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Srinivasa M. Srinivasula

Researcher at Indian Institute of Science Education and Research, Thiruvananthapuram

Publications -  104
Citations -  34769

Srinivasa M. Srinivasula is an academic researcher from Indian Institute of Science Education and Research, Thiruvananthapuram. The author has contributed to research in topics: Apoptosis & Caspase. The author has an hindex of 63, co-authored 98 publications receiving 32847 citations. Previous affiliations of Srinivasa M. Srinivasula include Thomas Jefferson University & National Institutes of Health.

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Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade

Peng Li, +6 more
- 14 Nov 1997 - 
TL;DR: Mutation of the active site of caspase-9 attenuated the activation of cazase-3 and cellular apoptotic response in vivo, indicating that casp enzyme-9 is the most upstream member of the apoptotic protease cascade that is triggered by cytochrome c and dATP.
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Guidelines for the use and interpretation of assays for monitoring autophagy

Daniel J. Klionsky, +1287 more
- 01 Apr 2012 - 
TL;DR: These guidelines are presented for the selection and interpretation of methods for use by investigators who aim to examine macroautophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
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IAPs block apoptotic events induced by caspase‐8 and cytochrome c by direct inhibition of distinct caspases

Quinn Deveraux, +8 more
- 15 Apr 1998 - 
TL;DR: It is demonstrated that IAPs can suppress different apoptotic pathways by inhibiting distinct caspases and identify pro‐caspase‐9 as a new target for IAP‐mediated inhibition of apoptosis.
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Structure-based discovery of an organic compound that binds Bcl-2 protein and induces apoptosis of tumor cells

Jia-Lun Wang, +8 more
- 20 Jun 2000 - 
TL;DR: The discovery of HA14-1, a small molecule and nonpeptidic ligand of a Bcl-2 surface pocket, provides a chemical probe to study B cl-2-regulated apoptotic pathways in vivo and could lead to the development of new therapeutic agents.
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Autoactivation of Procaspase-9 by Apaf-1-Mediated Oligomerization

Srinivasa M. Srinivasula, +3 more
- 01 Jun 1998 - 
TL;DR: It is shown that deletion of the Apaf-1 WD-40 repeats makes Apf-1 constitutively active and capable of processing procaspase-9 independent of cytochrome c/dATP and oligomerizing its precursor molecules.