Year |
Citation |
Score |
2024 |
Chavali SS, Chou SZ, Cao W, Pollard TD, De La Cruz EM, Sindelar CV. Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex. Nature Communications. 15: 2059. PMID 38448439 DOI: 10.1038/s41467-024-46179-x |
0.85 |
|
2023 |
Pollard TD, Korn ED. Discovery of the first unconventional myosin: myosin-I. Frontiers in Physiology. 14: 1324623. PMID 38046947 DOI: 10.3389/fphys.2023.1324623 |
0.631 |
|
2023 |
Chou SZ, Pollard TD. Cryo-EM structures of both ends of the actin filament explain why the barbed end elongates faster than the pointed end. Biorxiv : the Preprint Server For Biology. PMID 37214997 DOI: 10.1101/2023.05.12.540494 |
0.813 |
|
2023 |
Rosenbloom AD, Pollard TD. The proline-rich domain of fission yeast WASp (Wsp1p) interacts with actin filaments and inhibits actin polymerization. Febs Letters. PMID 36650956 DOI: 10.1002/1873-3468.14571 |
0.484 |
|
2022 |
Chou SZ, Chatterjee M, Pollard TD. Mechanism of actin filament branch formation by Arp2/3 complex revealed by a high-resolution cryo-EM structureof the branch junction. Proceedings of the National Academy of Sciences of the United States of America. 119: e2206722119. PMID 36442092 DOI: 10.1073/pnas.2206722119 |
0.839 |
|
2021 |
Nickaeen M, Berro J, Pollard TD, Slepchenko BM. A model of actin-driven endocytosis explains differences of endocytic motility in budding and fission yeast. Molecular Biology of the Cell. mbcE21070362. PMID 34910589 DOI: 10.1091/mbc.E21-07-0362 |
0.693 |
|
2021 |
Malla M, Pollard TD, Chen Q. Counting actin in contractile rings reveals novel contributions of cofilin and type II myosins to fission yeast cytokinesis. Molecular Biology of the Cell. mbcE21080376. PMID 34613787 DOI: 10.1091/mbc.E21-08-0376 |
0.404 |
|
2021 |
Rosenbloom AD, Kovar EW, Kovar DR, Loew LM, Pollard TD. Mechanism of actin filament nucleation. Biophysical Journal. PMID 34509503 DOI: 10.1016/j.bpj.2021.09.006 |
0.674 |
|
2020 |
Chou SZ, Pollard TD. Cryo-electron microscopy structures of pyrene-labeled ADP-P- and ADP-actin filaments. Nature Communications. 11: 5897. PMID 33214556 DOI: 10.1038/s41467-020-19762-1 |
0.834 |
|
2020 |
Zsolnay V, Katkar HH, Chou SZ, Pollard TD, Voth GA. Structural basis for polarized elongation of actin filaments. Proceedings of the National Academy of Sciences of the United States of America. PMID 33199648 DOI: 10.1073/pnas.2011128117 |
0.812 |
|
2020 |
Dundon SER, Pollard TD. Microtubule Nucleation Promoters Mto1 and Mto2 Regulate Cytokinesis in Fission Yeast. Molecular Biology of the Cell. mbcE19120686. PMID 32520628 DOI: 10.1091/Mbc.E19-12-0686 |
0.394 |
|
2020 |
Pandit NG, Cao W, Bibeau J, Johnson-Chavarria EM, Taylor EW, Pollard TD, De La Cruz EM. Force and phosphate release from Arp2/3 complex promote dissociation of actin filament branches. Proceedings of the National Academy of Sciences of the United States of America. PMID 32461373 DOI: 10.1073/Pnas.1911183117 |
0.693 |
|
2020 |
Pollard TD. Myosins in Cytokinesis. Advances in Experimental Medicine and Biology. 1239: 233-244. PMID 32451862 DOI: 10.1007/978-3-030-38062-5_11 |
0.445 |
|
2019 |
Sun Y, Schöneberg J, Chen X, Jiang T, Kaplan C, Xu K, Pollard TD, Drubin DG. Direct comparison of clathrin-mediated endocytosis in budding and fission yeast reveals conserved and evolvable features. Elife. 8. PMID 31829937 DOI: 10.7554/Elife.50749 |
0.476 |
|
2019 |
Chatterjee M, Pollard TD. The Functionally Important N-Terminal Half of Fission Yeast Mid1p Anillin Is Intrinsically Disordered and Undergoes Phase Separation. Biochemistry. PMID 31243991 DOI: 10.1021/Acs.Biochem.9B00217 |
