[ { "key": "68UWA4KE", "version": 63, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/68UWA4KE", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/68UWA4KE", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/58600/items/NF3BJI9P", "type": "application/json" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } } }, "data": { "key": "68UWA4KE", "version": 63, "parentItem": "NF3BJI9P", "itemType": "attachment", "linkMode": "linked_url", "title": "pdf", "accessDate": "2016-08-16T14:24:33Z", "url": "http://www.aimspress.com/article/10.3934/molsci.2016.3.426/pdf", "note": "", "contentType": "", "charset": "", "tags": [], "relations": {}, "dateAdded": "2016-08-16T14:24:33Z", "dateModified": "2016-08-16T14:24:33Z" } }, { "key": "NF3BJI9P", "version": 62, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/NF3BJI9P", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/NF3BJI9P", "type": "text/html" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } }, "creatorSummary": "Bansbach and Guilford", "parsedDate": "2016", "numChildren": 1 }, "data": { "key": "NF3BJI9P", "version": 62, "itemType": "journalArticle", "title": "Actin nitrosylation and its effect on myosin driven motility", "creators": [ { "creatorType": "author", "firstName": "H.M.", "lastName": "Bansbach" }, { "creatorType": "author", "firstName": "W.H.", "lastName": "Guilford" } ], "abstractNote": "The cytoskeletal protein actin can be nitrosylated, and others have shown that nitrosylation of actin can affect actin filament polymerization. However, the effects of nitrosylation on its interactions with the motor protein myosin are unknown. We therefore measured the effect of S-nitrosylation on the interactions of several actin isoforms with myosin. We used a modified coumarin switch assay to determine the number of nitrosylated cysteines in α-skeletal muscle, α-smooth muscle, and non-muscle (β and γ) actin in response to in vitro treatment with nitroso-L-cysteine—an endogenous nitric oxide (NO) donor. We also measured actin filament velocity over heavy meromyosin (HMM) using an in vitro motility assay, the isometric force generated by HMM using a laser trap, and the actin activated ATPase rates of HMM. We found that all three isoforms of actin were nitrosylated equally at ~2 sites per monomer. Nitrosylation of skeletal muscle α-actin reduced the velocity of actin filaments over HMM in a dose dependent fashion. The sliding velocities of all actin isoforms over HMM were reduced equally by ~24% when nitrosylated with 50 µM donor. Our data are consistent with actin nitrosylation causing an increase in the time myosin remains bound to actin during its hydrolytic cycle.", "publicationTitle": "AIMS Molecular Science", "publisher": "", "place": "", "date": "2016", "volume": "3", "issue": "3", "section": "", "partNumber": "", "partTitle": "", "pages": "426-438", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "", "citationKey": "", "url": "http://www.aimspress.com/article/10.3934/molsci.2016.3.426#", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2016-08-16T14:21:05Z", "dateModified": "2016-08-16T14:23:47Z" } }, { "key": "5W77RT6E", "version": 56, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/5W77RT6E", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/5W77RT6E", "type": "text/html" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } }, "creatorSummary": "Vikhorev et al.", "parsedDate": "2008-12-15", "numChildren": 1 }, "data": { "key": "5W77RT6E", "version": 56, "itemType": "journalArticle", "title": "Bending flexibility of actin filaments during motor-induced sliding", "creators": [ { "creatorType": "author", "firstName": "Petr G.", "lastName": "Vikhorev" }, { "creatorType": "author", "firstName": "Natalia N.", "lastName": "Vikhoreva" }, { "creatorType": "author", "firstName": "Alf", "lastName": "Månsson" } ], "abstractNote": "Muscle contraction and other forms of cell motility occur as a result of cyclic interactions between myosin molecules and actin filaments. Force generation is generally attributed to ATP-driven structural changes in myosin, whereas a passive role is ascribed to actin. However, some results challenge this view, predicting structural changes in actin during motor activity, e.g., when the actin filaments slide on a myosin-coated surface in vitro. Here, we analyzed statistical properties of the sliding filament paths, allowing us to detect changes of this type. It is interesting to note that evidence for substantial structural changes that led to increased bending flexibility of the filaments was found in phalloidin-stabilized, but not in phalloidin-free, actin filaments. The results are in accordance with the idea that a