Evidence that transporters associated with antigen processing translocate a major histocompatibility complex class I-binding peptide into the endoplasmic reticulum in an ATP-dependent manner
about
Identification of sequences in the human peptide transporter subunit TAP1 required for transporter associated with antigen processing (TAP) functionStructure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processingCloning and functional characterization of a subunit of the transporter associated with antigen processingAssembly, intracellular localization, and nucleotide binding properties of the human peptide transporters TAP1 and TAP2 expressed by recombinant vaccinia virusesMolecular mechanism and species specificity of TAP inhibition by herpes simplex virus ICP47Using the TAP component of the antigen-processing machinery as a molecular adjuvantHuman transporters associated with antigen processing (TAPs) select epitope precursor peptides for processing in the endoplasmic reticulum and presentation to T cellsWhat is the role of alternate splicing in antigen presentation by major histocompatibility complex class I molecules?Varicelloviruses avoid T cell recognition by UL49.5-mediated inactivation of the transporter associated with antigen processingThe N-terminal region of tapasin is required to stabilize the MHC class I loading complexThe transporter associated with antigen processing: function and implications in human diseasesFunctional asymmetry of the ATP-binding-cassettes of the ABC transporter TAP is determined by intrinsic properties of the nucleotide binding domainsCalnexin influences folding of human class I histocompatibility proteins but not their assembly with beta 2-microglobulinIdentification of an alternate splice form of tapasin in human melanoma.IFN-beta mediates coordinate expression of antigen-processing genes in RSV-infected pulmonary epithelial cells.Human cytomegalovirus UL18 utilizes US6 for evading the NK and T-cell responsesAn endoplasmic reticulum-targeting signal sequence enhances the immunogenicity of an immunorecessive simian virus 40 large T antigen cytotoxic T-lymphocyte epitope.The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a "molecular ruler" mechanism.Alternative Ii-independent antigen-processing pathway in leukemic blasts involves TAP-dependent peptide loading of HLA class II complexes.Intracellular surveillance: controlling the assembly of MHC class I-peptide complexes.Variability in immune response to pathogens: using measles vaccine to probe immunogenetic determinants of responseA vitellogenic-like carboxypeptidase expressed by human macrophages is localized in endoplasmic reticulum and membrane ruffles.Getting the inside out: the transporter associated with antigen processing (TAP) and the presentation of viral antigenAllosteric crosstalk between peptide-binding, transport, and ATP hydrolysis of the ABC transporter TAPA subset of HLA-B27 molecules contains peptides much longer than nonamers.Characterization of an incompletely assembled major histocompatibility class I molecule (H-2Kb) associated with unusually long peptides: implications for antigen processing and presentation.Automated benchmarking of peptide-MHC class I binding predictions.Stable binding of the herpes simplex virus ICP47 protein to the peptide binding site of TAPInduction of transporter associated with antigen processing by interferon gamma confers endothelial cell cytoprotection against natural killer-mediated lysisTapasin and other chaperones: models of the MHC class I loading complex.Characteristics of peptide and major histocompatibility complex class I/beta 2-microglobulin binding to the transporters associated with antigen processing (TAP1 and TAP2)Transporters from H-2b, H-2d, H-2s, H-2k, and H-2g7 (NOD/Lt) haplotype translocate similar sets of peptides.Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome.Misfolded major histocompatibility complex class I molecules accumulate in an expanded ER-Golgi intermediate compartmentThe human cytomegalovirus US6 glycoprotein inhibits transporter associated with antigen processing-dependent peptide translocation.Use of chimeric proteins to investigate the role of transporter associated with antigen processing (TAP) structural domains in peptide binding and translocation.Distinct functions and cooperative interaction of the subunits of the transporter associated with antigen processing (TAP).Modulation of the antigen transport machinery TAP by friends and enemies.T cell recognition of an HLA-A2-restricted epitope derived from a cleaved signal sequence.The peptide-binding motif for the human transporter associated with antigen processing
P2860
Q24290672-E37CF57A-A07F-4AF8-919B-930B05CF7236Q24291633-B4115608-911A-4346-AB83-85C23ED0827AQ24319850-E3BAB248-A2FF-4FE5-AF62-CF5FB0816ACAQ24337428-F0B612A4-3674-4B18-92FF-710A3E63194FQ24562414-5A561354-3E4F-4A0A-926B-7B761F324776Q25256237-F8631E36-C6DE-4D30-943B-B92BA6D84C61Q27485141-B4EAB1C1-B526-488B-84E8-BA9D29B812A9Q27491004-0EEF948B-BA78-44F1-9CEE-8B2077BFF77BQ28115772-884717C7-DD27-45C0-80EE-A63283009FFDQ28138178-DEE92BFB-CBC9-4391-868A-FA58737160E3Q28214433-E8525D7F-7D84-4373-AF28-BB954C3A1F18Q28214964-A02E8093-1978-4931-B196-C458E10C9826Q28609739-BC3368E7-ACF5-42DE-A02F-AED1E753AFA3Q30156803-515A5217-1AEC-44DC-8EAF-9EC7E9B33CE9Q31834062-87BA38A8-3CDD-405C-BEA4-ABCF778878C9Q33358676-85AB1291-406D-4397-9512-4ED1208CA052Q34069951-9C6F7966-D2DD-401E-8185-F037BB0E77BCQ34144506-42E975C2-9EE7-4124-9574-63C97344B462Q34155000-FA878C36-6C4D-47B3-967E-8F7505ED85F0Q34156622-8C18C943-1DDC-4378-A366-12729B44E3C8Q34384582-1FCA16BF-F8EB-433F-8566-1499A6BD567CQ34488006-C019A09B-C737-4C30-9C1B-828FC5A90CBCQ34754320-031F4318-029C-4522-AB75-35D49B57E201Q35037580-E4EBD262-62B6-48B8-95CE-13026C920B33Q35056650-366A9A68-881F-4CD4-88E4-1431025652FEQ35217978-4B774EAF-D209-42B7-B831-9A87F089079CQ35785418-7C48A601-181C-480D-AF9D-CF3F79FE0CCEQ35899978-0705B595-F9BE-4663-9059-F2ED3CAA7A56Q35919640-A5C7C5D6-8035-453F-90A4-F251B63D7594Q35922740-21AB7032-35CD-41C6-B4C3-7C35C0176400Q35999694-D55CFEEA-2F03-44C3-BFC6-5D6A60304F05Q36017645-1F72F410-0702-4EDF-8736-DDA3F945FDCBQ36027129-EE6FE6EE-072F-4F40-AFB0-D3E79C21EEE5Q36236255-34CD3C99-D460-4091-9E4C-5ABE95513271Q36242361-273CE6A8-4FA9-496D-9198-7E06FD46127AQ36300510-74DBA485-E4DD-4464-AC86-71409CF7A368Q36309663-F4DF3797-B536-4985-AFD7-42104942EF1AQ36344381-32A293DB-C807-4283-8C3B-7DDDCEEB5038Q36364011-7971280A-79F1-43BD-86BA-9EEB1C737D4EQ36365611-3CCC51A0-5A87-459D-9A09-49C19742D9AA
P2860
Evidence that transporters associated with antigen processing translocate a major histocompatibility complex class I-binding peptide into the endoplasmic reticulum in an ATP-dependent manner
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Evidence that transporters ass ...... lum in an ATP-dependent manner
@ast
Evidence that transporters ass ...... lum in an ATP-dependent manner
@en
type
label
Evidence that transporters ass ...... lum in an ATP-dependent manner
@ast
Evidence that transporters ass ...... lum in an ATP-dependent manner
@en
prefLabel
Evidence that transporters ass ...... lum in an ATP-dependent manner
@ast
Evidence that transporters ass ...... lum in an ATP-dependent manner
@en
P2093
P2860
P356
P1476
Evidence that transporters ass ...... lum in an ATP-dependent manner
@en
P2093
Anderson KS
Androlewicz MJ
Cresswell P
P2860
P304
P356
10.1073/PNAS.90.19.9130
P407
P577
1993-10-01T00:00:00Z