Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins. - Wikidata - wikimedia - TriplyDB

Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins.

Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins.

http://www.wikidata.org/entity/Q34451461

about

Major histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly status Mutagenic analysis of the 3' cis-acting elements of the rubella virus genome.ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly.Incomplete endoplasmic reticulum (ER) retention in immature thymocytes as revealed by surface expression of "ER-resident" molecular chaperones Suppressive roles of calreticulin in prostate cancer growth and metastasis ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum N-linked sugar-regulated protein folding and quality control in the ER Involvement of endoplasmic reticulum chaperones in the folding of hepatitis C virus glycoproteins Alpha-glucosidase inhibitors reduce dengue virus production by affecting the initial steps of virion morphogenesis in the endoplasmic reticulum Study of the mechanism of antiviral action of iminosugar derivatives against bovine viral diarrhea virus Antiviral effect of N-butyldeoxynojirimycin against bovine viral diarrhea virus correlates with misfolding of E2 envelope proteins and impairment of their association into E1-E2 heterodimers.The hepatitis C virus p7 protein forms an ion channel that is inhibited by long-alkyl-chain iminosugar derivatives What is the role of alternate splicing in antigen presentation by major histocompatibility complex class I molecules?NMR structure of the calreticulin P-domain Structural Basis of Carbohydrate Recognition by Calreticulin Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum.Cell wall 1,6-beta-glucan synthesis in Saccharomyces cerevisiae depends on ER glucosidases I and II, and the molecular chaperone BiP/Kar2p.N-Glycan-based ER Molecular Chaperone and Protein Quality Control System: The Calnexin Binding Cycle The N-terminal region of tapasin is required to stabilize the MHC class I loading complex Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit Calreticulin enhances the transcriptional activity of thyroid transcription factor-1 by binding to its homeodomain Folding of thyroglobulin in the calnexin/calreticulin pathway and its alteration by loss of Ca2+ from the endoplasmic reticulum Biosynthesis of inositol trisphosphate receptors: selective association with the molecular chaperone calnexin Functional relationship between calreticulin, calnexin, and the endoplasmic reticulum luminal domain of calnexin Differential modulation of SERCA2 isoforms by calreticulin.A hookworm allergen which strongly resembles calreticulin.Polypeptide binding properties of the chaperone calreticulin.Ion binding properties of the dehydrin ERD14 are dependent upon phosphorylation.Three-dimensional structure topology of the calreticulin P-domain based on NMR assignment.The calcium-binding activity of a vacuole-associated, dehydrin-like protein is regulated by phosphorylation.Alternative chaperone machinery may compensate for calreticulin/calnexin deficiency in Caenorhabditis elegans.Monitoring chaperone engagement of substrates in the endoplasmic reticulum of live cells Calreticulin: one protein, one gene, many functions.RIG-I, MDA5 and TLR3 synergistically play an important role in restriction of dengue virus infection.Most F508del-CFTR is targeted to degradation at an early folding checkpoint and independently of calnexin The role of UDP-Glc:glycoprotein glucosyltransferase 1 in the maturation of an obligate substrate prosaposin.Hijacking of host calreticulin is required for the white spot syndrome virus replication cycle.Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradation C1q receptors.

P2860

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P2860

Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins.

http://www.wikidata.org/entity/Q34451461

description

1995 nî lūn-bûn

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1995 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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1995 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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1995年の論文

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1995年学术文章

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1995年学术文章

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1995年学术文章

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1995年学术文章

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1995年学术文章

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1995年學術文章

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name

Transient, lectin-like associa ...... lular and viral glycoproteins.

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Transient, lectin-like associa ...... lular and viral glycoproteins.

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Transient, lectin-like associa ...... lular and viral glycoproteins.

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type

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Transient, lectin-like associa ...... lular and viral glycoproteins.

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Transient, lectin-like associa ...... lular and viral glycoproteins.

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Transient, lectin-like associa ...... lular and viral glycoproteins.

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Transient, lectin-like associa ...... lular and viral glycoproteins.

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Transient, lectin-like associa ...... lular and viral glycoproteins.

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Transient, lectin-like associa ...... lular and viral glycoproteins.

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Molecular Biology of the Cell

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Transient, lectin-like associa ...... lular and viral glycoproteins.

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Helenius A

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Ora A

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Peterson JR

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P2860

Inhibition of nuclear hormone receptor activity by calreticulin

Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1

Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment.

Assembly of asparagine-linked oligosaccharides

Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution

Retention of unassembled components of integral membrane proteins by calnexin

Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control

Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin)

The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins

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10.1091/MBC.6.9.1173

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9

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6

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8534914

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301275

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