[ { "key": "DC93AIV4", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/DC93AIV4", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/DC93AIV4", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/38635/items/E5B9C44B", "type": "application/json" } }, "meta": { "createdByUser": { "id": 519454, "username": "jlu4qt", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/jlu4qt", "type": "text/html" } } } }, "data": { "key": "DC93AIV4", "version": 1, "parentItem": "E5B9C44B", "itemType": "attachment", "linkMode": "linked_url", "title": "PubMed Central Link", "accessDate": "2011-05-02T19:18:07Z", "url": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2592363/", "note": "", "contentType": "text/html", "charset": "", "tags": [], "relations": {}, "dateAdded": "2011-05-02T19:18:07Z", "dateModified": "2011-05-02T19:18:07Z" } }, { "key": "E5B9C44B", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/E5B9C44B", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/E5B9C44B", "type": "text/html" } }, "meta": { "createdByUser": { "id": 519454, "username": "jlu4qt", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/jlu4qt", "type": "text/html" } } }, "creatorSummary": "Khalil et al.", "parsedDate": "2008-12-09", "numChildren": 1 }, "data": { "key": "E5B9C44B", "version": 1, "itemType": "journalArticle", "title": "Kinesin's cover-neck bundle folds forward to generate force", "creators": [ { "creatorType": "author", "firstName": "Ahmad S.", "lastName": "Khalil" }, { "creatorType": "author", "firstName": "David C.", "lastName": "Appleyard" }, { "creatorType": "author", "firstName": "Anna K.", "lastName": "Labno" }, { "creatorType": "author", "firstName": "Adrien", "lastName": "Georges" }, { "creatorType": "author", "firstName": "Martin", "lastName": "Karplus" }, { "creatorType": "author", "firstName": "Angela M.", "lastName": "Belcher" }, { "creatorType": "author", "firstName": "Wonmuk", "lastName": "Hwang" }, { "creatorType": "author", "firstName": "Matthew J.", "lastName": "Lang" } ], "abstractNote": "Each step of the kinesin motor involves a force-generating molecular rearrangement. Although significant progress has been made in elucidating the broad features of the kinesin mechanochemical cycle, molecular details of the force generation mechanism remain a mystery. Recent molecular dynamics simulations have suggested a mechanism in which the forward drive is produced when the N-terminal cover strand forms a β-sheet with the neck linker to yield the cover-neck bundle. We tested this proposal by comparing optical trapping motility measurements of cover strand mutants with the wild-type. Motility data, as well as kinetic analyses, revealed impairment of the force-generating capacity accompanied by a greater load dependence in the mechanochemical cycle. In particular, a mutant with the cover strand deleted functioned only marginally, despite the fact that the cover strand, the N-terminal “dangling end,” unlike the neck linker and nucleotide-binding pocket, is not involved with any previously considered energy transduction pathway. Furthermore, a constant assisting load, likely in lieu of a power stroke, was shown to rescue forward motility in the cover strand deletion mutant. Our results support a stepping mechanism driven by dynamic cover-neck bundle formation. They also suggest a strategy to generate motors with altered mechanical characteristics by targeting the force-generating element.", "publicationTitle": "", "publisher": "", "place": "", "date": "2008-12-9", "volume": "105", "issue": "49", "section": "", "partNumber": "", "partTitle": "", "pages": "19247-19252", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Proc Natl Acad Sci U S A", "DOI": "10.1073/pnas.0805147105", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "0027-8424", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "PubMed Central", "callNumber": "", "rights": "", "extra": "PMID: 19047639\nPMCID: 2592363", "tags": [], "collections": [], "relations": {}, "dateAdded": "2011-05-02T19:18:06Z", "dateModified": "2011-05-02T19:18:06Z" } }, { "key": "CAP9B3NZ", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/CAP9B3NZ", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/CAP9B3NZ", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/38635/items/K477IU78", "type": "application/json" } }, "meta": { "createdByUser": { "id": 519454, "username": "jlu4qt", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/jlu4qt", "type": "text/html" } } } }, "data": { "key": "CAP9B3NZ", "version": 1, "parentItem": "K477IU78", "itemType": "attachment", "linkMode": "linked_url", "title": "PubMed Central Link", "accessDate": "2011-05-02T06:18:46Z", "url": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1533991/", "note": "", "contentType": "text/html", "charset": "", "tags": [], "relations": {}, "dateAdded": "2011-05-02T06:18:46Z", "dateModified": "2011-05-02T06:18:46Z" } }, { "key": "K477IU78", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/K477IU78", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/K477IU78", "type": "text/html" } }, "meta": { "createdByUser": { "id": 519454, "username": "jlu4qt", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/jlu4qt", "type": "text/html" } } }, "creatorSummary": "Rosenfeld et al.", "parsedDate": "2003-05-16", "numChildren": 1 }, "data": { "key": "K477IU78", "version": 1, "itemType": "journalArticle", "title": "HOW KINESIN USES INTERNAL STRAIN TO WALK PROCESSIVELY", "creators": [ { "creatorType": "author", "firstName": "Steven