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dc.contributor.authorTutar, Y
dc.date.accessioned2019-07-27T12:10:23Z
dc.date.accessioned2019-07-28T10:21:57Z
dc.date.available2019-07-27T12:10:23Z
dc.date.available2019-07-28T10:21:57Z
dc.date.issued2006
dc.identifier.issn0929-8665
dc.identifier.urihttps://dx.doi.org/10.2174/092986606775338425
dc.identifier.urihttps://hdl.handle.net/20.500.12418/10920
dc.descriptionWOS: 000235725800013en_US
dc.descriptionPubMed ID: 16515459en_US
dc.description.abstractFunctional S100P requires dimer formation and dimerization might form for one of the two reasons: i. producing a pair of site for target protein binding or ii. modulation of cation binding affinity. The extent of exposed protein hydrophobicity was related to dimer formation.en_US
dc.language.isoengen_US
dc.publisherBENTHAM SCIENCE PUBL LTDen_US
dc.relation.isversionof10.2174/092986606775338425en_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectcalciumen_US
dc.subjectS100Pen_US
dc.subjectdimer formationen_US
dc.subjectcation bindingen_US
dc.subjectprostate canceren_US
dc.titleDimerization and ion binding properties of S100P proteinen_US
dc.typearticleen_US
dc.relation.journalPROTEIN AND PEPTIDE LETTERSen_US
dc.contributor.departmentCumhuriyet Univ Kimya Bolumu Biyokimya ABD, TR-58140 Sivas, Turkey -- Texas Tech Univ, Dept Chem & Biochem, Lubbock, TX 79409 USAen_US
dc.identifier.volume13en_US
dc.identifier.issue3en_US
dc.identifier.endpage306en_US
dc.identifier.startpage301en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US


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