α/β Hydrolase Fold: An Update

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dc.contributor.authorCarr, Paul D
dc.contributor.authorOllis, David
dc.date.accessioned2015-12-07T22:21:31Z
dc.date.issued2009
dc.date.updated2016-02-24T09:51:20Z
dc.description.abstractThe α/β hydrolase superfamily has rapidly expanded in recent years and continues to do so at an expeditious pace. According to the ESTHER database (http://bioweb.ensam.inra.fr/ESTHER) 29000 papers have been published cataloguing 89 family groups, compri
dc.identifier.issn0929-8665
dc.identifier.urihttp://hdl.handle.net/1885/20082
dc.publisherBentham Science Publishers Ltd
dc.sourceProtein and Peptide Letters
dc.subjectKeywords: hydrolase; animal; article; chemical structure; chemistry; enzyme active site; enzyme specificity; genetics; human; metabolism; multigene family; protein folding; protein tertiary structure; structure activity relation; Animals; Catalytic Domain; Humans;
dc.titleα/β Hydrolase Fold: An Update
dc.typeJournal article
local.bibliographicCitation.issue10
local.bibliographicCitation.lastpage1148
local.bibliographicCitation.startpage1137
local.contributor.affiliationCarr, Paul D, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationOllis, David, College of Physical and Mathematical Sciences, ANU
local.contributor.authoruidCarr, Paul D, u9206448
local.contributor.authoruidOllis, David, u9200080
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.identifier.absfor060112 - Structural Biology (incl. Macromolecular Modelling)
local.identifier.ariespublicationu2544221xPUB11
local.identifier.citationvolume16
local.identifier.doi10.2174/092986609789071298
local.identifier.scopusID2-s2.0-69549084345
local.type.statusPublished Version

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