Structural and biochemical basis of apoptotic activation by Smac/DIABLO
By J. Chai, Chunying Du, Jia-Wei Wu, S. Kyin, Xiaodong Wang, Yigong Shi. Nature, 2000
899 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/53d4a3e7e42db045c8fe52caa39af63ef51ef714
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Citations in the corpus
- Cellular mechanisms controlling caspase activation and function. (2013, background): “This inhibitory action of XIAP can be antagonized by mitochondrial proteins Smac/DIABLO and Omi/HtrA2, which are released during an apoptotic stimulus along with cytochrome c (Chai et al. 2000; Du et al. 2000).”
- Apoptosis in development (2000, background): “Whether or not RPR, GRIM and HID have any direct homologues in mammals, they nonetheless interact with components of Drosophila cell death machinery that are conserved, in particular the evolutionarily conserved inhibitor-of-apoptosis protein (IAP) family that in mammals are targets of the pro-”
- The role of mitochondrial factors in apoptosis: a Russian roulette with more than one bullet (2002, background): “Omi/HtrA2 interacts with both the BIR2 and BIR3 domains of XIAP, although with higher affinity for the BIR2, as opposed to Smac/DIABLO, which preferentially binds the BIR3 domain.17,20 This selectivity suggests that Omi/HtrA2 may promote preferentially caspase-3 activation rather than caspase-9 acti”
- Mechanism of XIAP-mediated inhibition of caspase-9. (2003, background): “…paper reports the crystal structure of chondrial protein Smac/DIABLO, which is released into caspase-9 in an inhibitory complex with the third bacu- the cytoplasm during apoptosis (Chai et al., 2000; Du loviral IAP repeat (BIR3) of XIAP at 2.4 Å resolution. et al., 2000; Verhagen et al., 2000).”
- Mechanisms of caspase activation and inhibition during apoptosis. (2002, background): “Whereas Cyt. c directly activates Apaf-1 and caspase-9, Smac/DIABLO interacts withMechanisms of IAP-Mediated Inhibition of Caspase-9 multiple IAPs and removes IAP-mediated inhibition of both initiator and effector caspases (Chai et al., 2000;Only processed caspase-9 is subject to inhibition by IAPs.”
- Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy (2006, background): “One Smac/DIABLO dimer binds one XIAP molecule by both IAP-binding motifs, one interacting with BIR2 and the other one with BIR3 (Huang et al., 2003).”
- Targeting IAP proteins for therapeutic intervention in cancer (2012, background): “SMAC promotes caspase activation and apoptosis by binding to several IAP proteins, including XIAP, c-IAP1 and c-IAP2, via its amino-terminal amino acid residues (Ala-Val-Pro-Ile) that are highly conserved through evolutio”
- Molecular mechanisms of caspase regulation during apoptosis (2004, background): “During apoptosis, SMAC/DIABLO is released from the intermembrane space of mitochondria into the cytosol, where it interacts with several IAPs and removes the IAP-mediated inhibition of both initiator and effector caspase”
- Autocrine TNFalpha signaling renders human cancer cells susceptible to Smac-mimetic-induced apoptosis. (2007, background): “Under normal conditions, Smac is sequestered in the mitochondria and is released into the cytosol only upon induction of apoptosis or mitochondrial dysfunction (Chai et al., 2000; Du et al., 2000).”
- Recent advances in the development of protein–protein interactions modulators: mechanisms and clinical trials (2020, background): “When the Smac released from the mitochondria, its N-terminal amino acids, alanine–valine–proline–isoleucine (AVPI) bind to the BIR3 domain of XIAP, which makes the XIAP lose the ability to combine with caspase, so as to promote apoptosis.(96,97) Fig.”
- Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain (2000, background): “Although undefined in the X-ray structure, the amino-terminal residues of Smac are critical for its functio”
- Proteases for Cell Suicide: Functions and Regulation of Caspases (2000, background): “The N-terminal regions of Smac, like those in Reaper, Grim, and Hid, are indispensable for its function (18).”