Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast. - Wikidata - wikimedia - TriplyDB

Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.

Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.

http://www.wikidata.org/entity/Q27939809

about

Congenital disorders of glycosylation type Ig is defined by a deficiency in dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferase Profile-based data base scanning for animal L-type lectins and characterization of VIPL, a novel VIP36-like endoplasmic reticulum protein Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP Getting in and out from calnexin/calreticulin cycles Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control EDEM1 reveals a quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sites Endoplasmic reticulum stress in the β-cell pathogenesis of type 2 diabetes Structure of Penicillium citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the endoplasmic reticulum and Golgi class I enzymes Modulation of activity by Arg407: structure of a fungal α-1,2-mannosidase in complex with a substrate analogue ELM1 is required for multidrug resistance in Saccharomyces cerevisiae.Free-oligosaccharide control in the yeast Saccharomyces cerevisiae: roles for peptide:N-glycanase (Png1p) and vacuolar mannosidase (Ams1p).Defining the glycan destruction signal for endoplasmic reticulum-associated degradation An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport Roles of protein-disulfide isomerase-mediated disulfide bond formation of yeast Mnl1p in endoplasmic reticulum-associated degradation A Complex of Htm1 and the Oxidoreductase Pdi1 Accelerates Degradation of Misfolded Glycoproteins.Yos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation.Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum Arms Race between Enveloped Viruses and the Host ERAD Machinery EDEM accelerates ERAD by preventing aberrant dimer formation of misfolded alpha1-antitrypsin Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD)A novel stress-induced EDEM variant regulating endoplasmic reticulum-associated glycoprotein degradation EDEM1 accelerates the trimming of alpha1,2-linked mannose on the C branch of N-glycans Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains EDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic reticulum-associated degradation and mannose trimming EDEM2 and OS-9 are required for ER-associated degradation of non-glycosylated sonic hedgehog.Redox diversity in ERAD-mediated protein retrotranslocation from the endoplasmic reticulum: a complex puzzle.The BiP molecular chaperone plays multiple roles during the biogenesis of torsinA, an AAA+ ATPase associated with the neurological disease early-onset torsion dystonia.Capturing protein interactions in the secretory pathway of living cells.Most F508del-CFTR is targeted to degradation at an early folding checkpoint and independently of calnexin Organizational diversity among distinct glycoprotein endoplasmic reticulum-associated degradation programs Characterization of Schizosaccharomyces pombe ER alpha-mannosidase: a reevaluation of the role of the enzyme on ER-associated degradation Mutations of an alpha1,6 mannosyltransferase inhibit endoplasmic reticulum-associated degradation of defective brassinosteroid receptors in Arabidopsis.Two distinctly localized p-type ATPases collaborate to maintain organelle homeostasis required for glycoprotein processing and quality control Inositol deacylation by Bst1p is required for the quality control of glycosylphosphatidylinositol-anchored proteins.A novel lectin in the secretory pathway. An elegant mechanism for glycoprotein elimination.Forcible destruction of severely misfolded mammalian glycoproteins by the non-glycoprotein ERAD pathway For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection.Ubiquitin-dependent protein degradation at the yeast endoplasmic reticulum and nuclear envelope.

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P2860

Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.

http://www.wikidata.org/entity/Q27939809

description

2001 nî lūn-bûn

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2001 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2001 թվականի մայիսին հրատարակված գիտական հոդված

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2001年の論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年论文

@wuu

name

Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.

@ast

Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.

@en

Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.

@nl

type

label

Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.

@ast

Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.

@en

Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.

@nl

prefLabel

Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.

@ast

Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.

@en

Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.

@nl

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Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.

@en

P2093

A Marcil

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

C A Jakob

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D Bodmer

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D Dignard

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D Y Thomas

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J J Bergeron

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M Aebi

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P Battig

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U Spirig

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P2860

STT3, a highly conserved protein required for yeast oligosaccharyl transferase activity in vivo

Crystal structure of a class I α1,2-mannosidase involved in N-glycan processing and endoplasmic reticulum quality control

Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation.

Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation.

N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast.

Glycoprotein biosynthesis in Saccharomyces cerevisiae. Isolation and characterization of the gene encoding a specific processing alpha-mannosidase.

Role of the cysteine residues in the alpha1,2-mannosidase involved in N-glycan biosynthesis in Saccharomyces cerevisiae. The conserved Cys340 and Cys385 residues form an essential disulfide bond.

Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure.

Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway.

New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae

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423-430

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scholarly article

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3465163

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10.1093/EMBO-REPORTS/KVE089

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5

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2

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2001-05-01T00:00:00Z

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11962403

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11375935

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1083883

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