{"_buckets": {"deposit": "971f4ae6-8c14-41d2-9c78-df5283119903"}, "_deposit": {"id": "4064", "owners": [], "pid": {"revision_id": 0, "type": "depid", "value": "4064"}, "status": "published"}, "_oai": {"id": "oai:soar-ir.repo.nii.ac.jp:00004064", "sets": ["461:462"]}, "item_6_biblio_info_6": {"attribute_name": "\u66f8\u8a8c\u60c5\u5831", "attribute_value_mlt": [{"bibliographicIssueDates": {"bibliographicIssueDate": "2006-09-15", "bibliographicIssueDateType": "Issued"}, "bibliographicIssueNumber": "6", "bibliographicPageEnd": "1894", "bibliographicPageStart": "1887", "bibliographicVolumeNumber": "108", "bibliographic_titles": [{"bibliographic_title": "Blood"}]}]}, "item_6_description_19": {"attribute_name": "\u5185\u5bb9\u8a18\u8ff0", "attribute_value_mlt": [{"subitem_description": "This research was originally published in Blood. Author(s).Kani, S; Terasawa, F; Yamauchi, K; Tozuka, M; Okumura, N. Title. Blood. 2006;108:1887-1894. \u00a9 by the American Society of Hematology.", "subitem_description_type": "Other"}]}, "item_6_description_30": {"attribute_name": "\u8cc7\u6e90\u30bf\u30a4\u30d7\uff08\u30b3\u30f3\u30c6\u30f3\u30c4\u306e\u7a2e\u985e\uff09", "attribute_value_mlt": [{"subitem_description": "Article", "subitem_description_type": "Other"}]}, "item_6_description_31": {"attribute_name": "\u30d5\u30a9\u30fc\u30de\u30c3\u30c8\uff1amime\u30bf\u30a4\u30d7", "attribute_value_mlt": [{"subitem_description": "application/pdf", "subitem_description_type": "Other"}]}, "item_6_description_5": {"attribute_name": "\u5f15\u7528", "attribute_value_mlt": [{"subitem_description": "BLOOD. 108(6): 1887-1894 (2006)", "subitem_description_type": "Other"}]}, "item_6_link_3": {"attribute_name": "\u4fe1\u5dde\u5927\u5b66\u7814\u7a76\u8005\u7dcf\u89a7\u3078\u306e\u30ea\u30f3\u30af", "attribute_value_mlt": [{"subitem_link_text": "Okumura, N", "subitem_link_url": "http://soar-rd.shinshu-u.ac.jp/profile/ja.OVnmgCkh.html"}]}, "item_6_link_67": {"attribute_name": "WoS", "attribute_value_mlt": [{"subitem_link_text": "Web of Science", "subitem_link_url": "http://gateway.isiknowledge.com/gateway/Gateway.cgi?\u0026GWVersion=2\u0026SrcAuth=ShinshuUniv\u0026SrcApp=ShinshuUniv\u0026DestLinkType=FullRecord\u0026DestApp=WOS\u0026KeyUT=000240394800024"}]}, "item_6_publisher_4": {"attribute_name": "\u51fa\u7248\u8005", "attribute_value_mlt": [{"subitem_publisher": "AMER SOC HEMATOLOGY"}]}, "item_6_relation_48": {"attribute_name": "DOI", "attribute_value_mlt": [{"subitem_relation_name": [{"subitem_relation_name_text": "10.1182/blood-2006-04-016485"}], "subitem_relation_type_id": {"subitem_relation_type_id_text": "http://dx.doi.org/10.1182/blood-2006-04-016485", "subitem_relation_type_select": "DOI"}}]}, "item_6_select_64": {"attribute_name": "\u8457\u8005\u7248\u30d5\u30e9\u30b0", "attribute_value_mlt": [{"subitem_select_item": "author"}]}, "item_6_source_id_35": {"attribute_name": "ISSN", "attribute_value_mlt": [{"subitem_source_identifier": "0006-4971", "subitem_source_identifier_type": "ISSN"}]}, "item_6_source_id_39": {"attribute_name": "NII ISSN", "attribute_value_mlt": [{"subitem_source_identifier": "0006-4971", "subitem_source_identifier_type": "ISSN"}]}, "item_6_source_id_40": {"attribute_name": "\u66f8\u8a8c\u30ec\u30b3\u30fc\u30c9ID", "attribute_value_mlt": [{"subitem_source_identifier": "AA00567156", "subitem_source_identifier_type": "NCID"}]}, "item_6_text_70": {"attribute_name": "wosonly keywords", "attribute_value_mlt": [{"subitem_text_value": "GLY-HIS-ARG; RECOMBINANT FIBRINOGEN; CRYSTAL-STRUCTURES; INTACT FIBRINOGEN; ALPHA-GAMMA; BETA-GAMMA; FRAGMENT-D; POLYMERIZATION; GAMMA-153CYS; SUBSTITUTION"}]}, "item_6_textarea_68": {"attribute_name": "wosonly abstract", "attribute_value_mlt": [{"subitem_textarea_value": "To examine the role of fibrinogen gamma-chain residue 387Ile in the assembly and secretion of this multichain protein, we synthesized a series of variants with substitution at gamma 387 by Arg, Leu, Met, Ala, or Asp. Only the variant gamma 387Asp showed impaired synthesis in the cells and very low secretion into the medium. In addition, we performed