Caspase structure, proteolytic substrates, and function during apoptotic cell death
Caspases play an essential role during apoptotic cell death. These enzymes define a new class of cysteine proteases and comprise a multi-gene family with more than a dozen distinct mammalian family members. The discrete and highly limited subset of cellular polypeptides that are cleaved by these pro...
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| Veröffentlicht in: | Cell death and differentiation 1999-11, Vol.6 (11), p.1028-1042 |
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| container_title | Cell death and differentiation |
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| creator | Nicholson, D W |
| description | Caspases play an essential role during apoptotic cell death. These enzymes define a new class of cysteine proteases and comprise a multi-gene family with more than a dozen distinct mammalian family members. The discrete and highly limited subset of cellular polypeptides that are cleaved by these proteases is sufficient to account for the majority of cellular and morphological events that occur during cell death. In some cases, caspases also play a contributory role in escalating the propensity for apoptosis, and in doing so may exacerbate disease pathogenesis. |
| doi_str_mv | 10.1038/sj.cdd.4400598 |
| format | Article |
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These enzymes define a new class of cysteine proteases and comprise a multi-gene family with more than a dozen distinct mammalian family members. The discrete and highly limited subset of cellular polypeptides that are cleaved by these proteases is sufficient to account for the majority of cellular and morphological events that occur during cell death. 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These enzymes define a new class of cysteine proteases and comprise a multi-gene family with more than a dozen distinct mammalian family members. The discrete and highly limited subset of cellular polypeptides that are cleaved by these proteases is sufficient to account for the majority of cellular and morphological events that occur during cell death. In some cases, caspases also play a contributory role in escalating the propensity for apoptosis, and in doing so may exacerbate disease pathogenesis.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Binding Sites</subject><subject>Caspase 1 - genetics</subject><subject>Caspase 1 - physiology</subject><subject>Caspase Inhibitors</subject><subject>Caspases - chemistry</subject><subject>Caspases - genetics</subject><subject>Caspases - physiology</subject><subject>Enzyme Activation</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Substrate Specificity</subject><issn>1350-9047</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo1kD1PwzAURT2AaCmsjMgTUxOeYzuxR1TxJVViAOboxc-FVGkSYnvov6cVZbrDPbo6uozdCMgFSHMftrkjypUC0NacsbmQGjILqpqxyxC2AFBWtrxgMwG6MqISc_a-wjBi8DzEKbmYJr_k4zREP3T72DoeUnNoMPqw5NgT36TexXboOaWp7b84jsMYhyPpfNdx8hi_r9j5Brvgr0-5YJ9Pjx-rl2z99vy6elhno5A2Zg0RCS00Cq_BuMIUVhkrZFmVRlfosQFXAIEqNYJyDYEjKRXRBsiZguSC3f3tHoR_kg-x3rXhqIG9H1KoSysLWSg4gLcnMDU7T_U4tTuc9vX_DfIXX1Je4g</recordid><startdate>199911</startdate><enddate>199911</enddate><creator>Nicholson, D W</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>199911</creationdate><title>Caspase structure, proteolytic substrates, and function during apoptotic cell death</title><author>Nicholson, D W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p139t-bddd1515a1e508c282948913676857aeab0c20d0465a04cbd0cd334ddf0dc82d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Binding Sites</topic><topic>Caspase 1 - genetics</topic><topic>Caspase 1 - physiology</topic><topic>Caspase Inhibitors</topic><topic>Caspases - chemistry</topic><topic>Caspases - genetics</topic><topic>Caspases - physiology</topic><topic>Enzyme Activation</topic><topic>Humans</topic><topic>Molecular Sequence Data</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nicholson, D W</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Cell death and differentiation</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nicholson, D W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Caspase structure, proteolytic substrates, and function during apoptotic cell death</atitle><jtitle>Cell death and differentiation</jtitle><addtitle>Cell Death Differ</addtitle><date>1999-11</date><risdate>1999</risdate><volume>6</volume><issue>11</issue><spage>1028</spage><epage>1042</epage><pages>1028-1042</pages><issn>1350-9047</issn><abstract>Caspases play an essential role during apoptotic cell death. These enzymes define a new class of cysteine proteases and comprise a multi-gene family with more than a dozen distinct mammalian family members. The discrete and highly limited subset of cellular polypeptides that are cleaved by these proteases is sufficient to account for the majority of cellular and morphological events that occur during cell death. In some cases, caspases also play a contributory role in escalating the propensity for apoptosis, and in doing so may exacerbate disease pathogenesis.</abstract><cop>England</cop><pmid>10578171</pmid><doi>10.1038/sj.cdd.4400598</doi><tpages>15</tpages></addata></record> |
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| ispartof | Cell death and differentiation, 1999-11, Vol.6 (11), p.1028-1042 |
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| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; SpringerLink Journals - AutoHoldings |
| subjects | Amino Acid Sequence Animals Apoptosis Binding Sites Caspase 1 - genetics Caspase 1 - physiology Caspase Inhibitors Caspases - chemistry Caspases - genetics Caspases - physiology Enzyme Activation Humans Molecular Sequence Data Substrate Specificity |
| title | Caspase structure, proteolytic substrates, and function during apoptotic cell death |
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