MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains.
about
ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly.Two polymorphisms facilitate differences in plasticity between two chicken major histocompatibility complex class I proteinsThe N-terminal region of tapasin is required to stabilize the MHC class I loading complexTapasin enhances assembly of transporters associated with antigen processing-dependent and -independent peptides with HLA-A2 and HLA-B27 expressed in insect cells.Human pathogen subversion of antigen presentation.Calreticulin: one protein, one gene, many functions.An endoplasmic reticulum-targeting signal sequence enhances the immunogenicity of an immunorecessive simian virus 40 large T antigen cytotoxic T-lymphocyte epitope.Intrasequence GFP in class I MHC molecules, a rigid probe for fluorescence anisotropy measurements of the membrane environment.HIV-1 protein Nef inhibits activity of ATP-binding cassette transporter A1 by targeting endoplasmic reticulum chaperone calnexinMajor histocompatibility complex class I-restricted antigen processing and presentation.Tapasin and other chaperones: models of the MHC class I loading complex.Direct delivery of exogenous MHC class I molecule-binding oligopeptides to the endoplasmic reticulum of viable cellsTwo novel routes of transporter associated with antigen processing (TAP)-independent major histocompatibility complex class I antigen processing.Physical and functional association of the major histocompatibility complex class I heavy chain alpha3 domain with the transporter associated with antigen processing.Generation of CD8+ T cells specific for transporter associated with antigen processing deficient cells.TAPBPR: a new player in the MHC class I presentation pathway.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.Mutant MHC class I molecules define interactions between components of the peptide-loading complex.Retention of empty MHC class I molecules by tapasin is essential to reconstitute antigen presentation in invertebrate cellsA transmembrane tail: interaction of tapasin with TAP and the MHC class I molecule.Alloreactivity, antigen recognition and T-cell selection: three diverse T-cell recognition problems with a common solution.In vitro reconstitution of the MHC class I peptide-loading complex.HLA-B polymorphism affects interactions with multiple endoplasmic reticulum proteins.Direct evidence for conformational dynamics in major histocompatibility complex class I molecules.A soluble major histocompatibility complex class I peptide-binding platform undergoes a conformational change in response to peptide epitopes.Stoichiometric tapasin interactions in the catalysis of major histocompatibility complex class I molecule assembly.
P2860
Q24533211-EBD5E4A8-B582-4BFB-8F33-3D965076957CQ27320198-758A2CDE-4F47-4104-A734-2D68079DEB6CQ28138178-8B86A142-C731-496D-AA66-BC755DA131D0Q33179056-6A8F215B-FA25-4016-AF53-E0C3D21B27D2Q33683402-CBCF6253-70D4-420C-AF71-2B190B7A0DD8Q33776572-17FFDC20-1BE0-403D-915B-803590DB7038Q34069951-6AD2F35F-A26B-42BA-925E-D5140D01828BQ34181563-7D803A04-2599-4E17-9D98-2A90578C63D8Q34355599-7267A1AB-6E3D-49BB-A426-080703882E56Q34941852-AE027646-ADD5-4227-9CD5-9DE8034F818FQ35922740-297ECE0D-1AF5-446D-B9DD-2A60DB850470Q36301001-60A626A1-30DC-4297-A126-EE30E54A5439Q36380657-61C518BD-3AD3-42D3-B98F-D1913312B16EQ36400499-0DBDAFFE-5538-4430-AACB-8D20A853341BQ36599550-AD9B2C43-9AAE-485B-AC7F-9A2E69C18B60Q38365574-65B36F61-0ED9-473A-AF67-904FCCFCA257Q40703743-F6D21C25-D007-4254-A8C2-67FC0544297EQ40740036-C953CAA0-DF84-4A36-BCBA-EF3E3D347260Q40976401-4D11D24D-D1D6-4941-92D7-DBA77CA76932Q41272865-CA499F71-18E2-4234-9B41-7EA722DF7A85Q41349742-3247EFB4-1CD0-48FE-BC51-19AC87E824F1Q42009953-8A9E9245-68CE-4F86-A0E9-1B12375F175FQ42637101-DB376AF2-8E50-444E-8305-9C0720E2E6B4Q47140871-2E6DB579-0641-4694-BFFF-AAA61B76A79BQ48034751-D257AED1-6B98-4666-B016-4015627EC0D2Q53626336-44CC93AA-86D5-4308-A7C3-0D27EA655DFD
P2860
MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
MHC class I molecules form ter ...... a their extracellular domains.
@ast
MHC class I molecules form ter ...... a their extracellular domains.
@en
type
label
MHC class I molecules form ter ...... a their extracellular domains.
@ast
MHC class I molecules form ter ...... a their extracellular domains.
@en
prefLabel
MHC class I molecules form ter ...... a their extracellular domains.
@ast
MHC class I molecules form ter ...... a their extracellular domains.
@en
P2093
P2860
P356
P1476
MHC class I molecules form ter ...... a their extracellular domains.
@en
P2093
D B Williams
E K Mitchell
G L Waneck
P A Peterson
P2860
P304
P356
10.1084/JEM.184.2.337
P407
P577
1996-08-01T00:00:00Z