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https://hdl.handle.net/2440/59374
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dc.contributor.author | Pietsch, M. | - |
dc.contributor.author | Chua, K. | - |
dc.contributor.author | Abell, A. | - |
dc.date.issued | 2010 | - |
dc.identifier.citation | Current Topics in Medicinal Chemistry, 2010; 10(3):270-293 | - |
dc.identifier.issn | 1568-0266 | - |
dc.identifier.issn | 1873-4294 | - |
dc.identifier.uri | http://hdl.handle.net/2440/59374 | - |
dc.description.abstract | The physiological roles of calpains are discussed, as are the associated pathological disorders that result from their over-activation. We also present practical information for establishing functional inhibition assays and an overview of X-ray crystal structures of calpain-inhibitor complexes to aid inhibitor design. These structures reveal the expected extended β-strand conformation for the inhibitor backbone, a geometry that has been engineered into inhibitors with the introduction of either an N-terminal heterocycle or a macrocycle that links the P<sub>1</sub> and P<sub>3</sub> residues. The structure and function of all the main classes of inhibitors are reviewed, with most examples being classified according to the nature of the C-terminal reactive warhead group that reacts with the active site cysteine of calpains. These inhibitor classes include epoxysuccinate derivatives, aldehydes, aldehyde prodrugs (hemiacetals) and α-keto carbonyl compounds. Inhibitors derived from the endogenous inhibitor calpastatin and examples lacking a warhead, are now known and these are also discussed. | - |
dc.description.statementofresponsibility | Markus Pietsch, Krystle C.H. Chua, Andrew D. Abell | - |
dc.language.iso | en | - |
dc.publisher | Bentham Science Publ Ltd | - |
dc.rights | Copyright Bentham Science Publishers Ltd. | - |
dc.source.uri | http://dx.doi.org/10.2174/156802610790725489 | - |
dc.subject | β-strand conformation | - |
dc.subject | Calpain | - |
dc.subject | calpain assay | - |
dc.subject | calpastatin | - |
dc.subject | crystal structure | - |
dc.subject | cysteine protease | - |
dc.subject | macrocycles | - |
dc.subject | protease inhibitors | - |
dc.title | Calpains: Attractive targets for the development of synthetic inhibitors | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.2174/156802610790725489 | - |
dc.relation.grant | http://purl.org/au-research/grants/arc/DP0771901 | - |
dc.relation.grant | http://purl.org/au-research/grants/arc/DP0771901 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Abell, A. [0000-0002-0604-2629] | - |
Appears in Collections: | Aurora harvest Chemistry publications |
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