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Multiple interactions of the cytosolic polyproline region of the CD95 ligand: hints for the reverse signal transduction capacity of a death factor

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成果类型:
期刊论文
作者:
Wenzel, J;Sanzenbacher, R;Ghadimi, M;Lewitzky, M;Zhou, QC;...
通讯作者:
Janssen, O
作者机构:
Univ Kiel, Inst Immunol, D-24105 Kiel, Germany.
Univ Oxford, John Radcliffe Hosp, Inst Mol Med, Imperial Canc Res Fund,Cell Signalling Lab, Oxford OX3 9DU, England.
Ctr China Normal Univ, Inst Organ Synth, Wuhan 430079, Peoples R China.
Case Western Reserve Univ, Dept Pathol, Cleveland, OH 44106 USA.
[Janssen, O] Univ Kiel, Inst Immunol, Michaelisstr 5, D-24105 Kiel, Germany.
通讯机构:
[Janssen, O] U
Univ Kiel, Inst Immunol, Michaelisstr 5, D-24105 Kiel, Germany.
语种:
英文
关键词:
CD95 ligand;Signal transduction;Src homology 3 domain;WW domain;Protein–protein interaction;T lymphocyte;CD95L, CD95 ligand;CKI, casein kinase I;SH, Src homology;TCR, T cell receptor;TNF, tumor necrosis factor
期刊:
FEBS Letters
ISSN:
0014-5793
年:
2001
卷:
509
期:
2
页码:
255-262
基金类别:
We thank Philip Leder (Harvard Medical School, Boston), Daniele Rotin (University of Toronto) and Marius Sudol (Mount Sinai Medical Center, New York) for generously providing the constructs encoding the WW domains. The work is supported by grants from the Deutsche Forschungsgemeinschaft (SFB415, project A9, to O.J.) and the University of Kiel (IZKF, project B4, to O.J.). Q.Z. was supported by a fellowship from the Chinese Scholarship Council. We thank Dana Becker for expert technical assistance.
机构署名:
本校为其他机构
院系归属:
化学学院
摘要:
The CD95/Fas/Apo-1 ligand is expressed on activated lymphocytes, NK cells, platelets, certain immune-privileged cells and some tumor cells and induces apoptosis through the death receptor CD95/Fas/Apo-1. In murine T cells, membrane-bound CD95L (Fas ligand) also acts as a costimulatory receptor to coordinate activation and function in vivo. The molecular basis for this reverse signal transduction is yet unknown. In the present report, we identify individual interaction domains of enzymes and adapter molecules that selectively interact with full-...

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