high-flexibility structural state of actin is a prerequisite for force production, but not the idea that a low-to-high flexibility transition of the actin filament should be an important component of the force-generating step per se. Finally, our data challenge the general view that phalloidin-stabilized filaments behave as native actin filaments in their interaction with myosin. This has important implications, since phalloidin stabilization is a routine procedure in most studies of actomyosin function.", "publicationTitle": "Biophysical Journal", "publisher": "", "place": "", "date": "Dec 15, 2008", "volume": "95", "issue": "12", "section": "", "partNumber": "", "partTitle": "", "pages": "5809-5819", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Biophys. J.", "DOI": "10.1529/biophysj.108.140335", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "1542-0086", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "eng", "libraryCatalog": "PubMed", "callNumber": "", "rights": "", "extra": "PMID: 18835897\nPMCID: PMC2599860", "tags": [ { "tag": "Actin Cytoskeleton", "type": 1 }, { "tag": "Actomyosin", "type": 1 }, { "tag": "Animals", "type": 1 }, { "tag": "Cattle", "type": 1 }, { "tag": "Movement", "type": 1 }, { "tag": "Myosin Subfragments", "type": 1 }, { "tag": "Phalloidine", "type": 1 }, { "tag": "Rabbits", "type": 1 }, { "tag": "Temperature", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2016-08-03T17:51:55Z", "dateModified": "2016-08-03T17:51:55Z" } }, { "key": "236JGGJD", "version": 56, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/236JGGJD", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/236JGGJD", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/58600/items/5W77RT6E", "type": "application/json" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } } }, "data": { "key": "236JGGJD", "version": 56, "parentItem": "5W77RT6E", "itemType": "attachment", "linkMode": "linked_url", "title": "PubMed entry", "accessDate": "2016-08-03T17:51:55Z", "url": "http://www.ncbi.nlm.nih.gov/pubmed/18835897", "note": "", "contentType": "text/html", "charset": "", "tags": [], "relations": {}, "dateAdded": "2016-08-03T17:51:55Z", "dateModified": "2016-08-03T17:51:55Z" } }, { "key": "FW5EXNKJ", "version": 55, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/FW5EXNKJ", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/FW5EXNKJ", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/58600/items/H3SEWKVI", "type": "application/json" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } } }, "data": { "key": "FW5EXNKJ", "version": 55, "parentItem": "H3SEWKVI", "itemType": "attachment", "linkMode": "linked_url", "title": "PubMed entry", "accessDate": "2016-08-03T17:45:25Z", "url": "http://www.ncbi.nlm.nih.gov/pubmed/11808777", "note": "", "contentType": "text/html", "charset": "", "tags": [], "relations": {}, "dateAdded": "2016-08-03T17:45:25Z", "dateModified": "2016-08-03T17:45:25Z" } }, { "key": "H3SEWKVI", "version": 55, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/H3SEWKVI", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/H3SEWKVI", "type": "text/html" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } }, "creatorSummary": "Tokuraku and Uyeda", "parsedDate": "2001", "numChildren": 1 }, "data": { "key": "H3SEWKVI", "version": 55, "itemType": "journalArticle", "title": "Phalloidin affects the myosin-dependent sliding velocities of actin filaments in a bound-divalent cation dependent manner", "creators": [ { "creatorType": "author", "firstName": "K.", "lastName": "Tokuraku" }, { "creatorType": "author", "firstName": "T. Q.", "lastName": "Uyeda" } ], "abstractNote": "We examined sliding velocities in vitro of four types of actin filaments, that is, filaments with Ca2+ or Mg2+ bound at the high affinity metal binding site, each with rhodamine phalloidin bound with a high or low stoichiometry. When surfaces coated with a high density of heavy meromyosin (HMM) were used, high stoichiometric concentrations of rhodamine phalloidin reduced sliding velocities of only Ca2+-actin filaments, by 40%. As the HMM density on surfaces was reduced, continuous movement of actin filaments became dependent on the presence of methylcellulose and sliding velocities of all four types became progressively slower. Interestingly, Ca2+-actin filaments with a high stoichiometric concentration of rhodamine phalloidin were the fastest among the four types of filaments on sparse HMM surfaces. In contrast, phalloidin did not affect steady state ATPase activities of HMM in the presence of Ca2+- or Mg2+-actin filaments. We speculate that the reversal of the order of sliding velocities among the four types of actin filaments between high