Understanding the obstacle of incompatibility at residue 156 within HLA-B*35 subtypes.

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Polymorphism at residue 156 of the new HLA-A*02:683 allele suggests immunological relevance.The polymorphism at residue 156 determines the HLA-B*35 restricted peptide repertoire during HCMV infection

P2860

Q48361316-85687625-C7A0-442B-98B7-E3A00B858E17 Q58724946-DBB6A4BA-5CD8-45D6-9645-9F593E6B2E81

P2860

Understanding the obstacle of incompatibility at residue 156 within HLA-B*35 subtypes.

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http://www.wikidata.org/entity/Q38804389

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2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

Understanding the obstacle of incompatibility at residue 156 within HLA-B*35 subtypes.

@en

type

Item

label

Understanding the obstacle of incompatibility at residue 156 within HLA-B*35 subtypes.

@en

prefLabel

Understanding the obstacle of incompatibility at residue 156 within HLA-B*35 subtypes.

@en

P1476

Understanding the obstacle of incompatibility at residue 156 within HLA-B*35 subtypes.

@en

P2093

Alexander A Celik

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

Christina Bade-Doeding

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

Heike Kunze-Schumacher

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

Rainer Blasczyk

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

Trevor Huyton

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

Trishna Manandhar

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

P2860

Tapasin interacts with the membrane-spanning domains of both TAP subunits and enhances the structural stability of TAP1 x TAP2 Complexes

A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes

Allele-specific differences in the interaction of MHC class I molecules with transporters associated with antigen processing

A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule

Impact of clonal competition for peptide-MHC complexes on the CD8+ T-cell repertoire selection in a persistent viral infection

A Molecular Basis for the Interplay between T Cells, Viral Mutants, and Human Leukocyte Antigen Micropolymorphism

Optimization of the MHC class I peptide cargo is dependent on tapasin

The interface between tapasin and MHC class I: identification of amino acid residues in both proteins that influence their interaction

Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP

P2888

s00251-015-0896-4

P304

247-260

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

P31

scholarly article

P356

10.1007/S00251-015-0896-4

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

P407

English

P433

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

P478

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

P50

Christina Bade-Döding

Heike Kunze-Schumacher

P577

2016-01-12T00:00:00Z

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

P5875

290432402

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

P6179

1052425589

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P698

26758079

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

P932

4799800

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

Understanding the obstacle of incompatibility at residue 156 within HLA-B*35 subtypes.

about

P2860

P2860

Understanding the obstacle of incompatibility at residue 156 within HLA-B*35 subtypes.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P6179

P698

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P6179

P698

P932