[ { "key": "MP4MQZTH", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/MP4MQZTH", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/MP4MQZTH", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/47225/items/AVQDTJBX", "type": "application/json" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } }, "numChildren": 0 }, "data": { "key": "MP4MQZTH", "version": 1, "parentItem": "AVQDTJBX", "itemType": "attachment", "linkMode": "imported_url", "title": "ScienceDirect Full Text PDF", "accessDate": "2011-10-26T15:04:44Z", "url": "http://www.sciencedirect.com/science?_ob=MiamiImageURL&_cid=271331&_user=709071&_pii=S0891584907005953&_check=y&_origin=&_coverDate=01-Jan-2008&view=c&wchp=dGLbVlB-zSkWA&md5=7fbad270bad85ec57407d92d3de381d5/1-s2.0-S0891584907005953-main.pdf", "note": "", "contentType": "application/pdf", "charset": "", "filename": "Snook et al. - 2008 - Peroxynitrite inhibits myofibrillar protein functi.pdf", "md5": "b78c2e5e4f010fd3ce85d8bf8be4ead2", "mtime": 1319641485558, "tags": [], "relations": {}, "dateAdded": "2011-10-26T15:05:15Z", "dateModified": "2011-10-26T15:05:40Z" } }, { "key": "Z76JFVFX", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/Z76JFVFX", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/Z76JFVFX", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/47225/items/AVQDTJBX", "type": "application/json" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } } }, "data": { "key": "Z76JFVFX", "version": 1, "parentItem": "AVQDTJBX", "itemType": "attachment", "linkMode": "imported_url", "title": "ScienceDirect Snapshot", "accessDate": "2011-10-26T15:04:46Z", "url": "http://www.sciencedirect.com/science/article/pii/S0891584907005953#sec1.3", "note": "", "contentType": "text/html", "charset": "utf-8", "filename": "S0891584907005953.html", "md5": null, "mtime": 1319641487082, "tags": [], "relations": {}, "dateAdded": "2011-10-26T15:05:15Z", "dateModified": "2011-10-26T15:05:40Z" } }, { "key": "AVQDTJBX", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/AVQDTJBX", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/AVQDTJBX", "type": "text/html" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } }, "creatorSummary": "Snook et al.", "parsedDate": "2008-01-01", "numChildren": 2 }, "data": { "key": "AVQDTJBX", "version": 1, "itemType": "journalArticle", "title": "Peroxynitrite inhibits myofibrillar protein function in an in vitro assay of motility", "creators": [ { "creatorType": "author", "firstName": "Jeremy H.", "lastName": "Snook" }, { "creatorType": "author", "firstName": "Jiahui", "lastName": "Li" }, { "creatorType": "author", "firstName": "Brian P.", "lastName": "Helmke" }, { "creatorType": "author", "firstName": "William H.", "lastName": "Guilford" } ], "abstractNote": "We determined the effects of peroxynitrite (ONOO−) on cardiac myosin, actin, and thin filaments in order to more clearly understand the impact of this reactive compound in ischemia/reperfusion injury and heart failure. Actin filaments, native thin filaments, and α-cardiac myosin from rat hearts were exposed to ONOO− in the presence of 2 mM bicarbonate. Filament velocities over myosin, calcium sensitivity, and relative force generated by myosin were assessed in an in vitro motility assay in the absence of reducing agents. ONOO− concentrations ≥ 10 μM significantly reduced the velocities of thin filaments or bare actin filaments over α-cardiac myosin when any of these proteins were exposed individually. These functional deficits were linearly related to the degree of tyrosine nitration, with myosin being the most sensitive. However, at 10 μM ONOO− the calcium sensitivity of thin filaments remained unchanged. Cotreatment of myosin and thin filaments, analogous to the in vivo situation, resulted in a significantly greater functional deficit. The load supported by myosin after ONOO− exposure was estimated using mixtures experiments to be increased threefold. These data suggest that nitration of myofibrillar proteins can contribute to cardiac contractile dysfunction in pathologic states in which ONOO− is liberated.", "publicationTitle": "Free Radical Biology and Medicine", "publisher": "", "place": "", "date": "January 1, 2008", "volume": "44", "issue": "1", "section": "", "partNumber": "", "partTitle": "", "pages": "14-23", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1016/j.freeradbiomed.2007.09.004", "citationKey": "", "url": "http://www.sciencedirect.com/science/article/pii/S0891584907005953", "accessDate": "2011-10-26T15:04:43Z", "PMID": "", "PMCID": "", "ISSN": "0891-5849", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "ScienceDirect", "callNumber": "", "rights": "", "extra": "", "tags": [ { "tag": "Actin", "type": 1 }, { "tag": "Cardiac muscle", "type": 1 }, { "tag": "Free radicals", "type": 1 }, { "tag": "Oxidative stress", "type": 1 }, { "tag": "myosin", "type": 1 } ], "collections": [ "A97KU5P2" ], "relations": {}, "dateAdded": "2011-10-26T15:05:15Z", "dateModified": "2011-10-26T15:05:15Z" } }, { "key": "VZFDJ26B", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/VZFDJ26B", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/VZFDJ26B", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/47225/items/NZC9THTB", "type": "application/json" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } } }, "data": { "key": "VZFDJ26B", "version": 1, "parentItem": "NZC9THTB", "itemType": "attachment", "linkMode": "linked_url", "title": "PubMed Central Link", "accessDate": "2011-08-05T15:16:02Z", "url": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1138137/", "note": "", "contentType": "text/html", "charset": "", "tags": [], "relations": {}, "dateAdded": "2011-08-05T15:16:02Z", "dateModified": "2011-08-05T15:16:02Z" } }, { "key": "NZC9THTB", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/NZC9THTB", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/NZC9THTB", "type": "text/html" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } }, "creatorSummary": "Stepkowski et al.", "parsedDate": "1994-05-15", "numChildren": 1 }, "data": { "key": "NZC9THTB", "version": 1, "itemType": "journalArticle", "title": "The actin-activated ATPase of co-polymer filaments of myosin and myosin-rod.", "creators": [ { "creatorType": "author", "firstName": "D", "lastName": "Stepkowski" }, { "creatorType": "author", "firstName": "A A", "lastName": "Orlova" }, { "creatorType": "author", "firstName": "C", "lastName": "Moos" } ], "abstractNote": "The actin activated ATPase of myosin at low ionic strength shows a complex dependence on actin concentration, in contrast with the simple hyperbolic actin activation kinetics of heavy meromyosin and subfragment-1. To investigate how the aggregation of myosin influences the actomyosin ATPase kinetics, we have studied the actin-activated ATPase of mixed filaments in which the myosin molecules are separated from each other by copolymerization with myosin rod. Electron microscopy of copolymer filaments, alone and bound to actin, indicates that the myosin heads are distributed randomly along the co-polymer filaments. The actin-activated ATPase of myosin decreases with increasing rod, approaching a plateau of about 30% of the control at a rod/myosin molar ratio of 4:1. The decrease in ATPase persists even at Vmax, the extrapolated limit at infinite actin, indicating that it is not due merely to the loss of cooperative actin binding. Furthermore, the actin dependence of the ATPase still shows a biphasic character like that of control myosin, even at rod/myosin ratio of 12:1, so this complexity is not probably due solely to the structural proximity of myosin molecules, but may involve a non-equivalence of myosin heads or myosin molecules in the filament environment.", "publicationTitle": "Biochemical Journal", "publisher": "", "place": "", "date": "1994-5-15", "volume": "300", "issue": "Pt 1", "section": "", "partNumber": "", "partTitle": "", "pages": "153-158", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Biochem J", "DOI": "", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "0264-6021", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "PubMed Central", "callNumber": "", "rights": "", "extra": "PMID: 8198528\nPMCID: 1138137", "tags": [], "collections": [ "A97KU5P2" ], "relations": {}, "dateAdded": "2011-08-05T15:16:02Z", "dateModified": "2011-08-05T15:16:02Z" } }, { "key": "6TVD3W83", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/6TVD3W83", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/6TVD3W83", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/47225/items/JKBVWCHW", "type": "application/json" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } }, "numChildren": 0 }, "data": { "key": "6TVD3W83", "version": 1, "parentItem": "JKBVWCHW", "itemType": "attachment", "linkMode": "imported_url", "title": "Full Text PDF", "accessDate": "2011-08-03T16:26:57Z", "url": "http://www.jbc.org/content/252/22/8300.full.pdf", "note": "", "contentType": "application/pdf", "charset": "", "filename": "Gordon et al. - 1977 - Comparative biochemistry of non-muscle actins..pdf", "md5": "2c3d642cfd012c52c653a8c21ab45759", "mtime": 1312388824240, "tags": [], "relations": {}, "dateAdded": "2011-08-03T16:26:57Z", "dateModified": "2011-08-03T17:42:13Z" } }, { "key": "MDP3KIBI", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/MDP3KIBI", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/MDP3KIBI", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/47225/items/JKBVWCHW", "type": "application/json" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } } }, "data": { "key": "MDP3KIBI", "version": 