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Donald W. Nicholson

Researcher at Merck & Co.

Publications -  176
Citations -  40607

Donald W. Nicholson is an academic researcher from Merck & Co.. The author has contributed to research in topics: Caspase & Apoptosis. The author has an hindex of 76, co-authored 176 publications receiving 39562 citations. Previous affiliations of Donald W. Nicholson include Johns Hopkins University School of Medicine & Ludwig Maximilian University of Munich.

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Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis

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.
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Caspases: killer proteases

TL;DR: Caspases (cysteinyl aspartate-specific proteinases) mediate highly specific proteolytic cleavage events in dying cells, which collectively manifest the apoptotic phenotype.
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Human ICE/CED-3 Protease Nomenclature

TL;DR: A committee of several scientists who have been involved in the identification and characterization of these enzymes have formed a committee, with the objective of proposing a nomenclature for the human members of this protease family that is sensible and easy to use.
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Guidelines for the use and interpretation of assays for monitoring cell death in higher eukaryotes

Lorenzo Galluzzi, +103 more
TL;DR: A nonexhaustive comparison of methods to detect cell death with apoptotic or nonapoptotic morphologies, their advantages and pitfalls is provided and the importance of performing multiple, methodologically unrelated assays to quantify dying and dead cells is emphasized.
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A Combinatorial Approach Defines Specificities of Members of the Caspase Family and Granzyme B FUNCTIONAL RELATIONSHIPS ESTABLISHED FOR KEY MEDIATORS OF APOPTOSIS

TL;DR: In this article, the authors used a positional scanning substrate combinatorial library to rigorously define individual specificities of the Caspase (interleukin-1beta converting enzyme/CED-3) family of cysteine proteases and the cytotoxic lymphocyte-derived serine protease granzyme B.