{"created":"2023-05-15T14:35:57.482593+00:00","id":46273,"links":{},"metadata":{"_buckets":{"deposit":"79df08cb-9a36-42f4-b5c3-4c25aa29774c"},"_deposit":{"created_by":1,"id":"46273","owners":[1],"pid":{"revision_id":0,"type":"depid","value":"46273"},"status":"published"},"_oai":{"id":"oai:repo.qst.go.jp:00046273","sets":["1"]},"author_link":["460894","460904","460893","460902","460903","460901","460895","460898","460899","460897","460896","460900"],"item_8_biblio_info_7":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2012-03","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"3","bibliographicPageEnd":"437","bibliographicPageStart":"433","bibliographicVolumeNumber":"35","bibliographic_titles":[{"bibliographic_title":"Biological & Pharmaceutical Bulletin"}]}]},"item_8_description_5":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"Phosphorylation of tyrosine residues by protein tyrosine kinases (PTK) and\nphosphotyrosine/Src homology 2 (SH2) domain interactions are crucial not only for \nsignal transduction but also for regulation of PTK activity. Tyrosine residues also\nreceive nitration and halogenation under oxidative conditions. It has been reported that nitration of tyrosine residue caused peptides to be a poor substrate for PTK and that nitrotyrosine residues could bind to SH2 domains as a phosphotyrosine mimic to activate Src family kinase. However, the effect of halogenation on tyrosine\nphosphorylation or SH2 domain binding is not well understood. We examined the\nphosphorylation of model peptides containing 3-halotyrosine or 3-nitrotyrosine using\ntypical receptor and nonreceptor tyrosine kinase (EGFR and Lck, respectively). The\nEGFR- and Lck-mediated phosphorylation was markedly inhibited by tyrosine\nhalogenation. Iodination showed the strongest inhibition of the phosphorylation among four types of halogenation, and its inhibitory effect was stronger than that of nitration. We also examined the effect of iodination and nitration of tyrosine residues on binding to the SH2 domain of Lck, using a model peptide containing the\nphosphoTyr-Glu-Glu-Ile motif, which has a high affinity for the SH2 domain. The\nrelative affinities of the modified peptides whose phosphotyrosine was substituted with unphosphorylated tyrosine, 3-nitrotyrosine, and 3-iodotyrosine, and of the model peptide were 0.024, 0.26, 1, and 16, respectively. These results suggest that tyrosine iodination may have an effect on the phosphorylation or binding to the SH2 domain similar to nitration. Tyrosine iodination possibly modulates signal transduction, with the potential impairment of cell function.","subitem_description_type":"Abstract"}]},"item_8_source_id_9":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"0918-6158","subitem_source_identifier_type":"ISSN"}]},"item_access_right":{"attribute_name":"アクセス権","attribute_value_mlt":[{"subitem_access_right":"metadata only access","subitem_access_right_uri":"http://purl.org/coar/access_right/c_14cb"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"Okamura, Toshimitsu"}],"nameIdentifiers":[{"nameIdentifier":"460893","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Kikuchi, Tatsuya"}],"nameIdentifiers":[{"nameIdentifier":"460894","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Nodaira, Mika"}],"nameIdentifiers":[{"nameIdentifier":"460895","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Odaka, Kenichi"}],"nameIdentifiers":[{"nameIdentifier":"460896","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Fukushi, Kiyoshi"}],"nameIdentifiers":[{"nameIdentifier":"460897","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Irie, Toshiaki"}],"nameIdentifiers":[{"nameIdentifier":"460898","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"岡村 敏充","creatorNameLang":"en"}],"nameIdentifiers":[{"nameIdentifier":"460899","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"菊池 達矢","creatorNameLang":"en"}],"nameIdentifiers":[{"nameIdentifier":"460900","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"野平 美佳","creatorNameLang":"en"}],"nameIdentifiers":[{"nameIdentifier":"460901","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"小高 謙一","creatorNameLang":"en"}],"nameIdentifiers":[{"nameIdentifier":"460902","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"福士 清","creatorNameLang":"en"}],"nameIdentifiers":[{"nameIdentifier":"460903","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"入江 俊章","creatorNameLang":"en"}],"nameIdentifiers":[{"nameIdentifier":"460904","nameIdentifierScheme":"WEKO"}]}]},"item_language":{"attribute_name":"言語","attribute_value_mlt":[{"subitem_language":"eng"}]},"item_resource_type":{"attribute_name":"資源タイプ","attribute_value_mlt":[{"resourcetype":"journal article","resourceuri":"http://purl.org/coar/resource_type/c_6501"}]},"item_title":"Effects of Halogenation on Tyrosine Phosphorylation and Peptide Binding to the Src Homology 2 Domain of Lymphocyte-Specific Protein Tyrosine Kinase","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"Effects of Halogenation on Tyrosine Phosphorylation and Peptide Binding to the Src Homology 2 Domain of Lymphocyte-Specific Protein Tyrosine Kinase"}]},"item_type_id":"8","owner":"1","path":["1"],"pubdate":{"attribute_name":"公開日","attribute_value":"2012-02-24"},"publish_date":"2012-02-24","publish_status":"0","recid":"46273","relation_version_is_last":true,"title":["Effects of Halogenation on Tyrosine Phosphorylation and Peptide Binding to the Src Homology 2 Domain of Lymphocyte-Specific Protein Tyrosine Kinase"],"weko_creator_id":"1","weko_shared_id":-1},"updated":"2023-05-15T23:53:49.583678+00:00"}