1, "parentItem": "JKBVWCHW", "itemType": "attachment", "linkMode": "imported_url", "title": "Snapshot", "accessDate": "2011-08-03T16:26:55Z", "url": "http://www.jbc.org/content/252/22/8300.full.pdf+html?frame=sidebar", "note": "", "contentType": "text/html", "charset": "utf-8", "filename": "8300.full.html", "md5": null, "mtime": 1312388816365, "tags": [], "relations": {}, "dateAdded": "2011-08-03T16:26:55Z", "dateModified": "2011-08-03T17:42:13Z" } }, { "key": "JKBVWCHW", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/JKBVWCHW", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/JKBVWCHW", "type": "text/html" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } }, "creatorSummary": "Gordon et al.", "parsedDate": "1977-11-25", "numChildren": 2 }, "data": { "key": "JKBVWCHW", "version": 1, "itemType": "journalArticle", "title": "Comparative biochemistry of non-muscle actins.", "creators": [ { "creatorType": "author", "firstName": "D J", "lastName": "Gordon" }, { "creatorType": "author", "firstName": "J L", "lastName": "Boyer" }, { "creatorType": "author", "firstName": "E D", "lastName": "Korn" } ], "abstractNote": "", "publicationTitle": "Journal of Biological Chemistry", "publisher": "", "place": "", "date": "November 25 , 1977", "volume": "252", "issue": "22", "section": "", "partNumber": "", "partTitle": "", "pages": "8300 -8309", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "", "citationKey": "", "url": "http://www.jbc.org/content/252/22/8300.short", "accessDate": "2011-08-03T16:26:54Z", "PMID": "", "PMCID": "", "ISSN": "", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "Highwire 2.0", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [ "A97KU5P2" ], "relations": {}, "dateAdded": "2011-08-03T16:26:54Z", "dateModified": "2011-08-03T16:26:54Z" } }, { "key": "6KDTFC93", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/6KDTFC93", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/6KDTFC93", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/47225/items/3H6JG7FF", "type": "application/json" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } }, "numChildren": 0 }, "data": { "key": "6KDTFC93", "version": 1, "parentItem": "3H6JG7FF", "itemType": "attachment", "linkMode": "imported_url", "title": "Full Text PDF", "accessDate": "2011-07-19T15:40:16Z", "url": "http://circres.ahajournals.org/content/72/1/219.full.pdf", "note": "", "contentType": "application/pdf", "charset": "", "filename": "Harris and Warshaw - 1993 - Smooth and skeletal muscle actin are mechanically .pdf", "md5": "09452aa4124bb76b7c8bf231c53b69f2", "mtime": 1311090020267, "tags": [], "relations": {}, "dateAdded": "2011-07-19T15:40:16Z", "dateModified": "2011-07-19T15:40:43Z" } }, { "key": "9VTCHSJP", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/9VTCHSJP", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/9VTCHSJP", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/47225/items/3H6JG7FF", "type": "application/json" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } } }, "data": { "key": "9VTCHSJP", "version": 1, "parentItem": "3H6JG7FF", "itemType": "attachment", "linkMode": "imported_url", "title": "Snapshot", "accessDate": "2011-07-19T15:40:12Z", "url": "http://circres.ahajournals.org/content/72/1/219.short", "note": "", "contentType": "text/html", "charset": "utf-8", "filename": "219.html", "md5": null, "mtime": 1311090013000, "tags": [], "relations": {}, "dateAdded": "2011-07-19T15:40:12Z", "dateModified": "2011-07-19T15:40:43Z" } }, { "key": "3H6JG7FF", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/3H6JG7FF", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/3H6JG7FF", "type": "text/html" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } }, "creatorSummary": "Harris and Warshaw", "parsedDate": "1993-01-01", "numChildren": 2 }, "data": { "key": "3H6JG7FF", "version": 1, "itemType": "journalArticle", "title": "Smooth and skeletal muscle actin are mechanically indistinguishable in the in vitro motility assay", "creators": [ { "creatorType": "author", "firstName": "DE", "lastName": "Harris" }, { "creatorType": "author", "firstName": "DM", "lastName": "Warshaw" } ], "abstractNote": "", "publicationTitle": "Circulation Research", "publisher": "", "place": "", "date": "January 01 , 1993", "volume": "72", "issue": "1", "section": "", "partNumber": "", "partTitle": "", "pages": "219 -224", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "", "citationKey": "", "url": "http://circres.ahajournals.org/content/72/1/219.abstract", "accessDate": "2011-07-19T15:40:09Z", "PMID": "", "PMCID": "", "ISSN": "", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "Highwire 2.0", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [ "A97KU5P2" ], "relations": {}, "dateAdded": "2011-07-19T15:40:09Z", "dateModified": "2011-07-19T15:40:09Z" } }, { "key": "XAD5KXH7", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/XAD5KXH7", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/XAD5KXH7", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/47225/items/S2SBAG7D", "type": "application/json" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } }, "numChildren": 0 }, "data": { "key": "XAD5KXH7", "version": 1, "parentItem": "S2SBAG7D", "itemType": "attachment", "linkMode": "imported_url", "title": "Full Text PDF", "accessDate": "2011-07-19T15:35:15Z", "url": "http://www.jbc.org/content/251/15/4778.full.pdf", "note": "", "contentType": "application/pdf", "charset": "", "filename": "Gordon et al. - 1976 - Characterization of cytoplasmic actin isolated fro.pdf", "md5": "dbda62beca8a06bade8b892f89c9aa5c", "mtime": 1311089723494, "tags": [], "relations": {}, "dateAdded": "2011-07-19T15:35:15Z", "dateModified": "2011-07-19T15:35:52Z" } }, { "key": "SVWATN38", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/SVWATN38", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/SVWATN38", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/47225/items/S2SBAG7D", "type": "application/json" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } } }, "data": { "key": "SVWATN38", "version": 1, "parentItem": "S2SBAG7D", "itemType": "attachment", "linkMode": "imported_url", "title": "Snapshot", "accessDate": "2011-07-19T15:35:08Z", "url": "http://www.jbc.org/content/251/15/4778.full.pdf+html?frame=sidebar", "note": "", "contentType": "text/html", "charset": "utf-8", "filename": "4778.full.html", "md5": null, "mtime": 1311089708399, "tags": [], "relations": {}, "dateAdded": "2011-07-19T15:35:08Z", "dateModified": "2011-07-19T15:35:52Z" } }, { "key": "S2SBAG7D", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/S2SBAG7D", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/S2SBAG7D", "type": "text/html" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } }, "creatorSummary": "Gordon et al.", "parsedDate": "1976", "numChildren": 2 }, "data": { "key": "S2SBAG7D", "version": 1, "itemType": "journalArticle", "title": "Characterization of cytoplasmic actin isolated from Acanthamoeba castellanii by a new method.", "creators": [ { "creatorType": "author", "firstName": "D J", "lastName": "Gordon" }, { "creatorType": "author", "firstName": "E", "lastName": "Eisenberg" }, { "creatorType": "author", "firstName": "E D", "lastName": "Korn" } ], "abstractNote": "Cytoplasmic actin has been isolated from Acanthamoeba castellanii by a new method, employing chromatography on DEAE-cellulose, that improves the yield by more than 20-fold over the previously reported method. This procedure should be particularly useful for isolating actin from cells in which it is present in relatively low concentration because the method does not depend initially on the polymerization of actin or its interaction with myosin. Systematic comparison of the properties of purified Acanthamoeba actin and rabbit skeletal muscle actin shows them to be similar in many ways: viscosity of F-actin, stoichiometry of bound nucleotide, stoichiometry of binding of muscle heavy meromyosin and myosin subfragment 1 in the absence of ATP, and ability to inhibit the KATPase activity of heavy meromyosin. The amino acid compositions of Acanthamoeba and muscle actin are also quite similar, but significant differences, especially the presence of epsilon-N-methyllysines in Acanthamoeba actin, have been confirmed. In addition to this structural difference, we find that Acanthamoeba actin is only one-third as effective as muscle actin as an activator of the MgATPase of muscle heavy meromyosin and subfragment 1. For Acanthamoeba actin, as for muscle actin, this activation exhibits hyperbolic dependence on actin concentration; i.e. the double reciprocal plot of ATPase activation versus actin concentration is linear. From these plots we find that the two actins give the same extrapolated ATPase activity at infinite actin concentration (Vmax) but differ by a factor of three in the concentration of actin needed to produce half-maximal activation (Kapp).", "publicationTitle": "Journal of Biological Chemistry", "publisher": "", "place": "", "date": "1976", "volume": "251", "issue": "15", "section": "", "partNumber": "", "partTitle": "", "pages": "4778 -4786", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "", "citationKey": "", "url": "http://www.jbc.org/content/251/15/4778.abstract", "accessDate": "2011-07-19T15:35:07Z", "PMID": "", "PMCID": "", "ISSN": "", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "Highwire 2.0", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [ "A97KU5P2" ], "relations": {}, "dateAdded": "2011-07-19T15:35:07Z", "dateModified": "2011-07-19T15:35:07Z" } }, { "key": "98SF7A6D", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/98SF7A6D", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/98SF7A6D", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/47225/items/E9AKB4TT", "type": "application/json" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } }, "numChildren": 0 }, "data": { "key": "98SF7A6D", "version": 1, "parentItem": "E9AKB4TT", "itemType": "attachment", "linkMode": "imported_url", "title": "Full Text PDF", "accessDate": "2011-07-18T20:10:51Z", "url": "http://circres.ahajournals.org/content/72/1/219.full.pdf", "note": "", "contentType": "application/pdf", "charset": "", "filename": "Harris and Warshaw - 1993 - Smooth and skeletal muscle actin are mechanically .pdf", "md5": "681221bda9a64c1a902014afd5557b6a", "mtime": 1311019855570, "tags": [], "relations": {}, "dateAdded": "2011-07-18T20:10:51Z", "dateModified": "2011-07-18T20:11:25Z" } }, { "key": "XH6AXVJZ", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/XH6AXVJZ", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/XH6AXVJZ", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/47225/items/E9AKB4TT", "type": "application/json" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } } }, "data": { "key": "XH6AXVJZ", "version": 1, "parentItem": "E9AKB4TT", "itemType": "attachment", "linkMode": "imported_url", "title": "Snapshot", "accessDate": "2011-07-18T20:10:50Z", "url": "http://circres.ahajournals.org/content/72/1/219.abstract", "note": "", "contentType": "text/html", "charset": "utf-8", "filename": "219.html", "md5": null, "mtime": 1311019850773, "tags": [], "relations": {}, "dateAdded": "2011-07-18T20:10:50Z", "dateModified": "2011-07-18T20:11:25Z" } }, { "key": "E9AKB4TT", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/E9AKB4TT", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/E9AKB4TT", "type": "text/html" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } }, "creatorSummary": "Harris and Warshaw", "parsedDate": "1993-01-01", "numChildren": 2 }, "data": { "key": "E9AKB4TT", "version": 1, "itemType": "journalArticle", "title": "Smooth and skeletal muscle actin are mechanically indistinguishable in the in vitro motility assay", "creators": [ { "creatorType": "author", "firstName": "DE", "lastName": "Harris" }, { "creatorType": "author", "firstName": "DM", "lastName": "Warshaw" } ], "abstractNote": "", "publicationTitle": "Circulation Research", "publisher": "", "place": "", "date": "January 01 , 1993", "volume": "72", "issue": "1", "section": "", "partNumber": "", "partTitle": "", "pages": "219 -224", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "", "citationKey": "", "url": "http://circres.ahajournals.org/content/72/1/219.abstract", "accessDate": "2011-07-18T20:10:48Z", "PMID": "", "PMCID": "", "ISSN": "", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "Highwire 2.0", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [ "A97KU5P2" ], "relations": {}, "dateAdded": "2011-07-18T20:10:48Z", "dateModified": "2011-07-18T20:10:48Z" } }, { "key": "5AEEV4CZ", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/5AEEV4CZ", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/5AEEV4CZ", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/47225/items/UQEUBKTH", "type": "application/json" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } } }, "data": { "key": "5AEEV4CZ", "version": 1, "parentItem": "UQEUBKTH", "itemType": "attachment", "linkMode": "imported_url", "title": "A Conformational Change in F-Actin When Myosin Binds:  Fluorescence Resonance Energy Transfer Detects an Increase in the Radial Coordinate of Cys-374† - Biochemistry (ACS Publications)", "accessDate": "2011-07-18T16:53:45Z", "url": "http://pubs.acs.org/doi/abs/10.1021/bi962588l", "note": "", "contentType": "text/html", "charset": "utf-8", "filename": "bi962588l.html", "md5": null, "mtime": 1311008027037, "tags": [], "relations": {}, "dateAdded": "2011-07-18T16:53:45Z", "dateModified": "2011-07-18T16:54:14Z" } }, { "key": "TTEGCAU9", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/TTEGCAU9", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/TTEGCAU9", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/47225/items/UQEUBKTH", "type": "application/json" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } } }, "data": { "key": "TTEGCAU9", "version": 1, "parentItem": "UQEUBKTH", "itemType": "attachment", "linkMode": "imported_url", "title": "ACS Full Text Snapshot", "accessDate": "2011-07-18T16:53:42Z", "url": "http://pubs.acs.org/doi/full/10.1021/bi962588l", "note": "", "contentType": "text/html", "charset": "utf-8", "filename": "bi962588l.html", "md5": null, "mtime": 