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  1. Article ; Online: TPX2.

    Wadsworth, Pat

    Current biology : CB

    2015  Volume 25, Issue 24, Page(s) R1156–8

    Abstract: TPX2 is a microtubule-associated protein that is required for mitotic spindle function. ...

    Abstract TPX2 is a microtubule-associated protein that is required for mitotic spindle function.
    MeSH term(s) Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Mitosis ; Mutation ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Spindle Apparatus/metabolism
    Chemical Substances Cell Cycle Proteins ; Microtubule-Associated Proteins ; Nuclear Proteins ; TPX2 protein, human
    Language English
    Publishing date 2015-12-21
    Publishing country England
    Document type Journal Article
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2015.10.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Spindle positioning: actin mediates pushing and pulling.

    Bezanilla, Magdalena / Wadsworth, Pat

    Current biology : CB

    2009  Volume 19, Issue 4, Page(s) R168–9

    Abstract: To divide asymmetrically, the mitotic spindle is moved from the cell center to the cortex, a process that requires astral microtubules and the microtubule-based motor dynein. New work examining spindle positioning in large oocytes shows that in these ... ...

    Abstract To divide asymmetrically, the mitotic spindle is moved from the cell center to the cortex, a process that requires astral microtubules and the microtubule-based motor dynein. New work examining spindle positioning in large oocytes shows that in these cells actin and actin polymerization plays a key role.
    MeSH term(s) Actins/metabolism ; Animals ; Cell Division/physiology ; Dyneins/metabolism ; Mice ; Microtubules/metabolism ; Myosins/metabolism ; Oocytes/cytology ; Spindle Apparatus/metabolism
    Chemical Substances Actins ; Myosins (EC 3.6.4.1) ; Dyneins (EC 3.6.4.2)
    Language English
    Publishing date 2009-02-26
    Publishing country England
    Document type Journal Article
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2008.12.026
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Mitotic functions of kinesin-5.

    Ferenz, Nick P / Gable, Alyssa / Wadsworth, Pat

    Seminars in cell & developmental biology

    2010  Volume 21, Issue 3, Page(s) 255–259

    Abstract: In all eukaryotic cells, molecular motor proteins play essential roles in spindle assembly and function. The homotetrameric kinesin-5 motors in particular generate outward forces that establish and maintain spindle bipolarity and contribute to ... ...

    Abstract In all eukaryotic cells, molecular motor proteins play essential roles in spindle assembly and function. The homotetrameric kinesin-5 motors in particular generate outward forces that establish and maintain spindle bipolarity and contribute to microtubule flux. Cell-cycle dependent phosphorylation of kinesin-5 motors regulates their localization to the mitotic spindle. Analysis of live cells further shows that kinesin-5 motors are highly dynamic in the spindle. Understanding the interactions of kinesin-5 motors with microtubules and other spindle proteins is likely to broaden the documented roles of kinesin-5 motors during cell division.
    MeSH term(s) Animals ; Caenorhabditis elegans ; Cell Cycle ; Cell Division ; Dyneins/metabolism ; Humans ; Kinesin/genetics ; Kinesin/metabolism ; Kinesin/physiology ; Mitosis ; Models, Biological ; Phosphorylation ; Saccharomyces cerevisiae ; Spindle Apparatus
    Chemical Substances KIF11 protein, human ; KIF5A protein, human ; Dyneins (EC 3.6.4.2) ; Kinesin (EC 3.6.4.4)
    Language English
    Publishing date 2010-01-28
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1312473-0
    ISSN 1096-3634 ; 1084-9521
    ISSN (online) 1096-3634
    ISSN 1084-9521
    DOI 10.1016/j.semcdb.2010.01.019
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  4. Article ; Online: Suppression of microtubule assembly kinetics by the mitotic protein TPX2.

    Reid, Taylor A / Schuster, Breanna M / Mann, Barbara J / Balchand, Sai Keshavan / Plooster, Melissa / McClellan, Mark / Coombes, Courtney E / Wadsworth, Pat / Gardner, Melissa K

    Journal of cell science

    2016  Volume 129, Issue 7, Page(s) 1319–1328

    Abstract: TPX2 is a widely conserved microtubule-associated protein that is required for mitotic spindle formation and function. Previous studies have demonstrated that TPX2 is required for the nucleation of microtubules around chromosomes; however, the molecular ... ...