and low densities of HMM relates with different axial elasticity of the actin filaments, so that stiffer filaments move slower on dense HMM surfaces, but faster on sparse surfaces, than elastic ones.", "publicationTitle": "Journal of Muscle Research and Cell Motility", "publisher": "", "place": "", "date": "2001", "volume": "22", "issue": "4", "section": "", "partNumber": "", "partTitle": "", "pages": "371-378", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "J. Muscle Res. Cell. Motil.", "DOI": "", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "0142-4319", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "eng", "libraryCatalog": "PubMed", "callNumber": "", "rights": "", "extra": "PMID: 11808777", "tags": [ { "tag": "Actin Cytoskeleton", "type": 1 }, { "tag": "Animals", "type": 1 }, { "tag": "Binding Sites", "type": 1 }, { "tag": "Calcium", "type": 1 }, { "tag": "Cations, Divalent", "type": 1 }, { "tag": "Magnesium", "type": 1 }, { "tag": "Methylcellulose", "type": 1 }, { "tag": "Muscle, Skeletal", "type": 1 }, { "tag": "Myosin Subfragments", "type": 1 }, { "tag": "Myosins", "type": 1 }, { "tag": "Phalloidine", "type": 1 }, { "tag": "Rabbits", "type": 1 }, { "tag": "Rhodamines", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2016-08-03T17:45:25Z", "dateModified": "2016-08-03T17:45:25Z" } }, { "key": "DK2HVFSQ", "version": 54, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/DK2HVFSQ", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/DK2HVFSQ", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/58600/items/QK8UHDGN", "type": "application/json" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } } }, "data": { "key": "DK2HVFSQ", "version": 54, "parentItem": "QK8UHDGN", "itemType": "attachment", "linkMode": "linked_url", "title": "ScienceDirect Snapshot", "accessDate": "2016-08-03T17:43:03Z", "url": "http://www.sciencedirect.com/science/article/pii/S0022283683713938", "note": "", "contentType": "text/html", "charset": "", "tags": [], "relations": {}, "dateAdded": "2016-08-03T17:43:03Z", "dateModified": "2016-08-03T17:43:03Z" } }, { "key": "QK8UHDGN", "version": 54, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/QK8UHDGN", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/QK8UHDGN", "type": "text/html" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } }, "creatorSummary": "Orlova and Egelman", "parsedDate": "1993-07-20", "numChildren": 1 }, "data": { "key": "QK8UHDGN", "version": 54, "itemType": "journalArticle", "title": "A Conformational Change in the Actin Subunit Can Change the Flexibility of the Actin Filament", "creators": [ { "creatorType": "author", "firstName": "A.", "lastName": "Orlova" }, { "creatorType": "author", "firstName": "E. H.", "lastName": "Egelman" } ], "abstractNote": "The mechanical properties of F-actin are very significant, given the central structural role played by actin filaments within muscle and the cytoskeleton. We have determined that actin can exist in a state that has a fourfold increase in flexibility over normal F-actin, and that this state can be induced by either a modification of the bound metals or of the nucleotide. Three-dimensional reconstructions from electron micrographs suggest that this increased flexibility arises from a rotation of subdomain-2, the smallest subdomain, of the actin subunit. The modulation of actin's flexibility by Ca2+ and Mg2+ may have important physiological consequences within the cell. Further, since it has been shown that myosin-decorated actin filaments are more flexible than pure F-actin, it is possible that myosin induces this more flexible state in actin.", "publicationTitle": "Journal of Molecular Biology", "publisher": "", "place": "", "date": "July 20, 1993", "volume": "232", "issue": "2", "section": "", "partNumber": "", "partTitle": "", "pages": "334-341", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Journal of Molecular Biology", "DOI": "10.1006/jmbi.1993.1393", "citationKey": "", "url": "http://www.sciencedirect.com/science/article/pii/S0022283683713938", "accessDate": "2016-08-03T17:43:03Z", "PMID": "", "PMCID": "", "ISSN": "0022-2836", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "ScienceDirect", "callNumber": "", "rights": "", "extra": "", "tags": [ { "tag": "Actin", "type": 1 }, { "tag": "electron microscopy", "type": 1 }, { "tag": "image analysis", "type": 1 }, { "tag": "polymer flexibility", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2016-08-03T17:43:03Z", "dateModified": "2016-08-03T17:43:03Z" } }, { "key": "XWQ4ASJQ", "version": 53, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/XWQ4ASJQ", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/XWQ4ASJQ", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/58600/items/DZBS8VQB", "type": "application/json" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } } }, "data": { "key": "XWQ4ASJQ", "version": 53, "parentItem": "DZBS8VQB", "itemType": "attachment", "linkMode": "linked_url", "title": "ScienceDirect Full Text PDF", "accessDate": "2016-08-03T15:28:46Z", "url": "http://www.sciencedirect.com/science/article/pii/S000634951630220X/pdfft?md5=4878a7d2017cebae30a1e4316d950a3a&pid=1-s2.0-S000634951630220X-main.pdf", "note": "", "contentType": "application/pdf", "charset": "", "tags": [], "relations": {}, "dateAdded": "2016-08-03T15:28:46Z", "dateModified": "2016-08-03T15:28:46Z" } }, { "key": "RKN3J2IW", "version": 53, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/RKN3J2IW", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/RKN3J2IW", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/58600/items/DZBS8VQB", "type": "application/json" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } } }, "data": { "key": "RKN3J2IW", "version": 53, "parentItem": "DZBS8VQB", "itemType": "attachment", "linkMode": "linked_url", "title": "ScienceDirect Snapshot", "accessDate": "2016-08-03T15:28:46Z", "url": "http://www.sciencedirect.com/science/article/pii/S000634951630220X", "note": "", "contentType": "text/html", "charset": "", "tags": [], "relations": {}, "dateAdded": "2016-08-03T15:28:46Z", "dateModified": "2016-08-03T15:28:46Z" } }, { "key": "DZBS8VQB", "version": 53, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/DZBS8VQB", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/DZBS8VQB", "type": "text/html" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } }, "creatorSummary": "Jégou and Romet-Lemonne", "parsedDate": "2016-05-24", "numChildren": 2 }, "data": { "key": "DZBS8VQB", "version": 53, "itemType": "journalArticle", "title": "Single Filaments to Reveal the Multiple Flavors of Actin", "creators": [ { "creatorType": "author", "firstName": "Antoine", "lastName": "Jégou" }, { "creatorType": "author", "firstName": "Guillaume", "lastName": "Romet-Lemonne" } ], "abstractNote": "A number of key cell processes rely on specific assemblies of actin filaments, which are all constructed from nearly identical building blocks: the abundant and extremely conserved actin protein. A central question in the field is to understand how different filament networks can coexist and be regulated. Discoveries in science are often related to technical advances. Here, we focus on the ongoing single filament revolution and discuss how these techniques have greatly contributed to our understanding of actin assembly. In particular, we highlight how they have refined our understanding of the many protein-based regulatory mechanisms that modulate actin assembly. It is now becoming apparent that other factors give filaments a specific identity that determines which proteins will bind to them. We argue that single filament techniques will play an essential role in the coming years as we try to understand the many ways actin filaments can take different flavors and unveil how these flavors modulate the action of regulatory proteins. We discuss different factors known to make actin filaments distinguishable by regulatory proteins and speculate on their possible consequences.", "publicationTitle": "Biophysical Journal", "publisher": "", "place": "", "date": "May 24, 2016", "volume": "110", "issue": "10", "section": "", "partNumber": "", "partTitle": "", "pages": "2138-2146", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Biophysical Journal", "DOI": "10.1016/j.bpj.2016.04.025", "citationKey": "", "url": "http://www.sciencedirect.com/science/article/pii/S000634951630220X", "accessDate": "2016-08-03T15:28:46Z", "PMID": "", "PMCID": "", "ISSN": "0006-3495", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "ScienceDirect", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2016-08-03T15:28:46Z", "dateModified": "2016-08-03T15:28:46Z" } }, { "key": "9CAV8UKQ", "version": 52, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/9CAV8UKQ", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/9CAV8UKQ", "type": "text/html" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } }, "creatorSummary": "Galkin et al.", "parsedDate": "2010-11", "numChildren": 2 }, "data": { "key": "9CAV8UKQ", "version": 52, "itemType": "journalArticle", "title": "Structural polymorphism in F-actin", "creators": [ { "creatorType": "author", "firstName": "Vitold E.", "lastName": "Galkin" }, { "creatorType": "author", "firstName": "Albina", "lastName": "Orlova" }, { "creatorType": "author", "firstName": "Gunnar F.", "lastName": "Schröder" }, { "creatorType": "author", "firstName": "Edward