[{"data":1,"prerenderedAt":-1},["ShallowReactive",2],{"_public_publisher_byId_c659ed6e-3450-4714-8476-0aa768719b3c":3,"_public_publication_all{\"sortAscending\":false,\"sortField\":\"updateTime\",\"page\":0,\"size\":10,\"facet\":true,\"searchKey\":\"publisherId:c659ed6e-3450-4714-8476-0aa768719b3c,\"}":81},{"code":4,"data":5,"meta":18},"SUCCESS",{"id":6,"createTime":7,"updateTime":8,"relativeEntities":9,"slug":10,"properties":11,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":20,"manageAffiliations":29,"indexDatabases":42,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},"c659ed6e-3450-4714-8476-0aa768719b3c","2023-12-05T06:52:46.657+00:00","2025-11-21T10:00:12.356+00:00",[],"Biophysical-Journal",{"issn":12,"title":14},{"VOID":13},"00063495",{"EN":15},"Biophysical Journal","PUBLISHER","PENDING",null,0,[21],{"id":22,"createTime":23,"updateTime":24,"relativeEntities":25,"label":26,"description":28,"parentId":18,"standard":18,"scholarHubFieldId":18},"a86091b2-a11b-4669-b693-653762a75923","2023-05-29T10:24:31.583+00:00","2023-11-21T08:11:28.198+00:00",[],{"EN":27},"Biophysics",{},[30],{"id":31,"createTime":32,"updateTime":33,"relativeEntities":34,"slug":35,"properties":36,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":40,"url":18,"parentIds":41,"statistic":18},"a4a936f8-3ebf-415c-94f9-5c50afa26a67","2023-05-29T10:24:30.972+00:00","2025-11-21T10:02:45.925+00:00",[],"Cell-Press",{"title":37},{"EN":38},"Cell Press","AFFILIATION",7,[],[43,62],{"id":44,"indexDatabase":45,"url":59,"indexYears":18,"academicFieldIds":60,"indexDatabaseRanking":18},"93007b82-315c-4ca3-a205-3a3872fc6ce6",{"id":46,"createTime":47,"updateTime":48,"relativeEntities":49,"label":50,"description":52,"key":55,"publicationTags":56,"standard":18},"a4921856-b128-4d9f-8f1f-e80813d3bbd4","2023-05-22T09:59:31.026+00:00","2025-11-21T10:07:52.153+00:00",[],{"EN":51,"VI":51},"ISI\u002FSCIE - Science Citation Index Expanded",{"VI":53,"EN":54},"Cơ sở dữ liệu SCIE","SCIE database","scie",[57,58],"SCIE","ISI","https:\u002F\u002Fmjl.clarivate.com\u002Fsearch-results?issn=0006-3495",[61],"d875699a-416e-4523-bcb9-17b1b64de061",{"id":63,"indexDatabase":64,"url":76,"indexYears":77,"academicFieldIds":78,"indexDatabaseRanking":80},"a8374f8a-be13-4d3f-97f2-3264d460438f",{"id":65,"createTime":66,"updateTime":67,"relativeEntities":68,"label":69,"description":71,"key":73,"publicationTags":74,"standard":18},"3c7051d4-eb7d-4c57-a56b-36fc74c5d1e9","2023-05-22T09:57:18.509+00:00","2025-11-21T10:07:52.274+00:00",[],{"EN":70,"VI":70},"Scopus - Elsevier",{"EN":70,"VI":72},"Cơ sở dữ liệu Scopus thuộc Elsevier","scopus",[75],"SCOPUS","https:\u002F\u002Fwww.scopus.com\u002Fsourceid\u002F14859","1960-2025",[79],"de92cf1a-2f51-4173-92e5-47b52fde9929","SCOPUS__Q1",{"meta":82,"data":84},{"total":83},"12064",[85,167,266,312,392,498,577,724,821,988],{"id":86,"createTime":87,"updateTime":88,"relativeEntities":89,"slug":90,"properties":91,"entityType":102,"verifyStatus":17,"verifyTime":88,"verifyNote":103,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":104,"fullTextUrl":18,"authors":105,"publicationType":135,"publisherRelationship":136,"citationCount":18,"citationInfo":18,"publishDate":164,"publishYear":165,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":166},"d1909ade-becb-47cb-a103-b0b99370b8e4","2023-11-03T19:39:39.131+00:00","2025-01-23T23:59:47.233+00:00",[],"The-Bacillus-subtilis-RNA-Helicase-YxiN-is-Distended-in-Solution",{"pii":92,"references":94,"abstract":96,"title":98,"doi":100},{"VOID":93},"S0006349508707550",{"VOID":95},"null\nnull\nnull\nnull\nnull\nnull\nnull\nnull\nnull\nnull\nnull\nnull\nnull\nnull",{"EN":97},"The Bacillus subtilis YxiN protein is a modular three-domain RNA helicase of the DEx(D\u002FH)-box protein family. The first two domains form the highly conserved helicase core, and the third domain confers RNA target binding specificity. Small angle x-ray scattering on YxiN and two-domain fragments thereof shows that the protein has a distended structure in solution, in contrast to helicases involved in replication processes. These data are consistent with a chaperone activity in which the carboxy-terminal domain of YxiN tethers the protein to the vicinity of its targets and the helicase core is free to transiently interact with RNA duplexes, possibly to melt out misfolded elements of secondary structure.",{"EN":99},"The Bacillus subtilis RNA Helicase YxiN is Distended in Solution",{"VOID":101},"10.1529\u002Fbiophysj.107.120709","PUBLICATION","Author affiliation is blank","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0006349508707550",[106,114,121,128],{"id":107,"sortIndex":19,"researcher":18,"roles":108,"affiliations":110,"properties":111},"200023f1-2b6c-43bd-b34f-7726c820c1b3",[109],"AUTHOR",[],{"title":112},{"VI":113},"YaoXiong Hu",{"id":115,"sortIndex":19,"researcher":18,"roles":116,"affiliations":117,"properties":118},"9ef6c745-bdd1-4af6-b5a2-1f7f32198ca4",[109],[],{"title":119},{"VI":120},"David B. McKay",{"id":122,"sortIndex":19,"researcher":18,"roles":123,"affiliations":124,"properties":125},"2de66227-341e-4324-a2be-c5780770ee92",[109],[],{"title":126},{"VI":127},"Shuying Wang",{"id":129,"sortIndex":19,"researcher":18,"roles":130,"affiliations":131,"properties":132},"e0b29166-f454-4c90-8365-a7aef41fac1d",[109],[],{"title":133},{"VI":134},"Michael T. Overgaard","ARTICLE",{"url":104,"publisher":137,"properties":159},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":138,"slug":10,"properties":139,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":142,"manageAffiliations":143,"indexDatabases":144,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":140,"title":141},{"VOID":13},{"EN":15},[],[],[145,152],{"id":44,"indexDatabase":146,"url":59,"indexYears":18,"academicFieldIds":151,"indexDatabaseRanking":18},{"id":46,"createTime":47,"updateTime":48,"relativeEntities":147,"label":148,"description":149,"key":55,"publicationTags":150,"standard":18},[],{"EN":51,"VI":51},{"VI":53,"EN":54},[57,58],[61],{"id":63,"indexDatabase":153,"url":76,"indexYears":77,"academicFieldIds":158,"indexDatabaseRanking":80},{"id":65,"createTime":66,"updateTime":67,"relativeEntities":154,"label":155,"description":156,"key":73,"publicationTags":157,"standard":18},[],{"EN":70,"VI":70},{"EN":70,"VI":72},[75],[79],{"volume":160,"pages":162},{"VOID":161},"94",{"VOID":163},"L01","2008-01-01",2008,false,{"id":168,"createTime":169,"updateTime":170,"relativeEntities":171,"slug":172,"properties":173,"entityType":102,"verifyStatus":178,"verifyTime":170,"verifyNote":179,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":180,"fullTextUrl":18,"authors":181,"publicationType":135,"publisherRelationship":236,"citationCount":18,"citationInfo":18,"publishDate":264,"publishYear":265,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":166},"a46e2a9b-3f9f-483e-9cc0-79e737e0dedc","2023-12-23T11:23:42.059+00:00","2025-01-16T23:59:37.965+00:00",[],"Probability-assessment-of-conformational-ensembles-sugar-repuckering-in-a-DNA-duplex-in-solution",{"title":174,"doi":176},{"EN":175},"Probability assessment of conformational ensembles: sugar repuckering in a DNA duplex in solution",{"VOID":177},"10.1016\u002Fs0006-3495(95)80181-5","VERIFIED","Auto Verify","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0006349595801815",[182,198,211,223],{"id":183,"sortIndex":184,"researcher":18,"roles":185,"affiliations":186,"properties":195},"64a7222e-5561-4b82-8fbe-0e6668610a10",2,[109],[187],{"id":18,"sortIndex":19,"affiliation":188,"properties":18},{"id":189,"createTime":190,"updateTime":190,"relativeEntities":191,"slug":18,"properties":192,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"2e00878b-e2b5-4dcd-8ee7-36a81ca328cc","2023-12-23T11:23:42.151+00:00",[],{"title":193},{"VI":194},"Department of Pharmaceutical Chemistry, University of California, San Francisco 