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NMR-based modelling revealed an alpha helical structure for cytoplasmic domain of the alpha subunit of Fc epsilon RI, the high affinity IgE receptor

dc.contributor.authorZloh, Mire
dc.contributor.authorThomas, R.
dc.contributor.authorReid, R. E.
dc.contributor.authorGibbons, W.A.
dc.date.accessioned2014-06-04T10:30:33Z
dc.date.available2014-06-04T10:30:33Z
dc.date.issued1997
dc.identifier.citationZloh , M , Thomas , R , Reid , R E & Gibbons , W A 1997 , ' NMR-based modelling revealed an alpha helical structure for cytoplasmic domain of the alpha subunit of Fc epsilon RI, the high affinity IgE receptor ' , Biochemical Society Transactions , vol. 25 , no. 1 , pp. 55S . https://doi.org/10.1042/bst025055s
dc.identifier.issn0300-5127
dc.identifier.otherPURE: 1458476
dc.identifier.otherPURE UUID: ba6fa145-abb1-45d9-8000-1dc3f0466622
dc.identifier.otherPubMed: 9056953
dc.identifier.otherScopus: 0031057378
dc.identifier.urihttp://hdl.handle.net/2299/13616
dc.language.isoeng
dc.relation.ispartofBiochemical Society Transactions
dc.titleNMR-based modelling revealed an alpha helical structure for cytoplasmic domain of the alpha subunit of Fc epsilon RI, the high affinity IgE receptoren
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.contributor.institutionDepartment of Pharmacy
dc.contributor.institutionMedicinal and Analytical Chemistry
dc.description.statusPeer reviewed
rioxxterms.versionofrecordhttps://doi.org/10.1042/bst025055s
rioxxterms.typeOther
herts.preservation.rarelyaccessedtrue


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