S.", "lastName": "Rosenfeld" }, { "creatorType": "author", "firstName": "Polly M.", "lastName": "Fordyce" }, { "creatorType": "author", "firstName": "Geraldine M.", "lastName": "Jefferson" }, { "creatorType": "author", "firstName": "Peter H.", "lastName": "King" }, { "creatorType": "author", "firstName": "Steven M.", "lastName": "Block" } ], "abstractNote": "The ability of kinesin to travel long distances on its microtubule track without dissociating has led to a variety of models to explain how this remarkable degree of processivity is maintained. All of these require that the two motor domains remain enzymatically “out of phase,” a behavior that would ensure that, at any given time, one motor is strongly attached to the microtubule. The maintenance of this coordination over many mechanochemical cycles has never been explained, because key steps in the cycle could not be directly observed. We have addressed this issue by applying several novel spectroscopic approaches to monitor motor dissociation, phosphate release, and nucleotide binding during processive movement by a dimeric kinesin construct. Our data argue that the major effect of the internal strain generated when both motor domains of kinesin bind the microtubule is to block ATP from binding to the leading motor. This effect guarantees the two motor domains remain out of phase for many mechanochemical cycles and provides an efficient and adaptable mechanism for the maintenance of processive movement.", "publicationTitle": "The Journal of biological chemistry", "publisher": "", "place": "", "date": "2003-5-16", "volume": "278", "issue": "20", "section": "", "partNumber": "", "partTitle": "", "pages": "18550-18556", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "J Biol Chem", "DOI": "10.1074/jbc.M300849200", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "0021-9258", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "PubMed Central", "callNumber": "", "rights": "", "extra": "PMID: 12626516\nPMCID: 1533991", "tags": [], "collections": [], "relations": {}, "dateAdded": "2011-05-02T06:18:45Z", "dateModified": "2011-05-02T06:18:45Z" } }, { "key": "EKWXNHP2", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/EKWXNHP2", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/EKWXNHP2", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/38635/items/S7459T9T", "type": "application/json" } }, "meta": { "createdByUser": { "id": 520501, "username": "skv5ks", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/skv5ks", "type": "text/html" } } } }, "data": { "key": "EKWXNHP2", "version": 1, "parentItem": "S7459T9T", "itemType": "attachment", "linkMode": "linked_url", "title": "PubMed Central Link", "accessDate": "2011-05-02T06:07:32Z", "url": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2174365/", "note": "", "contentType": "text/html", "charset": "", "tags": [], "relations": {}, "dateAdded": "2011-05-02T06:07:32Z", "dateModified": "2011-05-02T06:07:32Z" } }, { "key": "S7459T9T", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/S7459T9T", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/S7459T9T", "type": "text/html" } }, "meta": { "createdByUser": { "id": 520501, "username": "skv5ks", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/skv5ks", "type": "text/html" } } }, "creatorSummary": "Tomishige and Vale", "parsedDate": "2000-11-27", "numChildren": 1 }, "data": { "key": "S7459T9T", "version": 1, "itemType": "journalArticle", "title": "Controlling Kinesin by Reversible Disulfide Cross-Linking", "creators": [ { "creatorType": "author", "firstName": "Michio", "lastName": "Tomishige" }, { "creatorType": "author", "firstName": "Ronald D.", "lastName": "Vale" } ], "abstractNote": "Conventional kinesin, a dimeric molecular motor, uses ATP-dependent conformational changes to move unidirectionally along a row of tubulin subunits on a microtubule. Two models have been advanced for the major structural change underlying kinesin motility: the first involves an unzippering/zippering of a small peptide (neck linker) from the motor catalytic core and the second proposes an unwinding/rewinding of the adjacent coiled-coil (neck coiled-coil). Here, we have tested these models using disulfide cross-linking of cysteines engineered into recombinant kinesin motors. When the neck linker motion was prevented by cross-linking, kinesin ceased unidirectional movement and only showed brief one-dimensional diffusion along microtubules. Motility fully recovered upon adding reducing agents to reverse the cross-link. When the neck linker motion was partially restrained, single kinesin motors showed biased diffusion towards the microtubule plus end but could not move effectively against a load imposed by an optical trap. Thus, partial movement of the neck linker suffices for directionality but not for normal processivity or force generation. In contrast, preventing neck coiled-coil unwinding by disulfide cross-linking had relatively little effect on motor activity, although the average run length of single kinesin molecules decreased by 30–50%. These studies indicate that conformational changes in the neck linker, not in the neck coiled-coil, drive processive movement by the kinesin motor.", "publicationTitle": "The Journal of Cell Biology", "publisher": "", "place": "", "date": "2000-11-27", "volume": "151", "issue": "5", "section": "", "partNumber": "", "partTitle": "", "pages": "1081-1092", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "J Cell