94143–0446.",{"title":196},{"VI":197},"A. Kumar",{"id":199,"sortIndex":200,"researcher":18,"roles":201,"affiliations":202,"properties":208},"99450db4-71c0-4d2d-9384-2b7ea95e7bc8",3,[109],[203],{"id":18,"sortIndex":19,"affiliation":204,"properties":18},{"id":189,"createTime":190,"updateTime":190,"relativeEntities":205,"slug":18,"properties":206,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":207},{"VI":194},{"title":209},{"VI":210},"T.L. James",{"id":212,"sortIndex":19,"researcher":18,"roles":213,"affiliations":214,"properties":220},"ac5f02a4-ea20-44c2-93a5-5db671533230",[109],[215],{"id":18,"sortIndex":19,"affiliation":216,"properties":18},{"id":189,"createTime":190,"updateTime":190,"relativeEntities":217,"slug":18,"properties":218,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":219},{"VI":194},{"title":221},{"VI":222},"N.B. Ulyanov",{"id":224,"sortIndex":225,"researcher":18,"roles":226,"affiliations":227,"properties":233},"effcc91e-615e-42c4-8ae4-9e1b0090cf98",1,[109],[228],{"id":18,"sortIndex":19,"affiliation":229,"properties":18},{"id":189,"createTime":190,"updateTime":190,"relativeEntities":230,"slug":18,"properties":231,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":232},{"VI":194},{"title":234},{"VI":235},"U. Schmitz",{"url":180,"publisher":237,"properties":259},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":238,"slug":10,"properties":239,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":242,"manageAffiliations":243,"indexDatabases":244,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":240,"title":241},{"VOID":13},{"EN":15},[],[],[245,252],{"id":44,"indexDatabase":246,"url":59,"indexYears":18,"academicFieldIds":251,"indexDatabaseRanking":18},{"id":46,"createTime":47,"updateTime":48,"relativeEntities":247,"label":248,"description":249,"key":55,"publicationTags":250,"standard":18},[],{"EN":51,"VI":51},{"VI":53,"EN":54},[57,58],[61],{"id":63,"indexDatabase":253,"url":76,"indexYears":77,"academicFieldIds":258,"indexDatabaseRanking":80},{"id":65,"createTime":66,"updateTime":67,"relativeEntities":254,"label":255,"description":256,"key":73,"publicationTags":257,"standard":18},[],{"EN":70,"VI":70},{"EN":70,"VI":72},[75],[79],{"volume":260,"pages":262},{"VOID":261},"68",{"VOID":263},"13-24","1995-01-01",1995,{"id":267,"createTime":268,"updateTime":269,"relativeEntities":270,"slug":271,"properties":272,"entityType":102,"verifyStatus":17,"verifyTime":269,"verifyNote":277,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":278,"fullTextUrl":18,"authors":279,"publicationType":135,"publisherRelationship":280,"citationCount":18,"citationInfo":18,"publishDate":310,"publishYear":311,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":166},"474933d2-2549-41d4-81af-dbefee082844","2024-01-30T15:36:15.883+00:00","2024-09-15T23:59:25.864+00:00",[],"Thermal-Imaging-of-Receptor-Activated-Heat-Production-in-Single-Cells",{"title":273,"doi":275},{"EN":274},"Thermal Imaging of Receptor-Activated Heat Production in Single Cells",{"VOID":276},"10.1016\u002FS0006-3495(98)77769-0","Author title is blank","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0006349598777690",[],{"url":278,"publisher":281,"properties":303},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":282,"slug":10,"properties":283,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":286,"manageAffiliations":287,"indexDatabases":288,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":284,"title":285},{"VOID":13},{"EN":15},[],[],[289,296],{"id":44,"indexDatabase":290,"url":59,"indexYears":18,"academicFieldIds":295,"indexDatabaseRanking":18},{"id":46,"createTime":47,"updateTime":48,"relativeEntities":291,"label":292,"description":293,"key":55,"publicationTags":294,"standard":18},[],{"EN":51,"VI":51},{"VI":53,"EN":54},[57,58],[61],{"id":63,"indexDatabase":297,"url":76,"indexYears":77,"academicFieldIds":302,"indexDatabaseRanking":80},{"id":65,"createTime":66,"updateTime":67,"relativeEntities":298,"label":299,"description":300,"key":73,"publicationTags":301,"standard":18},[],{"EN":70,"VI":70},{"EN":70,"VI":72},[75],[79],{"volume":304,"pages":306,"issue":308},{"VOID":305},"74",{"VOID":307},"82-89",{"VOID":309},"1","1998-01-01",1998,{"id":313,"createTime":314,"updateTime":314,"relativeEntities":315,"slug":316,"properties":317,"entityType":102,"verifyStatus":17,"verifyTime":314,"verifyNote":103,"syncStatus":17,"languages":332,"translateLanguages":18,"viewCount":19,"primaryUrl":334,"fullTextUrl":18,"authors":335,"publicationType":135,"publisherRelationship":356,"citationCount":386,"citationInfo":387,"publishDate":389,"publishYear":390,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":391,"isForceReanalyzing":166},"1265473c-c74b-4158-a4b5-5bfc6979d1c1","2024-09-25T23:59:25.823+00:00",[],"Electric-Impedance-and-Rectification-of-Fused-Anion-Cation-Membranes-in-Solution",{"mag":318,"keywords":320,"pmc":321,"openalex":323,"abstract":325,"title":326,"pm":328,"doi":330},{"VOID":319},"2042744424",{},{"VOID":322},"1367461",{"VOID":324},"W2042744424",{},{"EN":327},"Electric Impedance and Rectification of Fused Anion-Cation Membranes in Solution",{"VOID":329},"14130438",{"VOID":331},"10.1016\u002Fs0006-3495(64)86774-6",[333],"EN","https:\u002F\u002Flinkinghub.elsevier.com\u002Fretrieve\u002Fpii\u002FS0006349564867746",[336,347],{"id":337,"sortIndex":19,"researcher":18,"roles":338,"affiliations":339,"properties":340},"2e4b4173-437a-4ded-b4c2-524817f1a4a0",[],[],{"openalex":341,"orcid":343,"title":345},{"VOID":342},"A5059658016",{"VOID":344},"https:\u002F\u002Forcid.org\u002F0000-0002-4544-6554",{"EN":346},"Manuel Schwartz",{"id":348,"sortIndex":225,"researcher":18,"roles":349,"affiliations":350,"properties":351},"1e3bbfdd-49a1-4fda-8f4d-2774db5fa5fd",[],[],{"openalex":352,"title":354},{"VOID":353},"A5046962395",{"EN":355},"Carl T. Case",{"url":18,"publisher":357,"properties":379},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":358,"slug":10,"properties":359,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":362,"manageAffiliations":363,"indexDatabases":364,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":360,"title":361},{"VOID":13},{"EN":15},[],[],[365,372],{"id":44,"indexDatabase":366,"url":59,"indexYears":18,"academicFieldIds":371,"indexDatabaseRanking":18},{"id":46,"createTime":47,"updateTime":48,"relativeEntities":367,"label":368,"description":369,"key":55,"publicationTags":370,"standard":18},[],{"EN":51,"VI":51},{"VI":53,"EN":54},[57,58],[61],{"id":63,"indexDatabase":373,"url":76,"indexYears":77,"academicFieldIds":378,"indexDatabaseRanking":80},{"id":65,"createTime":66,"updateTime":67,"relativeEntities":374,"label":375,"description":376,"key":73,"publicationTags":377,"standard":18},[],{"EN":70,"VI":70},{"EN":70,"VI":72},[75],[79],{"volume":380,"pages":382,"issue":384},{"VOID":381},"4",{"VOID":383},"137-149",{"VOID":385},"2",13,{"total":386,"publishYear":18,"statisticByYear":388},{"2014":225,"2017":225},"1964-03-01",1964,[],{"id":393,"createTime":394,"updateTime":394,"relativeEntities":395,"slug":396,"properties":397,"entityType":102,"verifyStatus":178,"verifyTime":394,"verifyNote":179,"syncStatus":17,"languages":412,"translateLanguages":18,"viewCount":19,"primaryUrl":413,"fullTextUrl":18,"authors":414,"publicationType":135,"publisherRelationship":457,"citationCount":486,"citationInfo":487,"publishDate":495,"publishYear":496,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":497,"isForceReanalyzing":166},"d0b7d494-46b3-48e0-bea7-beec3f2e0260","2024-09-25T23:59:24.445+00:00",[],"A-Quantitative-Analysis-of-the-Voltage-Current-Relationships-of-Fixed-Charge-Membranes-and-the-Associated-Property-of-Punch-Through-",{"mag":398,"keywords":400,"pmc":401,"openalex":403,"abstract":405,"title":406,"pm":408,"doi":410},{"VOID":399},"1965721419",{},{"VOID":402},"1367766",{"VOID":404},"W1965721419",{},{"EN":407},"A Quantitative Analysis of the Voltage-Current