The generation of SDS-stable HLA DR dimers is independent of efficinet peptide binding
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概要
著者
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Koning Frits
Department Of Immunohematology And Blood Transfusion Leiden University Medical Center
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Vermeulen Corine
Department Of Immunohaematology And Blood Bank Leiden University Medical Center University Medical C
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Vermeulen Corine
Departments Of Immunohaematology And Bloodband University Hospital Ledden
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VERRECK Frank
Departments of Immunohaematology and Bloodband, University Hospital Ledden
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POEL Anja
Departments of Immunohaematology and Bloodband, University Hospital Ledden
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JORITSMA Patricia
Departments of Immunohaematology and Bloodband, University Hospital Ledden
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AMONS Reinout
Departments of Medical Biochemistry, Sylvius Laboratories, Wassenaarseweg
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COLIGAN John
Labortory of Molecular Structure, National Institute of Allergy and Infectius Diseases, NIH
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DRIJIFHOUT Wouter
Departments of Immunohaematology and Bloodband, University Hospital Ledden
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Poel Anja
Departments Of Immunohaematology And Bloodband University Hospital Ledden
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Coligan John
Labortory Of Molecular Structure National Institute Of Allergy And Infectius Diseases Nih
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Coligan John
Laboratory Of Molecular Structure Niaid Nci
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Verreck Frank
Departments Of Immunohaematology And Bloodband University Hospital Ledden
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Amons Reinout
Department Of Immunohaematology And Blood Bank Leiden University Medical Center University Medical C
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Amons Reinout
Departments Of Medical Biochemistry Sylvius Laboratories Wassenaarseweg
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Joritsma Patricia
Departments Of Immunohaematology And Bloodband University Hospital Ledden
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Drijifhout Wouter
Departments Of Immunohaematology And Bloodband University Hospital Ledden
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Koning Frits
Department Of Immunohaematology And Blood Bank Leiden University Medical Center University Medical C
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Koning Frits
Departments Of Immunohaematology And Bloodband University Hospital Ledden
関連論文
- The generation of SDS-stable HLA DR dimers is independent of efficinet peptide binding
- Definition of agonists and design of antagonists ofr alloreactive T cell clones using synthetic peptide libraries
- Human dendritic cells shed a functional, soluble form of the mannose receptor
- Strongly increased efficiency of altered peptide ligands by mannosylation
- Immunization with mannosylated peptide induces poor T cell effector functions despite enhanced antigen presentation
- Molecular analysis of presentation by HLA-A2.1 of a promiscuously binding V3 loop peptide from the HIV-1 envelope protein to human cytotoxic T lymphocytes