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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.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.institutionPsychopharmacology, Drug Misuse and Novel Psychoactive Substances Unit
dc.contributor.institutionCentre for Health Services and Clinical Research
dc.description.statusPeer reviewed
rioxxterms.versionofrecord10.1042/bst025055s
rioxxterms.typeOther
herts.preservation.rarelyaccessedtrue


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