H.", "lastName": "Egelman" } ], "abstractNote": "Actin has maintained an exquisite degree of sequence conservation over large evolutionary distances for reasons that are not understood. The desire to explain phenomena from muscle contraction to cytokinesis in mechanistic detail has driven the generation of an atomic model of the actin filament (F-actin). Here we use electron cryomicroscopy to show that frozen-hydrated actin filaments contain a multiplicity of different structural states. We show (at ~10 Å resolution) that subdomain 2 can be disordered and can make multiple contacts with the C terminus of a subunit above it. We link a number of disease-causing mutations in the human ACTA1 gene to the most structurally dynamic elements of actin. Because F-actin is structurally polymorphic, it cannot be described using only one atomic model and must be understood as an ensemble of different states.\nView full text", "publicationTitle": "Nature Structural & Molecular Biology", "publisher": "", "place": "", "date": "November 2010", "volume": "17", "issue": "11", "section": "", "partNumber": "", "partTitle": "", "pages": "1318-1323", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Nat Struct Mol Biol", "DOI": "10.1038/nsmb.1930", "citationKey": "", "url": "http://www.nature.com/nsmb/journal/v17/n11/abs/nsmb.1930.html", "accessDate": "2016-08-03T15:26:05Z", "PMID": "", "PMCID": "", "ISSN": "1545-9993", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "en", "libraryCatalog": "www.nature.com", "callNumber": "", "rights": "© 2010 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.", "extra": "", "tags": [ { "tag": "Actin", "type": 1 }, { "tag": "structural biology", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2016-08-03T15:26:05Z", "dateModified": "2016-08-03T15:26:05Z" } }, { "key": "DQIMI3WR", "version": 52, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/DQIMI3WR", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/DQIMI3WR", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/58600/items/9CAV8UKQ", "type": "application/json" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } } }, "data": { "key": "DQIMI3WR", "version": 52, "parentItem": "9CAV8UKQ", "itemType": "attachment", "linkMode": "linked_url", "title": "Full Text PDF", "accessDate": "2016-08-03T15:26:05Z", "url": "http://www.nature.com/nsmb/journal/v17/n11/pdf/nsmb.1930.pdf", "note": "", "contentType": "application/pdf", "charset": "", "tags": [], "relations": {}, "dateAdded": "2016-08-03T15:26:05Z", "dateModified": "2016-08-03T15:26:05Z" } }, { "key": "FMKV2WKF", "version": 52, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/FMKV2WKF", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/FMKV2WKF", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/58600/items/9CAV8UKQ", "type": "application/json" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } } }, "data": { "key": "FMKV2WKF", "version": 52, "parentItem": "9CAV8UKQ", "itemType": "attachment", "linkMode": "linked_url", "title": "Snapshot", "accessDate": "2016-08-03T15:26:05Z", "url": "http://www.nature.com/nsmb/journal/v17/n11/abs/nsmb.1930.html", "note": "", "contentType": "text/html", "charset": "", "tags": [], "relations": {}, "dateAdded": "2016-08-03T15:26:05Z", "dateModified": "2016-08-03T15:26:05Z" } }, { "key": "58DBZTZ6", "version": 51, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/58DBZTZ6", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/58DBZTZ6", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/58600/items/WQXNWMJQ", "type": "application/json" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } } }, "data": { "key": "58DBZTZ6", "version": 51, "parentItem": "WQXNWMJQ", "itemType": "attachment", "linkMode": "linked_url", "title": "ScienceDirect Snapshot", "accessDate": "2016-08-01T21:30:57Z", "url": "http://www.sciencedirect.com/science/article/pii/S000634959580072X", "note": "", "contentType": "text/html", "charset": "", "tags": [], "relations": {}, "dateAdded": "2016-08-01T21:30:57Z", "dateModified": "2016-08-01T21:30:57Z" } }, { "key": "WQXNWMJQ", "version": 51, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/WQXNWMJQ", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/WQXNWMJQ", "type": "text/html" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } }, "creatorSummary": "Kim et al.", "parsedDate": "1995-11-01", "numChildren": 1 }, "data": { "key": "WQXNWMJQ", "version": 51, "itemType": "journalArticle", "title": "Conformational changes in subdomain 2 of G-actin: fluorescence probing by dansyl ethylenediamine attached to Gln-41", "creators": [ { "creatorType": "author", "firstName": "E.", "lastName": "Kim" }, { "creatorType": "author", "firstName": "M.", "lastName": "Motoki" }, { "creatorType": "author", "firstName": "K.", "lastName": "Seguro" }, { "creatorType": "author", "firstName": "A.", "lastName": "Muhlrad" }, { "creatorType": "author", "firstName": "E.", "lastName": "Reisler" } ], "abstractNote": "Gln-41 on G-actin was specifically labeled with a fluorescent probe, dansyl ethylenediamine (DED), via transglutaminase reaction to explore the conformational changes in subdomain 2 of actin. Replacement of Ca2+ with Mg2+ and ATP with ADP on G-actin produced large changes in the emission properties of DED. These substitutions resulted in blue shifts in the wavelength of maximum emission and increases in DED fluorescence. Excitation of labeled actin at 295 nm revealed energy transfer from tryptophans to DED. Structure considerations and Cu2+ quenching experiments suggested that Trp-79 and/or Trp-86 serves as energy donors to DED. Energy transfer from these residues to DED on Gln-41 increased with the replacement of Ca2+ with Mg2+ and ATP with ADP. Polymerization of Mg-G-actin with MgCl2 resulted in much smaller changes in DED fluorescence than divalent cation substitution. This suggests that the conformation of loop 38–52 on actin is primed for the polymerization reaction by the substitution of Ca2+ with Mg2+ on G-actin.", "publicationTitle": "Biophysical Journal", "publisher": "", "place": "", "date": "November 1, 1995", "volume": "69", "issue": "5", "section": "", "partNumber": "", "partTitle": "", "pages": "2024-2032", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Biophysical Journal", "DOI": "10.1016/S0006-3495(95)80072-X", "citationKey": "", "url": "http://www.sciencedirect.com/science/article/pii/S000634959580072X", "accessDate": "2016-08-01T21:30:57Z", "PMID": "", "PMCID": "", "ISSN": "0006-3495", "archive": "", "archiveLocation": "", "shortTitle": "Conformational changes in subdomain 2 of G-actin", "language": "", "libraryCatalog": "ScienceDirect", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2016-08-01T21:30:57Z", "dateModified": "2016-08-01T21:30:57Z" } }, { "key": "4EQGKB97", "version": 50, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/4EQGKB97", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/4EQGKB97", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/58600/items/UQTTBEF7", "type": "application/json" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } } }, "data": { "key": "4EQGKB97", "version": 50, "parentItem": "UQTTBEF7", "itemType": "attachment", "linkMode": "linked_url", "title": "ScienceDirect Full Text PDF", "accessDate": "2016-07-28T19:12:17Z", "url": "http://www.sciencedirect.com/science/article/pii/S0003986109003129/pdfft?md5=ace09ab995c6d4700ff1001ed9371fba&pid=1-s2.0-S0003986109003129-main.pdf", "note": "", "contentType": "application/pdf", "charset": "", "tags": [], "relations": {}, "dateAdded": "2016-07-28T19:12:17Z", "dateModified": "2016-07-28T19:12:17Z" } }, { "key": "UQTTBEF7", "version": 50, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/UQTTBEF7", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/UQTTBEF7", "type": "text/html" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } }, "creatorSummary": "Vikhoreva et al.", "parsedDate": "2009-11", "numChildren": 2 }, "data": { "key": "UQTTBEF7", "version": 50, "itemType": "journalArticle", "title": "The in vitro motility assay parameters of actin filaments from Mytilus edulis exposed in vivo to copper ions", "creators": [ { "creatorType": "author", "firstName": "Natalia N.", "lastName": "Vikhoreva" }, { "creatorType": "author", "firstName": "Petr G.", "lastName": "Vikhorev" }, { "creatorType": "author", "firstName": "Maria A.", "lastName": "Fedorova" }, { "creatorType": "author", "firstName": "Ralf", "lastName": "Hoffmann" }, { "creatorType": "author", "firstName": "Alf", "lastName": "Månsson" }, { "creatorType": "author", "firstName": "Nadezda V.", "lastName": "Kuleva" } ], "abstractNote": "One important aspect of oxidative stress is chemical modification of lipids, proteins and nucleic acids. Copper has been shown to be one of the agents causing oxidative stress. In muscles copper binds to Cys-374 of the actin monomer and catalyzes interchain S–S bond formation in F-actin. The aim of the present work was to study the functional consequences of actin modifications, induced by copper treatment of Mytilus edulisin vivo, on the in vitro motility parameters of isolated actin filaments from foot and adductor muscles. CuCl2 treatment reduced the sliding velocity of actin filaments extracted from foot muscle by about 22% and increased their flexibility by 1.7 times, while had no effect on the motility and flexibility of adductor actin. Using immunoblotting