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            "abstractNote": "The Chlamydomonas flagellar surface exhibits interesting adhesive properties that are associated with flagellar surface motility. This dynamic surface property can be exhibited as the binding and movement of small polystyrene microspheres or as the interaction of the flagellar surface with a solid substrate followed by whole cell locomotion, termed ldquogliding.rdquo In order to identify flagellar surface proteins that mediate substrate interaction during flagellar surface motility, two immobilized iodination systems were employed that mimic the conditions for flagellar surface motility: small polystyrene microspheres derivatized with lactoperoxidase, and large glass beads derivatized with Iodogen. Use of these iodination conditions resulted in preferential iodination of a high-molecular-weight glycoprotein with apparent molecular weight of 300,000-350,000. These results suggest this glycoprotein as a major candidate for the surface-exposed adhesive component that directly interacts with the substrate and couples the substrate to a system of force transduction presumed to be located within the flagellum.",
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                    "firstName": "Robert A.",
                    "lastName": "Bloodgood"
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                    "firstName": "Nancy L.",
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            "abstractNote": "Summary The biflagellate green algaChlamydomonas can exhibit substrate-associated gliding motility in addition to its ability to swim through a liquid medium. The flagella are the organelles responsible for both forms of whole-cell locomotion although the mechanism in each case is very different. In this study, we demonstrate that the binding of polystyrene microspheres to the flagellar surface ofChlamydomonas initiates clustering of the major flagellar-membrane glycoprotein, which is known to be involved in motility-associated substrate adhesion. In addition, we demonstrate that microsphere binding to the flagellar surface initiates the same transmembrane signaling pathway that is initiated by antibody- or lectin-induced crosslinking of the major flagellar-membrane glycoprotein. In each case, the signaling pathway involves the activation of a calciumdependent protein phosphatase that dephosphorylates a flagellar phosphoprotein known to be associated with the major flagellar-membrane glycoprotein. Bound microspheres are translocated along the flagellar surface at approximately the same velocity as whole-cell gliding motility. Previous observations suggest that microsphere binding and translocation along the flagellar surface may be a reflection of the same force-transducing system responsible for whole-cell gliding motility. In which case, these observations suggest that the transmembrane signaling pathway initiated by crosslinking the major flagellar-membrane glycoprotein is the same one that is activated when the cell contacts a physiological substrate by its flagellar surface.",
            "publicationTitle": "Protoplasma",
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            "date": "March 01, 1998",
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            "itemType": "journalArticle",
            "title": "The transmembrane signaling pathway involved in directed movements of Chlamydomonas flagellar membrane glycoproteins involves the dephosphorylation of a 60-kD phosphoprotein that binds to the major flagellar membrane glycoprotein",
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                    "firstName": "RA",
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                    "lastName": "Salomonsky"
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            "abstractNote": "",
            "publicationTitle": "J Cell Biol",
            "publisher": "",
            "place": "",
            "date": "1994",
            "volume": "",
            "issue": "127",
            "section": "",
            "partNumber": "",
            "partTitle": "",
            "pages": "803-811",
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            "creatorSummary": "Allersma et al.",
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            "version": 1,
            "itemType": "journalArticle",
            "title": "Two-Dimensional Tracking of ncd Motility by Back Focal Plane Interferometry",
            "creators": [
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                    "creatorType": "author",
                    "firstName": "Miriam W.",
                    "lastName": "Allersma"
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                {
                    "creatorType": "author",
                    "firstName": "Frederick",
                    "lastName": "Gittes"
                },
                {
                    "creatorType": "author",
                    "firstName": "Michael J.",
                    "lastName": "deCastro"
                },
                {
                    "creatorType": "author",
                    "firstName": "Russell J.",
                    "lastName": "Stewart"
                },
                {
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                    "firstName": "Christoph F.",
                    "lastName": "Schmidt"
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            ],