    Abstract TPX2 is a widely conserved microtubule-associated protein that is required for mitotic spindle formation and function. Previous studies have demonstrated that TPX2 is required for the nucleation of microtubules around chromosomes; however, the molecular mechanism by which TPX2 promotes microtubule nucleation remains a mystery. In this study, we found that TPX2 acts to suppress tubulin subunit off-rates during microtubule assembly and disassembly, thus allowing for the support of unprecedentedly slow rates of plus-end microtubule growth, and also leading to a dramatically reduced microtubule shortening rate. These changes in microtubule dynamics can be explained in computational simulations by a moderate increase in tubulin-tubulin bond strength upon TPX2 association with the microtubule lattice, which in turn acts to reduce the departure rate of tubulin subunits from the microtubule ends. Thus, the direct suppression of tubulin subunit off-rates by TPX2 during microtubule growth and shortening could provide a molecular mechanism to explain the nucleation of new microtubules in the presence of TPX2.
    MeSH term(s) Animals ; Cell Line ; Microtubule-Associated Proteins/metabolism ; Microtubules/metabolism ; Mitosis/physiology ; Sf9 Cells ; Spindle Apparatus/metabolism ; Spodoptera ; Tubulin/metabolism
    Chemical Substances Microtubule-Associated Proteins ; Tubulin
    Language English
    Publishing date 2016-04-01
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.178806
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Centrosome maturation: measurement of microtubule nucleation throughout the cell cycle by using GFP-tagged EB1.

    Piehl, Michelle / Tulu, U Serdar / Wadsworth, Pat / Cassimeris, Lynne

    Proceedings of the National Academy of Sciences of the United States of America

    2004  Volume 101, Issue 6, Page(s) 1584–1588

    Abstract: Understanding how cells regulate microtubule nucleation during the cell cycle has been limited by the inability to directly observe nucleation from the centrosome. To view nucleation in living cells, we imaged GFP-tagged EB1, a microtubule tip-binding ... ...

    Abstract Understanding how cells regulate microtubule nucleation during the cell cycle has been limited by the inability to directly observe nucleation from the centrosome. To view nucleation in living cells, we imaged GFP-tagged EB1, a microtubule tip-binding protein, and determined rates of nucleation by counting the number of EB1-GFP comets emerging from the centrosome over time. Nucleation rate increased 4-fold between G(2) and prophase and continued to rise through anaphase and telophase, reaching a maximum of 7 times interphase rates. We tested several models for centrosome maturation, including gamma-tubulin recruitment and increased centrosome size. The centrosomal concentration of gamma-tubulin reached a maximum at metaphase, and centrosome size increased through anaphase, whereas nucleation remained high through telophase, implying the presence of additional regulatory processes. Injection of anti-gamma-tubulin antibodies significantly blocked nucleation during metaphase but was less effective during anaphase, suggesting that a nucleation mechanism independent of gamma-tubulin contributes to centrosome function after metaphase.
    MeSH term(s) Animals ; Cell Cycle ; Centrosome/ultrastructure ; Fluorescent Antibody Technique ; Green Fluorescent Proteins ; LLC-PK1 Cells ; Luminescent Proteins/metabolism ; Microtubule-Associated Proteins/metabolism ; Microtubules/ultrastructure
    Chemical Substances EB1 microtubule binding proteins ; Luminescent Proteins ; Microtubule-Associated Proteins ; Green Fluorescent Proteins (147336-22-9)
    Language English
    Publishing date 2004-02-10
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.0308205100
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  6. Article ; Online: The chemical basis of serine palmitoyltransferase inhibition by myriocin.

    Wadsworth, John M / Clarke, David J / McMahon, Stephen A / Lowther, Jonathan P / Beattie, Ashley E / Langridge-Smith, Pat R R / Broughton, Howard B / Dunn, Teresa M / Naismith, James H / Campopiano, Dominic J

    Journal of the American Chemical Society

    2013  Volume 135, Issue 38, Page(s) 14276–14285

    Abstract: Sphingolipids (SLs) are essential components of cellular membranes formed from the condensation of L-serine and a long-chain acyl thioester. This first step is catalyzed by the pyridoxal-5'-phosphate (PLP)-dependent enzyme serine palmitoyltransferase ( ... ...

