The lectin chaperone calnexin utilizes polypeptide-based interactions to associate with many of its substrates in vivo.
about
Major histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly statusGetting in and out from calnexin/calreticulin cyclesN-linked sugar-regulated protein folding and quality control in the ERN-Glycan-based ER Molecular Chaperone and Protein Quality Control System: The Calnexin Binding CycleLocalization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulinMonitoring chaperone engagement of substrates in the endoplasmic reticulum of live cellsCalnexin Delta 185-520 partially reverses the misprocessing of the Delta F508 cystic fibrosis transmembrane conductance regulator.HIV-1 protein Nef inhibits activity of ATP-binding cassette transporter A1 by targeting endoplasmic reticulum chaperone calnexinRole of calnexin in the glycan-independent quality control of proteolipid protein.Delta F508 CFTR pool in the endoplasmic reticulum is increased by calnexin overexpression.Peptide-based interactions with calnexin target misassembled membrane proteins into endoplasmic reticulum-derived multilamellar bodies.Cyclophilin C Participates in the US2-Mediated Degradation of Major Histocompatibility Complex Class I Molecules.Tapasin and other chaperones: models of the MHC class I loading complex.The interplay between folding-facilitating mechanisms in Trypanosoma cruzi endoplasmic reticulum.Endoplasmic reticulum chaperones stabilize nicotinic receptor subunits and regulate receptor assembly.N-linked glycosylation is required for nicotinic receptor assembly but not for subunit associations with calnexinLectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules.Mechanisms of pre-apoptotic calreticulin exposure in immunogenic cell death.ERp57 does not require interactions with calnexin and calreticulin to promote assembly of class I histocompatibility molecules, and it enhances peptide loading independently of its redox activitySpecific ER quality control components required for biogenesis of the plant innate immune receptor EFR.Protein secretion and the endoplasmic reticulum.The many functions of the endoplasmic reticulum chaperones and folding enzymes.Contributions of the Lectin and Polypeptide Binding Sites of Calreticulin to Its Chaperone Functions in Vitro and in Cells.Relationship between calnexin and BiP in suppressing aggregation and promoting refolding of protein and glycoprotein substrates.Increase of calnexin gene dosage boosts the secretion of heterologous proteins by Hansenula polymorpha.Surface calreticulin mediates muramyl dipeptide-induced apoptosis in RK13 cells.The primary substrate binding site in the b' domain of ERp57 is adapted for endoplasmic reticulum lectin association.Lectin-deficient calnexin is capable of binding class I histocompatibility molecules in vivo and preventing their degradation.Maturation of hepatic lipase. Formation of functional enzyme in the endoplasmic reticulum is the rate-limiting step in its secretion.Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteinsLectin-mediated retention of p62 facilitates p62-E1 heterodimerization in endoplasmic reticulum of Semliki Forest virus-infected cells.D1 and D2 dopamine receptor expression is regulated by direct interaction with the chaperone protein calnexin.Productive folding of tyrosinase ectodomain is controlled by the transmembrane anchor.Functions of ERp57 in the folding and assembly of major histocompatibility complex class I molecules.A Novel Potential Signal Peptide Sequence and Overexpression of ER-Resident Chaperones Enhance Heterologous Protein Secretion in Thermotolerant Methylotrophic Yeast Ogataea thermomethanolica.Glycan-independent role of calnexin in the intracellular retention of Charcot-Marie-tooth 1A Gas3/PMP22 mutants.Calreticulin promotes folding of functional human leukocyte antigen class I molecules in vitro.Association of the thyrotropin receptor with calnexin, calreticulin and BiP. Efects on the maturation of the receptor.Identification of specific glycoforms of major histocompatibility complex class I heavy chains suggests that class I peptide loading is an adaptation of the quality control pathway involving calreticulin and ERp57.Mutant MHC class I molecules define interactions between components of the peptide-loading complex.
P2860
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P2860
The lectin chaperone calnexin utilizes polypeptide-based interactions to associate with many of its substrates in vivo.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
2001年论文
@zh
2001年论文
@zh-cn
name
The lectin chaperone calnexin ...... any of its substrates in vivo.
@en
type
label
The lectin chaperone calnexin ...... any of its substrates in vivo.
@en
prefLabel
The lectin chaperone calnexin ...... any of its substrates in vivo.
@en
P2860
P356
P1476
The lectin chaperone calnexin ...... any of its substrates in vivo.
@en
P2093
Danilczyk UG
Williams DB
P2860
P304
25532-25540
P356
10.1074/JBC.M100270200
P407
P577
2001-05-03T00:00:00Z