1311008023208, "tags": [], "relations": {}, "dateAdded": "2011-07-18T16:53:42Z", "dateModified": "2011-07-18T16:54:14Z" } }, { "key": "Q4HX974E", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/Q4HX974E", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/Q4HX974E", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/47225/items/UQEUBKTH", "type": "application/json" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } }, "numChildren": 0 }, "data": { "key": "Q4HX974E", "version": 1, "parentItem": "UQEUBKTH", "itemType": "attachment", "linkMode": "imported_url", "title": "ACS Full Text PDF", "accessDate": "2011-07-18T16:53:40Z", "url": "http://pubs.acs.org/doi/pdf/10.1021/bi962588l", "note": "", "contentType": "application/pdf", "charset": "", "filename": "Moens and dos Remedios - 1997 - A Conformational Change in F-Actin When Myosin Bin.pdf", "md5": "c3a9e6add90c0ab92feb00583dbee8de", "mtime": 1311008020271, "tags": [], "relations": {}, "dateAdded": "2011-07-18T16:53:40Z", "dateModified": "2011-07-18T16:54:14Z" } }, { "key": "UQEUBKTH", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/UQEUBKTH", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/UQEUBKTH", "type": "text/html" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } }, "creatorSummary": "Moens and dos Remedios", "parsedDate": "1997-06-01", "numChildren": 3 }, "data": { "key": "UQEUBKTH", "version": 1, "itemType": "journalArticle", "title": "A Conformational Change in F-Actin When Myosin Binds:  Fluorescence Resonance Energy Transfer Detects an Increase in the Radial Coordinate of Cys-374†", "creators": [ { "creatorType": "author", "firstName": "Pierre D. J.", "lastName": "Moens" }, { "creatorType": "author", "firstName": "Cristobal G.", "lastName": "dos Remedios" } ], "abstractNote": "Interactions of myosin with actin filaments probably induce conformational changes in actin which are crucial for its function. Fluorescence resonance energy transfer spectroscopy can determine changes in distance (range 10−100 Å) between two probes and therefore can sense conformational changes in proteins. We have investigated changes in the radial coordinates of fluorescent probes bound to Cys-374 of F-actin when either of the isozymes (S1A1 and S1A2) of myosin subfragment 1 (S-1) bind. Using 5-[[2-[(iodoacetyl)amino]ethyl]amino]naphthalene-1-sulfonic acid and N-(4-dimethylamino-3,5-dinitrophenyl)maleimide as donor and acceptor probes, respectively, we calculated a radius of 13−14 Å. This distance increased by ≈4.5 Å upon addition of S-1. No differences were detected between the effects of S1A1 and S1A2. This increase is reversed by MgATP. The average position of the probes on Cys-374 is closer to the filament axis than expected from the current models of F-actin. S-1 increases the radial position of Cys-374 either by direct interaction or via an allosteric conformational change associated with its binding.", "publicationTitle": "Biochemistry", "publisher": "", "place": "", "date": "June 01, 1997", "volume": "36", "issue": "24", "section": "", "partNumber": "", "partTitle": "", "pages": "7353-7360", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1021/bi962588l", "citationKey": "", "url": "http://dx.doi.org/10.1021/bi962588l", "accessDate": "2011-07-18T16:53:39Z", "PMID": "", "PMCID": "", "ISSN": "", "archive": "", "archiveLocation": "", "shortTitle": "A Conformational Change in F-Actin When Myosin Binds", "language": "", "libraryCatalog": "ACS Publications", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [ "A97KU5P2" ], "relations": {}, "dateAdded": "2011-07-18T16:53:39Z", "dateModified": "2011-07-18T16:53:39Z" } }, { "key": "VNBI4IE8", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/VNBI4IE8", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/VNBI4IE8", "type": "text/html" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } }, "creatorSummary": "Crosbie et al.", "parsedDate": "1994-11", "numChildren": 0 }, "data": { "key": "VNBI4IE8", "version": 1, "itemType": "journalArticle", "title": "Structural connectivity in actin: effect of C-terminal modifications on the properties of actin", "creators": [ { "creatorType": "author", "firstName": "R H", "lastName": "Crosbie" }, { "creatorType": "author", "firstName": "C", "lastName": "Miller" }, { "creatorType": "author", "firstName": "P", "lastName": "Cheung" }, { "creatorType": "author", "firstName": "T", "lastName": "Goodnight" }, { "creatorType": "author", "firstName": "A", "lastName": "Muhlrad" }, { "creatorType": "author", "firstName": "E", "lastName": "Reisler" } ], "abstractNote": "In this study, we use fluorescent probes and proteolytic digestions to demonstrate structural coupling between distant regions of actin. We show that modifications of Cys-374 in the C-terminus of actin slow the rate of nucleotide exchange in the nucleotide cleft. Conformational coupling between the C-terminus