Biol", "DOI": "", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "0021-9525", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "PubMed Central", "callNumber": "", "rights": "", "extra": "PMID: 11086009\nPMCID: 2174365", "tags": [], "collections": [], "relations": {}, "dateAdded": "2011-05-02T06:07:31Z", "dateModified": "2011-05-02T06:07:31Z" } }, { "key": "2TSR2GNP", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/2TSR2GNP", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/2TSR2GNP", "type": "text/html" } }, "meta": { "createdByUser": { "id": 519454, "username": "jlu4qt", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/jlu4qt", "type": "text/html" } } }, "creatorSummary": "Keshavarzian et al.", "parsedDate": "2003-05-01", "numChildren": 0 }, "data": { "key": "2TSR2GNP", "version": 1, "itemType": "journalArticle", "title": "Increases in free radicals and cytoskeletal protein oxidation and nitration in the colon of patients with inflammatory bowel disease", "creators": [ { "creatorType": "author", "firstName": "A", "lastName": "Keshavarzian" }, { "creatorType": "author", "firstName": "A", "lastName": "Banan" }, { "creatorType": "author", "firstName": "A", "lastName": "Farhadi" }, { "creatorType": "author", "firstName": "S", "lastName": "Komanduri" }, { "creatorType": "author", "firstName": "E", "lastName": "Mutlu" }, { "creatorType": "author", "firstName": "Y", "lastName": "Zhang" }, { "creatorType": "author", "firstName": "J Z", "lastName": "Fields" } ], "abstractNote": "Background: Overproduction of colonic oxidants contributes to mucosal injury in inflammatory bowel disease (IBD) but the mechanisms are unclear. Our recent findings using monolayers of intestinal cells suggest that the mechanism could be oxidant induced damage to cytoskeletal proteins. However, oxidants and oxidative damage have not been well characterised in IBD mucosa.Aims: To determine whether there are increases in oxidants and in tissue and cytoskeletal protein oxidation in IBD mucosa.Methods: We measured nitric oxide (NO) and markers of oxidative injury (carbonylation and nitrotyrosination) to tissue and cytoskeletal proteins in colonic mucosa from IBD patients (ulcerative colitis, Crohn’s disease, specific colitis) and controls. Outcomes were correlated with IBD severity score.Results: Inflamed mucosa showed the greatest increases in oxidants and oxidative damage. Smaller but still significant increases were seen in normal appearing mucosa of patients with active and inactive IBD. Tissue NO levels correlated with oxidative damage. Actin was markedly (>50%) carbonylated and nitrated in inflamed tissues of active IBD, less so in normal appearing tissues. Tubulin carbonylation occurred in parallel; tubulin nitration was not observed. NO and all measures of oxidative damage in tissue and cytoskeletal proteins in the mucosa correlated with IBD severity. Disruption of the actin cytoarchitecture was primarily within the epithelial cells and paracellular area.Conclusions: Oxidant levels increase in IBD along with oxidation of tissue and cytoskeletal proteins. Oxidative injury correlated with disease severity but is also present in substantial amounts in normal appearing mucosa of IBD patients, suggesting that oxidative injury does not necessarily lead to tissue injury and is not entirely a consequence of tissue injury. Marked actin oxidation (>50%)—which appears to result from cumulative oxidative damage—was only seen in inflamed mucosa, suggesting that oxidant induced cytoskeletal disruption is required for tissue injury, mucosal disruption, and IBD flare up.", "publicationTitle": "Gut", "publisher": "", "place": "", "date": "May 01 , 2003", "volume": "52", "issue": "5", "section": "", "partNumber": "", "partTitle": "", "pages": "720 -728", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1136/gut.52.5.720", "citationKey": "", "url": "http://gut.bmj.com/content/52/5/720.abstract", "accessDate": "2011-05-02T03:22:40Z", "PMID": "", "PMCID": "", "ISSN": "", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "Highwire 2.0", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2011-05-02T03:22:40Z", "dateModified": "2011-05-02T03:22:40Z" } }, { "key": "GSU6VUJB", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/GSU6VUJB", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/GSU6VUJB", "type": "text/html" } }, "meta": { "createdByUser": { "id": 520501, "username": "skv5ks", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/skv5ks", "type": "text/html" } } }, "creatorSummary": "Dalle-Donne et al.", "parsedDate": "2003-03", "numChildren": 0 }, "data": { "key": "GSU6VUJB", "version": 1, "itemType": "journalArticle", "title": "Protein carbonyl groups as biomarkers of oxidative stress", "creators": [ { "creatorType": "author", "firstName": "Isabella", "lastName": "Dalle-Donne" }, { "creatorType": "author", "firstName": "Ranieri", "lastName": "Rossi" }, { "creatorType": "author", "firstName": "Daniela", "lastName": "Giustarini" }, { "creatorType": "author", "firstName": "Aldo", "lastName": "Milzani" }, { "creatorType": "author", "firstName": "Roberto", "lastName": "Colombo" } ], "abstractNote": "Oxidative stress, an imbalance toward the pro-oxidant side of the pro-oxidant/antioxidant homeostasis, occurs in several human diseases. Among these diseases are those in which high levels of protein carbonyl (CO) groups have been observed, including Alzheimer's disease (AD), rheumatoid arthritis, diabetes, sepsis, chronic renal failure, and respiratory distress syndrome. What relationships might be among high level of protein