dc.contributor.author | Tutar, Y | |
dc.date.accessioned | 2019-07-27T12:10:23Z | |
dc.date.accessioned | 2019-07-28T10:21:57Z | |
dc.date.available | 2019-07-27T12:10:23Z | |
dc.date.available | 2019-07-28T10:21:57Z | |
dc.date.issued | 2006 | |
dc.identifier.issn | 0929-8665 | |
dc.identifier.uri | https://dx.doi.org/10.2174/092986606775338425 | |
dc.identifier.uri | https://hdl.handle.net/20.500.12418/10920 | |
dc.description | WOS: 000235725800013 | en_US |
dc.description | PubMed ID: 16515459 | en_US |
dc.description.abstract | Functional 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.iso | eng | en_US |
dc.publisher | BENTHAM SCIENCE PUBL LTD | en_US |
dc.relation.isversionof | 10.2174/092986606775338425 | en_US |
dc.rights | info:eu-repo/semantics/closedAccess | en_US |
dc.subject | calcium | en_US |
dc.subject | S100P | en_US |
dc.subject | dimer formation | en_US |
dc.subject | cation binding | en_US |
dc.subject | prostate cancer | en_US |
dc.title | Dimerization and ion binding properties of S100P protein | en_US |
dc.type | article | en_US |
dc.relation.journal | PROTEIN AND PEPTIDE LETTERS | en_US |
dc.contributor.department | Cumhuriyet Univ Kimya Bolumu Biyokimya ABD, TR-58140 Sivas, Turkey -- Texas Tech Univ, Dept Chem & Biochem, Lubbock, TX 79409 USA | en_US |
dc.identifier.volume | 13 | en_US |
dc.identifier.issue | 3 | en_US |
dc.identifier.endpage | 306 | en_US |
dc.identifier.startpage | 301 | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |