{"created":"2023-07-27T06:39:06.569653+00:00","id":27428,"links":{},"metadata":{"_buckets":{"deposit":"c6e761b0-1468-4b29-af79-7205bd17caf7"},"_deposit":{"created_by":3,"id":"27428","owners":[3],"pid":{"revision_id":0,"type":"depid","value":"27428"},"status":"published"},"_oai":{"id":"oai:kanazawa-u.repo.nii.ac.jp:00027428","sets":["1777:1778:1779"]},"author_link":["47690","47689","23232","47688"],"item_4_biblio_info_8":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"1991-01-01","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"11","bibliographicPageEnd":"2684","bibliographicPageStart":"2679","bibliographicVolumeNumber":"72","bibliographic_titles":[{"bibliographic_title":"Journal of General Virology"}]}]},"item_4_description_21":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"Processing of the measles virus haemagglutinin (H) protein was analysed by the pulse-chase method, immunoprecipitation with an anti-H monoclonal antibody and SDS-polyacrylamide gel electrophoresis, combined with the addition of carbonyl cyanide m-chlorophenylhydrazone (CCCP) or monensin (inhibitors of intracellular processing of secretory proteins) to cultures and digestion of the protein with endoglycosidase H or neuraminidase. The apparent M(r) of the H protein was increased from 74K to 78K during the chase period. Addition of either CCCP or monensin to the chase medium inhibited the appearance of the 78K H protein, but not the immunoreactivity of the H protein or dimer formation, suggesting that these two events occur in the rough endoplasmic reticulum. The 74K H protein processed in the presence of CCCP was fully sensitive to endoglycosidase H digestion, whereas the 74K H protein processed in the presence of monensin was partially resistant to endoglycosidase H. In experiments using 3H-labelled sugars, [3H]galactose was incorporated into the 74K H protein in the presence of monensin. Neuraminidase treatment increased the electrophoretic mobility of the 78K H protein to 74K. Only the 78K H protein was detected on the surface of untreated cells, and it was resistant to endoglycosidase H digestion. These data suggest that after galactose addition sialic acid is added to the H protein in the trans-Golgi complex and then the mature 78K H protein is transported to the cell surface.","subitem_description_type":"Abstract"}]},"item_4_publisher_17":{"attribute_name":"出版者","attribute_value_mlt":[{"subitem_publisher":"Society for General Microbiology"}]},"item_4_relation_12":{"attribute_name":"DOI","attribute_value_mlt":[{"subitem_relation_type":"isIdenticalTo","subitem_relation_type_id":{"subitem_relation_type_id_text":"https://doi.org/10.1099/0022-1317-72-11-2679","subitem_relation_type_select":"DOI"}}]},"item_4_source_id_11":{"attribute_name":"NCID","attribute_value_mlt":[{"subitem_source_identifier":"AA00698722","subitem_source_identifier_type":"NCID"}]},"item_4_source_id_9":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"0022-1317","subitem_source_identifier_type":"ISSN"}]},"item_4_version_type_25":{"attribute_name":"著者版フラグ","attribute_value_mlt":[{"subitem_version_resource":"http://purl.org/coar/version/c_970fb48d4fbd8a85","subitem_version_type":"VoR"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"Ogura, Hisashi"}],"nameIdentifiers":[{},{}]},{"creatorNames":[{"creatorName":"Sato, Hiroshi"}],"nameIdentifiers":[{},{},{}]},{"creatorNames":[{"creatorName":"Kamiya, Shigeru"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Nakamura, Shinichi"}],"nameIdentifiers":[{}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2017-10-05"}],"displaytype":"detail","filename":"CA-PR-SATO-H-2679.pdf","filesize":[{"value":"3.4 MB"}],"format":"application/pdf","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"CA-PR-SATO-H-2679.pdf","url":"https://kanazawa-u.repo.nii.ac.jp/record/27428/files/CA-PR-SATO-H-2679.pdf"},"version_id":"ff1d632c-4430-423c-b06d-92f27dd7b0e5"}]},"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":"Glycosylation of measles virus haemagglutinin protein in infected cells","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"Glycosylation of measles virus haemagglutinin protein in infected cells"}]},"item_type_id":"4","owner":"3","path":["1779"],"pubdate":{"attribute_name":"公開日","attribute_value":"2017-10-05"},"publish_date":"2017-10-05","publish_status":"0","recid":"27428","relation_version_is_last":true,"title":["Glycosylation of measles virus haemagglutinin protein in infected cells"],"weko_creator_id":"3","weko_shared_id":3},"updated":"2023-07-27T11:10:34.516751+00:00"}