CO groups, oxidative stress, and diseases remain uncertain.The usage of protein CO groups as biomarkers of oxidative stress has some advantages in comparison with the measurement of other oxidation products because of the relative early formation and the relative stability of carbonylated proteins. Most of the assays for detection of protein CO groups involve derivatisation of the carbonyl group with 2,4-dinitrophenylhydrazine (DNPH), which leads to formation of a stable dinitrophenyl (DNP) hydrazone product. This then can be detected by various means, such as spectrophotometric assay, enzyme-linked immunosorbent assay (ELISA), and one-dimensional or two-dimensional electrophoresis followed by Western blot immunoassay. At present, the measurement of protein CO groups after their derivatisation with DNPH is the most widely utilized measure of protein oxidation.", "publicationTitle": "Clinica Chimica Acta; International Journal of Clinical Chemistry", "publisher": "", "place": "", "date": "Mar 2003", "volume": "329", "issue": "1-2", "section": "", "partNumber": "", "partTitle": "", "pages": "23-38", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Clin. Chim. Acta", "DOI": "", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pubmed/12589963", "accessDate": "2011-05-02T02:59:44Z", "PMID": "", "PMCID": "", "ISSN": "0009-8981", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 12589963", "tags": [ { "tag": "Animals", "type": 1 }, { "tag": "Antibiotics, Antineoplastic", "type": 1 }, { "tag": "Biological Markers", "type": 1 }, { "tag": "Body Weight", "type": 1 }, { "tag": "Cardiomyopathies", "type": 1 }, { "tag": "Creatine Kinase", "type": 1 }, { "tag": "Doxorubicin", "type": 1 }, { "tag": "Echocardiography", "type": 1 }, { "tag": "Isoenzymes", "type": 1 }, { "tag": "Male", "type": 1 }, { "tag": "Myocardium", "type": 1 }, { "tag": "Organ Size", "type": 1 }, { "tag": "Oxidative Stress", "type": 1 }, { "tag": "Rats", "type": 1 }, { "tag": "Rats, Wistar", "type": 1 }, { "tag": "Troponin I", "type": 1 }, { "tag": "Troponin T", "type": 1 }, { "tag": "Ventricular Function, Left", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2011-05-02T02:59:44Z", "dateModified": "2011-05-02T02:59:44Z" } }, { "key": "BHR3M2IZ", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/BHR3M2IZ", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/BHR3M2IZ", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/38635/items/27RMP3W5", "type": "application/json" } }, "meta": { "createdByUser": { "id": 520501, "username": "skv5ks", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/skv5ks", "type": "text/html" } } } }, "data": { "key": "BHR3M2IZ", "version": 1, "parentItem": "27RMP3W5", "itemType": "attachment", "linkMode": "imported_url", "title": "Snapshot", "accessDate": "2011-04-29T21:13:21Z", "url": "http://hmg.oxfordjournals.org/content/17/9/1245.full.pdf+html?frame=sidebar", "note": "", "contentType": "text/html", "charset": "utf-8", "filename": "1245.full.html", "md5": null, "mtime": 1304111596136, "tags": [], "relations": {}, "dateAdded": "2011-04-29T21:13:21Z", "dateModified": "2011-04-29T21:13:36Z" } }, { "key": "27RMP3W5", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/27RMP3W5", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/27RMP3W5", "type": "text/html" } }, "meta": { "createdByUser": { "id": 520501, "username": "skv5ks", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/skv5ks", "type": "text/html" } } }, "creatorSummary": "Ebbing et al.", "parsedDate": "2008-05-01", "numChildren": 1 }, "data": { "key": "27RMP3W5", "version": 1, "itemType": "journalArticle", "title": "Effect of spastic paraplegia mutations in KIF5A kinesin on transport activity", "creators": [ { "creatorType": "author", "firstName": "Bettina", "lastName": "Ebbing" }, { "creatorType": "author", "firstName": "Klaudiusz", "lastName": "Mann" }, { "creatorType": "author", "firstName": "Agata", "lastName": "Starosta" }, { "creatorType": "author", "firstName": "Johann", "lastName": "Jaud" }, { "creatorType": "author", "firstName": "Ludger", "lastName": "Schöls" }, { "creatorType": "author", "firstName": "Rebecca", "lastName": "Schüle" }, { "creatorType": "author", "firstName": "Günther", "lastName": "Woehlke" } ], "abstractNote": "Hereditary spastic paraplegia (HSP) is a neurodegenerative disease caused by motoneuron degeneration. It is linked to at least 30 loci, among them SPG10, which causes dominant forms and originates in point mutations in the neuronal Kinesin-1 gene (KIF5A). Here, we investigate the motility of KIF5A and four HSP mutants. All mutations are single amino-acid exchanges and located in kinesin's motor or neck domain. The mutation in the neck (A361V) did not change the gliding properties in vitro, the others either reduced microtubule affinity or gliding velocity or both. In laser-trapping assays, none of the mutants moved more than a few steps along microtubules. Motility assays with mixtures of homodimeric wild-type, homodimeric mutant and heterodimeric wild-type/mutant motors revealed that only one mutant (N256S) reduces the gliding velocity at ratios present in heterozygous patients, whereas the others (K253N, R280C) do not. Attached to quantum dots as artificial cargo, mixtures involving N256S mutants produced slower cargo populations lagging behind in transport, whereas mixtures with the other mutants led to populations of quantum dots that rarely bound to microtubules. These differences indicate that the dominant inheritance of SPG10 is caused by two