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http://purl.uniprot.org/citations/1322833http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1322833http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1322833http://www.w3.org/2000/01/rdf-schema#comment"Membrane interactions of tetradecapeptide toxin mastoparan (MP) and analogues (MP-3, MP-X and polistes MP), as indicated by inhibition of various enzymatic and cellular activities, were investigated. MP-3 was found to be the least active in inhibiting protein kinase C (PKC; activated by phosphatidylserine vesicles, synaptosomal membranes or phorbol ester), synaptosomal membrane Na,K-ATPase and proliferation and viability of leukemia HL60 cells. MP-3, however, was as active as others in inhibiting PKC activated by arachidonate monomers and phorbol ester binding. The unique properties of MP-3, the [des-Ile1-Asn2]-analogue of MP, might be related to its low functional amphiphilicity compared to others and useful in further delineating biological activities associated with or regulated by membranes."xsd:string
http://purl.uniprot.org/citations/1322833http://purl.org/dc/terms/identifier"doi:10.1016/0014-5793(92)80694-c"xsd:string
http://purl.uniprot.org/citations/1322833http://purl.org/dc/terms/identifier"doi:10.1016/0014-5793(92)80694-c"xsd:string
http://purl.uniprot.org/citations/1322833http://purl.uniprot.org/core/author"Kim Y.S."xsd:string
http://purl.uniprot.org/citations/1322833http://purl.uniprot.org/core/author"Kim Y.S."xsd:string
http://purl.uniprot.org/citations/1322833http://purl.uniprot.org/core/author"Kuo J.F."xsd:string
http://purl.uniprot.org/citations/1322833http://purl.uniprot.org/core/author"Kuo J.F."xsd:string
http://purl.uniprot.org/citations/1322833http://purl.uniprot.org/core/author"Raynor R.L."xsd:string
http://purl.uniprot.org/citations/1322833http://purl.uniprot.org/core/author"Raynor R.L."xsd:string
http://purl.uniprot.org/citations/1322833http://purl.uniprot.org/core/author"Zheng B."xsd:string
http://purl.uniprot.org/citations/1322833http://purl.uniprot.org/core/author"Zheng B."xsd:string
http://purl.uniprot.org/citations/1322833http://purl.uniprot.org/core/author"Vogler W.R."xsd:string
http://purl.uniprot.org/citations/1322833http://purl.uniprot.org/core/author"Vogler W.R."xsd:string
http://purl.uniprot.org/citations/1322833http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1322833http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1322833http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/1322833http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/1322833http://purl.uniprot.org/core/pages"275-279"xsd:string
http://purl.uniprot.org/citations/1322833http://purl.uniprot.org/core/pages"275-279"xsd:string
http://purl.uniprot.org/citations/1322833http://purl.uniprot.org/core/title"Membrane interactions of mastoparan analogues related to their differential effects on protein kinase C, Na, K-ATPase and HL60 cells."xsd:string
http://purl.uniprot.org/citations/1322833http://purl.uniprot.org/core/title"Membrane interactions of mastoparan analogues related to their differential effects on protein kinase C, Na, K-ATPase and HL60 cells."xsd:string
http://purl.uniprot.org/citations/1322833http://purl.uniprot.org/core/volume"307"xsd:string
http://purl.uniprot.org/citations/1322833http://purl.uniprot.org/core/volume"307"xsd:string