TAPBPR bridges UDP-glucose:glycoprotein glucosyltransferase 1 onto MHC class I to provide quality control in the antigen presentation pathway.
about
Editing peptide presentation to T cells.Structure of the TAPBPR-MHC I complex defines the mechanism of peptide loading and editing.Crystal structure of a TAPBPR-MHC I complex reveals the mechanism of peptide editing in antigen presentation.Interdomain conformational flexibility underpins the activity of UGGT, the eukaryotic glycoprotein secretion checkpoint.Whole genome duplications have provided teleosts with many roads to peptide loaded MHC class I molecules.The Role of Molecular Flexibility in Antigen Presentation and T Cell Receptor-Mediated Signaling
P2860
TAPBPR bridges UDP-glucose:glycoprotein glucosyltransferase 1 onto MHC class I to provide quality control in the antigen presentation pathway.
description
2017 nî lūn-bûn
@nan
2017 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2017 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2017年の論文
@ja
2017年論文
@yue
2017年論文
@zh-hant
2017年論文
@zh-hk
2017年論文
@zh-mo
2017年論文
@zh-tw
2017年论文
@wuu
name
TAPBPR bridges UDP-glucose:gly ...... antigen presentation pathway.
@ast
TAPBPR bridges UDP-glucose:gly ...... antigen presentation pathway.
@en
type
label
TAPBPR bridges UDP-glucose:gly ...... antigen presentation pathway.
@ast
TAPBPR bridges UDP-glucose:gly ...... antigen presentation pathway.
@en
prefLabel
TAPBPR bridges UDP-glucose:gly ...... antigen presentation pathway.
@ast
TAPBPR bridges UDP-glucose:gly ...... antigen presentation pathway.
@en
P2093
P2860
P50
P356
P1433
P1476
TAPBPR bridges UDP-glucose:gly ...... antigen presentation pathway.
@en
P2093
Andreas Neerincx
Clemens Hermann
Nico Trautwein
Robin Antrobus
Stefan Stevanović
P2860
P356
10.7554/ELIFE.23049
P407
P577
2017-04-20T00:00:00Z