different mechanisms that both reduce the gross cargo flux, leading to deficient supply of the synapse.", "publicationTitle": "Human Molecular Genetics", "publisher": "", "place": "", "date": "May 01 , 2008", "volume": "17", "issue": "9", "section": "", "partNumber": "", "partTitle": "", "pages": "1245 -1252", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1093/hmg/ddn014", "citationKey": "", "url": "http://hmg.oxfordjournals.org/content/17/9/1245.abstract", "accessDate": "2011-04-29T21:13:20Z", "PMID": "", "PMCID": "", "ISSN": "", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "Highwire 2.0", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2011-04-29T21:13:20Z", "dateModified": "2011-04-29T21:13:20Z" } }, { "key": "3GN32EFN", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/3GN32EFN", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/3GN32EFN", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/38635/items/RD2WF54T", "type": "application/json" } }, "meta": { "createdByUser": { "id": 519454, "username": "jlu4qt", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/jlu4qt", "type": "text/html" } } } }, "data": { "key": "3GN32EFN", "version": 1, "parentItem": "RD2WF54T", "itemType": "attachment", "linkMode": "imported_url", "title": "Snapshot", "accessDate": "2011-04-28T15:20:27Z", "url": "http://jcb.rupress.org/content/152/5/959.abstract", "note": "", "contentType": "text/html", "charset": "utf-8", "filename": "959.html", "md5": null, "mtime": 1304004022225, "tags": [], "relations": {}, "dateAdded": "2011-04-28T15:20:27Z", "dateModified": "2011-04-29T20:27:24Z" } }, { "key": "UGIJWMEJ", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/UGIJWMEJ", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/UGIJWMEJ", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/38635/items/SN42T5KG", "type": "application/json" } }, "meta": { "createdByUser": { "id": 519454, "username": "jlu4qt", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/jlu4qt", "type": "text/html" } } } }, "data": { "key": "UGIJWMEJ", "version": 1, "parentItem": "SN42T5KG", "itemType": "attachment", "linkMode": "imported_url", "title": "Nature Snapshot", "accessDate": "2011-04-28T15:20:07Z", "url": "http://www.nature.com/emboj/journal/v22/n3/full/7594947a.html", "note": "", "contentType": "text/html", "charset": "utf-8", "filename": "7594947a.html", "md5": null, "mtime": 1304004002862, "tags": [], "relations": {}, "dateAdded": "2011-04-28T15:20:07Z", "dateModified": "2011-04-29T20:27:03Z" } }, { "key": "TNDMPIXQ", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/TNDMPIXQ", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/TNDMPIXQ", "type": "text/html" } }, "meta": { "createdByUser": { "id": 520501, "username": "skv5ks", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/skv5ks", "type": "text/html" } } }, "numChildren": 0 }, "data": { "key": "TNDMPIXQ", "version": 1, "itemType": "attachment", "linkMode": "imported_url", "title": "props.pdf", "accessDate": "2011-04-29T06:02:27Z", "url": "http://ocw.mit.edu/courses/materials-science-and-engineering/3-11-mechanics-of-materials-fall-1999/modules/props.pdf", "note": "", "contentType": "application/pdf", "charset": "windows-1252", "filename": "props.pdf", "md5": "b5bbfc572add144e103ca05a4fd5aaeb", "mtime": 1304056947416, "tags": [], "collections": [], "relations": {}, "dateAdded": "2011-04-29T06:02:27Z", "dateModified": "2011-04-29T06:02:43Z" } }, { "key": "2IFKTNVH", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/2IFKTNVH", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/2IFKTNVH", "type": "text/html" } }, "meta": { "createdByUser": { "id": 520501, "username": "skv5ks", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/skv5ks", "type": "text/html" } } }, "numChildren": 0 }, "data": { "key": "2IFKTNVH", "version": 1, "itemType": "document", "title": "", "creators": [], "abstractNote": "", "type": "", "date": "", "publisher": "", "place": "", "DOI": "", "citationKey": "", "url": "", "accessDate": "", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2011-04-29T06:02:10Z", "dateModified": "2011-04-29T06:02:10Z" } }, { "key": "RD2WF54T", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/RD2WF54T", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/RD2WF54T", "type": "text/html" } }, "meta": { "createdByUser": { "id": 519454, "username": "jlu4qt", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/jlu4qt", "type": "text/html" } } }, "creatorSummary": "Verhey et al.", "parsedDate": "2001-03-05", "numChildren": 1 }, "data": { "key": "RD2WF54T", "version": 1, "itemType": "journalArticle", "title": "Cargo of Kinesin Identified as Jip Scaffolding Proteins and Associated Signaling Molecules", "creators": [ { "creatorType": "author", "firstName": "Kristen J.", "lastName": "Verhey" }, { "creatorType": "author", "firstName": "Debra", "lastName": "Meyer" }, { "creatorType": "author", "firstName": "Reneé", "lastName": "Deehan" }, { "creatorType": "author", "firstName": "John", "lastName": "Blenis" }, { "creatorType": "author", "firstName": "Bruce J.", "lastName": "Schnapp" }, { "creatorType": "author", "firstName": "Tom A.", "lastName": "Rapoport" }, { "creatorType": "author", "firstName": "Ben", "lastName": "Margolis" } ], "abstractNote": "The cargo that the molecular motor kinesin moves along microtubules has been elusive. We searched for binding partners of the COOH terminus of kinesin light chain, which contains tetratricopeptide repeat (TPR) motifs. Three proteins were found, the c-jun NH2-terminal