0.347 |
|
2019 |
Nickaeen M, Berro J, Pollard TD, Slepchenko BM. Actin assembly produces sufficient forces for endocytosis in yeast. Molecular Biology of the Cell. mbcE19010059. PMID 31242058 DOI: 10.1091/Mbc.E19-01-0059 |
0.732 |
|
2019 |
Chou SZ, Pollard TD. Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides. Proceedings of the National Academy of Sciences of the United States of America. PMID 30760599 DOI: 10.1073/Pnas.1807028115 |
0.83 |
|
2019 |
Pollard TD, O'Shaughnessy B. Molecular Mechanism of Cytokinesis. Annual Review of Biochemistry. PMID 30649923 DOI: 10.1146/Annurev-Biochem-062917-012530 |
0.685 |
|
2018 |
Pollard TD. Evolution of research on cellular motility over five decades. Biophysical Reviews. PMID 30377975 DOI: 10.1007/S12551-018-0473-9 |
0.356 |
|
2018 |
Fujiwara I, Zweifel ME, Courtemanche N, Pollard TD. Latrunculin A Accelerates Actin Filament Depolymerization in Addition to Sequestering Actin Monomers. Current Biology : Cb. PMID 30270183 DOI: 10.1016/J.Cub.2018.07.082 |
0.54 |
|
2018 |
Espinoza-Sanchez S, Metskas LA, Chou SZ, Rhoades E, Pollard TD. Conformational changes in Arp2/3 complex induced by ATP, WASp-VCA, and actin filaments. Proceedings of the National Academy of Sciences of the United States of America. PMID 30150414 DOI: 10.1073/Pnas.1717594115 |
0.837 |
|
2018 |
Dey SK, Pollard TD. Involvement of Septation Initiation Network (SIN) in events during cytokinesis in fission yeast. Journal of Cell Science. PMID 30072443 DOI: 10.1242/Jcs.216895 |
0.424 |
|
2018 |
Aydin F, Courtemanche N, Pollard TD, Voth GA. Gating mechanisms during actin filament elongation by formins. Elife. 7. PMID 30035712 DOI: 10.7554/Elife.37342 |
0.503 |
|
2018 |
Pollard TD, Goldman RD. Overview of the Cytoskeleton from an Evolutionary Perspective. Cold Spring Harbor Perspectives in Biology. 10. PMID 29967009 DOI: 10.1101/Cshperspect.A030288 |
0.445 |
|
2018 |
Aydin F, Courtemanche N, Pollard TD, Voth GA. Author response: Gating mechanisms during actin filament elongation by formins Elife. DOI: 10.7554/Elife.37342.032 |
0.443 |
|
2017 |
Arasada R, Sayyad WA, Berro J, Pollard TD. High-speed super-resolution imaging of the proteins in fission yeast clathrin-mediated endocytic actin patches. Molecular Biology of the Cell. PMID 29212877 DOI: 10.1091/Mbc.E17-06-0415 |
0.808 |
|
2017 |
Friend JE, Sayyad WA, Arasada R, McCormick CD, Heuser JE, Pollard TD. Fission yeast Myo2: Molecular organization and diffusion in the cytoplasm. Cytoskeleton (Hoboken, N.J.). PMID 29205883 DOI: 10.1002/Cm.21425 |
0.801 |
|
2017 |
Pollard TD. A Third Look at the Structure of Leiomodin Bound to Actin. Biophysical Journal. 113: 762-764. PMID 28834712 DOI: 10.1016/J.Bpj.2017.07.008 |
0.353 |
|
2017 |
Pollard TD. Nine unanswered questions about cytokinesis. The Journal of Cell Biology. PMID 28807993 DOI: 10.1083/Jcb.201612068 |
0.353 |
|
2017 |
Pollard TD. Tribute to Fumio Oosawa the pioneer in actin biophysics. Cytoskeleton (Hoboken, N.J.). PMID 28618211 DOI: 10.1002/Cm.21379 |
0.483 |
|
2017 |
Pollard TD. Cytoplasmic movements outside the living cell. Nature Reviews. Molecular Cell Biology. PMID 28559574 DOI: 10.1038/Nrm.2017.54 |
0.379 |
|
2017 |
Akamatsu M, Lin Y, Bewersdorf J, Pollard TD. Analysis of interphase node proteins in fission yeast by quantitative and super resolution fluorescence microscopy. Molecular Biology of the Cell. PMID 28539404 DOI: 10.1091/Mbc.E16-07-0522 |
