Proofreading of Peptide-MHC Complexes through Dynamic Multivalent Interactions.
about
Partial Dissociation of Truncated Peptides Influences the Structural Dynamics of the MHCI Binding GrooveDirect evidence for conformational dynamics in major histocompatibility complex class I molecules.Structure of the human MHC-I peptide-loading complex.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.Exploiting non-canonical translation to identify new targets for T cell-based cancer immunotherapy.
P2860
Proofreading of Peptide-MHC Complexes through Dynamic Multivalent Interactions.
description
2017 nî lūn-bûn
@nan
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
2017年论文
@zh
2017年论文
@zh-cn
name
Proofreading of Peptide-MHC Complexes through Dynamic Multivalent Interactions.
@en
Proofreading of Peptide-MHC Complexes through Dynamic Multivalent Interactions.
@nl
type
label
Proofreading of Peptide-MHC Complexes through Dynamic Multivalent Interactions.
@en
Proofreading of Peptide-MHC Complexes through Dynamic Multivalent Interactions.
@nl
prefLabel
Proofreading of Peptide-MHC Complexes through Dynamic Multivalent Interactions.
@en
Proofreading of Peptide-MHC Complexes through Dynamic Multivalent Interactions.
@nl
P2860
P356
P1476
Proofreading of Peptide-MHC Complexes through Dynamic Multivalent Interactions.
@en
P2860
P356
10.3389/FIMMU.2017.00065
P577
2017-02-08T00:00:00Z