kinase (JNK)–interacting proteins (JIPs) JIP-1, JIP-2, and JIP-3, which are scaffolding proteins for the JNK signaling pathway. Concentration of JIPs in nerve terminals requires kinesin, as evident from the analysis of JIP COOH-terminal mutants and dominant negative kinesin constructs. Coprecipitation experiments suggest that kinesin carries the JIP scaffolds preloaded with cytoplasmic (dual leucine zipper–bearing kinase) and transmembrane signaling molecules (the Reelin receptor, ApoER2). These results demonstrate a direct interaction between conventional kinesin and a cargo, indicate that motor proteins are linked to their membranous cargo via scaffolding proteins, and support a role for motor proteins in spatial regulation of signal transduction pathways.", "publicationTitle": "The Journal of Cell Biology", "publisher": "", "place": "", "date": "March 05 , 2001", "volume": "152", "issue": "5", "section": "", "partNumber": "", "partTitle": "", "pages": "959 -970", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1083/jcb.152.5.959", "citationKey": "", "url": "http://jcb.rupress.org/content/152/5/959.abstract", "accessDate": "2011-04-28T15:20:26Z", "PMID": "", "PMCID": "", "ISSN": "", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "Highwire 2.0", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2011-04-28T15:20:26Z", "dateModified": "2011-04-28T15:20:26Z" } }, { "key": "SN42T5KG", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/SN42T5KG", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/SN42T5KG", "type": "text/html" } }, "meta": { "createdByUser": { "id": 519454, "username": "jlu4qt", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/jlu4qt", "type": "text/html" } } }, "creatorSummary": "Schafer et al.", "parsedDate": "2003-02-03", "numChildren": 1 }, "data": { "key": "SN42T5KG", "version": 1, "itemType": "journalArticle", "title": "A conserved tyrosine in the neck of a fungal kinesin regulates the catalytic motor core", "creators": [ { "creatorType": "author", "firstName": "Friederike", "lastName": "Schafer" }, { "creatorType": "author", "firstName": "Dominga", "lastName": "Deluca" }, { "creatorType": "author", "firstName": "Ulrike", "lastName": "Majdic" }, { "creatorType": "author", "firstName": "Joachim", "lastName": "Kirchner" }, { "creatorType": "author", "firstName": "Manfred", "lastName": "Schliwa" }, { "creatorType": "author", "firstName": "Luis", "lastName": "Moroder" }, { "creatorType": "author", "firstName": "Gunther", "lastName": "Woehlke" } ], "abstractNote": "", "publicationTitle": "EMBO J", "publisher": "", "place": "", "date": "February 03, 2003", "volume": "22", "issue": "3", "section": "", "partNumber": "", "partTitle": "", "pages": "450-458", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "EMBO J", "DOI": "10.1093/emboj/cdg036", "citationKey": "", "url": "http://dx.doi.org/10.1093/emboj/cdg036", "accessDate": "2011-04-28T15:20:06Z", "PMID": "", "PMCID": "", "ISSN": "0261-4189", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "Nature", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2011-04-28T15:20:06Z", "dateModified": "2011-04-28T15:20:06Z" } }, { "key": "BSF5EBVD", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/BSF5EBVD", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/BSF5EBVD", "type": "text/html" } }, "meta": { "createdByUser": { "id": 519454, "username": "jlu4qt", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/jlu4qt", "type": "text/html" } } }, "creatorSummary": "Garcia et al.", "parsedDate": "2009-10-13", "numChildren": 0 }, "data": { "key": "BSF5EBVD", "version": 1, "itemType": "journalArticle", "title": "Tyrosines in the kinesin-5 head domain are necessary for phosphorylation by Wee1 and for mitotic spindle integrity", "creators": [ { "creatorType": "author", "firstName": "Kristin", "lastName": "Garcia" }, { "creatorType": "author", "firstName": "Jason", "lastName": "Stumpff" }, { "creatorType": "author", "firstName": "Tod", "lastName": "Duncan" }, { "creatorType": "author", "firstName": "Tin Tin", "lastName": "Su" } ], "abstractNote": "Mitotic spindle assembly and maintenance relies on kinesin-5 motors that act as bipolar homotetramers to crosslink microtubules. Kinesin-5 motors have been the subject of extensive structure-function analysis, but the regulation of their activity in the context of mitotic progression remains less well understood. We report here that Drosophila kinesin-5 (KLP61F) is regulated by Drosophila Wee1 (dWee1). Wee1 tyrosine kinases are known to regulate mitotic entry via inhibitory phosphorylation of Cdk1. Recently, we showed that dWee1 also plays a role in mitotic spindle positioning through gamma-tubulin and spindle fidelity through an unknown mechanism. Here, we investigated whether a KLP61F-dWee1 interaction could explain the latter role of dWee1. We found that dWee1 phosphorylates KLP61F in vitro on three tyrosines within the head domain, the catalytic region that mediates movement along microtubules. In vivo, KLP61F with tyrosine-->phenylalanine mutations fails to complement a klp61f mutant and dominantly induces spindle defects similar to ones seen in dwee1 mutants. We propose that phosphorylation of the KLP61F catalytic domain by dWee1 is important for the motor's function. This study identifies a second substrate for a Wee1 kinase and provides evidence for phosphoregulation of a kinesin in the head domain.", "publicationTitle": "Current Biology: CB", "publisher": "", "place": "", "date": "Oct 13, 