S
Sabina Sperandio
Researcher at Buck Institute for Research on Aging
Publications - 15
Citations - 2863
Sabina Sperandio is an academic researcher from Buck Institute for Research on Aging. The author has contributed to research in topics: Paraptosis & Apoptosis. The author has an hindex of 11, co-authored 15 publications receiving 2722 citations. Previous affiliations of Sabina Sperandio include Sanford-Burnham Institute for Medical Research & University of California, San Diego.
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Journal ArticleDOI
A unified model for apical caspase activation.
Kelly M. Boatright,Martin Renatus,Fiona L. Scott,Sabina Sperandio,Hwain Shin,Irene M. Pedersen,Jean-Ehrland Ricci,Wade Edris,Daniel P. Sutherlin,Douglas R. Green,Guy S. Salvesen +10 more
TL;DR: A unified caspase activation hypothesis is proposed whereby apical caspases are activated by dimerization of monomeric zymogens, and single amino acid substitutions at the dimer interface abrogate the activity of caspased-8 and -9 introduced into recipient mammalian cells.
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An alternative, nonapoptotic form of programmed cell death
TL;DR: It is shown that this form of programmed cell death is driven by an alternative caspase-9 activity that is Apaf-1-independent, and should lead to new insight into cell death programs and their roles in development and degeneration.
Journal ArticleDOI
Paraptosis: mediation by MAP kinases and inhibition by AIP-1/Alix.
Sabina Sperandio,Sabina Sperandio,Karen S. Poksay,I de Belle,M J Lafuente,B Liu,Jamal Nasir,Dale E. Bredesen,Dale E. Bredesen +8 more
TL;DR: It is reported that paraptosis, an alternative, nonapoptotic cell death program that may be induced by the insulin-like growth factor I receptor, is mediated by mitogen-activated protein kinases (MAPKs) and inhibited by AIP-1/Alix.
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The Apoptosome Activates Caspase-9 by Dimerization
TL;DR: It is shown that both Hofmeister salts and a reconstituted mini-apoptosome activate caspase-9 by a second-order process, compatible with a conserved dimer-driven process, ruling out the requirement for allosteric activation and supporting an induced proximity dimerization model for apical caspases activation in vivo.
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p75NTR and the concept of cellular dependence: seeing how the other half die.
Dale E. Bredesen,Xin Ye,Andrea Tasinato,Sabina Sperandio,James Wang,Nuria Assa-Munt,Shahrooz Rabizadeh,Shahrooz Rabizadeh +7 more
TL;DR: This work has found that the prototype for this form of signaling – the common neurotrophin receptor, p75NTR – creates a state of cellular dependence (or addiction) on neurotrophins, and that this effect requires an `addiction/dependence domain' (ADD) in the intracytoplasmic region of p 75NTR.