and the DNasal loop in subdomain II is observed in proteolytic digestion experiments in which a new C-terminal cleavage site is exposed upon DNasel binding. The functional consequences of C-terminal modification are evident from S-1 ATPase activity and the in vitro motility experiments with modified actins. Pyrene actin, labeled at Cys-374, activates S-1 ATPase activity only half as well as control actin. This reduction is attributed to a lower Vmax value because the affinity of pyrene actin to S-1 is not significantly altered. The in vitro sliding velocity of pyrene actin is also decreased. However, IAEDANS labeling of actin (also at Cys-374) enhances the Vmax of acto-S-1 ATPase activity and the in vitro sliding velocity by approximately 25%. These results are discussed in terms of conformational coupling between distant regions in actin and the functional implications of the interactions of actin-binding proteins with the C-terminus of actin.", "publicationTitle": "Biophysical Journal", "publisher": "", "place": "", "date": "Nov 1994", "volume": "67", "issue": "5", "section": "", "partNumber": "", "partTitle": "", "pages": "1957-1964", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Biophys. J", "DOI": "10.1016/S0006-3495(94)80678-2", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pubmed/7858132", "accessDate": "2011-07-18T13:11:06Z", "PMID": "", "PMCID": "", "ISSN": "0006-3495", "archive": "", "archiveLocation": "", "shortTitle": "Structural connectivity in actin", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 7858132", "tags": [ { "tag": "Actins", "type": 1 }, { "tag": "Animals", "type": 1 }, { "tag": "Binding Sites", "type": 1 }, { "tag": "Biophysical Phenomena", "type": 1 }, { "tag": "Biophysics", "type": 1 }, { "tag": "Fluorescent Dyes", "type": 1 }, { "tag": "Molecular Structure", "type": 1 }, { "tag": "Myosins", "type": 1 }, { "tag": "Naphthalenesulfonates", "type": 1 }, { "tag": "Peptide Fragments", "type": 1 }, { "tag": "Polymers", "type": 1 }, { "tag": "Protein Conformation", "type": 1 }, { "tag": "Rabbits", "type": 1 }, { "tag": "Structure-Activity Relationship", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2011-07-18T13:11:06Z", "dateModified": "2011-07-18T13:11:06Z" } }, { "key": "I6N4KZC8", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/I6N4KZC8", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/I6N4KZC8", "type": "text/html" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } }, "creatorSummary": "Crosbie et al.", "parsedDate": "1994-11", "numChildren": 0 }, "data": { "key": "I6N4KZC8", "version": 1, "itemType": "journalArticle", "title": "Structural connectivity in actin: effect of C-terminal modifications on the properties of actin", "creators": [ { "creatorType": "author", "firstName": "R H", "lastName": "Crosbie" }, { "creatorType": "author", "firstName": "C", "lastName": "Miller" }, { "creatorType": "author", "firstName": "P", "lastName": "Cheung" }, { "creatorType": "author", "firstName": "T", "lastName": "Goodnight" }, { "creatorType": "author", "firstName": "A", "lastName": "Muhlrad" }, { "creatorType": "author", "firstName": "E", "lastName": "Reisler" } ], "abstractNote": "In this study, we use fluorescent probes and proteolytic digestions to demonstrate structural coupling between distant regions of actin. We show that modifications of Cys-374 in the C-terminus of actin slow the rate of nucleotide exchange in the nucleotide cleft. Conformational coupling between the C-terminus and the DNasal loop in subdomain II is observed in proteolytic digestion experiments in which a new C-terminal cleavage site is exposed upon DNasel binding. The functional consequences of C-terminal modification are evident from S-1 ATPase activity and the in vitro motility experiments with modified actins. Pyrene actin, labeled at Cys-374, activates S-1 ATPase activity only half as well as control actin. This reduction is attributed to a lower Vmax value because the affinity of pyrene actin to S-1 is not significantly altered. The in vitro sliding velocity of pyrene actin is also decreased. However, IAEDANS labeling of actin (also at Cys-374) enhances the Vmax of acto-S-1 ATPase activity and the in vitro sliding velocity by approximately 25%. These results are discussed in terms of conformational coupling between distant regions in actin and the functional implications of the interactions of actin-binding proteins with the C-terminus of actin.", "publicationTitle": "Biophysical Journal", "publisher": "", "place": "", "date": "Nov 1994", "volume": "67", "issue": "5", "section": "", "partNumber": "", "partTitle": "", "pages": "1957-1964", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Biophys. J", "DOI": "10.1016/S0006-3495(94)80678-2", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pubmed/7858132", "accessDate": "2011-07-18T13:10:53Z", "PMID": "", "PMCID": "", "ISSN": "0006-3495", "archive": "", "archiveLocation": "", "shortTitle": "Structural