0.342 |
|
2017 |
Laplante C, Pollard TD. Response to Zambon et al. Current Biology : Cb. 27: R101-R102. PMID 28171751 DOI: 10.1016/J.Cub.2016.12.025 |
0.326 |
|
2017 |
Aydin F, Courtemanche N, Pollard TD, Voth GA. The Role of Intermolecular Interactions in the Polymerization of Actin by Formins Biophysical Journal. 112: 560a. DOI: 10.1016/J.Bpj.2016.11.3017 |
0.519 |
|
2017 |
Thiyagarajan S, Chin H, Karatekin E, Pollard TD, O'Shaughnessy B. Fission Yeast Contractile Ring Tension Increases ∼2-Fold Throughout Constriction and Regulates Septum Closure but does not Set the Constriction Rate Biophysical Journal. 112: 30a. DOI: 10.1016/J.Bpj.2016.11.196 |
0.772 |
|
2017 |
Anderson KL, Page C, Swift MF, Suraneni P, Janssen ME, Pollard TD, Li R, Volkmann N, Hanein D. Redefining the Role of the Arp2/3 Complex: Regulation of Morphology at the Leading Edge Biophysical Journal. 112: 16a. DOI: 10.1016/J.Bpj.2016.11.120 |
0.464 |
|
2016 |
Anderson KL, Page C, Swift MF, Suraneni P, E W Janssen M, Pollard TD, Li R, Volkmann N, Hanein D. Nano-scale actin-network characterization of fibroblast cells lacking functional Arp2/3 complex. Journal of Structural Biology. PMID 28013022 DOI: 10.1016/J.Jsb.2016.12.010 |
0.46 |
|
2016 |
Pollard TD. What We Know and Do Not Know About Actin. Handbook of Experimental Pharmacology. PMID 27873086 DOI: 10.1007/164_2016_44 |
0.498 |
|
2016 |
Pollard TD. Theory from the Oster Laboratory Leaps Ahead of Experiment in Understanding Actin-Based Cellular Motility. Biophysical Journal. 111: 1589-1592. PMID 27760345 DOI: 10.1016/J.Bpj.2016.08.044 |
0.441 |
|
2016 |
Antonny B, Burd C, De Camilli P, Chen E, Daumke O, Faelber K, Ford M, Frolov VA, Frost A, Hinshaw JE, Kirchhausen T, Kozlov MM, Lenz M, Low HH, McMahon H, ... ... Pollard TD, et al. Membrane fission by dynamin: what we know and what we need to know. The Embo Journal. PMID 27670760 DOI: 10.15252/Embj.201694613 |
0.315 |
|
2016 |
Laplante C, Huang F, Tebbs IR, Bewersdorf J, Pollard TD. Molecular organization of cytokinesis nodes and contractile rings by super-resolution fluorescence microscopy of live fission yeast. Proceedings of the National Academy of Sciences of the United States of America. PMID 27647921 DOI: 10.1073/Pnas.1608252113 |
0.819 |
|
2016 |
Courtemanche N, Pollard TD, Chen Q. Avoiding artefacts when counting polymerized actin in live cells with LifeAct fused to fluorescent proteins. Nature Cell Biology. PMID 27159499 DOI: 10.1038/Ncb3351 |
0.564 |
|
2016 |
Pollard TD. Actin and Actin-Binding Proteins. Cold Spring Harbor Perspectives in Biology. PMID 26988969 DOI: 10.1101/Cshperspect.A018226 |
0.553 |
|
2016 |
O'Shaughnessy B, Pollard TD. Mechanistic biological modeling thrives. Science (New York, N.Y.). 351: 234-5. PMID 26816369 DOI: 10.1126/Science.351.6270.234-C |
0.491 |
|
2016 |
Laplante C, Huang F, Bewersdorf J, Pollard TD. High-Speed Super-Resolution Imaging of Live Fission Yeast Cells. Methods in Molecular Biology (Clifton, N.J.). 1369: 45-57. PMID 26519304 DOI: 10.1007/978-1-4939-3145-3_4 |
0.308 |
|
2016 |
Wang S, Chin HF, Karatekin E, Pollard TD, O'Shaughnessy B. Two Isoforms of Myosin-II Account for the Tension of the Fission Yeast Cytokinetic Ring Biophysical Journal. 110: 618a. DOI: 10.1016/J.Bpj.2015.11.3317 |
0.789 |
|
2015 |
Pollard TD. New Light on Growth Cone Navigation. Developmental Cell. 35: 672-3. PMID 26702827 DOI: 10.1016/J.Devcel.2015.12.002 |
0.322 |
|
2015 |
