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Title:
Structure of CD26 (Dipeptidyl Peptidase IV) and Function in Human T Cell Activation | SpringerLink
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1996 was the 10th anniversary of the establishment of the cluster of differentiation antigen, CD26 by the Second Workshop and Conference on Human Leukocyte Differentiation Antigens1. First described as a T cell activation antigen, CD26 was found to he strongly...
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solid-phase immobilized anti-1f7 anti-if7 monoclonal antibody month download article/chapter mouse thymocyte-activating molecule mitogen-activated protein kinase hiv infection 8 membrane-anchoring domain proline-dependent structural dipeptidyl peptidase iv privacy choices/manage cookies terminal signal sequence dipetidyl peptidase iv antigen-specific cd4+ device instant download leukocyte typing iv receptor-mediated uptake chapter cellular peptidases martin luther university von dem borne leukocyte typing ii protein tyrosine kinases protein tyrosine phosphatases antigen rective memory cell activation antigen european economic area subsequent work showed severe combined immunodeficiency neo-plastic progression distinct epitopes recognized fcr-mediated crosslinking key costimulatory molecule surface protease involved download preview pdf conditions privacy policy diseases martin hegen cell surface ectopeptidase cell surface modulation harvard medical school oxford university press rui-ping dong activated nk cells mononuclear blood cells cells arc defined accepting optional cookies journal finder publish check access human lupus nephritis tcr-cd3 complex ethics access chikao morimotoย &ย stuart
Schema {๐บ๏ธ}
ScholarlyArticle:
headline:Structure of CD26 (Dipeptidyl Peptidase IV) and Function in Human T Cell Activation
pageEnd:116
pageStart:109
image:https://media.springernature.com/w153/springer-static/cover/book/978-1-4757-9613-1.jpg
genre:
Biomedical and Life Sciences
Biomedical and Life Sciences (R0)
isPartOf:
name:Cellular Peptidases in Immune Functions and Diseases
isbn:
978-1-4757-9613-1
978-1-4757-9615-5
type:Book
publisher:
name:Springer US
logo:
url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
type:ImageObject
type:Organization
author:
name:Martin Hegen
affiliation:
name:Harvard Medical School
address:
name:Division of Tumor Immunology Dana-Farber Cancer Institute and Department of Medicine, Harvard Medical School, Boston, USA
type:PostalAddress
type:Organization
type:Person
name:Junichi Kameoka
affiliation:
name:Harvard Medical School
address:
name:Division of Tumor Immunology Dana-Farber Cancer Institute and Department of Medicine, Harvard Medical School, Boston, USA
type:PostalAddress
type:Organization
type:Person
name:Rui-Ping Dong
affiliation:
name:Harvard Medical School
address:
name:Division of Tumor Immunology Dana-Farber Cancer Institute and Department of Medicine, Harvard Medical School, Boston, USA
type:PostalAddress
type:Organization
type:Person
name:Chikao Morimoto
affiliation:
name:Harvard Medical School
address:
name:Division of Tumor Immunology Dana-Farber Cancer Institute and Department of Medicine, Harvard Medical School, Boston, USA
type:PostalAddress
type:Organization
type:Person
name:Stuart F. Schlossman
affiliation:
name:Harvard Medical School
address:
name:Division of Tumor Immunology Dana-Farber Cancer Institute and Department of Medicine, Harvard Medical School, Boston, USA
type:PostalAddress
type:Organization
type:Person
keywords:Tyrosine Phosphorylation, Adenosine Deaminase, Dipeptidyl Peptidase, Severe Combine Immunodeficiency Disease, Induce Tyrosine Phosphorylation
description:1996 was the 10th anniversary of the establishment of the cluster of differentiation antigen, CD26 by the Second Workshop and Conference on Human Leukocyte Differentiation Antigens1. First described as a T cell activation antigen, CD26 was found to he strongly expressed on subsets of both activated CD4 and CD8 T cells2. Subsequent work showed the expression of CD26 on activated Nk cells, B cells and B cell lines and demonstrated CD26 expression on a variety of different cell types, most abundantly on epithelia of the intestine, prostate and the proximal tubuli of the kidneys3,4,5. Furthermore, it was demonstrated that CD26 possesses enzymatic activity, dipeptidyl peptidase IV (DPP IV; EC 3.4.14.5), in its extracellular domain4 and is identical to the previously described adenosine deaminase (ADA, EC 3.5.4.4) binding protein6,7. Recent studies indicate that CD26 plays a seminal role in T cell costimulation and may be involved in severe combined immunodeficiency and HIV infection 8,9.
datePublished:1997
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name:Harvard Medical School
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name:Division of Tumor Immunology Dana-Farber Cancer Institute and Department of Medicine, Harvard Medical School, Boston, USA
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name:Harvard Medical School
address:
name:Division of Tumor Immunology Dana-Farber Cancer Institute and Department of Medicine, Harvard Medical School, Boston, USA
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name:Harvard Medical School
address:
name:Division of Tumor Immunology Dana-Farber Cancer Institute and Department of Medicine, Harvard Medical School, Boston, USA
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name:Division of Tumor Immunology Dana-Farber Cancer Institute and Department of Medicine, Harvard Medical School, Boston, USA
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name:Harvard Medical School
address:
name:Division of Tumor Immunology Dana-Farber Cancer Institute and Department of Medicine, Harvard Medical School, Boston, USA
type:PostalAddress
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name:Junichi Kameoka
affiliation:
name:Harvard Medical School
address:
name:Division of Tumor Immunology Dana-Farber Cancer Institute and Department of Medicine, Harvard Medical School, Boston, USA
type:PostalAddress
type:Organization
name:Rui-Ping Dong
affiliation:
name:Harvard Medical School
address:
name:Division of Tumor Immunology Dana-Farber Cancer Institute and Department of Medicine, Harvard Medical School, Boston, USA
type:PostalAddress
type:Organization
name:Chikao Morimoto
affiliation:
name:Harvard Medical School
address:
name:Division of Tumor Immunology Dana-Farber Cancer Institute and Department of Medicine, Harvard Medical School, Boston, USA
type:PostalAddress
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name:Stuart F. Schlossman
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