Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD) - Wikidata - awgldk - TriplyDB

Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD)

Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD)

http://www.wikidata.org/entity/Q28255326

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Proteomics analysis of the interactome of N-myc downstream regulated gene 1 and its interactions with the androgen response program in prostate cancer cells CNIH4 interacts with newly synthesized GPCR and controls their export from the endoplasmic reticulum Cytoplasmic destruction of p53 by the endoplasmic reticulum-resident ubiquitin ligase 'Synoviolin'The unfolded protein response in retinal vascular diseases: implications and therapeutic potential beyond protein folding The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology Dissecting the ER-associated degradation of a misfolded polytopic membrane protein.Analysis of quality control substrates in distinct cellular compartments reveals a unique role for Rpn4p in tolerating misfolded membrane proteins.Plant Virus Infection and the Ubiquitin Proteasome Machinery: Arms Race along the Endoplasmic Reticulum ER chaperones in mammalian development and human diseases Dystonia-associated mutations cause premature degradation of torsinA protein and cell-type-specific mislocalization to the nuclear envelope The bZIP Transcription Factor HAC-1 Is Involved in the Unfolded Protein Response and Is Necessary for Growth on Cellulose in Neurospora crassa A contiguous compartment functions as endoplasmic reticulum and endosome/lysosome in Giardia lamblia.Ubiquitin conjugation triggers misfolded protein sequestration into quality control foci when Hsp70 chaperone levels are limiting.A role for protein phosphorylation in cytochrome P450 3A4 ubiquitin-dependent proteasomal degradation Ubiquitylation in ERAD: reversing to go forward?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 Mannosidase I inhibition rescues the human alpha-sarcoglycan R77C recurrent mutation.The B7-1 cytoplasmic tail enhances intracellular transport and mammalian cell surface display of chimeric proteins in the absence of a linear ER export motif.Kinetochore genes are required to fully activate secretory pathway expansion in S. cerevisiae under induced ER stress.The THERMOSENSITIVE MALE STERILE 1 Interacts with the BiPs via DnaJ Domain and Stimulates Their ATPase Enzyme Activities in Arabidopsis Role of Derlin-1 protein in proteostasis regulation of ATP-sensitive potassium channels.The Candida albicans Kar2 protein is essential and functions during the translocation of proteins into the endoplasmic reticulum.Hsp70 promotes epithelial sodium channel functional expression by increasing its association with coat complex II and its exit from endoplasmic reticulum.Degradation Signals for Ubiquitin-Proteasome Dependent Cytosolic Protein Quality Control (CytoQC) in Yeast Flo11p-independent control of "mat" formation by hsp70 molecular chaperones and nucleotide exchange factors in yeast Cellular proteolytic systems in P450 degradation: evolutionary conservation from Saccharomyces cerevisiae to mammalian liver.Oxidoreductase interactions include a role for ERp72 engagement with mutant thyroglobulin from the rdw/rdw rat dwarf.The activities and function of molecular chaperones in the endoplasmic reticulum.How early studies on secreted and membrane protein quality control gave rise to the ER associated degradation (ERAD) pathway: the early history of ERAD.The Hsp110 molecular chaperone stabilizes apolipoprotein B from endoplasmic reticulum-associated degradation (ERAD)Influence of Hsp70s and their regulators on yeast prion propagation Heat shock proteins in antigen trafficking--implications on antigen presentation to T cells.Cholera toxin: an intracellular journey into the cytosol by way of the endoplasmic reticulum.The endoplasmic reticulum in cardiovascular health and disease.Insights on the trafficking and retro-translocation of glycosphingolipid-binding bacterial toxins.Cholera: pathophysiology and emerging therapeutic targets.Chaperoning proteins for destruction: diverse roles of Hsp70 chaperones and their co-chaperones in targeting misfolded proteins to the proteasome A molecular web: endoplasmic reticulum stress, inflammation, and oxidative stress.ER stress causes widespread protein aggregation and prion formation.Roles of silkworm endoplasmic reticulum chaperones in the secretion of recombinant proteins expressed by baculovirus system.

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Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD)

http://www.wikidata.org/entity/Q28255326

description

2005 nî lūn-bûn

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2005 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2005年の論文

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2005年論文

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2005年论文

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Roles of molecular chaperones ...... -associated degradation (ERAD)

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Roles of molecular chaperones ...... -associated degradation (ERAD)

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Roles of molecular chaperones ...... -associated degradation (ERAD)

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Roles of molecular chaperones ...... -associated degradation (ERAD)

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Roles of molecular chaperones ...... -associated degradation (ERAD)

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Roles of molecular chaperones ...... -associated degradation (ERAD)

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Roles of molecular chaperones ...... -associated degradation (ERAD)

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Journal of Biochemistry

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Roles of molecular chaperones ...... -associated degradation (ERAD)

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Jeffrey L Brodsky

http://www.w3.org/2001/XMLSchema#string

Kunio Nakatsukasa

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Shuh-ichi Nishikawa

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P2860

Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle

A membrane protein required for dislocation of misfolded proteins from the ER

A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol

Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains

Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction

A novel ER alpha-mannosidase-like protein accelerates ER-associated degradation

Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control

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

Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast.

The J-protein family: modulating protein assembly, disassembly and translocation.

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2076326

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10.1093/JB/MVI068

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5

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137

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2005-05-01T00:00:00Z

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7798802

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15944407

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P921

molecular chaperones

endoplasmic reticulum

quality control