Structural and biochemical basis of apoptotic activation by Smac/DIABLO
Article Abstract:
Research is presented concerning the programmed cell death which is carried out by caspases and which is a vital process in the homeostasis and development of metazoans. The influence of mitochondrial proteins is discussed.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis
Article Abstract:
Research is presented concerning the interaction which occurs between the active caspase-9-Apaf-1 holoenzyme complex and the X-linked inhibitor-of-apoptosis protein through binding to the amino terminus of the linker peptide.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2001
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Structure of the CED-4-CED-9 complex provides insights into programmed cell death Caenorhabditis elegans
Article Abstract:
The crystal structure of the CED-4-CED-9 complex at 2.6 Angstrom resolution, and a complete reconstitution of the CED-3 activation pathway using homogeneous proteins of CED-4, CED-9 and EGL-1 are reported. EGL-binding induces pronounced conformational changes in CED-9 that results in the dissociation of the CED-4 dimer from CED-9.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
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