Mistargeting of the lectin ERGIC-53 to the endoplasmic reticulum of HeLa cells impairs the secretion of a lysosomal enzyme. - Test2 - elhamkhani - TriplyDB

Mistargeting of the lectin ERGIC-53 to the endoplasmic reticulum of HeLa cells impairs the secretion of a lysosomal enzyme.

Mistargeting of the lectin ERGIC-53 to the endoplasmic reticulum of HeLa cells impairs the secretion of a lysosomal enzyme.

http://www.wikidata.org/entity/Q36256238

about

Sec24 proteins and sorting at the endoplasmic reticulum p125 is a novel mammalian Sec23p-interacting protein with structural similarity to phospholipid-modifying proteins Sequential steps and checkpoints in the early exocytic compartment during secretory IgM biogenesis Profile-based data base scanning for animal L-type lectins and characterization of VIPL, a novel VIP36-like endoplasmic reticulum protein Proteomics of endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46 O-fucosylation is required for ADAMTS13 secretion The cargo receptors Surf4, endoplasmic reticulum-Golgi intermediate compartment (ERGIC)-53, and p25 are required to maintain the architecture of ERGIC and Golgi.Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms N-linked sugar-regulated protein folding and quality control in the ER Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum Structural Characterization of Carbohydrate Binding by LMAN1 Protein Provides New Insight into the Endoplasmic Reticulum Export of Factors V (FV) and VIII (FVIII)Mice deficient in LMAN1 exhibit FV and FVIII deficiencies and liver accumulation of α1-antitrypsin Lectins and traffic in the secretory pathway The ordered and compartment-specfific autoproteolytic removal of the furin intramolecular chaperone is required for enzyme activation.Protein interaction profiling of the p97 adaptor UBXD1 points to a role for the complex in modulating ERGIC-53 trafficking.Quantitative ER <--> Golgi transport kinetics and protein separation upon Golgi exit revealed by vesicular integral membrane protein 36 dynamics in live cells.Identification of ERGIC-53 as an intracellular transport receptor of alpha1-antitrypsin.EF-hand domains of MCFD2 mediate interactions with both LMAN1 and coagulation factor V or VIII.From the ER to the golgi: insights from the study of combined factors V and VIII deficiency.Capturing protein interactions in the secretory pathway of living cells.The lectin ERGIC-53 is a cargo transport receptor for glycoproteins.Carbohydrate- and conformation-dependent cargo capture for ER-exit Heat shock induces preferential translation of ERGIC-53 and affects its recycling pathway.Molecular basis of LMAN1 in coordinating LMAN1-MCFD2 cargo receptor formation and ER-to-Golgi transport of FV/FVIII Role of Sec24 isoforms in selective export of membrane proteins from the endoplasmic reticulum Requirement of a leucine residue for (apical) membrane expression of type IIb NaPi cotransporters.Combined deficiency of factor V and factor VIII is due to mutations in either LMAN1 or MCFD2 The COPII pathway and hematologic disease Cysteine cathepsin non-inhibitory binding partners: modulating intracellular trafficking and function.Recent developments in the understanding of the combined deficiency of FV and FVIII.Glycoprotein folding and quality-control mechanisms in protein-folding diseases Ser1928 phosphorylation by PKA stimulates the L-type Ca2+ channel CaV1.2 and vasoconstriction during acute hyperglycemia and diabetes.Inherited hematological disorders due to defects in coat protein (COP)II complex.Insights into animal and plant lectins with antimicrobial activities.Mannose-dependent endoplasmic reticulum (ER)-Golgi intermediate compartment-53-mediated ER to Golgi trafficking of coagulation factors V and VIII.LMAN1 is a molecular chaperone for the secretion of coagulation factor VIII.Roles for alpha(2)p24 and COPI in endoplasmic reticulum cargo exit site formation.The intracellular cargo receptor ERGIC-53 is required for the production of infectious arenavirus, coronavirus, and filovirus particles.Human cytomegalovirus immediate early glycoprotein US3 retains MHC class I molecules by transient association.Cytoplasmic tail motifs mediate endoplasmic reticulum localization and export of transmembrane reporters in the protozoan parasite Toxoplasma gondii.

P2860

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P2860

Mistargeting of the lectin ERGIC-53 to the endoplasmic reticulum of HeLa cells impairs the secretion of a lysosomal enzyme.

http://www.wikidata.org/entity/Q36256238

description

1998 nî lūn-bûn

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1998年学术文章

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Mistargeting of the lectin ERG ...... cretion of a lysosomal enzyme.

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Mistargeting of the lectin ERG ...... cretion of a lysosomal enzyme.

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Mistargeting of the lectin ERG ...... cretion of a lysosomal enzyme.

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Mistargeting of the lectin ERG ...... cretion of a lysosomal enzyme.

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Mistargeting of the lectin ERG ...... cretion of a lysosomal enzyme.

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Mistargeting of the lectin ERG ...... cretion of a lysosomal enzyme.

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Mistargeting of the lectin ERG ...... cretion of a lysosomal enzyme.

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P2860

Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa

Sequence and overexpression of GPP130/GIMPc: evidence for saturable pH-sensitive targeting of a type II early Golgi membrane protein

ERGIC-53, a membrane protein of the endoplasmic reticulum-Golgi intermediate compartment, is identical to MR60, an intracellular mannose-specific lectin of myelomonocytic cells

Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments

Mutations in the ER-Golgi intermediate compartment protein ERGIC-53 cause combined deficiency of coagulation factors V and VIII

Tight control of gene expression in mammalian cells by tetracycline-responsive promoters

ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins

The mammalian protein (rbet1) homologous to yeast Bet1p is primarily associated with the pre-Golgi intermediate compartment and is involved in vesicular transport from the endoplasmic reticulum to the Golgi apparatus

Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum.

A putative novel class of animal lectins in the secretory pathway homologous to leguminous lectins

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377-389

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2

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142

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13606234

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9679138

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endoplasmic reticulum

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2133042

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