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Antonio Postigo
Researcher at London Research Institute
Publications - 11
Citations - 961
Antonio Postigo is an academic researcher from London Research Institute. The author has contributed to research in topics: Innate immune system & Virus. The author has an hindex of 10, co-authored 11 publications receiving 875 citations. Previous affiliations of Antonio Postigo include Francis Crick Institute.
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Journal ArticleDOI
F-Actin Is an Evolutionarily Conserved Damage-Associated Molecular Pattern Recognized by DNGR-1, a Receptor for Dead Cells
Susan Ahrens,Santiago Zelenay,David Sancho,Pavel Hanč,Svend Kjaer,Christoph Feest,Georgina C. Fletcher,Charlotte H. Durkin,Antonio Postigo,Mark Skehel,Facundo D. Batista,Barry J. Thompson,Michael Way,Caetano Reis e Sousa,Oliver Schulz +14 more
TL;DR: The identification of F-actin as a DNGR-1 ligand suggests that cytoskeletal exposure is a universal sign of cell damage that can be targeted by the innate immune system to initiate immunity.
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Point Mutation in trkB Causes Loss of NT4-Dependent Neurons without Major Effects on Diverse BDNF Responses
Liliana Minichiello,Franca Casagranda,Rosa Soler Tatche,Cheryl L. Stucky,Antonio Postigo,Gary R. Lewin,Alun M. Davies,Rüdiger Klein +7 more
TL;DR: While the Ras/MAPK pathway is required for in vitro differentiation of neuronal cells, trkB(shc/shc) mutant mice do not show any defects in BDNF-dependent differentiation of CNS neurons or in the function of sensory neurons that mediate innocuous touch.
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Distinct requirements for TrkB and TrkC signaling in target innervation by sensory neurons
Antonio Postigo,Anna Maria Calella,Bernd Fritzsch,Marlies Knipper,David M. Katz,Andreas Eilers,Thomas Schimmang,Gary R. Lewin,Rüdiger Klein,Liliana Minichiello +9 more
TL;DR: Using mice with TrkB or TrkC receptors lacking the docking site for Shc adaptors, it is shown that TrkB and TrKC promote survival of sensory neurons mainly through Shc site-independent pathways, suggesting that these receptors use similar pathways to prevent apoptosis.
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Vaccinia virus F1L protein promotes virulence by inhibiting inflammasome activation
Motti Gerlic,Benjamin Faustin,Antonio Postigo,Eric Chi-Wang Yu,Martina Proell,Naran Gombosuren,Maryla Krajewska,Rachel Flynn,Michael Croft,Michael Way,Arnold C. Satterthwait,Robert C. Liddington,Shahram Salek-Ardakani,Shu-ichi Matsuzawa,John C. Reed +14 more
TL;DR: A hexapeptide from F1L is necessary and sufficient for inhibiting the NLRP1 inflammasome in vitro, thus identifying a peptidyl motif required for binding and inhibitingNLRP1.
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Interaction of F1L with the BH3 domain of Bak is responsible for inhibiting vaccinia-induced apoptosis
TL;DR: It is demonstrated that F1L, which has no sequence homology to Bcl-2 family members, inhibits apoptosis at the level of mitochondria by binding to Bak and uses this specific, BH3-like domain to bind and inhibit Bak at the mitochondria.