Jurgenson CT, Pollard TD. Crystals of the Arp2/3 complex in two new space groups with structural information about actin-related protein 2 and potential WASP binding sites. Acta Crystallographica. Section F, Structural Biology Communications. 71: 1161-8. PMID 26323303 DOI: 10.1107/S2053230X15013515 |
0.304 |
|
2015 |
Thiyagarajan S, Munteanu EL, Arasada R, Pollard TD, O'Shaughnessy B. The fission yeast cytokinetic contractile ring regulates septum shape and closure. Journal of Cell Science. 128: 3672-81. PMID 26240178 DOI: 10.1242/Jcs.166926 |
0.566 |
|
2015 |
Laplante C, Berro J, Karatekin E, Hernandez-Leyva A, Lee R, Pollard TD. Three myosins contribute uniquely to the assembly and constriction of the fission yeast cytokinetic contractile ring. Current Biology : Cb. 25: 1955-65. PMID 26144970 DOI: 10.1016/J.Cub.2015.06.018 |
0.78 |
|
2015 |
Arasada R, Pollard TD. A role for F-BAR protein Rga7p during cytokinesis in S. pombe. Journal of Cell Science. 128: 2259-68. PMID 25977474 DOI: 10.1242/Jcs.162974 |
0.411 |
|
2015 |
Courtemanche N, Gifford SM, Simpson MA, Pollard TD, Koleske AJ. Abl2/Abl-related gene stabilizes actin filaments, stimulates actin branching by actin-related protein 2/3 complex, and promotes actin filament severing by cofilin. The Journal of Biological Chemistry. 290: 4038-46. PMID 25540195 DOI: 10.1074/Jbc.M114.608117 |
0.563 |
|
2015 |
Pu, Akamatsu M, Pollard TD. The septation initiation network controls the assembly of nodes containing Cdr2p for cytokinesis in fission yeast. Journal of Cell Science. 128: 441-6. PMID 25501814 DOI: 10.1242/Jcs.160077 |
0.333 |
|
2015 |
Baker JL, Courtemanche N, Parton DL, McCullagh M, Pollard TD, Voth GA. Electrostatic interactions between the Bni1p Formin FH2 domain and actin influence actin filament nucleation. Structure (London, England : 1993). 23: 68-79. PMID 25482541 DOI: 10.1016/J.Str.2014.10.014 |
0.498 |
|
2015 |
Chen Q, Courtemanche N, Pollard TD. Aip1 promotes actin filament severing by cofilin and regulates constriction of the cytokinetic contractile ring. The Journal of Biological Chemistry. 290: 2289-300. PMID 25451933 DOI: 10.1074/Jbc.M114.612978 |
0.543 |
|
2015 |
Baker JL, Courtemanche N, Parton DL, McCullagh M, Pollard TD, Voth GA. Actin Filament Nucleation is Influenced by Electrostatic Interactions with the Bni1p Formin FH2 Domain Biophysical Journal. 108: 508a. DOI: 10.1016/J.Bpj.2014.11.2782 |
0.509 |
|
2015 |
Huang F, Laplante CE, Lin Y, Pollard TD, Bewersdorf J. Video-Rate Super Resolution Microscopy in Living Cells Biophysical Journal. 108: 475a. DOI: 10.1016/J.Bpj.2014.11.2599 |
0.314 |
|
2015 |
Chin HF, Karatekin E, Pollard TD, O'shaughnessy B. Measurements and Simulations of the Fission Yeast Cytokinetic Ring Tension during Constriction Biophysical Journal. 108: 26a. DOI: 10.1016/J.Bpj.2014.11.165 |
0.785 |
|
2014 |
Pollard TD. The value of mechanistic biophysical information for systems-level understanding of complex biological processes such as cytokinesis. Biophysical Journal. 107: 2499-507. PMID 25468329 DOI: 10.1016/J.Bpj.2014.10.031 |
0.32 |
|
2014 |
Arasada R, Pollard TD. Contractile ring stability in S. pombe depends on F-BAR protein Cdc15p and Bgs1p transport from the Golgi complex. Cell Reports. 8: 1533-44. PMID 25159149 DOI: 10.1016/J.Celrep.2014.07.048 |
0.397 |
|
2014 |
Berro J, Pollard TD. Synergies between Aip1p and capping protein subunits (Acp1p and Acp2p) in clathrin-mediated endocytosis and cell polarization in fission yeast. Molecular Biology of the Cell. 25: 3515-27. PMID 25143407 DOI: 10.1091/Mbc.E13-01-0005 |
0.794 |
|
