in the endoplasmic reticulum Saccharomyces cerevisiae Rot1p is an ER-localized membrane protein that may function with BiP/Kar2p in protein folding.An essential dimer-forming subregion of the endoplasmic reticulum stress sensor Ire1.Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins.Protein kinase Snf1 is involved in the proper regulation of the unfolded protein response in Saccharomyces cerevisiae.The Saccharomyces cerevisiae YFR041C/ERJ5 gene encoding a type I membrane protein with a J domain is required to preserve the folding capacity of the endoplasmic reticulum.Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP Activation profiles of HSPA5 during the glomerular mesangial cell stress response to chemical injury Big data mining powers fungal research: recent advances in fission yeast systems biology approaches.Expression profiling on soybean leaves reveals integration of ER- and osmotic-stress pathways.The BiP molecular chaperone plays multiple roles during the biogenesis of torsinA, an AAA+ ATPase associated with the neurological disease early-onset torsion dystonia.Stable binding of ATF6 to BiP in the endoplasmic reticulum stress response.J domain co-chaperone specificity defines the role of BiP during protein translocation On the mechanism of sensing unfolded protein in the endoplasmic reticulum.Low level genome mistranslations deregulate the transcriptome and translatome and generate proteotoxic stress in yeast.Genome-wide expression analysis upon constitutive activation of the HacA bZIP transcription factor in Aspergillus niger reveals a coordinated cellular response to counteract ER stress Direct association of unfolded proteins with mammalian ER stress sensor, IRE1β The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response.A review of the mammalian unfolded protein response.Proteostasis regulation at the endoplasmic reticulum: a new perturbation site for targeted cancer therapy.Unfolding the unfolded protein response: unique insights into brain ischemia.Tight regulation of the unfolded protein sensor Ire1 by its intramolecularly antagonizing subdomain.Activation of the unfolded protein response pathway causes ceramide accumulation in yeast and INS-1E insulinoma cells.Kar2p availability defines distinct forms of endoplasmic reticulum stress in living cells.Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Enhancing antibody folding and secretion by tailoring the Saccharomyces cerevisiae endoplasmic reticulum.The unfolded protein response and its role in intestinal homeostasis and inflammation.Endoplasmic reticulum stress and the making of a professional secretory cell.The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum Translational infidelity-induced protein stress results from a deficiency in Trm9-catalyzed tRNA modifications.Nonmuscle myosin IIB links cytoskeleton to IRE1α signaling during ER stress.Endoplasmic reticulum stress sensing in the unfolded protein response The Cek1‑mediated MAP kinase pathway regulates exposure of α‑1,2 and β‑1,2‑mannosides in the cell wall of Candida albicans modulating immune recognition Insufficient ER-stress response causes selective mouse cerebellar granule cell degeneration resembling that seen in congenital disorders of glycosylation.Fine-tuning of the unfolded protein response: Assembling the IRE1alpha interactome.Stress sensing in plants by an ER stress sensor/transducer, bZIP28 Inter-regulation of the unfolded protein response and auxin signaling Virus-induced ER stress and the unfolded protein response UPR Signal Activation by Luminal Sensor Domains.

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Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins.

http://www.wikidata.org/entity/Q27931697

description

2003 nî lūn-bûn

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2003 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2003年の論文

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Genetic evidence for a role of ...... mulation of unfolded proteins.

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Genetic evidence for a role of ...... mulation of unfolded proteins.

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Genetic evidence for a role of ...... mulation of unfolded proteins.

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Genetic evidence for a role of ...... mulation of unfolded proteins.

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Genetic evidence for a role of ...... mulation of unfolded proteins.

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Genetic evidence for a role of ...... mulation of unfolded proteins.

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Genetic evidence for a role of ...... mulation of unfolded proteins.

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Molecular Biology of the Cell

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Hiroshi Abe

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Ileana C Farcasanu

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Kenji Kohno

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Masato Takeuchi

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Yuki I Kimata

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Yukio Kimata

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Yusuke Shimizu

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P2860

Translational control by the ER transmembrane kinase/ribonuclease IRE1 under ER stress

XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor

Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development

A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells

IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response

A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae

Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation.

A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus.

Purification and characterization of BiP/Kar2 protein from Saccharomyces cerevisiae.

BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane.

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