Literature DB >> 10578177

Caspase inhibitors.

P G Ekert1, J Silke, D L Vaux.   

Abstract

Caspases are the key effector molecules of the physiological death process known as apoptosis, although some are involved in activation of cytokines, rather than cell death. They exist in most of our cells as inactive precursors (zymogens) that kill the cell once activated. Caspases can be controlled in two ways. The processing and activation of a caspase can be regulated by molecules such as FADD, APAF-1, Bcl-2 family members, FLIP and IAPs. Active caspases can be controlled by a variety of inhibitors that directly interact with the protease. This review describes the later direct caspase inhibitors that have been identified, products of both viral and cellular genes, and artificial caspase inhibitors that have been developed both as research tools and as pharmaceutical agents to inhibit cell death in vivo.

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Year:  1999        PMID: 10578177     DOI: 10.1038/sj.cdd.4400594

Source DB:  PubMed          Journal:  Cell Death Differ        ISSN: 1350-9047            Impact factor:   15.828


  89 in total

Review 1.  The kinder side of killer proteases: caspase activation contributes to neuroprotection and CNS remodeling.

Authors:  B McLaughlin
Journal:  Apoptosis       Date:  2004-03       Impact factor: 4.677

2.  Phytaspase, a relocalisable cell death promoting plant protease with caspase specificity.

Authors:  Nina V Chichkova; Jane Shaw; Raisa A Galiullina; Georgina E Drury; Alexander I Tuzhikov; Sang Hyon Kim; Markus Kalkum; Teresa B Hong; Elena N Gorshkova; Lesley Torrance; Andrey B Vartapetian; Michael Taliansky
Journal:  EMBO J       Date:  2010-01-28       Impact factor: 11.598

3.  A sensitive near-infrared fluorescent probe for caspase-mediated apoptosis: Synthesis and application in cell imaging.

Authors:  Yepeng Luan; Qiuhong Yang; Yumei Xie; Shaofeng Duan; Shuang Cai; M L Forrest
Journal:  Drug Discov Ther       Date:  2011-01-01

Review 4.  Apoptosis, pyroptosis, and necrosis: mechanistic description of dead and dying eukaryotic cells.

Authors:  Susan L Fink; Brad T Cookson
Journal:  Infect Immun       Date:  2005-04       Impact factor: 3.441

5.  A vacuolar processing enzyme, deltaVPE, is involved in seed coat formation at the early stage of seed development.

Authors:  Satoru Nakaune; Kenji Yamada; Maki Kondo; Tomohiko Kato; Satoshi Tabata; Mikio Nishimura; Ikuko Hara-Nishimura
Journal:  Plant Cell       Date:  2005-02-10       Impact factor: 11.277

6.  Response to bistability in apoptosis: roles of bax, bcl-2, and mitochondrial permeability transition pores.

Authors:  Thomas Eissing; Steffen Waldherr; Frank Allgöwer; Peter Scheurich; Eric Bullinger
Journal:  Biophys J       Date:  2007-02-02       Impact factor: 4.033

7.  Temporal relationships between ceramide production, caspase activation and mitochondrial dysfunction in cell lines with varying sensitivity to anti-Fas-induced apoptosis.

Authors:  C Rodriguez-Lafrasse; G Alphonse; P Broquet; M T Aloy; P Louisot; R Rousson
Journal:  Biochem J       Date:  2001-07-15       Impact factor: 3.857

Review 8.  Use of fluorescently labeled caspase inhibitors as affinity labels to detect activated caspases.

Authors:  Jerzy Grabarek; Paul Amstad; Zbigniew Darzynkiewicz
Journal:  Hum Cell       Date:  2002-03       Impact factor: 4.174

9.  The NRIF3 family of transcriptional coregulators induces rapid and profound apoptosis in breast cancer cells.

Authors:  Dangsheng Li; Sharmistha Das; Tatsuya Yamada; Herbert H Samuels
Journal:  Mol Cell Biol       Date:  2004-05       Impact factor: 4.272

10.  Membrane dielectric changes indicate induced apoptosis in HL-60 cells more sensitively than surface phosphatidylserine expression or DNA fragmentation.

Authors:  Xujing Wang; Frederick F Becker; Peter R C Gascoyne
Journal:  Biochim Biophys Acta       Date:  2002-08-31
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