Relationships of Fixed Charge Membranes and the Associated Property of “Punch-Through”",{"VOID":409},"5863437",{"VOID":411},"10.1016\u002Fs0006-3495(65)86745-5",[333],"https:\u002F\u002Flinkinghub.elsevier.com\u002Fretrieve\u002Fpii\u002FS0006349565867455",[415],{"id":416,"sortIndex":19,"researcher":18,"roles":417,"affiliations":418,"properties":450},"c03ccb47-f2ab-4a2e-9917-fcc65f26d826",[],[419,430,440],{"id":420,"sortIndex":184,"affiliation":421,"properties":18},"3562f9f3-1d89-4121-b077-4f70fc56ec51",{"id":422,"createTime":423,"updateTime":424,"relativeEntities":425,"slug":426,"properties":427,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"e2349b7a-2920-4dd8-8853-dbae0d196c5c","2024-02-07T07:11:10.366+00:00","2025-02-10T07:28:19.487+00:00",[],"School-of-Biological-Sciences-University-of-Sydney-Sydney-New-South-Wales-Australia",{"title":428},{"VI":429},"School of Biological Sciences, University of Sydney, Sydney, New South Wales, Australia",{"id":431,"sortIndex":19,"affiliation":432,"properties":18},"155aa4e8-8109-4187-914a-eefdf83998d1",{"id":433,"createTime":434,"updateTime":434,"relativeEntities":435,"slug":436,"properties":437,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"865e2755-c07a-4cc8-ac45-f830b1b94ab9","2024-09-25T23:59:24.460+00:00",[],"Division-of-Food-Preservation-and",{"title":438},{"EN":439},"Division of Food Preservation and",{"id":441,"sortIndex":225,"affiliation":442,"properties":18},"43509d8e-8899-4be5-9e21-1963193acc39",{"id":443,"createTime":444,"updateTime":444,"relativeEntities":445,"slug":446,"properties":447,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"329b89a7-fa95-491d-a9be-6e198f880d03","2024-09-25T23:59:24.463+00:00",[],"From-the-Plant-Physiology-Unit-",{"title":448},{"EN":449},"From the Plant Physiology Unit,",{"openalex":451,"orcid":453,"title":455},{"VOID":452},"A5047065377",{"VOID":454},"https:\u002F\u002Forcid.org\u002F0000-0001-7306-1793",{"EN":456},"H.G.L. Coster",{"url":18,"publisher":458,"properties":480},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":459,"slug":10,"properties":460,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":463,"manageAffiliations":464,"indexDatabases":465,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":461,"title":462},{"VOID":13},{"EN":15},[],[],[466,473],{"id":44,"indexDatabase":467,"url":59,"indexYears":18,"academicFieldIds":472,"indexDatabaseRanking":18},{"id":46,"createTime":47,"updateTime":48,"relativeEntities":468,"label":469,"description":470,"key":55,"publicationTags":471,"standard":18},[],{"EN":51,"VI":51},{"VI":53,"EN":54},[57,58],[61],{"id":63,"indexDatabase":474,"url":76,"indexYears":77,"academicFieldIds":479,"indexDatabaseRanking":80},{"id":65,"createTime":66,"updateTime":67,"relativeEntities":475,"label":476,"description":477,"key":73,"publicationTags":478,"standard":18},[],{"EN":70,"VI":70},{"EN":70,"VI":72},[75],[79],{"volume":481,"pages":483,"issue":485},{"VOID":482},"5",{"VOID":484},"669-686",{"VOID":482},289,{"total":486,"publishYear":18,"statisticByYear":488},{"2012":489,"2013":490,"2014":491,"2015":40,"2016":492,"2017":489,"2018":493,"2019":494,"2020":493,"2021":200,"2022":489,"2023":493,"2024":225},5,8,11,10,4,6,"1965-09-01",1965,[],{"id":499,"createTime":500,"updateTime":500,"relativeEntities":501,"slug":502,"properties":503,"entityType":102,"verifyStatus":178,"verifyTime":500,"verifyNote":179,"syncStatus":17,"languages":518,"translateLanguages":18,"viewCount":19,"primaryUrl":519,"fullTextUrl":18,"authors":520,"publicationType":135,"publisherRelationship":543,"citationCount":571,"citationInfo":572,"publishDate":574,"publishYear":575,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":576,"isForceReanalyzing":166},"d576d707-d9b6-4a65-a0b9-03b0e94306ca","2024-09-25T23:59:24.965+00:00",[],"Space-Charge-Regions-in-Fixed-Charge-Membranes-and-the-Associated-Property-of-Capacitance",{"mag":504,"keywords":506,"pmc":507,"openalex":509,"abstract":511,"title":512,"pm":514,"doi":516},{"VOID":505},"2088932125",{},{"VOID":508},"1366404",{"VOID":510},"W2088932125",{},{"EN":513},"Space Charge Regions in Fixed Charge Membranes and the Associated Property of Capacitance",{"VOID":515},"19431319",{"VOID":517},"10.1016\u002Fs0006-3495(62)86848-9",[333],"https:\u002F\u002Flinkinghub.elsevier.com\u002Fretrieve\u002Fpii\u002FS0006349562868489",[521],{"id":522,"sortIndex":19,"researcher":18,"roles":523,"affiliations":524,"properties":536},"59456542-2a16-447e-85a3-6fd43d34e6bb",[],[525],{"id":526,"sortIndex":19,"affiliation":527,"properties":18},"37a13a43-f095-46c7-8d8a-b9d052e60118",{"id":528,"createTime":529,"updateTime":530,"relativeEntities":531,"slug":532,"properties":533,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"932617c0-913d-4d78-8930-56a55ef2ebc9","2024-08-31T16:04:29.329+00:00","2025-02-06T09:58:30.025+00:00",[],"From-The-Rockefeller-Institute",{"title":534},{"EN":535},"From The Rockefeller Institute",{"openalex":537,"orcid":539,"title":541},{"VOID":538},"A5067735705",{"VOID":540},"https:\u002F\u002Forcid.org\u002F0000-0003-4466-3378",{"EN":542},"Alexander Mauro",{"url":18,"publisher":544,"properties":566},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":545,"slug":10,"properties":546,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":549,"manageAffiliations":550,"indexDatabases":551,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":547,"title":548},{"VOID":13},{"EN":15},[],[],[552,559],{"id":44,"indexDatabase":553,"url":59,"indexYears":18,"academicFieldIds":558,"indexDatabaseRanking":18},{"id":46,"createTime":47,"updateTime":48,"relativeEntities":554,"label":555,"description":556,"key":55,"publicationTags":557,"standard":18},[],{"EN":51,"VI":51},{"VI":53,"EN":54},[57,58],[61],{"id":63,"indexDatabase":560,"url":76,"indexYears":77,"academicFieldIds":565,"indexDatabaseRanking":80},{"id":65,"createTime":66,"updateTime":67,"relativeEntities":561,"label":562,"description":563,"key":73,"publicationTags":564,"standard":18},[],{"EN":70,"VI":70},{"EN":70,"VI":72},[75],[79],{"volume":567,"pages":568,"issue":570},{"VOID":385},{"VOID":569},"179-198",{"VOID":385},208,{"total":571,"publishYear":18,"statisticByYear":573},{"2012":184,"2013":225,"2014":40,"2015":492,"2016":200,"2017":200,"2018":225,"2019":494,"2020":489,"2021":200,"2022":489,"2023":490,"2024":184},"1962-03-01",1962,[],{"id":578,"createTime":579,"updateTime":579,"relativeEntities":580,"slug":18,"properties":581,"entityType":102,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":588,"fullTextUrl":18,"authors":589,"publicationType":135,"publisherRelationship":694,"citationCount":18,"citationInfo":18,"publishDate":722,"publishYear":723,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":166},"e6de65f6-4708-47af-bac3-44f32af5133d","2023-12-13T23:59:15.269+00:00",[],{"references":582,"title":584,"doi":586},{"VOID":583},"Prusiner, 1998, Prions, Proc. Natl. Acad. Sci. USA, 95, 13363, 10.1073\u002Fpnas.95.23.13363\nAguzzi, 2004, Mammalian prion biology: one century of evolving concepts, Cell, 116, 313, 10.1016\u002FS0092-8674(03)01031-6\nStöhr, 2008, Mechanisms of prion protein assembly into amyloid, Proc. Natl. Acad. Sci. USA, 105, 2409, 10.1073\u002Fpnas.0712036105\nAguzzi, 2008, Molecular mechanisms of prion pathogenesis, Annu. Rev. Pathol., 3, 11, 10.1146\u002Fannurev.pathmechdis.3.121806.154326\nSandberg, 2011, Prion propagation and toxicity in vivo occur in two distinct mechanistic phases, Nature, 470, 540, 10.1038\u002Fnature09768\nSoto, 2011, Prion hypothesis: the end of the controversy?, Trends Biochem. Sci., 36, 151, 10.1016\u002Fj.tibs.2010.11.001\nBarlow, 1976, The fate of ME7 scrapie infection in rats, guinea-pigs and rabbits, Res. Vet. Sci., 21, 110, 10.1016\u002FS0034-5288(18)33406-4\nGibbs, 1973, Experimental subacute spongiform virus encephalopathies in primates and other laboratory animals, Science, 182, 67, 