Characterization of two receptors for TRAIL.

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1997

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info:eu-repo/semantics/altIdentifier/doi/10.1016/S0014-5793(97)01231-3

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info:eu-repo/semantics/altIdentifier/pmid/9373179

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info:eu-repo/semantics/altIdentifier/pissn/0014-5793

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info:eu-repo/semantics/altIdentifier/urn/urn:nbn:ch:serval-BIB_25D695CC2FFE9

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P. Schneider et al., « Characterization of two receptors for TRAIL. », Serveur académique Lausannois, ID : 10.1016/S0014-5793(97


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Two receptors for TRAIL, designated TRAIL-R2 and TRAIL-R3, have been identified. Both are members of the tumor necrosis factor receptor family. TRAIL-R2 is structurally similar to the death-domain-containing receptor TRAIL-R1 (DR-4), and is capable of inducing apoptosis. In contrast, TRAIL-R3 does not promote cell death. TRAIL-R3 is highly glycosylated and is membrane bound via a putative phosphatidylinositol anchor. The extended structure of TRAIL-R3 is due to the presence of multiple threonine-, alanine-, proline- and glutamine-rich repeats (TAPE repeats). TRAIL-R2 shows a broad tissue distribution, whereas the expression of TRAIL-R3 is restricted to peripheral blood lymphocytes (PBLs) and skeletal muscle. All three TRAIL receptors bind TRAIL with similar affinity, suggesting a complex regulation of TRAIL-mediated signals.

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