thrombin-catalyzed fibrin polymerization and factor (F) XIIIa-catalyzed cross-linking of the gamma-chain for 4 variants. The degree of lateral aggregation of proto-fibrils into fibrin fibers was slightly reduced for gamma 387Arg and Ala, and moderately reduced for gamma 387Leu and Met. Although the FXIIIa-catalyzed cross-linking for all of the variants was slower than that for gamma 387Ile, that of gamma 387Arg was much more markedly impaired than that of the others. In summary, our studies demonstrated that the specific residue at gamma 387 or the conformation of gamma 388-411 residues, but not the length of the gamma C tail, is critical for fibrinogen assembly and subsequent secretion. Moreover, this residue or the conformation is also important for not only the lateral aggregation of fibrin polymers but also the FXIIIa-catalyzed cross-linking of the gamma-chain. Interestingly, our results clearly indicate that the conformations critical for these 2 functions are different from each other."}]}, "item_creator": {"attribute_name": "\u8457\u8005", "attribute_type": "creator", "attribute_value_mlt": [{"creatorNames": [{"creatorName": "Kani,  S"}], "nameIdentifiers": [{"nameIdentifier": "8983", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "Terasawa,  F"}], "nameIdentifiers": [{"nameIdentifier": "8984", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "Yamauchi,  K"}], "nameIdentifiers": [{"nameIdentifier": "8985", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "Tozuka,  M"}], "nameIdentifiers": [{"nameIdentifier": "8986", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "Okumura,  N"}], "nameIdentifiers": [{"nameIdentifier": "8987", "nameIdentifierScheme": "WEKO"}]}]}, "item_files": {"attribute_name": "\u30d5\u30a1\u30a4\u30eb\u60c5\u5831", "attribute_type": "file", "attribute_value_mlt": [{"accessrole": "open_date", "date": [{"dateType": "Available", "dateValue": "2015-09-24"}], "displaytype": "detail", "download_preview_message": "", "file_order": 0, "filename": "BLOODmanuscript.pdf", "filesize": [{"value": "909.2 kB"}], "format": "application/pdf", "future_date_message": "", "is_thumbnail": false, "licensetype": "license_free", "mimetype": "application/pdf", "size": 909200.0, "url": {"label": "BLOODmanuscript.pdf", "url": "https://soar-ir.repo.nii.ac.jp/record/4064/files/BLOODmanuscript.pdf"}, "version_id": "50e4eb6c-e269-422c-b182-c30d6da15972"}]}, "item_language": {"attribute_name": "\u8a00\u8a9e", "attribute_value_mlt": [{"subitem_language": "eng"}]}, "item_resource_type": {"attribute_name": "\u8cc7\u6e90\u30bf\u30a4\u30d7", "attribute_value_mlt": [{"resourcetype": "journal article", "resourceuri": "http://purl.org/coar/resource_type/c_6501"}]}, "item_title": "Analysis of fibrinogen variants at gamma 387Ile shows that the side chain of gamma 387 and the tertiary structure of the gamma C-terminal tail are important not only for assembly and secretion of fibrinogen but also for lateral aggregation of protofibrils and XIIIa-catalyzed gamma-gamma dimer formation", "item_titles": {"attribute_name": "\u30bf\u30a4\u30c8\u30eb", "attribute_value_mlt": [{"subitem_title": "Analysis of fibrinogen variants at gamma 387Ile shows that the side chain of gamma 387 and the tertiary structure of the gamma C-terminal tail are important not only for assembly and secretion of fibrinogen but also for lateral aggregation of protofibrils and XIIIa-catalyzed gamma-gamma dimer formation"}]}, "item_type_id": "6", "owner": "1", "path": ["461/462"], "permalink_uri": "http://hdl.handle.net/10091/189", "pubdate": {"attribute_name": "\u516c\u958b\u65e5", "attribute_value": "2007-04-25"}, "publish_date": "2007-04-25", "publish_status": "0", "recid": "4064", "relation": {}, "relation_version_is_last": true, "title": ["Analysis of fibrinogen variants at gamma 387Ile shows that the side chain of gamma 387 and the tertiary structure of the gamma C-terminal tail are important not only for assembly and secretion of fibrinogen but also for lateral aggregation of protofibrils and XIIIa-catalyzed gamma-gamma dimer formation"], "weko_shared_id": null}