10.1126\u002Fscience.182.4107.67\nLoftus, 1997, Characterization of a prion protein (PrP) gene from rabbit; a species with apparent resistance to infection by prions, Gene, 184, 215, 10.1016\u002FS0378-1119(96)00598-7\nVorberg, 2003, Multiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoform, J. Virol., 77, 2003, 10.1128\u002FJVI.77.3.2003-2009.2003\nSoto, 2009, Constraining the loop, releasing prion infectivity, Proc. Natl. Acad. Sci. USA, 106, 10, 10.1073\u002Fpnas.0811625106\nSigurdson, 2009, De novo generation of a transmissible spongiform encephalopathy by mouse transgenesis, Proc. Natl. Acad. Sci. USA, 106, 304, 10.1073\u002Fpnas.0810680105\nWen, 2010, Unique structural characteristics of the rabbit prion protein, J. Biol. Chem., 285, 31682, 10.1074\u002Fjbc.M110.118844\nKhan, 2010, Prion disease susceptibility is affected by β-structure folding propensity and local side-chain interactions in PrP, Proc. Natl. Acad. Sci. USA, 107, 19808, 10.1073\u002Fpnas.1005267107\nNisbet, 2010, Residues surrounding the glycosylphosphatidylinositol anchor attachment site of PrP modulate prion infection: insight from the resistance of rabbits to prion disease, J. Virol., 84, 6678, 10.1128\u002FJVI.02709-09\nFernandez-Funez, 2010, Sequence-dependent prion protein misfolding and neurotoxicity, J. Biol. Chem., 285, 36897, 10.1074\u002Fjbc.M110.174391\nBocharova, 2005, In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrPSc, J. Mol. Biol., 346, 645, 10.1016\u002Fj.jmb.2004.11.068\nBocharova, 2006, Annealing prion protein amyloid fibrils at high temperature results in extension of a proteinase K-resistant core, J. Biol. Chem., 281, 2373, 10.1074\u002Fjbc.M510840200\nLührs, 2006, Amyloid formation by recombinant full-length prion proteins in phospholipid bicelle solutions, J. Mol. Biol., 357, 833, 10.1016\u002Fj.jmb.2006.01.016\nMo, 2009, Low micromolar zinc accelerates the fibrillization of human Tau via bridging of Cys-291 and Cys-322, J. Biol. Chem., 284, 34648, 10.1074\u002Fjbc.M109.058883\nZhu, 2010, Quantitative characterization of heparin binding to Tau protein: implication for inducer-mediated Tau filament formation, J. Biol. Chem., 285, 3592, 10.1074\u002Fjbc.M109.035691\nBellotti, 2008, Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases, Curr. Opin. Struct. Biol., 18, 771, 10.1016\u002Fj.sbi.2008.10.001\nEllis, 2001, Macromolecular crowding: an important but neglected aspect of the intracellular environment, Curr. Opin. Struct. Biol., 11, 114, 10.1016\u002FS0959-440X(00)00172-X\nEllis, 2006, Protein aggregation in crowded environments, Biol. Chem., 387, 485, 10.1515\u002FBC.2006.064\nZhou, 2008, Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences, Annu. Rev. Biophys., 37, 375, 10.1146\u002Fannurev.biophys.37.032807.125817\nZhou, 2004, Mixed macromolecular crowding accelerates the oxidative refolding of reduced, denatured lysozyme: implications for protein folding in intracellular environments, J. Biol. Chem., 279, 55109, 10.1074\u002Fjbc.M409086200\nDu, 2006, Mixed macromolecular crowding accelerates the refolding of rabbit muscle creatine kinase: implications for protein folding in physiological environments, J. Mol. Biol., 364, 469, 10.1016\u002Fj.jmb.2006.09.018\nZhou, 2009, Crowded cell-like environment accelerates the nucleation step of amyloidogenic protein misfolding, J. Biol. Chem., 284, 30148, 10.1074\u002Fjbc.M109.002832\nJiao, 2010, Attractive protein-polymer interactions markedly alter the effect of macromolecular crowding on protein association equilibria, Biophys. J., 99, 914, 10.1016\u002Fj.bpj.2010.05.013\nBokvist, 2007, Misfolding of amyloidogenic proteins at membrane surfaces: the impact of macromolecular crowding, J. Am. Chem. Soc., 129, 14848, 10.1021\u002Fja076059o\nShtilerman, 2002, Molecular crowding accelerates fibrillization of α-synuclein: could an increase in the cytoplasmic protein concentration induce Parkinson's disease?, Biochemistry, 41, 3855, 10.1021\u002Fbi0120906\nUversky, 2002, Accelerated α-synuclein fibrillation in crowded milieu, FEBS Lett., 515, 99, 10.1016\u002FS0014-5793(02)02446-8\nHatters, 2002, Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II, J. Biol. Chem., 277, 7824, 10.1074\u002Fjbc.M110429200\nBaron, 2002, Conversion of raft associated prion protein to the protease-resistant state requires insertion of PrP-res (PrPSc) into contiguous membranes, EMBO J., 21, 1031, 10.1093\u002Femboj\u002F21.5.1031\nChesebro, 2010, Fatal transmissible amyloid encephalopathy: a new type of prion disease associated with lack of prion protein membrane anchoring, PLoS Pathog., 6, e1000800, 10.1371\u002Fjournal.ppat.1000800\nChattopadhyay, 2008, Initiation and elongation in fibrillation of ALS-linked superoxide dismutase, Proc. Natl. Acad. Sci. USA, 105, 18663, 10.1073\u002Fpnas.0807058105\nNaiki, 1989, Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1, Anal. Biochem., 177, 244, 10.1016\u002F0003-2697(89)90046-8\nPrusiner, 1983, Scrapie prions aggregate to form amyloid-like birefringent rods, Cell, 35, 349, 10.1016\u002F0092-8674(83)90168-X\nHope, 1988, Fibrils from brains of cows with new cattle disease contain scrapie-associated protein, Nature, 336, 390, 10.1038\u002F336390a0\nGasset, 1993, Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity, Proc. Natl. Acad. Sci. USA, 90, 1, 10.1073\u002Fpnas.90.1.1\nJackson, 1999, Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations, Science, 283, 1935, 10.1126\u002Fscience.283.5409.1935\nPan, 1993, Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins, Proc. Natl. Acad. Sci. USA, 90, 10962, 10.1073\u002Fpnas.90.23.10962\nZandomeneghi, 2004, FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils, Protein Sci., 13, 3314, 10.1110\u002Fps.041024904\nBolton, 1982, Identification of a protein that purifies with the scrapie prion, Science, 218, 1309, 10.1126\u002Fscience.6815801\nMcKinley, 1983, A protease-resistant protein is a structural component of the scrapie prion, Cell, 35, 57, 10.1016\u002F0092-8674(83)90207-6\nNotari, 2008, Characterization of truncated forms of abnormal prion protein in Creutzfeldt-Jakob disease, J. Biol. Chem., 283, 30557, 10.1074\u002Fjbc.M801877200\nParchi, 2000, Genetic influence on the structural variations of the abnormal prion protein, Proc. Natl. Acad. Sci. USA, 97, 10168, 10.1073\u002Fpnas.97.18.10168\nQin, 2009, Atomistic modeling of macromolecular crowding predicts modest increases in protein folding and binding stability, Biophys. J., 97, 12, 10.1016\u002Fj.bpj.2009.03.066\nBatra, 2009, Effect of macromolecular crowding on protein binding stability: modest stabilization and significant biological consequences, Biophys. J., 97, 906, 10.1016\u002Fj.bpj.2009.05.032\nOstapchenko, 2010, Two amyloid States of the prion protein display significantly different folding patterns, J. Mol. Biol., 400, 908, 10.1016\u002Fj.jmb.2010.05.051\nCobb, 2007, Molecular architecture of human prion protein amyloid: a parallel, in-register β-structure, Proc. Natl. Acad. Sci. USA, 104, 18946, 10.1073\u002Fpnas.0706522104\nLu, 2007, β-sheet core of human prion protein amyloid fibrils as determined by hydrogen\u002Fdeuterium exchange, Proc. Natl. Acad. Sci. USA, 104, 1510, 10.1073\u002Fpnas.0608447104\nTycko, 2010, The α-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel β-sheet structure in PrP fibrils: evidence from solid state nuclear magnetic resonance, Biochemistry, 49, 9488, 10.1021\u002Fbi1013134\nBaskakov, 2007, Branched chain mechanism of polymerization and ultrastructure of prion protein amyloid fibrils, FEBS J., 274, 3756, 10.1111\u002Fj.1742-4658.2007.05916.x\nPeretz, 2001, Antibodies inhibit prion propagation and clear cell cultures of prion infectivity, Nature, 412, 739, 10.1038\u002F35089090\nCaughey, 2009, Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions, Annu. Rev. Biochem., 78, 177, 