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.
about
Major histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly statusComplement regulation at the molecular level: The structure of decay-accelerating factorDownregulation of ERp57 expression is associated with poor prognosis in early-stage cervical cancerHuman serum IgM glycosylation: identification of glycoforms that can bind to mannan-binding lectin.Essential glycan-dependent interactions optimize MHC class I peptide loadingA role for UDP-glucose glycoprotein glucosyltransferase in expression and quality control of MHC class I moleculesA systematic study of glycopeptide esterification for the semi-quantitative determination of sialylation in antibodies.Glycosylation of prion strains in transmissible spongiform encephalopathies.Tapasin and other chaperones: models of the MHC class I loading complex.SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER.Mechanisms of MHC class I-restricted antigen processing and cross-presentation.Functional significance of tapasin membrane association and disulfide linkage to ERp57 in MHC class I presentationLectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules.Early phagosomes in dendritic cells form a cellular compartment sufficient for cross presentation of exogenous antigensCalreticulin-dependent recycling in the early secretory pathway mediates optimal peptide loading of MHC class I molecules.Human follicular lymphoma cells contain oligomannose glycans in the antigen-binding site of the B-cell receptor.Variable region heavy chain glycosylation determines the anticoagulant activity of a factor VIII antibody.Distinct functions for the glycans of tapasin and heavy chains in the assembly of MHC class I molecules.Importance of N-linked glycosylation in the functional expression of murine CD1d1.Calreticulin promotes folding of functional human leukocyte antigen class I molecules in vitro.Monoglucosylated glycans in the secreted human complement component C3: implications for protein biosynthesis and structure.Interaction of mannan binding lectin with alpha2 macroglobulin via exposed oligomannose glycans: a conserved feature of the thiol ester protein family?N-linked glycosylation selectively regulates the generic folding of HLA-Cw1.
P2860
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P2860
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.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
Identification of specific gly ...... olving calreticulin and ERp57.
@en
type
label
Identification of specific gly ...... olving calreticulin and ERp57.
@en
prefLabel
Identification of specific gly ...... olving calreticulin and ERp57.
@en
P2093
P2860
P356
P1476
Identification of specific gly ...... olving calreticulin and ERp57.
@en
P2093
Catherine M Radcliffe
David J Harvey
Gundo Diedrich
Pauline M Rudd
Peter Cresswell
Raymond A Dwek
P2860
P304
46415-46423
P356
10.1074/JBC.M202466200
P407
P577
2002-09-15T00:00:00Z