Inhibition of Human Caspases by Peptide-based and Macromolecular Inhibitors
Margarita Garcia-Calvo,Erin P. Peterson,Barbara Leiting,Rejean Ruel,Donald W. Nicholson,Nancy A. Thornberry +5 more
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TLDR
The results obtained with peptide-based inhibitors are in accord with those predicted from the substrate specificity studies described earlier, and the cowpox serpin CrmA is a potent and selective inhibitor of Group I and most Group III caspases, suggesting that this virus facilitates infection through inhibition of both apoptosis and the host inflammatory response.About:
This article is published in Journal of Biological Chemistry.The article was published on 1998-12-04 and is currently open access. It has received 999 citations till now. The article focuses on the topics: Caspase & Serpin.read more
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The biochemistry of apoptosis
TL;DR: The basic components of the death machinery are reviewed, how they interact to regulate apoptosis in a coordinated manner is described, and the main pathways that are used to activate cell death are discussed.
Journal ArticleDOI
The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta.
TL;DR: In this article, the inflammasome is identified as a caspase-activating complex that comprises caspases-1, casp-5, Pycard/Asc, and NALP1, a Pyrin domain-containing protein sharing structural homology with NODs.
Mammalian caspases: structure ,a ctivation ,s ubstrates, and functions during apoptosis
TL;DR: Caspases, a family of cysteine-dependent aspartate-directed proteases, are prominent among the death proteases as discussed by the authors, and they play critical roles in initiation and execution of this process.
Journal ArticleDOI
Mammalian Caspases: Structure, Activation, Substrates, and Functions During Apoptosis
TL;DR: This work has shown that apoptotic cell death is a genetically programmed, morphologically distinct form of cell death that can be triggered by a variety of physiological and pathological stimuli, and that proteases play critical roles in initiation and execution of this process.
Journal ArticleDOI
Apoptosis, pyroptosis, and necrosis: mechanistic description of dead and dying eukaryotic cells
Susan L. Fink,Brad T. Cookson +1 more
TL;DR: A wide variety of pathogenic microorganisms have been demonstrated to cause eukaryotic cell death, either as a consequence of infecting host cells or by producing toxic products, and apoptosis in many of these systems is characterized as apoptosis.
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Molecular Cloning: A Laboratory Manual
TL;DR: Molecular Cloning has served as the foundation of technical expertise in labs worldwide for 30 years as mentioned in this paper and has been so popular, or so influential, that no other manual has been more widely used and influential.
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Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade
Peng Li,Deepak Nijhawan,Imawati Budihardjo,Srinivasa M. Srinivasula,Manzoor Ahmad,Emad S. Alnemri,Xiaodong Wang +6 more
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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Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
Donald W. Nicholson,Ambereen Ali,Nancy A. Thornberry,John P. Vaillancourt,C K Ding,Michel Gallant,Yves Gareau,Patrick R. Griffin,Marc Labelle,Yuri Lazebnik +9 more
TL;DR: A potent peptide aldehyde inhibitor has been developed and shown to prevent apoptotic events in vitro, suggesting that apopain/CPP32 is important for the initiation of apoptotic cell death.
Journal ArticleDOI
FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death--inducing signaling complex.
Marta Muzio,Arul M. Chinnaiyan,Frank C. Kischkel,Karen O'Rourke,Andrej Shevchenko,Jian Ni,Carsten Scaffidi,James D. Bretz,Mei Zhang,Reiner L. Gentz,Matthias Mann,Peter H. Krammer,Marcus E. Peter,Vishva M. Dixit +13 more
TL;DR: This work utilized nano-electrospray tandem mass spectrometry to identify CAP3 and CAP4, components of the CD95 (Fas/APO-1) death-inducing signaling complex, and found a novel 55 kDa protein, designated FLICE, which has homology to both FADD and the ICE/CED-3 family of cysteine proteases.
Journal ArticleDOI
A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes.
Nancy A. Thornberry,Herbert G. Bull,Jimmy R. Calaycay,Kevin T. Chapman,Andrew D. Howard,Matthew J. Kostura,Douglas K. Miller,Susan M. Molineaux,Jeffrey R. Weidner,John G. Aunins,Keith O. Elliston,Julia M. Ayala,Francesca J. Casano,Jayne Chin,Gloria J.-F. Ding,Linda A. Egger,Erin P. Gaffney,Guadalupe A. Limjuco,Oksana C. Palyha,S.M. Raju,Anna M. Rolando,J. Paul Salley,Ting-Ting Yamin,Terry D. Lee,John E. Shively,Malcolm MacCross,Richard A. Mumford,John A. Schmidt,Michael J. Tocci +28 more
TL;DR: Purification and cloning of the complementary DNA indicates that IL-lβ-converting enzyme is composed of two nonidentical subunits that are derived from a single proenzyme, possibly by autoproteolysis.