10.1146\u002Fannurev.biochem.78.082907.145410",{"EN":585},"Fibril Formation of the Rabbit\u002FHuman\u002FBovine Prion Proteins",{"VOID":587},"10.1016\u002Fj.bpj.2011.08.018","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0006349511009647",[590,607,622,634,646,658,670,682],{"id":591,"sortIndex":225,"researcher":18,"roles":592,"affiliations":593,"properties":604},"e892fe77-c385-4f8f-8931-72be4514de83",[109],[594],{"id":18,"sortIndex":19,"affiliation":595,"properties":18},{"id":596,"createTime":597,"updateTime":598,"relativeEntities":599,"slug":600,"properties":601,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"b0ee837e-9819-4ed1-bd44-6d2383bf803a","2024-01-03T11:50:32.495+00:00","2025-02-09T11:20:10.275+00:00",[],"State-Key-Laboratory-of-Virology-College-of-Life-Sciences-Wuhan-University-Wuhan-China",{"title":602},{"VI":603},"State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, China",{"title":605},{"VI":606},"Xu Yan",{"id":608,"sortIndex":493,"researcher":18,"roles":609,"affiliations":610,"properties":619},"79730c71-a702-491c-aac0-b223360e83d1",[109],[611],{"id":18,"sortIndex":19,"affiliation":612,"properties":18},{"id":613,"createTime":614,"updateTime":614,"relativeEntities":615,"slug":18,"properties":616,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"8f77426a-b5db-414a-ab26-0e3480e1e259","2024-01-21T22:19:33.979+00:00",[],{"title":617},{"VI":618},"Laboratory of Proteomics, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China",{"title":620},{"VI":621},"Zheng-Sheng Xie",{"id":623,"sortIndex":489,"researcher":18,"roles":624,"affiliations":625,"properties":631},"179aadd5-654c-490f-af41-89bcee1f0ae9",[109],[626],{"id":18,"sortIndex":19,"affiliation":627,"properties":18},{"id":596,"createTime":597,"updateTime":598,"relativeEntities":628,"slug":600,"properties":629,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":630},{"VI":603},{"title":632},{"VI":633},"Geng-Fu Xiao",{"id":635,"sortIndex":19,"researcher":18,"roles":636,"affiliations":637,"properties":643},"5003958b-0250-4fc0-a261-8230b9bc3e43",[109],[638],{"id":18,"sortIndex":19,"affiliation":639,"properties":18},{"id":596,"createTime":597,"updateTime":598,"relativeEntities":640,"slug":600,"properties":641,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":642},{"VI":603},{"title":644},{"VI":645},"Zheng Zhou",{"id":647,"sortIndex":184,"researcher":18,"roles":648,"affiliations":649,"properties":655},"4028de1a-d815-442b-bb9f-367efd441636",[109],[650],{"id":18,"sortIndex":19,"affiliation":651,"properties":18},{"id":596,"createTime":597,"updateTime":598,"relativeEntities":652,"slug":600,"properties":653,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":654},{"VI":603},{"title":656},{"VI":657},"Kai Pan",{"id":659,"sortIndex":200,"researcher":18,"roles":660,"affiliations":661,"properties":667},"acf97c0c-4a0a-486c-b17d-142b6b9ac44c",[109],[662],{"id":18,"sortIndex":19,"affiliation":663,"properties":18},{"id":596,"createTime":597,"updateTime":598,"relativeEntities":664,"slug":600,"properties":665,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":666},{"VI":603},{"title":668},{"VI":669},"Jie Chen",{"id":671,"sortIndex":40,"researcher":18,"roles":672,"affiliations":673,"properties":679},"b1d0d639-505c-44bc-a575-a50683187b8b",[109],[674],{"id":18,"sortIndex":19,"affiliation":675,"properties":18},{"id":596,"createTime":597,"updateTime":598,"relativeEntities":676,"slug":600,"properties":677,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":678},{"VI":603},{"title":680},{"VI":681},"Yi Liang",{"id":683,"sortIndex":494,"researcher":18,"roles":684,"affiliations":685,"properties":691},"95a81452-feac-473c-a85b-4a4218d0528c",[109],[686],{"id":18,"sortIndex":19,"affiliation":687,"properties":18},{"id":613,"createTime":614,"updateTime":614,"relativeEntities":688,"slug":18,"properties":689,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":690},{"VI":618},{"title":692},{"VI":693},"Fu-Quan Yang",{"url":588,"publisher":695,"properties":717},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":696,"slug":10,"properties":697,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":700,"manageAffiliations":701,"indexDatabases":702,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":698,"title":699},{"VOID":13},{"EN":15},[],[],[703,710],{"id":44,"indexDatabase":704,"url":59,"indexYears":18,"academicFieldIds":709,"indexDatabaseRanking":18},{"id":46,"createTime":47,"updateTime":48,"relativeEntities":705,"label":706,"description":707,"key":55,"publicationTags":708,"standard":18},[],{"EN":51,"VI":51},{"VI":53,"EN":54},[57,58],[61],{"id":63,"indexDatabase":711,"url":76,"indexYears":77,"academicFieldIds":716,"indexDatabaseRanking":80},{"id":65,"createTime":66,"updateTime":67,"relativeEntities":712,"label":713,"description":714,"key":73,"publicationTags":715,"standard":18},[],{"EN":70,"VI":70},{"EN":70,"VI":72},[75],[79],{"volume":718,"pages":720},{"VOID":719},"101",{"VOID":721},"1483-1492","2011-09-01",2011,{"id":725,"createTime":726,"updateTime":726,"relativeEntities":727,"slug":18,"properties":728,"entityType":102,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":735,"fullTextUrl":18,"authors":736,"publicationType":135,"publisherRelationship":791,"citationCount":18,"citationInfo":18,"publishDate":819,"publishYear":820,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":166},"3b7d68b3-7a75-4da7-b8a0-f59284886762","2024-01-08T23:59:13.636+00:00",[],{"references":729,"title":731,"doi":733},{"VOID":730},"Adman, 1991, Copper protein structures, Adv. Protein Chem., 42, 144\nAkke, 2002, NMR methods for characterizing microsecond to millisecond dynamics in recognition and catalysis, Curr. Opin. Struct. Biol., 12, 642, 10.1016\u002FS0959-440X(02)00369-X\nArcangeli, 1999, Long-term molecular dynamics simulation of copper azurin: structure, dynamics and functionality, Biophys. Chem., 78, 247, 10.1016\u002FS0301-4622(99)00029-0\nArcangeli, 2001, Concerted motions in copper plastocyanin and azurin: an essential dynamics study, Biophys. Chem., 90, 45, 10.1016\u002FS0301-4622(01)00128-4\nArtymiuk, 1979, Crystallographic studies of the dynamic properties of lysozyme, Nature (Lond.), 280, 563, 10.1038\u002F280563a0\nBakowies, 2002, Water in protein cavities: a procedure to identify internal water and exchange pathways and application to fatty acid-binding protein, Prot. Struct. Funct. Genet., 47, 534, 10.1002\u002Fprot.10079\nBrooks, 1988\nBuckle, 1996, Structural and energetic responses to cavity-creating mutations in hydrophobic cores: observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities, Biochemistry, 35, 4298, 10.1021\u002Fbi9524676\nCioni, 1998, Acrylamide quenching of protein phosphorescence as a monitor of structural fluctuations in the globular fold, J. Am. Chem. Soc., 120, 11749, 10.1021\u002Fja9820543\nCioni, 2002, Effect of heavy water on protein flexibility, Biophys. J., 82, 3246, 10.1016\u002FS0006-3495(02)75666-X\nCioni, 2002, Tryptophan phosphorescence and pressure effects on protein structure, B.B.A. Prot. Struct. Mol. Biol., 1595, 116\nCioni, 1996, Pressure effects on the structure of oligomeric proteins prior to subunit dissociation, J. Mol. Biol., 263, 789, 10.1006\u002Fjmbi.1996.0616\nEngeseth, 1986, Studies of thermally induced denaturation of azurin and azurin derivatives by differential scanning calorimetry: evidence for copper selectivity, Biochemistry, 25, 2448, 10.1021\u002Fbi00357a023\nEnglander, 1996, Mechanisms and uses of hydrogen exchange, Curr. Opin. Struct. Biol., 6, 18, 10.1016\u002FS0959-440X(96)80090-X\nFarver, 1996, Structure-function correlation of intramolecular electron transfer in wild-type and single-site mutated azurins, Chem. Phys., 204, 271, 10.1016\u002F0301-0104(95)00294-4\nGabellieri, 1996, Effects of NAD+ binding on the luminescence of tryptophan 84 of Glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus, Biochemistry, 