2009", "volume": "19", "issue": "19", "section": "", "partNumber": "", "partTitle": "", "pages": "1670-1676", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Curr. Biol", "DOI": "10.1016/j.cub.2009.08.013", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pubmed/19800237", "accessDate": "2011-04-28T15:15:53Z", "PMID": "", "PMCID": "", "ISSN": "1879-0445", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 19800237", "tags": [ { "tag": "Animals", "type": 1 }, { "tag": "Blotting, Western", "type": 1 }, { "tag": "Cell Cycle Proteins", "type": 1 }, { "tag": "Drosophila", "type": 1 }, { "tag": "Drosophila Proteins", "type": 1 }, { "tag": "Immunoprecipitation", "type": 1 }, { "tag": "Kinesin", "type": 1 }, { "tag": "Microtubule-Associated Proteins", "type": 1 }, { "tag": "Mitotic Spindle Apparatus", "type": 1 }, { "tag": "Mutagenesis, Site-Directed", "type": 1 }, { "tag": "Nuclear Proteins", "type": 1 }, { "tag": "Phosphorylation", "type": 1 }, { "tag": "Protein-Tyrosine Kinases", "type": 1 }, { "tag": "Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization", "type": 1 }, { "tag": "Tyrosine", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2011-04-28T15:15:53Z", "dateModified": "2011-04-28T15:15:53Z" } }, { "key": "BIEMR9EE", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/BIEMR9EE", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/BIEMR9EE", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/38635/items/TT48KVNI", "type": "application/json" } }, "meta": { "createdByUser": { "id": 519454, "username": "jlu4qt", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/jlu4qt", "type": "text/html" } } } }, "data": { "key": "BIEMR9EE", "version": 1, "parentItem": "TT48KVNI", "itemType": "attachment", "linkMode": "linked_url", "title": "PubMed Central Link", "accessDate": "2011-04-28T14:29:37Z", "url": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC329575/", "note": "", "contentType": "text/html", "charset": "", "tags": [], "relations": {}, "dateAdded": "2011-04-28T14:29:37Z", "dateModified": "2011-04-28T14:29:37Z" } }, { "key": "TT48KVNI", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/TT48KVNI", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/TT48KVNI", "type": "text/html" } }, "meta": { "createdByUser": { "id": 519454, "username": "jlu4qt", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/jlu4qt", "type": "text/html" } } }, "creatorSummary": "Walker and Shah", "parsedDate": "1988-02", "numChildren": 1 }, "data": { "key": "TT48KVNI", "version": 1, "itemType": "journalArticle", "title": "Evidence suggesting a role for hydroxyl radical in gentamicin-induced acute renal failure in rats.", "creators": [ { "creatorType": "author", "firstName": "P D", "lastName": "Walker" }, { "creatorType": "author", "firstName": "S V", "lastName": "Shah" } ], "abstractNote": "The protective effect of hydroxyl radical scavengers and iron chelators has strongly implicated the hydroxyl radical in several models of tissue injury. Based on in vitro studies showing gentamicin-enhanced generation of reactive oxygen metabolites in renal cortical mitochondria, we examined the effect of hydroxyl radical scavengers and iron chelators in gentamicin-induced acute renal failure. Rats treated with gentamicin (G) alone (100 mg/kg, s.c. x 8 d) developed advanced renal failure (BUN 215 +/- 30 mg/dl) compared to saline-treated controls (BUN 16 +/- 1 mg/dl, P less than 0.001). In contrast, rats treated with gentamicin and either dimethylthiourea (DMTU, an hydroxyl radical scavenger, 125 mg/kg, i.p. twice a day) or deferoxamine (DFO, an iron chelator, 20 mg/day by osmotic pump) had significantly lower BUN (G + DMTU 48.8 +/- 8 mg/dl, P less than 0.001, n = 8; G + DFO 30 +/- 7 mg/dl, P less than 0.001, n = 8). In separate experiments, treatment with two other hydroxyl radical scavengers (dimethyl sulfoxide or sodium benzoate) and a second iron chelator (2,3,dihydroxybenzoic acid) had a similar protective effect on renal function (as measured by both BUN and creatinine). In addition, histological evidence of damage was markedly reduced by the interventional agents. Finally, concurrent treatment with DMTU prevented the gentamicin induced increase in renal cortical malondialdehyde content (G: 4.4 +/- 0.2 nmol/mg; G + DMTU: 3.1 +/- 0.2 nmol/mg, P less than 0.0001, n = 8) suggesting that the protective effect of DMTU was related to free radical mechanisms rather than to some other effect. Taken together, these data strongly support a role for hydroxyl radical or a similar oxidant in gentamicin-induced acute renal failure.", "publicationTitle": "Journal of Clinical Investigation", "publisher": "", "place": "", "date": "1988-2", "volume": "81", "issue": "2", "section": "", "partNumber": "", "partTitle": "", "pages": "334-341", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "J Clin Invest", "DOI": "", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "0021-9738", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "PubMed Central", "callNumber": "", "rights": "", "extra": "PMID: 3123518\nPMCID: 329575", "tags": [], "collections": [], "relations": {}, "dateAdded": "2011-04-28T14:29:36Z", "dateModified": "2011-04-28T14:29:36Z" } }, { "key": "Q2T6NFKZ", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/Q2T6NFKZ", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/Q2T6NFKZ", "type": "text/html" }, "up": { "href": "https://api.zotero.org/groups/38635/items/WHZFGVSZ", "type": "application/json" } }, "meta": { "createdByUser": { "id": 