techniques we found that copper ions induced carbonylation in foot but not in adductor actin. In samples of foot actin an increase in cross-linked oligomers and truncated monomers was detected. Carbonylated structures of actin and corresponding changes in its functional properties may be considered as biomarkers for environmental monitoring.", "publicationTitle": "Archives of Biochemistry and Biophysics", "publisher": "", "place": "", "date": "November 2009", "volume": "491", "issue": "1–2", "section": "", "partNumber": "", "partTitle": "", "pages": "32-38", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Archives of Biochemistry and Biophysics", "DOI": "10.1016/j.abb.2009.09.014", "citationKey": "", "url": "http://www.sciencedirect.com/science/article/pii/S0003986109003129", "accessDate": "2016-07-28T19:12:17Z", "PMID": "", "PMCID": "", "ISSN": "0003-9861", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "ScienceDirect", "callNumber": "", "rights": "", "extra": "", "tags": [ { "tag": "Actin structure", "type": 1 }, { "tag": "Copper ions", "type": 1 }, { "tag": "Flexibility", "type": 1 }, { "tag": "In vitro motility assay", "type": 1 }, { "tag": "Mussel", "type": 1 }, { "tag": "Oxidative modifications", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2016-07-28T19:12:17Z", "dateModified": "2016-07-28T19:12:17Z" } }, { "key": "8TRBZ6NB", "version": 50, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/8TRBZ6NB", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/8TRBZ6NB", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/58600/items/UQTTBEF7", "type": "application/json" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } } }, "data": { "key": "8TRBZ6NB", "version": 50, "parentItem": "UQTTBEF7", "itemType": "attachment", "linkMode": "linked_url", "title": "ScienceDirect Snapshot", "accessDate": "2016-07-28T19:12:17Z", "url": "http://www.sciencedirect.com/science/article/pii/S0003986109003129", "note": "", "contentType": "text/html", "charset": "", "tags": [], "relations": {}, "dateAdded": "2016-07-28T19:12:17Z", "dateModified": "2016-07-28T19:12:17Z" } }, { "key": "ZHRGC2ST", "version": 46, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/ZHRGC2ST", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/ZHRGC2ST", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/58600/items/XV5XP57D", "type": "application/json" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } } }, "data": { "key": "ZHRGC2ST", "version": 46, "parentItem": "XV5XP57D", "itemType": "attachment", "linkMode": "linked_url", "title": "PubMed Central Link", "accessDate": "2013-05-13T21:43:13Z", "url": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3477893/", "note": "", "contentType": "text/html", "charset": "", "tags": [], "relations": {}, "dateAdded": "2013-05-13T21:43:13Z", "dateModified": "2013-05-13T21:43:13Z" } }, { "key": "XV5XP57D", "version": 46, "library": { "type": "group", "id": 58600, "name": "Guilford_Actin NO", "links": { "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/58600/items/XV5XP57D", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/guilford_actin_no/items/XV5XP57D", "type": "text/html" } }, "meta": { "createdByUser": { "id": 190601, "username": "whg2n", "name": "Will Guilford", "links": { "alternate": { "href": "https://www.zotero.org/whg2n", "type": "text/html" } } }, "creatorSummary": "Roknic et al.", "parsedDate": "2012-10", "numChildren": 2 }, "data": { "key": "XV5XP57D", "version": 46, "itemType": "journalArticle", "title": "Mutation analysis of Netrin 1 and HMX3 genes in patients with superior semicircular canal dehiscence syndrome", "creators": [ { "creatorType": "author", "firstName": "Nikola", "lastName": "Roknic" }, { "creatorType": "author", "firstName": "Alexander", "lastName": "Huber" }, { "creatorType": "author", "firstName": "Stefan C. A.", "lastName": "Hegemann" }, { "creatorType": "author", "firstName": "Rudolf", "lastName": "Hausler" }, { "creatorType": "author", "firstName": "Nicolas", "lastName": "Gurtler" } ], "abstractNote": "Conclusion\nIn spite of its absence in the control population, there is questionable evidence for the alteration c.114C->T in the HMX3 gene being implicated in the development of superior semicircular canal dehiscence (SSCD). However, the concept of a complex disease is valid for SSCD and a possible molecular origin can neither be confirmed nor excluded by the results of this study.\n\nObjectives\nSSCD was first described in 1998 by Minor et al. While the etiology is not clear, findings from both temporal bone CT and histologic studies suggest a congenital or developmental origin. In recent years, a couple of genes regulating inner ear morphogenesis have been described. Specifically, Netrin-1 and HMX3 have been shown to be critically involved in the formation of the SCC. Molecular alterations in these two genes might lead to a disturbed development of this canal and might represent an explanation for SSCD.