35, 12549, 10.1021\u002Fbi960231b\nGalley, 1976, Heterogeneity in protein emission spectra\nGilardi, 1994, Unique environment of Trp-48 in Pseudomonas aeruginosa azurin as probed by site-directed mutagenesis and dynamic fluorescence spectroscopy, Biochemistry, 33, 1425, 10.1021\u002Fbi00172a020\nGonnelli, 1995, Phosphorescence lifetime of tryptophan in proteins, Biochemistry, 34, 13847, 10.1021\u002Fbi00042a017\nHammann, 1996, X-ray crystal structure of the two site-specific mutants Ile7Ser and Phe110Ser of azurin from Pseudomonas aeruginosa, J. Mol. Biol., 255, 362, 10.1006\u002Fjmbi.1996.0029\nHansen, 1996, Detection of pH-dependent conformational change in azurin by time-resolved phosphorescence, Biophys. J., 71, 2138, 10.1016\u002FS0006-3495(96)79414-6\nKerwin, 2002, Interactions between PEG and type I soluble tumor necrosis factor receptor: modulation by pH and by PEGylation at the N-terminus, Protein Sci., 11, 1825, 10.1110\u002Fps.0208102\nKroes, 1998, Time-resolved fluorescence study of azurin variants: conformational heterogeneity and tryptophan mobility, Biophys. J., 75, 2441, 10.1016\u002FS0006-3495(98)77688-X\nLakowicz, 1973, Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale, Biochemistry, 12, 4171, 10.1021\u002Fbi00745a021\nMei, 1999, The effect of pressure and guanidine hydrochloride on azurins mutated in the hydrophobic core, Eur. J. Biochem., 265, 619, 10.1046\u002Fj.1432-1327.1999.00751.x\nMei, 1996, Probing the structure and mobility of Pseudomonas aeruginosa azurin by circular dichroism and dynamic fluorescence anisotropy, Protein Sci., 5, 2248, 10.1002\u002Fpro.5560051111\nMulder, 2001, Measurements of slow (microseconds-milliseconds) time scale dynamics in protein side chains by15N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme, J. Am. Chem. Soc., 123, 967, 10.1021\u002Fja003447g\nMulder, 2002, Slow internal dynamics in proteins: application of NMR relaxation dispersion spectroscopy to methyl groups in a cavity mutant of T4 lysozyme, J. Am. Chem. Soc., 124, 1443, 10.1021\u002Fja0119806\nMunro, 1979, Subnanosecond motions of tryptophan residues in proteins, Proc. Natl. Acad. Sci. USA, 76, 56, 10.1073\u002Fpnas.76.1.56\nNar, 1992, Characterization and crystal structure of zinc azurin, a by-product of heterologous expression in E. coli of Pseudomonas aeruginosa copper azurin, Eur. J. Biochem., 205, 1123, 10.1111\u002Fj.1432-1033.1992.tb16881.x\nNar, 1991, Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0, J. Mol. Biol., 221, 765, 10.1016\u002F0022-2836(91)80173-R\nNar, 1992, Crystal structure of Pseudomonas aeruginosa apo-azurin at 1.85Å resolution, FEBS Lett., 306, 119, 10.1016\u002F0014-5793(92)80981-L\nPalmer III, 2001, NMR probes of molecular dynamics: overview and comparison with other techniques, Annu. Rev. Biophys. Biomol. Struct., 30, 129, 10.1146\u002Fannurev.biophys.30.1.129\nPalmer III, 2001, Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules, Methods Enzymol., 339, 204, 10.1016\u002FS0076-6879(01)39315-1\nPozdnyakova, 2002, Studies of Pseudomonas aeruginosa azurin mutants: cavities in β-barrel do not affect refolding speed, Biophys. J., 82, 2645, 10.1016\u002FS0006-3495(02)75606-3\nQuillin, 2000, Size versus polarizability in protein-ligand interactions: binding of noble gases within engineered cavities in phage T4 lysozyme, J. Mol. Biol., 302, 955, 10.1006\u002Fjmbi.2000.4063\nSaviotti, 1974, Room temperature phosphorescence and the dynamic aspects of protein structure, Proc. Natl. Acad. Sci. USA, 71, 4154, 10.1073\u002Fpnas.71.10.4154\nSchauerte, 1997, Time-resolved room temperature tryptophan phosphorescence in proteins, Methods Enzymol., 278, 49, 10.1016\u002FS0076-6879(97)78006-6\nSkrynnikov, 2001, Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: application to methionine residues in a cavity mutant of T4 lysozyme, J. Am. Chem. Soc., 123, 4556, 10.1021\u002Fja004179p\nStrambini, 1991, Phosphorescence from Trp-48 in azurin: influence of Cu(II), Cu(I), Ag(I) and Cd(II) at the coordination site, J. Phys. Chem., 95, 4352, 10.1021\u002Fj100164a034\nStrambini, 1989, Tryptophan phosphorescence as monitor of protein flexibility, J. Mol. Liq., 42, 155, 10.1016\u002F0167-7322(89)80031-5\nStrambini, 1995, Tryptophan phosphorescence in fluid solution, J. Am. Chem. Soc., 117, 7646, 10.1021\u002Fja00134a008\nStrambini, 1998, Tyrosine quenching of tryptophan in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus, Biophys. J., 74, 3165, 10.1016\u002FS0006-3495(98)78022-1\nTang, 1998, Native protein fluctuations: the conformational-motion temperature and the inverse correlation of protein flexibility with protein stability, J. Biomol. Struct. Dyn., 16, 397, 10.1080\u002F07391102.1998.10508256\nTsai, 2001, The inverse relationship between protein dynamics and thermal stability, Biophys. J., 81, 2339, 10.1016\u002FS0006-3495(01)75880-8\nvan de Kamp, 1992, Complete sequential 1H nuclear magnetic resonance assignments and solution secondary structure of the blue copper protein azurin from Pseudomonas aeruginosa, Biochemistry, 31, 10194, 10.1021\u002Fbi00157a006\nVan de Kamp, 1990, Involvement of the hydrophobic patch of azurin in the electron-transfer reactions with cytochrome-C551 and nitrite reductase, Eur. J. Biochem., 194, 109, 10.1111\u002Fj.1432-1033.1990.tb19434.x\nVanderkooi, 1991, Tryptophan phosphorescence from proteins at room temperature, 113\nWagner, 1986, Observation of internal mobility of proteins by nuclear magnetic resonance in solution, Methods Enzymol., 131, 307, 10.1016\u002F0076-6879(86)31047-4\nZaccai, 2000, How soft is a protein? A protein dynamics force constant measured by neutron scattering, Science, 288, 1604, 10.1126\u002Fscience.288.5471.1604",{"EN":732},"Effects of Cavity-Forming Mutations on the Internal Dynamics of Azurin",{"VOID":734},"10.1016\u002Fs0006-3495(04)74189-2","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0006349504741892",[737,752,767,779],{"id":738,"sortIndex":200,"researcher":18,"roles":739,"affiliations":740,"properties":749},"ae446d33-76ca-41d1-b4cb-c4eb993cb563",[109],[741],{"id":18,"sortIndex":19,"affiliation":742,"properties":18},{"id":743,"createTime":744,"updateTime":744,"relativeEntities":745,"slug":18,"properties":746,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"288fc136-c406-4d9e-bdb8-dc3e9e4b6aa8","2024-02-08T02:23:16.600+00:00",[],{"title":747},{"VI":748},"Istituto di Biofisica, Consiglio Nazionale delle Ricerche, Area della Ricerca di Pisa, Pisa, Italy",{"title":750},{"VI":751},"Giovanni B. Strambini",{"id":753,"sortIndex":225,"researcher":18,"roles":754,"affiliations":755,"properties":764},"13a6919c-2f2c-4ea6-9e20-89312fa867af",[109],[756],{"id":18,"sortIndex":19,"affiliation":757,"properties":18},{"id":758,"createTime":759,"updateTime":759,"relativeEntities":760,"slug":18,"properties":761,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"9e5e822f-b279-407d-85e8-6b6057d8da90","2023-12-31T21:37:38.918+00:00",[],{"title":762},{"VI":763},"Leiden Institute of Chemistry, Gorlaeus Laboratories, Leiden University, Leiden, The Netherlands",{"title":765},{"VI":766},"Ellen de Waal",{"id":768,"sortIndex":184,"researcher":18,"roles":769,"affiliations":770,"properties":776},"7f14a10e-4522-418f-aba8-2db9cd3785a4",[109],[771],{"id":18,"sortIndex":19,"affiliation":772,"properties":18},{"id":758,"createTime":759,"updateTime":759,"relativeEntities":773,"slug":18,"properties":774,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":775},{"VI":763},{"title":777},{"VI":778},"Gerard W. Canters",{"id":780,"sortIndex":19,"researcher":18,"roles":781,"affiliations":782,"properties":788},"b6ec58f0-a902-4299-93fb-d21e44a28573",[109],[783],{"id":18,"sortIndex":19,"affiliation":784,"properties":18},{"id":743,"createTime":744,"updateTime":744,"relativeEntities":785,"slug":18,"properties":786,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":787},{"VI":748},{"title":789},{"VI":790},"Patrizia