Multiple residues in the transmembrane helix and connecting peptide of mouse tapasin stabilize the transporter associated with the antigen-processing TAP2 subunit.
about
Assembly of the MHC I peptide-loading complex determined by a conserved ionic lock-switch.HIV-1 protein Nef inhibits activity of ATP-binding cassette transporter A1 by targeting endoplasmic reticulum chaperone calnexinTapasin modification on the intracellular epitope HBcAg18-27 enhances HBV-specific CTL immune response and inhibits hepatitis B virus replication in vivo.Tapasin discriminates peptide-human leukocyte antigen-A*02:01 complexes formed with natural ligands.Newly discovered viral E3 ligase pK3 induces endoplasmic reticulum-associated degradation of class I major histocompatibility proteins and their membrane-bound chaperonesViral proteins interfering with antigen presentation target the major histocompatibility complex class I peptide-loading complex.Adapter-mediated substrate selection for endoplasmic reticulum-associated degradation.The peptide-loading complex--antigen translocation and MHC class I loading.The TAP translocation machinery in adaptive immunity and viral escape mechanisms.Three tapasin docking sites in TAP cooperate to facilitate transporter stabilization and heterodimerization.Influence of the tapasin C terminus on the assembly of MHC class I allotypes.A transmembrane tail: interaction of tapasin with TAP and the MHC class I molecule.Direct evidence that the N-terminal extensions of the TAP complex act as autonomous interaction scaffolds for the assembly of the MHC I peptide-loading complexA natural tapasin isoform lacking exon 3 modifies peptide loading complex function.
P2860
Q27304851-E087DCF4-AA08-4421-86FD-15471B70F819Q34355599-313A8AD4-A960-4300-BF60-8F18CED31B95Q34409291-E9360E35-48EC-4C8B-ABC2-6A44CC25E79AQ35063474-7D7C0C45-B5AC-48B6-A433-A4C50EBC2622Q35922527-B29A318E-009F-4442-B501-0FC7896884A6Q37151597-97E58DFB-D39E-49EF-9589-89FD3B939CEEQ37285218-33988969-7DB0-44C4-A3D5-B451913FB39FQ37474825-1B99F744-59EE-44A8-83F5-16C61A5EEAE5Q37941760-3AE19745-23F5-4C5A-8D08-AA70DB2F3626Q39026675-2868CB4C-78D7-47D0-874C-4C9A391EDE4DQ39923928-A438F5C6-5E52-4902-8386-4F04FDBA8D9DQ41272865-9FE92AA8-EBB7-4F5D-B99A-8052550BC939Q41853333-4E0A68FC-4862-447B-9A82-6D2A52637A56Q46799331-59BCA3EE-9498-402F-AAB0-1EC602F6757B
P2860
Multiple residues in the transmembrane helix and connecting peptide of mouse tapasin stabilize the transporter associated with the antigen-processing TAP2 subunit.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Multiple residues in the trans ...... tigen-processing TAP2 subunit.
@en
type
label
Multiple residues in the trans ...... tigen-processing TAP2 subunit.
@en
prefLabel
Multiple residues in the trans ...... tigen-processing TAP2 subunit.
@en
P2860
P356
P1476
Multiple residues in the trans ...... tigen-processing TAP2 subunit.
@en
P2093
Frank Momburg
Martina Papadopoulos
P2860
P304
P356
10.1074/JBC.M610429200
P407
P577
2007-01-23T00:00:00Z