            "abstractNote": "A technique for detecting the displacement of micron-sized optically trapped probes using far-field interference is introduced, theoretically explained, and used to study the motility of the ncd motor protein. Bead motions in the focal plane relative to the optical trap were detected by measuring laser intensity shifts in the back-focal plane of the microscope condenser by projection on a quadrant diode. This detection method is two-dimensional, largely independent of the position of the trap in the field of view and has ~10-[mu]s time resolution. The high resolution makes it possible to apply spectral analysis to measure dynamic parameters such as local viscosity and attachment compliance. A simple quantitative theory for back-focal-plane detection was derived that shows that the laser intensity shifts are caused primarily by a far-field interference effect. The theory predicts the detector response to bead displacement, without adjustable parameters, with good accuracy. To demonstrate the potential of the method, the ATP-dependent motility of ncd, a kinesin-related motor protein, was observed with an in vitro bead assay. A fusion protein consisting of truncated ncd (amino acids 195-685) fused with glutathione-S-transferase was adsorbed to silica beads, and the axial and lateral motions of the beads along the microtubule surface were observed with high spatial and temporal resolution. The average axial velocity of the ncd-coated beads was 230 ± 30 nm/s (average ± SD). Spectral analysis of bead motion showed the increase in viscous drag near the surface; we also found that any elastic constraints of the moving motors are much smaller than the constraints due to binding in the presence of the nonhydrolyzable nucleotide adenylylimidodiphosphate.",
            "publicationTitle": "Biophysical Journal",
            "publisher": "",
            "place": "",
            "date": "February 1998",
            "volume": "74",
            "issue": "2",
            "section": "",
            "partNumber": "",
            "partTitle": "",
            "pages": "1074-1085",
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            "seriesTitle": "",
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            "journalAbbreviation": "",
            "DOI": "10.1016/S0006-3495(98)74031-7",
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            "url": "http://www.sciencedirect.com/science/article/B94RW-4V295RH-1C/2/e61378ad23510eebe2a7afc4df48b32a",
            "accessDate": "2010-08-09T21:28:13Z",
            "PMID": "",
            "PMCID": "",
            "ISSN": "0006-3495",
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            "libraryCatalog": "ScienceDirect",
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            "dateAdded": "2011-02-23T19:56:52Z",
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    {
        "key": "T6CMRBHR",
        "version": 1,
        "library": {
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            },
            "creatorSummary": "Badoual et al.",
            "parsedDate": "2002-05-14",
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        "data": {
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            "version": 1,
            "itemType": "journalArticle",
            "title": "Bidirectional cooperative motion of molecular motors",
            "creators": [
                {
                    "creatorType": "author",
                    "firstName": "M.",
                    "lastName": "Badoual"
                },
                {
                    "creatorType": "author",
                    "firstName": "F.",
                    "lastName": "Jülicher"
                },
                {
                    "creatorType": "author",
                    "firstName": "J.",
                    "lastName": "Prost"
                }
            ],
            "abstractNote": "Recently, in a beautiful set of experiments, it has been shown that a Ncd mutant, NK11, which lacks directionality in its individual motion, was able to exhibit a new kind of directed motion in motility assays (Endow, S. A. & Higuchi, H. (2000) Nature (London) 406, 913–916): the filaments keep a given velocity for a while and then suddenly move in the opposite direction with similar velocity. We show that these observations nicely illustrate the concept of dynamic transitions in motor collections introduced earlier in the case of an infinite number of motors. We investigate the experimentally relevant case of a finite number of motors both when directionality is present (kinesins, myosins, Ncd) and absent (NK11). Using a symmetric two-state model, we demonstrate that bidirectional motion is the signature of a dynamic transition that results from the collective behavior of many motors acting on the same filament. For motors exhibiting directional bias individually, an asymmetric two-state model is appropriate. In that case, dynamic transitions exist for motor collections in the presence of an external force. We give predictions for the dependence of motion on ATP concentration, external forces, and the number of motors involved. In particular, we show that the reversal time grows exponentially with the number of motors per filament.",
            "publicationTitle": "Proceedings of the National Academy of Sciences of the United States of America",
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            "place": "",
            "date": "May 14 , 2002",
            "volume": "99",
            "issue": "10",
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            "pages": "6696 -6701",
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            "DOI": "10.1073/pnas.102692399",
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