Cioni",{"url":735,"publisher":792,"properties":814},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":793,"slug":10,"properties":794,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":797,"manageAffiliations":798,"indexDatabases":799,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":795,"title":796},{"VOID":13},{"EN":15},[],[],[800,807],{"id":44,"indexDatabase":801,"url":59,"indexYears":18,"academicFieldIds":806,"indexDatabaseRanking":18},{"id":46,"createTime":47,"updateTime":48,"relativeEntities":802,"label":803,"description":804,"key":55,"publicationTags":805,"standard":18},[],{"EN":51,"VI":51},{"VI":53,"EN":54},[57,58],[61],{"id":63,"indexDatabase":808,"url":76,"indexYears":77,"academicFieldIds":813,"indexDatabaseRanking":80},{"id":65,"createTime":66,"updateTime":67,"relativeEntities":809,"label":810,"description":811,"key":73,"publicationTags":812,"standard":18},[],{"EN":70,"VI":70},{"EN":70,"VI":72},[75],[79],{"volume":815,"pages":817},{"VOID":816},"86",{"VOID":818},"1149-1159","2004-02-01",2004,{"id":822,"createTime":823,"updateTime":824,"relativeEntities":825,"slug":826,"properties":827,"entityType":102,"verifyStatus":178,"verifyTime":824,"verifyNote":179,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":832,"fullTextUrl":18,"authors":833,"publicationType":135,"publisherRelationship":958,"citationCount":18,"citationInfo":18,"publishDate":986,"publishYear":987,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":166},"b136ee7f-9bbe-4772-99c3-16bcce6a470a","2024-01-19T21:34:57.414+00:00","2025-01-11T23:59:00.034+00:00",[],"Electrophysiological-effects-of-ryanodine-derivatives-on-the-sheep-cardiac-sarcoplasmic-reticulum-calcium-release-channel",{"title":828,"doi":830},{"EN":829},"Electrophysiological effects of ryanodine derivatives on the sheep cardiac sarcoplasmic reticulum calcium-release channel",{"VOID":831},"10.1016\u002Fs0006-3495(96)79777-1","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0006349596797771",[834,849,861,873,885,897,909,921,933,945],{"id":835,"sortIndex":489,"researcher":18,"roles":836,"affiliations":837,"properties":846},"22c64001-f818-46b8-8518-bd89a2b11dc5",[109],[838],{"id":18,"sortIndex":19,"affiliation":839,"properties":18},{"id":840,"createTime":841,"updateTime":841,"relativeEntities":842,"slug":18,"properties":843,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"e00e5ae0-80c9-4250-8ac5-d18561ca8e3d","2024-01-19T21:34:57.460+00:00",[],{"title":844},{"VI":845},"Cardiac Medicine, National Heart and Lung Institute, Imperial College, University of London, London, England.",{"title":847},{"VI":848},"J.A. Airey",{"id":850,"sortIndex":200,"researcher":18,"roles":851,"affiliations":852,"properties":858},"33e5355d-b760-46ae-a976-6151f32fb3e5",[109],[853],{"id":18,"sortIndex":19,"affiliation":854,"properties":18},{"id":840,"createTime":841,"updateTime":841,"relativeEntities":855,"slug":18,"properties":856,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":857},{"VI":845},{"title":859},{"VI":860},"P. Deslongchamps",{"id":862,"sortIndex":490,"researcher":18,"roles":863,"affiliations":864,"properties":870},"88646f9d-6b8a-4a27-8081-d64f180b9b92",[109],[865],{"id":18,"sortIndex":19,"affiliation":866,"properties":18},{"id":840,"createTime":841,"updateTime":841,"relativeEntities":867,"slug":18,"properties":868,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":869},{"VI":845},{"title":871},{"VI":872},"H.R. Besch",{"id":874,"sortIndex":19,"researcher":18,"roles":875,"affiliations":876,"properties":882},"b0144817-efd1-4c18-adfa-a9b3b9b11e4a",[109],[877],{"id":18,"sortIndex":19,"affiliation":878,"properties":18},{"id":840,"createTime":841,"updateTime":841,"relativeEntities":879,"slug":18,"properties":880,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":881},{"VI":845},{"title":883},{"VI":884},"A. Tinker",{"id":886,"sortIndex":184,"researcher":18,"roles":887,"affiliations":888,"properties":894},"b22d0eb6-d515-47ea-96dc-2e3dc668abdb",[109],[889],{"id":18,"sortIndex":19,"affiliation":890,"properties":18},{"id":840,"createTime":841,"updateTime":841,"relativeEntities":891,"slug":18,"properties":892,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":893},{"VI":845},{"title":895},{"VI":896},"L. Ruest",{"id":898,"sortIndex":494,"researcher":18,"roles":899,"affiliations":900,"properties":906},"d9727bd5-4065-4577-8236-1efa8db5c4b7",[109],[901],{"id":18,"sortIndex":19,"affiliation":902,"properties":18},{"id":840,"createTime":841,"updateTime":841,"relativeEntities":903,"slug":18,"properties":904,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":905},{"VI":845},{"title":907},{"VI":908},"K. Gerzon",{"id":910,"sortIndex":225,"researcher":18,"roles":911,"affiliations":912,"properties":918},"aed57ca3-3241-457c-a069-6edf4a71dd5c",[109],[913],{"id":18,"sortIndex":19,"affiliation":914,"properties":18},{"id":840,"createTime":841,"updateTime":841,"relativeEntities":915,"slug":18,"properties":916,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":917},{"VI":845},{"title":919},{"VI":920},"J.L. Sutko",{"id":922,"sortIndex":493,"researcher":18,"roles":923,"affiliations":924,"properties":930},"86afe6f0-46ae-424a-92fc-9c5b89945931",[109],[925],{"id":18,"sortIndex":19,"affiliation":926,"properties":18},{"id":840,"createTime":841,"updateTime":841,"relativeEntities":927,"slug":18,"properties":928,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":929},{"VI":845},{"title":931},{"VI":932},"W. Welch",{"id":934,"sortIndex":40,"researcher":18,"roles":935,"affiliations":936,"properties":942},"fcdbab07-d6e5-4a29-9def-fc587c8ddff1",[109],[937],{"id":18,"sortIndex":19,"affiliation":938,"properties":18},{"id":840,"createTime":841,"updateTime":841,"relativeEntities":939,"slug":18,"properties":940,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":941},{"VI":845},{"title":943},{"VI":944},"K.R. Bidasee",{"id":946,"sortIndex":947,"researcher":18,"roles":948,"affiliations":949,"properties":955},"5daea521-50b4-484e-bc7d-eed6aca1ec5d",9,[109],[950],{"id":18,"sortIndex":19,"affiliation":951,"properties":18},{"id":840,"createTime":841,"updateTime":841,"relativeEntities":952,"slug":18,"properties":953,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":954},{"VI":845},{"title":956},{"VI":957},"A.J. Williams",{"url":832,"publisher":959,"properties":981},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":960,"slug":10,"properties":961,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":964,"manageAffiliations":965,"indexDatabases":966,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":962,"title":963},{"VOID":13},{"EN":15},[],[],[967,974],{"id":44,"indexDatabase":968,"url":59,"indexYears":18,"academicFieldIds":973,"indexDatabaseRanking":18},{"id":46,"createTime":47,"updateTime":48,"relativeEntities":969,"label":970,"description":971,"key":55,"publicationTags":972,"standard":18},[],{"EN":51,"VI":51},{"VI":53,"EN":54},[57,58],[61],{"id":63,"indexDatabase":975,"url":76,"indexYears":77,"academicFieldIds":980,"indexDatabaseRanking":80},{"id":65,"createTime":66,"updateTime":67,"relativeEntities":976,"label":977,"description":978,"key":73,"publicationTags":979,"standard":18},[],{"EN":70,"VI":70},{"EN":70,"VI":72},[75],[79],{"volume":982,"pages":984},{"VOID":983},"70",{"VOID":985},"2110-2119","1996-05-01",1996,{"id":989,"createTime":990,"updateTime":991,"relativeEntities":992,"slug":993,"properties":994,"entityType":102,"verifyStatus":178,"verifyTime":991,"verifyNote":179,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":1001,"fullTextUrl":18,"authors":1002,"publicationType":135,"publisherRelationship":1044,"citationCount":18,"citationInfo":18,"publishDate":1072,"publishYear":1073,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":18,"openAccess":18,"references":18,"isForceReanalyzing":166},"0fb810ca-d9b4-427b-af37-2828bf94142c","2024-01-05T16:34:48.609+00:00","2025-02-16T23:58:59.809+00:00",[],"Dimerization-and-Its-Role-in-GMP-Formation-by-Human-Guanylate-Binding-Proteins",{"references":995,"title":997,"doi":999},{"VOID":996},"Praefcke, 