Recruitment of MHC class I molecules by tapasin into the transporter associated with antigen processing-associated complex is essential for optimal peptide loading
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Tapasin-related protein TAPBPR is an additional component of the MHC class I presentation pathwayTapasin enhances MHC class I peptide presentation according to peptide half-lifeIdentification of an alternate splice form of tapasin in human melanoma.The binding of TAPBPR and Tapasin to MHC class I is mutually exclusive.TAPBPR alters MHC class I peptide presentation by functioning as a peptide exchange catalystTAPBPR isoforms exhibit altered association with MHC class I.Pathways of antigen processing.A highly conserved sequence of the viral TAP inhibitor ICP47 is required for freezing of the peptide transport cycleMechanisms of function of tapasin, a critical major histocompatibility complex class I assembly factorMajor histocompatibility complex class I-restricted antigen processing and presentation.Productive association between MHC class I and tapasin requires the tapasin transmembrane/cytosolic region and the tapasin C-terminal Ig-like domain.The ABCs of immunology: structure and function of TAP, the transporter associated with antigen processing.Dynamics of major histocompatibility complex class I association with the human peptide-loading complex.MHC class I alleles and their exploration of the antigen-processing machinery.Accessory molecules in the assembly of major histocompatibility complex class I/peptide complexes: how essential are they for CD8(+) T-cell immune responses?The optimization of peptide cargo bound to MHC class I molecules by the peptide-loading complex.Multiple structural and epigenetic defects in the human leukocyte antigen class I antigen presentation pathway in a recurrent metastatic melanoma following immunotherapy.Functional significance of tapasin membrane association and disulfide linkage to ERp57 in MHC class I presentationIntracellular peptide transporters in human--compartmentalization of the "peptidome".Interaction of TAPBPR, a tapasin homolog, with MHC-I molecules promotes peptide editing.Targeted degradation of ABC transporters in health and disease.ERAAP and tapasin independently edit the amino and carboxyl termini of MHC class I peptides.Viral proteins interfering with antigen presentation target the major histocompatibility complex class I peptide-loading complex.Redox-regulated export of the major histocompatibility complex class I-peptide complexes from the endoplasmic reticulumThe same major histocompatibility complex polymorphism involved in control of HIV influences peptide binding in the mouse H-2Ld system.Adapter-mediated substrate selection for endoplasmic reticulum-associated degradation.MHC class I antigen presentation: learning from viral evasion strategies.Classical and non-classical MHC I molecule manipulation by human cytomegalovirus: so many targets—but how many arrows in the quiver?Three tapasin docking sites in TAP cooperate to facilitate transporter stabilization and heterodimerization.Effect of a tapasin mutant on the assembly of the mouse MHC class I molecule H2-K(d).Comparative analysis of the impact of a free cysteine in tapasin on the maturation and surface expression of murine MHC class I allotypes.Influence of the tapasin C terminus on the assembly of MHC class I allotypes.Differential contribution of TAP and tapasin to HLA class I antigen expression.Aggregate formation by ERp57-deficient MHC class I peptide-loading complexes.Multiple residues in the transmembrane helix and connecting peptide of mouse tapasin stabilize the transporter associated with the antigen-processing TAP2 subunit.Competition for access to the rat major histocompatibility complex class I peptide-loading complex reveals optimization of peptide cargo in the absence of transporter associated with antigen processing (TAP) association.Functional dissection of the transmembrane domains of the transporter associated with antigen processing (TAP).Generation of a functional, soluble tapasin protein from an alternatively spliced mRNA.A transmembrane tail: interaction of tapasin with TAP and the MHC class I molecule.Human cytomegalovirus disrupts the major histocompatibility complex class I peptide-loading complex and inhibits tapasin gene transcription.
P2860
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P2860
Recruitment of MHC class I molecules by tapasin into the transporter associated with antigen processing-associated complex is essential for optimal peptide loading
description
2002 nî lūn-bûn
@nan
2002 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
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
name
Recruitment of MHC class I mol ...... al for optimal peptide loading
@ast
Recruitment of MHC class I mol ...... al for optimal peptide loading
@en
Recruitment of MHC class I mol ...... al for optimal peptide loading
@nl
type
label
Recruitment of MHC class I mol ...... al for optimal peptide loading
@ast
Recruitment of MHC class I mol ...... al for optimal peptide loading
@en
Recruitment of MHC class I mol ...... al for optimal peptide loading
@nl
prefLabel
Recruitment of MHC class I mol ...... al for optimal peptide loading
@ast
Recruitment of MHC class I mol ...... al for optimal peptide loading
@en
Recruitment of MHC class I mol ...... al for optimal peptide loading
@nl
P2093
P1476
Recruitment of MHC class I mol ...... al for optimal peptide loading
@en
P2093
Frank Momburg
Günter J Hämmerling
Harald Kropshofer
Nadja Bulbuc
Ofer Mandelboim
Pamela Tan
P304
P356
10.4049/JIMMUNOL.168.4.1950
P407
P577
2002-02-15T00:00:00Z