519454, "username": "jlu4qt", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/jlu4qt", "type": "text/html" } } } }, "data": { "key": "Q2T6NFKZ", "version": 1, "parentItem": "WHZFGVSZ", "itemType": "attachment", "linkMode": "imported_url", "title": "Snapshot", "accessDate": "2011-04-28T14:28:48Z", "url": "http://www.pnas.org/content/95/17/9738.short", "note": "", "contentType": "text/html", "charset": "utf-8", "filename": "9738.html", "md5": null, "mtime": 1304000928309, "tags": [], "relations": {}, "dateAdded": "2011-04-28T14:28:48Z", "dateModified": "2011-04-28T14:29:20Z" } }, { "key": "WHZFGVSZ", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/WHZFGVSZ", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/WHZFGVSZ", "type": "text/html" } }, "meta": { "createdByUser": { "id": 519454, "username": "jlu4qt", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/jlu4qt", "type": "text/html" } } }, "creatorSummary": "Balasubramanian et al.", "parsedDate": "1998", "numChildren": 1 }, "data": { "key": "WHZFGVSZ", "version": 1, "itemType": "journalArticle", "title": "DNA strand breaking by the hydroxyl radical is governed by the accessible surface areas of the hydrogen atoms of the DNA backbone", "creators": [ { "creatorType": "author", "firstName": "Bhavani", "lastName": "Balasubramanian" }, { "creatorType": "author", "firstName": "Wendy K.", "lastName": "Pogozelski" }, { "creatorType": "author", "firstName": "Thomas D.", "lastName": "Tullius" } ], "abstractNote": "Despite extensive study, there is little experimental information available as to which of the deoxyribose hydrogen atoms of duplex DNA reacts most with the hydroxyl radical. To investigate this question, we prepared a set of double-stranded DNA molecules in which deuterium had been incorporated specifically at each position in the deoxyribose of one of the four nucleotides. We then measured deuterium kinetic isotope effects on the rate of cleavage of DNA by the hydroxyl radical. These experiments demonstrate that the hydroxyl radical reacts with the various hydrogen atoms of the deoxyribose in the order 5′ H > 4′ H > 3′ H ≈ 2′ H ≈ 1′ H. This order of reactivity parallels the exposure to solvent of the deoxyribose hydrogens. Our work therefore reveals the structural basis of the reaction of the hydroxyl radical with DNA. These results also provide information on the mechanism of DNA damage caused by ionizing radiation as well as atomic-level detail for the interpretation of hydroxyl radical footprints of DNA-protein complexes and chemical probe experiments on the structure of RNA and DNA in solution.", "publicationTitle": "Proceedings of the National Academy of Sciences", "publisher": "", "place": "", "date": "1998", "volume": "95", "issue": "17", "section": "", "partNumber": "", "partTitle": "", "pages": "9738 -9743", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1073/pnas.95.17.9738", "citationKey": "", "url": "http://www.pnas.org/content/95/17/9738.abstract", "accessDate": "2011-04-28T14:28:47Z", "PMID": "", "PMCID": "", "ISSN": "", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "Highwire 2.0", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2011-04-28T14:28:47Z", "dateModified": "2011-04-28T14:28:47Z" } }, { "key": "7U5EJ9W7", "version": 1, "library": { "type": "group", "id": 38635, "name": "BME2104 TB_JU_SV", "links": { "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/38635/items/7U5EJ9W7", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/bme2104_tb_ju_sv/items/7U5EJ9W7", "type": "text/html" } }, "meta": { "createdByUser": { "id": 519319, "username": "Tyler Brobst", "name": "", "links": { "alternate": { "href": "https://www.zotero.org/tyler_brobst", "type": "text/html" } } }, "creatorSummary": "Hahlen et al.", "parsedDate": "2006-07-07", "numChildren": 0 }, "data": { "key": "7U5EJ9W7", "version": 1, "itemType": "journalArticle", "title": "Feedback of the kinesin-1 neck-linker position on the catalytic site", "creators": [ { "creatorType": "author", "firstName": "Katrin", "lastName": "Hahlen" }, { "creatorType": "author", "firstName": "Bettina", "lastName": "Ebbing" }, { "creatorType": "author", "firstName": "Jörg", "lastName": "Reinders" }, { "creatorType": "author", "firstName": "Judith", "lastName": "Mergler" }, { "creatorType": "author", "firstName": "Albert", "lastName": "Sickmann" }, { "creatorType": "author", "firstName": "Guenther", "lastName": "Woehlke" } ], "abstractNote": "Kinesin-1 motor proteins step along microtubules by a mechanism in which the heads cycle through microtubule-bound and unbound states in an interlaced fashion. An important contribution to head-head coordination arises from the action of the neck-linker that docks onto the core motor domain upon ATP binding. We show here that the docked neck-linker not only guides the microtubule-unbound head to the next microtubule binding site but also signals its position to the head to which it is attached. Cross-linking studies on mutated kinesin constructs reveal that residues at the interface motor core/docked neck-linker, among them most importantly a conserved tyrosine, are involved in this feedback. The primary effect of the docked neck-linker is a reduced microtubule binding affinity in the ADP state.", "publicationTitle": "The Journal of Biological Chemistry", "publisher": "", "place": "", "date": "Jul 7, 2006", "volume": "281", "issue": "27", "section": "", "partNumber": "", "partTitle": "", "pages": "18868-18877", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "J. Biol. 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