\n\nMethods\nDNA was extracted from whole blood of 15 patients with SSCD. The coding sequences of Netrin-1 and HMX3 were amplified by PCR and sequenced.\n\nResults\nOne sequence alteration, heterozygous c.114C->T (conservative change without alteration of amino acid) in exon 1 of HMX3, was detected in 2 of 15 patients but not in 300 control chromosomes. The study was supported in part by the Emilia-Guggenheim-Schnurr-Foundation, Basel, Switzerland.", "publicationTitle": "Acta Oto-Laryngologica", "publisher": "", "place": "", "date": "2012-10", "volume": "132", "issue": "10", "section": "", "partNumber": "", "partTitle": "", "pages": "1061-1065", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Acta Otolaryngol", "DOI": "10.3109/00016489.2012.681797", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3477893/", "accessDate": "2013-05-13T21:43:13Z", "PMID": "", "PMCID": "", "ISSN": "0001-6489", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "PubMed Central", "callNumber": "", "rights": "", "extra": "PMID: 22779713\nPMCID: PMC3477893", "tags": [], "collections": [], "relations": {}, "dateAdded": "2013-05-13T21:43:13Z", "dateModified": "2013-05-13T21:43:13Z" } }, { "key": "UEE3849Z", "version": 46, "library": { "type": "group", "id": 58600, "name": 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"name": "", "links": { "alternate": { "href": "https://www.zotero.org/hmbansbach", "type": "text/html" } } }, "creatorSummary": "Guo and Guilford", "parsedDate": "2004", "numChildren": 2 }, "data": { "key": "UQQADNIZ", "version": 1, "itemType": "journalArticle", "title": "The tail of myosin reduces actin filament velocity in the in vitro motility assay", "creators": [ { "creatorType": "author", "firstName": "Bin", "lastName": "Guo" }, { "creatorType": "author", "firstName": "William H.", "lastName": "Guilford" } ], "abstractNote": "It has been observed that heavy meromyosin (HMM) propels actin filaments to higher velocities than native myosin in the in vitro motility assay, yet the reason for this difference has remained unexplained. Since the major difference between these two proteins is the presence of the tail in native myosin, we tested the hypothesis that unknown interactions between actin and the tail (LMM) slow motility in native myosin. Chymotryptic HMM and LMM were mixed in a range of molar ratios (0–5 LMM/HMM) and compared to native rat skeletal myosin in the in vitro motility assay at 30°C. Increasing proportions of LMM to HMM slowed actin filament velocities, becoming equivalent to native myosin at a ratio of 3 LMM/HMM. NH 4+-ATPase assays demonstrated that HMM concentrations on the surface were constant and independent of LMM concentration, arguing against a simple displacement mechanism. Relationships between velocity and the number of available heads suggested that the duty cycle of HMM was not altered by the presence of LMM. HMM prepared with a lower chymotrypsin concentration and with very short digestion times moved actin at the same high velocity. The difference between velocities of actin filament propelled by HMM and HMM/LMM decreased with increasing ionic strength, suggesting that ionic bonds between myosin tail and actin filaments may play a role in slowing filament velocity. These data suggest the high velocities of actin filaments over HMM result from the absence of drag generated by the myosin tail, and not from proteolytic nicking of the motor domain. Cell Motil. Cytoskeleton 59:264–272, 2004. © 2004 Wiley-Liss, Inc.", "publicationTitle": "Cell Motility and the Cytoskeleton", "publisher": "", "place": "", "date": "2004", "volume": "59", "issue": "4", "section": "", "partNumber": "", "partTitle": "", "pages": "264–272", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1002/cm.20040", "citationKey": "", "url": "http://onlinelibrary.wiley.com/doi/10.1002/cm.20040/abstract", "accessDate": "2012-12-12T17:15:09Z", "PMID": "", "PMCID": "", "ISSN": "1097-0169", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "en", "libraryCatalog": "Wiley Online Library", "callNumber": "", "rights": "Copyright © 2004 Wiley-Liss, Inc.", "extra": "", "tags": [ { "tag": "ATPase assay", "type": 1 }, { "tag": "heavy meromyosin", "type": 1 }, { "tag": "ionic strength", "type": 1 }, { "tag": "light meromyosin", "type": 1 }, { "tag": "motility assay", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2012-12-12T17:15:09Z", "dateModified": "2012-12-12T17:15:09Z" } } ]