Artificial Death Switches: Induction of Apoptosis by Chemically Induced Caspase Multimerization

Steller argues that the identification of proteins that promote and inhibit aggregation and understanding their precise molecular mechanism of action will almost certainly provide many new interesting opportunities to control cell death in therapeutically relevant ways.

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Bibliographic Details
Published inProceedings of the National Academy of Sciences - PNAS Vol. 95; no. 10; pp. 5421 - 5422
Main Author Steller, Hermann
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences of the United States of America 12.05.1998
National Acad Sciences
National Academy of Sciences
The National Academy of Sciences
Subjects
Aggregation
Animal cells
Animals
Apoptosis
Apoptosis - drug effects
Caspase 1
Caspase 3
Caspases
Cell death
Cell division
Cellular biology
Commentary
Cysteine Endopeptidases - chemistry
Cysteine Endopeptidases - metabolism
Dimerization
Enzyme Activation
Enzyme Precursors - chemistry
Enzyme Precursors - metabolism
Gene therapy
Genetic Therapy - methods
Lead
Molecules
Protein Conformation
Proteins
Structure-Activity Relationship
Zymogens
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Summary:Steller argues that the identification of proteins that promote and inhibit aggregation and understanding their precise molecular mechanism of action will almost certainly provide many new interesting opportunities to control cell death in therapeutically relevant ways.
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ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.95.10.5421