Functional dissection of the transmembrane domains of the transporter associated with antigen processing (TAP).
about
The first N-terminal transmembrane helix of each subunit of the antigenic peptide transporter TAP is essential for independent tapasin bindingIdentification of a lysosomal peptide transport system induced during dendritic cell developmentSelective and ATP-dependent translocation of peptides by the homodimeric ATP binding cassette transporter TAP-like (ABCB9)Assembly of the MHC I peptide-loading complex determined by a conserved ionic lock-switch.Viral inhibition of the transporter associated with antigen processing (TAP): a striking example of functional convergent evolutionVaricelloviruses avoid T cell recognition by UL49.5-mediated inactivation of the transporter associated with antigen processingOptimized purification of a heterodimeric ABC transporter in a highly stable form amenable to 2-D crystallizationTetrameric structure of SUR2B revealed by electron microscopy of oriented single particlesBiogenesis of functional antigenic peptide transporter TAP requires assembly of pre-existing TAP1 with newly synthesized TAP2Role of the N-terminal transmembrane domain in the endo-lysosomal targeting and function of the human ABCB6 protein.A negative feedback modulator of antigen processing evolved from a frameshift in the cowpox virus genome.Large-scale validation of methods for cytotoxic T-lymphocyte epitope prediction.Varicellovirus UL 49.5 proteins differentially affect the function of the transporter associated with antigen processing, TAP.Pathways of antigen processing.A highly conserved sequence of the viral TAP inhibitor ICP47 is required for freezing of the peptide transport cycleConformation of peptides bound to the transporter associated with antigen processing (TAP)NetCTLpan: pan-specific MHC class I pathway epitope predictionsSingle residue within the antigen translocation complex TAP controls the epitope repertoire by stabilizing a receptive conformation.An evolutionary analysis of antigen processing and presentation across different timescales reveals pervasive selection.Epstein-Barr viral BNLF2a protein hijacks the tail-anchored protein insertion machinery to block antigen processing by the transport complex TAP.Sterol transfer by ABCG5 and ABCG8: in vitro assay and reconstitution.Dynamics of major histocompatibility complex class I association with the human peptide-loading complex.Viral modulation of antigen presentation: manipulation of cellular targets in the ER and beyond.Membrane topology of human ABC proteins.Modulation of the antigen transport machinery TAP by friends and enemies.ABC transporter architecture and regulatory roles of accessory domains.Use of Functional Polymorphisms To Elucidate the Peptide Binding Site of TAP Complexes.Uptake or extrusion: crystal structures of full ABC transporters suggest a common mechanism.Structural arrangement of the transmission interface in the antigen ABC transport complex TAP.Viral proteins interfering with antigen presentation target the major histocompatibility complex class I peptide-loading complex.MHC class I assembly: out and about.The peptide-loading complex--antigen translocation and MHC class I loading.pqiABC and yebST, Putative mce Operons of Escherichia coli, Encode Transport Pathways and Contribute to Membrane Integrity.Crystal structure and mechanistic basis of a functional homolog of the antigen transporter TAP.Running the gauntlet: from peptide generation to antigen presentation by MHC class I.The TAP translocation machinery in adaptive immunity and viral escape mechanisms.Classical and non-classical MHC I molecule manipulation by human cytomegalovirus: so many targets—but how many arrows in the quiver?A dual inhibition mechanism of herpesviral ICP47 arresting a conformationally thermostable TAP complex.An annular lipid belt is essential for allosteric coupling and viral inhibition of the antigen translocation complex TAP (transporter associated with antigen processing).Single nucleotide polymorphisms in the FcγR3A and TAP1 genes impact ADCC in cynomolgus monkey PBMCs.
P2860
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P2860
Functional dissection of the transmembrane domains of the transporter associated with antigen processing (TAP).
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Functional dissection of the t ...... with antigen processing (TAP).
@en
type
label
Functional dissection of the t ...... with antigen processing (TAP).
@en
prefLabel
Functional dissection of the t ...... with antigen processing (TAP).
@en
P2093
P2860
P356
P1476
Functional dissection of the t ...... with antigen processing (TAP).
@en
P2093
Christoph Kyritsis
Joachim Koch
Renate Guntrum
Susanne Heintke
P2860
P304
10142-10147
P356
10.1074/JBC.M312816200
P407
P50
P577
2003-12-15T00:00:00Z