    Abstract Sphingolipids (SLs) are essential components of cellular membranes formed from the condensation of L-serine and a long-chain acyl thioester. This first step is catalyzed by the pyridoxal-5'-phosphate (PLP)-dependent enzyme serine palmitoyltransferase (SPT) which is a promising therapeutic target. The fungal natural product myriocin is a potent inhibitor of SPT and is widely used to block SL biosynthesis despite a lack of a detailed understanding of its molecular mechanism. By combining spectroscopy, mass spectrometry, X-ray crystallography, and kinetics, we have characterized the molecular details of SPT inhibition by myriocin. Myriocin initially forms an external aldimine with PLP at the active site, and a structure of the resulting co-complex explains its nanomolar affinity for the enzyme. This co-complex then catalytically degrades via an unexpected 'retro-aldol-like' cleavage mechanism to a C18 aldehyde which in turn acts as a suicide inhibitor of SPT by covalent modification of the essential catalytic lysine. This surprising dual mechanism of inhibition rationalizes the extraordinary potency and longevity of myriocin inhibition.
    MeSH term(s) Crystallography, X-Ray ; Fatty Acids, Monounsaturated/chemistry ; Kinetics ; Mutation ; Recombinant Proteins/chemistry ; Serine C-Palmitoyltransferase/antagonists & inhibitors ; Serine C-Palmitoyltransferase/chemistry ; Serine C-Palmitoyltransferase/genetics ; Sphingomonas/enzymology ; Sphingomonas/genetics
    Chemical Substances Fatty Acids, Monounsaturated ; Recombinant Proteins ; Serine C-Palmitoyltransferase (EC 2.3.1.50) ; thermozymocidin (YRM4E8R9ST)
    Language English
    Publishing date 2013-09-11
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021/ja4059876
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  7. Article: The Chemical Basis of Serine Palmitoyltransferase Inhibition by Myriocin

    Wadsworth, John M / Beattie Ashley E / Broughton Howard B / Campopiano Dominic J / Clarke David J / Dunn Teresa M / Langridge-Smith Pat R. R / Lowther Jonathan P / McMahon Stephen A / Naismith James H

    Journal of the American Chemical Society. 2013 Sept. 25, v. 135, no. 38

    2013  

    Abstract: Sphingolipids (SLs) are essential components of cellular membranes formed from the condensation of l-serine and a long-chain acyl thioester. This first step is catalyzed by the pyridoxal-5′-phosphate (PLP)-dependent enzyme serine palmitoyltransferase ( ... ...

    Abstract Sphingolipids (SLs) are essential components of cellular membranes formed from the condensation of l-serine and a long-chain acyl thioester. This first step is catalyzed by the pyridoxal-5′-phosphate (PLP)-dependent enzyme serine palmitoyltransferase (SPT) which is a promising therapeutic target. The fungal natural product myriocin is a potent inhibitor of SPT and is widely used to block SL biosynthesis despite a lack of a detailed understanding of its molecular mechanism. By combining spectroscopy, mass spectrometry, X-ray crystallography, and kinetics, we have characterized the molecular details of SPT inhibition by myriocin. Myriocin initially forms an external aldimine with PLP at the active site, and a structure of the resulting co-complex explains its nanomolar affinity for the enzyme. This co-complex then catalytically degrades via an unexpected ‘retro-aldol-like’ cleavage mechanism to a C18 aldehyde which in turn acts as a suicide inhibitor of SPT by covalent modification of the essential catalytic lysine. This surprising dual mechanism of inhibition rationalizes the extraordinary potency and longevity of myriocin inhibition.
    Keywords active sites ; aldehydes ; biosynthesis ; cell membranes ; enzyme inhibitors ; fungi ; lysine ; mass spectrometry ; pyridoxal phosphate ; serine ; serine C-palmitoyltransferase ; sphingolipids ; X-ray diffraction
    Language English
    Dates of publication 2013-0925
    Size p. 14276-14285.
    Publishing place American Chemical Society
    Document type Article
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021%2Fja4059876
    Database NAL-Catalogue (AGRICOLA)

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  8. Article: A critique of the international consensus statement on ADHD.

    Timimi, Sami / Moncrieff, Joanna / Jureidini, Jon / Leo, Jonathan / Cohen, David / Whitfield, Charles / Double, Duncan / Bindman, Jonathan / Andrews, Henry / Asen, Eia / Bracken, Pat / Duncan, Barry / Dunlap, Michaele / Albert, Galves / Green, Michael / Greening, Tom / Hill, Janice / Huws, Rhodri / Karon, Bertram /
    Kean, Brian / McCubbin, Michael / Miatra, Begum / Mosher, Loren / Parry, Sue / DuBose Ravenel, S / Riccio, Dominick / Shulman, Richard / Stolzer, Jeanne / Thomas, Phil / Vimpani, Graham / Wadsworth, Al / Walker, Dave / Wetzel, Norbert / White, Rupert

    Clinical child and family psychology review

    2004  Volume 7, Issue 1, Page(s) 59–63; discussion 65–9

    MeSH term(s) Attention Deficit Disorder with Hyperactivity ; Attitude to Health ; Consensus ; Humans ; International Cooperation
    Language English
    Publishing date 2004-04-19
    Publishing country United States
    Document type Comment ; Journal Article
    ZDB-ID 1445774-x
    ISSN 1096-4037
    ISSN 1096-4037
    DOI 10.1023/b:ccfp.0000020192.49298.7a
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