I-Ag7 is subject to post-translational chaperoning by CLIP. - Wikidata - wikimedia - TriplyDB

I-Ag7 is subject to post-translational chaperoning by CLIP.

I-Ag7 is subject to post-translational chaperoning by CLIP.

http://www.wikidata.org/entity/Q34013568

about

γδ T cells recognize the insulin B:9-23 peptide antigen when it is dimerized through thiol oxidation.On the perils of poor editing: regulation of peptide loading by HLA-DQ and H2-A molecules associated with celiac disease and type 1 diabetes.Immunological Basis for Rapid Progression of Diabetes in Older NOD Mouse Recipients Post BM-HSC Transplantation Accelerated turnover of MHC class II molecules in nonobese diabetic mice is developmentally and environmentally regulated in vivo and dispensable for autoimmunity.MHC Class II Protein Turnover In vivo and Its Relevance for Autoimmunity in Non-Obese Diabetic Mice.Transgene expression in various organs post BM-HSC transplantation.Comparison of transduction efficiency among various lentiviruses containing GFP reporter in bone marrow hematopoietic stem cell transplantation.An insertion mutant in DQA1*0501 restores susceptibility to HLA-DM: implications for disease associations.

P2860

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P2860

I-Ag7 is subject to post-translational chaperoning by CLIP.

http://www.wikidata.org/entity/Q34013568

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

I-Ag7 is subject to post-translational chaperoning by CLIP.

@ast

I-Ag7 is subject to post-translational chaperoning by CLIP.

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I-Ag7 is subject to post-translational chaperoning by CLIP.

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type

label

I-Ag7 is subject to post-translational chaperoning by CLIP.

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I-Ag7 is subject to post-translational chaperoning by CLIP.

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I-Ag7 is subject to post-translational chaperoning by CLIP.

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prefLabel

I-Ag7 is subject to post-translational chaperoning by CLIP.

@ast

I-Ag7 is subject to post-translational chaperoning by CLIP.

@en

I-Ag7 is subject to post-translational chaperoning by CLIP.

@nl

P1433

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P2860

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P1433

International Immunology

P1476

I-Ag7 is subject to post-translational chaperoning by CLIP

@en

P2093

Cornelia H Rinderknecht

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

Elizabeth D Mellins

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

Nan Wang

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

Ning Lu

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

Oliver Crespo

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

Phi Truong

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

Tieying Hou

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

P2860

Binding domain regulation of MHC class II molecule assembly, trafficking, fate, and function

Achieving stability through editing and chaperoning: regulation of MHC class II peptide binding and expression

HLA-DM acts as a molecular chaperone and rescues empty HLA-DR molecules at lysosomal pH

Identification of MHC class II-restricted peptide ligands, including a glutamic acid decarboxylase 65 sequence, that stimulate diabetogenic T cells from transgenic BDC2.5 nonobese diabetic mice.

The I-Ag7 MHC class II molecule linked to murine diabetes is a promiscuous peptide binder.

Determination of the HLA-DM interaction site on HLA-DR molecules.

Natural peptides selected by diabetogenic DQ8 and murine I-A(g7) molecules show common sequence specificity.

Prevention of diabetes in nonobese diabetic mice by anti-I-A monoclonal antibodies: transfer of protection by splenic T cells

Nonclassical MHC class II molecules.

Complexes of two cohorts of CLIP peptides and HLA-DQ2 of the autoimmune DR3-DQ2 haplotype are poor substrates for HLA-DM

P304

705-716

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

P31

scholarly article

P356

10.1093/INTIMM/DXQ056

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

P433

8

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

P478

22

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

P50

Narendiran Rajasekaran

P577

2010-06-13T00:00:00Z

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

P5875

44672730

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

P698

20547545

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

P921

molecular chaperones

P932

2908477

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