Codification of bidentate pMHC interaction with TCR and its co-receptor.

about

Avidity characterization of genetically engineered T-cells with novel and established approaches.Public T cell receptors confer high-avidity CD4 responses to HIV controllers αβ T Cell Receptor Mechanosensing Forces out Serial Engagement

P2860

Q36076472-0722A974-2E20-4F21-ABA7-97B88190F086 Q36951735-C1A12E47-0F0D-457F-8940-D437ED3767C9 Q56884990-D94CF932-0DC1-4B86-BA87-76604B688552

P2860

Codification of bidentate pMHC interaction with TCR and its co-receptor.

Item

http://www.wikidata.org/entity/Q38394531

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

2015年论文

@zh

2015年论文

@zh-cn

name

Codification of bidentate pMHC interaction with TCR and its co-receptor.

@en

type

Item

label

Codification of bidentate pMHC interaction with TCR and its co-receptor.

@en

prefLabel

Codification of bidentate pMHC interaction with TCR and its co-receptor.

@en

P1476

Codification of bidentate pMHC interaction with TCR and its co-receptor.

@en

P2093

Ellis L Reinherz

http://www.w3.org/2001/XMLSchema#string

Jia-huai Wang

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal structure of the human CD4 N-terminal two-domain fragment complexed to a class II MHC molecule

Force generation upon T cell receptor engagement

The crystal structure of a TL/CD8alphaalpha complex at 2.1 A resolution: implications for modulation of T cell activation and memory

A zinc clasp structure tethers Lck to T cell coreceptors CD4 and CD8

Structural Basis of the CD8 /MHC Class I Interaction: Focused Recognition Orients CD8 to a T Cell Proximal Position

Crystal structure of a complete ternary complex of T-cell receptor, peptide-MHC, and CD4

Crystal structure of the complex between human CD8alpha(alpha) and HLA-A2

Differential thymic selection outcomes stimulated by focal structural alteration in peptide/major histocompatibility complex ligands

Structural basis of CD8 coreceptor function revealed by crystallographic analysis of a murine CD8alphaalpha ectodomain fragment in complex with H-2Kb

αβ T cell receptors that do not undergo major histocompatibility complex-specific thymic selection possess antibody-like recognition specificities

P304

300-306

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1016/J.IT.2015.03.004

http://www.w3.org/2001/XMLSchema#string

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P577

2015-03-26T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

25818864

http://www.w3.org/2001/XMLSchema#string

P932

4420642

http://www.w3.org/2001/XMLSchema#string

Codification of bidentate pMHC interaction with TCR and its co-receptor.

about

P2860

P2860

Codification of bidentate pMHC interaction with TCR and its co-receptor.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P932