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dc.contributor.authorCygler, M
dc.contributor.authorGrochulski, P
dc.contributor.authorBlanchard, H
dc.date.accessioned2006-06-15
dc.date.accessioned2014-11-12T04:52:42Z
dc.date.accessioned2017-03-02T00:30:54Z
dc.date.available2014-11-12T04:52:42Z
dc.date.available2017-03-02T00:30:54Z
dc.date.issued2002
dc.identifier.isbn1-59259-183-3
dc.identifier.doi10.1385/1-59259-183-3:243
dc.identifier.urihttp://hdl.handle.net/10072/64581
dc.description.abstractCalpains are calcium-regulated neutral cysteine proteases that include ubiquitous, as well as tissue-specific, isoforms. The ubiquitous isoforms, μ- and m-calpains are intracellular, nonlysosomal proteases (1). The tissue-specific isoforms include calpain 3, which is found in skeletal muscle, and stomach-specific nCL–2 (2). The calpains catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction, although definitive physiological roles are not yet ascertained. They are also thought to contribute to the tissue damage that follows ischemia and reperfusion in conditions such as stroke and cardiac infarct (3,4), stimulating a search for specific and clinically acceptable inhibitors aimed at both the active site and also the Ca2+-binding domains (5). The calpains are heterodimers that consist of an 80-kDa catalytic subunit (the large subunit), and a 30-kDa regulatory subunit (the small subunit).
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherHumana Press
dc.publisher.placeBiotechnology Research Institute, NRC
dc.publisher.urihttp://dx.doi.org/10.1385/1592591833
dc.relation.ispartofbooktitleMethods in Molecular Biology
dc.relation.ispartofchapter16
dc.relation.ispartofchapternumbers21
dc.relation.ispartofpagefrom243
dc.relation.ispartofpageto260
dc.relation.ispartofvolume172
dc.subject.fieldofresearchOther Chemical Sciences
dc.subject.fieldofresearchBiochemistry and Cell Biology
dc.subject.fieldofresearchcode0399
dc.subject.fieldofresearchcode0601
dc.titleCrystallisation and structural details of Ca2+ induced conformational changes in the EF-hand domain VI of Calpain
dc.typeBook chapter
dc.type.descriptionB1 - Chapters
dc.type.codeb1x
gro.facultyInstitute for Glycomics
gro.hasfulltextNo Full Text
gro.griffith.authorBlanchard, Helen


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