connectivity in actin", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 7858132", "tags": [ { "tag": "Actins", "type": 1 }, { "tag": "Animals", "type": 1 }, { "tag": "Binding Sites", "type": 1 }, { "tag": "Biophysical Phenomena", "type": 1 }, { "tag": "Biophysics", "type": 1 }, { "tag": "Fluorescent Dyes", "type": 1 }, { "tag": "Molecular Structure", "type": 1 }, { "tag": "Myosins", "type": 1 }, { "tag": "Naphthalenesulfonates", "type": 1 }, { "tag": "Peptide Fragments", "type": 1 }, { "tag": "Polymers", "type": 1 }, { "tag": "Protein Conformation", "type": 1 }, { "tag": "Rabbits", "type": 1 }, { "tag": "Structure-Activity Relationship", "type": 1 } ], "collections": [ "A97KU5P2" ], "relations": {}, "dateAdded": "2011-07-18T13:10:53Z", "dateModified": "2011-07-18T13:10:53Z" } }, { "key": "77HZGGTN", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/77HZGGTN", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/77HZGGTN", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/47225/items/B8MP38T7", "type": "application/json" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } } }, "data": { "key": "77HZGGTN", "version": 1, "parentItem": "B8MP38T7", "itemType": "attachment", "linkMode": "linked_url", "title": "PubMed Central Link", "accessDate": "2011-07-15T20:46:48Z", "url": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1225570/", "note": "", "contentType": "text/html", "charset": "", "tags": [], "relations": {}, "dateAdded": "2011-07-15T20:46:48Z", "dateModified": "2011-07-15T20:46:48Z" } }, { "key": "B8MP38T7", "version": 1, "library": { "type": "group", "id": 47225, "name": "BME Guilford Lab", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/47225/items/B8MP38T7", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme_guilford_lab/items/B8MP38T7", "type": "text/html" } }, "meta": { "createdByUser": { "id": 507581, "username": "hmbansbach", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } }, "creatorSummary": "Crosbie et al.", "parsedDate": "1994-11", "numChildren": 1 }, "data": { "key": "B8MP38T7", "version": 1, "itemType": "journalArticle", "title": "Structural connectivity in actin: effect of C-terminal modifications on the properties of actin.", "creators": [ { "creatorType": "author", "firstName": "R H", "lastName": "Crosbie" }, { "creatorType": "author", "firstName": "C", "lastName": "Miller" }, { "creatorType": "author", "firstName": "P", "lastName": "Cheung" }, { "creatorType": "author", "firstName": "T", "lastName": "Goodnight" }, { "creatorType": "author", "firstName": "A", "lastName": "Muhlrad" }, { "creatorType": "author", "firstName": "E", "lastName": "Reisler" } ], "abstractNote": "In this study, we use fluorescent probes and proteolytic digestions to demonstrate structural coupling between distant regions of actin. We show that modifications of Cys-374 in the C-terminus of actin slow the rate of nucleotide exchange in the nucleotide cleft. Conformational coupling between the C-terminus and the DNasal loop in subdomain II is observed in proteolytic digestion experiments in which a new C-terminal cleavage site is exposed upon DNasel binding. The functional consequences of C-terminal modification are evident from S-1 ATPase activity and the in vitro motility experiments with modified actins. Pyrene actin, labeled at Cys-374, activates S-1 ATPase activity only half as well as control actin. This reduction is attributed to a lower Vmax value because the affinity of pyrene actin to S-1 is not significantly altered. The in vitro sliding velocity of pyrene actin is also decreased. However, IAEDANS labeling of actin (also at Cys-374) enhances the Vmax of acto-S-1 ATPase activity and the in vitro sliding velocity by approximately 25%. These results are discussed in terms of conformational coupling between distant regions in actin and the functional implications of the interactions of actin-binding proteins with the C-terminus of actin.", "publicationTitle": "Biophysical Journal", "publisher": "", "place": "", "date": "1994-11", "volume": "67", "issue": "5", "section": "", "partNumber": "", "partTitle": "", "pages": "1957-1964", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Biophys J", "DOI": "", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "0006-3495", "archive": "", "archiveLocation": "", "shortTitle": "Structural connectivity in actin", "language": "", "libraryCatalog": "PubMed Central", "callNumber": "", "rights": "", "extra": "PMID: 7858132\nPMCID: 1225570", "tags": [], "collections": [], "relations": {}, "dateAdded": "2011-07-15T20:46:48Z", "dateModified": "2011-07-15T20:46:48Z" } } ]