2004, The dynamin superfamily: universal membrane tubulation and fission molecules?, Nat. Rev. Mol. Cell Biol., 5, 133, 10.1038\u002Fnrm1313\nOlszewski, 2006, In silico genomic analysis of the human and murine guanylate-binding protein (GBP) gene clusters, J. Interferon Cytokine Res., 26, 328, 10.1089\u002Fjir.2006.26.328\nCheng, 1983, Interferon induction of fibroblast proteins with guanylate binding activity, J. Biol. Chem., 258, 7746, 10.1016\u002FS0021-9258(18)32242-7\nBoehm, 1998, Two families of GTPases dominate the complex cellular response to IFN-γ, J. Immunol., 161, 6715, 10.4049\u002Fjimmunol.161.12.6715\nAnderson, 1999, Interferon-induced guanylate binding protein-1 (GBP-1) mediates an antiviral effect against vesicular stomatitis virus and encephalomyocarditis virus, Virology, 256, 8, 10.1006\u002Fviro.1999.9614\nGuenzi, 2003, The guanylate binding protein-1 GTPase controls the invasive and angiogenic capability of endothelial cells through inhibition of MMP-1 expression, EMBO J., 22, 3772, 10.1093\u002Femboj\u002Fcdg382\nDuan, 2006, GBP1 over-expression is associated with a paclitaxel resistance phenotype, Cancer Chemother. Pharmacol., 571, 25, 10.1007\u002Fs00280-005-0026-3\nModiano, 2005, Golgi targeting of human guanylate-binding protein-1 requires nucleotide binding, isoprenylation, and an IFN-γ-inducible cofactor, Proc. Natl. Acad. Sci. USA, 102, 8680, 10.1073\u002Fpnas.0503227102\nCarter, 2005, Inhibition of VSV and EMCV replication by the interferon-induced GTPase, mGBP-2: differential requirement for wild-type GTP binding domain, Arch. Virol., 150, 1213, 10.1007\u002Fs00705-004-0489-2\nGuimarães, 2009, Interferon-inducible guanylate binding protein (GBP)-2: a novel p53-regulated tumor marker in esophageal squamous cell carcinomas, Int. J. Cancer., 124, 272, 10.1002\u002Fijc.23944\nSchwemmle, 1994, The interferon-induced 67-kDa guanylate-binding protein (hGBP1) is a GTPase that converts GTP to GMP, J. Biol. Chem., 269, 11299, 10.1016\u002FS0021-9258(19)78125-3\nNeun, 1996, GTPase properties of the interferon-induced human guanylate-binding protein 2, FEBS Lett., 390, 69, 10.1016\u002F0014-5793(96)00628-X\nPrakash, 2000, Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins, Nature, 403, 567, 10.1038\u002F35000617\nPrakash, 2000, Triphosphate structure of guanylate-binding protein 1 and implications for nucleotide binding and GTPase mechanism, EMBO J., 19, 4555, 10.1093\u002Femboj\u002F19.17.4555\nKunzelmann, 2005, Nucleotide binding and self-stimulated GTPase activity of human guanylate-binding protein 1 (hGBP1), Methods Enzymol., 404, 512, 10.1016\u002FS0076-6879(05)04045-0\nPraefcke, 2004, Identification of residues in the human guanylate-binding protein 1 critical for nucleotide binding and cooperative GTP hydrolysis, J. Mol. Biol., 344, 257, 10.1016\u002Fj.jmb.2004.09.026\nAbdullah, 2009, Role of individual domains and identification of internal gap in human guanylate binding protein-1, J. Mol. Biol., 386, 690, 10.1016\u002Fj.jmb.2008.12.060\nCardamone, 1992, Spectrofluorimetric assessment of the surface hydrophobicity of proteins, Biochem. J., 282, 589, 10.1042\u002Fbj2820589\nMatulis, 1998, 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation, Biophys. J., 74, 422, 10.1016\u002FS0006-3495(98)77799-9\nMoens, 2004, Detection of tryptophan to tryptophan energy transfer in proteins, Protein J., 23, 79, 10.1023\u002FB:JOPC.0000016261.97474.2e\nde Oliveira, 2001, The effect of resonance energy homotransfer on the intrinsic tryptophan fluorescence emission of the bothropstoxin-I dimer, Biochem. Biophys. Res. Commun., 284, 1011, 10.1006\u002Fbbrc.2001.5073\nParikh, 1974, Topics in the methodology of substitution reactions with agarose, Methods Enzymol., 34, 77, 10.1016\u002FS0076-6879(74)34009-8\nHermanson, 1992\nHermanson, 1985, Preparing antibody resins, 31\nEngvall, 1980, Enzyme immunoassay ELISA and EMIT, Methods Enzymol., 70, 419, 10.1016\u002FS0076-6879(80)70067-8\nMuhlberg, 1997, Domain structure and intramolecular regulation of dynamin GTPase, EMBO J., 16, 6676, 10.1093\u002Femboj\u002F16.22.6676\nRamachandran, 2007, The dynamin middle domain is critical for tetramerization and higher-order self-assembly, EMBO J., 26, 559, 10.1038\u002Fsj.emboj.7601491\nDi Paolo, 1999, Intramolecular backfolding of the carboxyl-terminal end of MxA protein is a prerequisite for its oligomerization, J. Biol. Chem., 274, 32071, 10.1074\u002Fjbc.274.45.32071\nGhosh, 2006, How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP, Nature, 440, 101, 10.1038\u002Fnature04510\nScheffzek, 1997, The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants, Science, 277, 333, 10.1126\u002Fscience.277.5324.333\nRittinger, 1997, Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue, Nature, 389, 758, 10.1038\u002F39651",{"EN":998},"Dimerization and Its Role in GMP Formation by Human Guanylate Binding Proteins",{"VOID":1000},"10.1016\u002Fj.bpj.2010.07.025","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0006349510008970",[1003,1020,1032],{"id":1004,"sortIndex":225,"researcher":18,"roles":1005,"affiliations":1006,"properties":1017},"c7e0bc04-73d1-4a37-b877-29df60d009aa",[109],[1007],{"id":18,"sortIndex":19,"affiliation":1008,"properties":18},{"id":1009,"createTime":1010,"updateTime":1011,"relativeEntities":1012,"slug":1013,"properties":1014,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},"7edd563a-d7fa-4fe5-a0e8-15f5a2ce4627","2024-01-20T19:59:42.022+00:00","2024-10-10T01:08:16.986+00:00",[],"National-Institute-of-Immunology-New-Delhi-India",{"title":1015},{"VI":1016},"National Institute of Immunology, New Delhi India",{"title":1018},{"VI":1019},"Meena Balakumari",{"id":1021,"sortIndex":184,"researcher":18,"roles":1022,"affiliations":1023,"properties":1029},"217c0f6f-1618-4550-905c-ec0d5f51040d",[109],[1024],{"id":18,"sortIndex":19,"affiliation":1025,"properties":18},{"id":1009,"createTime":1010,"updateTime":1011,"relativeEntities":1026,"slug":1013,"properties":1027,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1028},{"VI":1016},{"title":1030},{"VI":1031},"Apurba Kumar Sau",{"id":1033,"sortIndex":19,"researcher":18,"roles":1034,"affiliations":1035,"properties":1041},"bb46e554-136d-4fc4-92eb-df62b8388a44",[109],[1036],{"id":18,"sortIndex":19,"affiliation":1037,"properties":18},{"id":1009,"createTime":1010,"updateTime":1011,"relativeEntities":1038,"slug":1013,"properties":1039,"entityType":39,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19},[],{"title":1040},{"VI":1016},{"title":1042},{"VI":1043},"Nazish Abdullah",{"url":1001,"publisher":1045,"properties":1067},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1046,"slug":10,"properties":1047,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":1050,"manageAffiliations":1051,"indexDatabases":1052,"url":18,"thumbnailPath":18,"statistic":18,"gsStatistic":18,"type":18,"analyzePriority":18},[],{"issn":1048,"title":1049},{"VOID":13},{"EN":15},[],[],[1053,1060],{"id":44,"indexDatabase":1054,"url":59,"indexYears":18,"academicFieldIds":1059,"indexDatabaseRanking":18},{"id":46,"createTime":47,"updateTime":48,"relativeEntities":1055,"label":1056,"description":1057,"key":55,"publicationTags":1058,"standard":18},[],{"EN":51,"VI":51},{"VI":53,"EN":54},[57,58],[61],{"id":63,"indexDatabase":1061,"url":76,"indexYears":77,"academicFieldIds":1066,"indexDatabaseRanking":80},{"id":65,"createTime":66,"updateTime":67,"relativeEntities":1062,"label":1063,"description":1064,"key":73,"publicationTags":1065,"standard":18},[],{"EN":70,"VI":70},{"EN":70,"VI":72},[75],[79],{"volume":1068,"pages":1070},{"VOID":1069},"99",{"VOID":1071},"2235-2244","2010-10-01",2010]