Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain-swapped dimer that binds a highly selective subset of BH3-containing death ligands-Reference-Cited by-同舟云学术

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Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain-swapped dimer that binds a highly selective subset of BH3-containing death ligands

Published:2008-06-13 Issue:10 Volume:15 Page:1564-1571
ISSN:1350-9047
Container-title:Cell Death & Differentiation
language:en
Short-container-title:Cell Death Differ

Author:

Kvansakul M,Yang H,Fairlie W D,Czabotar P E,Fischer S F,Perugini M A,Huang D C S,Colman P M

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology

Link

http://www.nature.com/articles/cdd200883.pdf

Reference40 articles.

1. Cuconati A, White E . Viral homologs of BCL-2: role of apoptosis in the regulation of virus infection. Genes Dev 2002; 16: 2465–2478.

2. Adams JM, Cory S . The Bcl-2 apoptotic switch in cancer development and therapy. Oncogene 2007; 26: 1324–1337.

3. Youle RJ, Strasser A . The BCL-2 protein family: opposing activities that mediate cell death. Nat Rev Cell Biol 2008; 9: 47–59.

4. Sattler M, Liang H, Nettesheim D, Meadows RP, Harlan JE, Eberstadt M et al. Structure of Bcl-xL–Bak peptide complex: recognition between regulators of apoptosis. Science 1997; 275: 983–986.

5. Liu X, Dai S, Zhu Y, Marrack P, Kappler JW . The structure of a Bcl-xL/Bim fragment complex: implications for Bim function. Immunity 2003; 19: 341–352.

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