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dc.contributor.authorKahn, Richard A.
dc.contributor.authorLambright, David G.
dc.date2022-08-11T08:10:18.000
dc.date.accessioned2022-08-23T17:03:36Z
dc.date.available2022-08-23T17:03:36Z
dc.date.issued2015-11-03
dc.date.submitted2016-04-13
dc.identifier.citationStructure. 2015 Nov 3;23(11):1971-3. doi: 10.1016/j.str.2015.10.002. <a href="http://dx.doi.org/10.1016/j.str.2015.10.002">Link to article on publisher's site</a>
dc.identifier.issn0969-2126 (Linking)
dc.identifier.doi10.1016/j.str.2015.10.002
dc.identifier.pmid26536378
dc.identifier.urihttp://hdl.handle.net/20.500.14038/44461
dc.description.abstractIn this issue of Structure, Jian et al. (2015) report the crystal structures of the apo- and dibutyryl-PI(4,5)P2 bound forms of the PH domain from the ARF GAP, ASAP1. This PH domain has two anionic phospholipid binding sites proposed to work in concert to regulate ASAP1 GAP activity.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=26536378&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1016/j.str.2015.10.002
dc.subjectBiochemistry
dc.subjectMolecular Biology
dc.subjectStructural Biology
dc.titleA PH Domain with Dual Phospholipid Binding Sites Regulates the ARF GAP, ASAP1
dc.typeJournal Article
dc.source.journaltitleStructure (London, England : 1993)
dc.source.volume23
dc.source.issue11
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/pmm_pp/55
dc.identifier.contextkey8471539
html.description.abstract<p>In this issue of Structure, Jian et al. (2015) report the crystal structures of the apo- and dibutyryl-PI(4,5)P2 bound forms of the PH domain from the ARF GAP, ASAP1. This PH domain has two anionic phospholipid binding sites proposed to work in concert to regulate ASAP1 GAP activity.</p>
dc.identifier.submissionpathpmm_pp/55
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.contributor.departmentProgram in Molecular Medicine
dc.source.pages1971-3


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