2014 |
Berro J, Pollard TD. Local and global analysis of endocytic patch dynamics in fission yeast using a new "temporal superresolution" realignment method. Molecular Biology of the Cell. 25: 3501-14. PMID 25143395 DOI: 10.1091/Mbc.E13-01-0004 |
0.753 |
|
2014 |
Stachowiak MR, Laplante C, Chin HF, Guirao B, Karatekin E, Pollard TD, O'Shaughnessy B. Mechanism of cytokinetic contractile ring constriction in fission yeast. Developmental Cell. 29: 547-61. PMID 24914559 DOI: 10.1016/J.Devcel.2014.04.021 |
0.774 |
|
2014 |
Goss JW, Kim S, Bledsoe H, Pollard TD. Characterization of the roles of Blt1p in fission yeast cytokinesis. Molecular Biology of the Cell. 25: 1946-57. PMID 24790095 DOI: 10.1091/Mbc.E13-06-0300 |
0.413 |
|
2014 |
Akamatsu M, Berro J, Pu KM, Tebbs IR, Pollard TD. Cytokinetic nodes in fission yeast arise from two distinct types of nodes that merge during interphase. The Journal of Cell Biology. 204: 977-88. PMID 24637325 DOI: 10.1083/Jcb.201307174 |
0.764 |
|
2014 |
Laplante C, Berro J, Karatekin E, Hernandez-Leyva A, Lee R, Pollard TD. Three Myosins Contribute Uniquely to the Assembly and Constriction of the Fission Yeast Cytokinetic Contractile Ring Current Biology. DOI: 10.1016/j.cub.2015.06.018 |
0.736 |
|
2014 |
Chin HF, Stachowiak MR, Laplante C, Karatekin E, Pollard TD, O'Shaughnessy B. Experimental Measurement and Simulations of the Cytokinetic Ring Tension in Fission Yeast Biophysical Journal. 106: 177a. DOI: 10.1016/J.Bpj.2013.11.1003 |
0.782 |
|
2013 |
Pollard TD, Goldman YE. Remembrance of Hugh E. Huxley, a founder of our field. Cytoskeleton (Hoboken, N.J.). 70: 471-5. PMID 24106169 DOI: 10.1002/Cm.21141 |
0.436 |
|
2013 |
McCormick CD, Akamatsu MS, Ti SC, Pollard TD. Measuring affinities of fission yeast spindle pole body proteins in live cells across the cell cycle. Biophysical Journal. 105: 1324-35. PMID 24047983 DOI: 10.1016/J.Bpj.2013.08.017 |
0.807 |
|
2013 |
Courtemanche N, Pollard TD. Interaction of profilin with the barbed end of actin filaments. Biochemistry. 52: 6456-66. PMID 23947767 DOI: 10.1021/Bi400682N |
0.557 |
|
2013 |
Chen Q, Pollard TD. Actin filament severing by cofilin dismantles actin patches and produces mother filaments for new patches. Current Biology : Cb. 23: 1154-62. PMID 23727096 DOI: 10.1016/J.Cub.2013.05.005 |
0.542 |
|
2013 |
Courtemanche N, Lee JY, Pollard TD, Greene EC. Tension modulates actin filament polymerization mediated by formin and profilin. Proceedings of the National Academy of Sciences of the United States of America. 110: 9752-7. PMID 23716666 DOI: 10.1073/Pnas.1308257110 |
0.519 |
|
2013 |
Tebbs IR, Pollard TD. Separate roles of IQGAP Rng2p in forming and constricting the Schizosaccharomyces pombe cytokinetic contractile ring. Molecular Biology of the Cell. 24: 1904-17. PMID 23615450 DOI: 10.1091/Mbc.E12-10-0775 |
0.809 |
|
2013 |
Pollard TD, De La Cruz EM. Take advantage of time in your experiments: a guide to simple, informative kinetics assays. Molecular Biology of the Cell. 24: 1103-10. PMID 23580192 DOI: 10.1091/Mbc.E13-01-0030 |
0.58 |
|
2012 |
Saha S, Pollard TD. Characterization of structural and functional domains of the anillin-related protein Mid1p that contribute to cytokinesis in fission yeast. Molecular Biology of the Cell. 23: 3993-4007. PMID 22918954 DOI: 10.1091/Mbc.E12-07-0536 |
0.559 |
|
2012 |
Saha S, Pollard TD. Anillin-related protein Mid1p coordinates the assembly of the cytokinetic contractile ring in fission yeast. Molecular Biology of the Cell. 23: 3982-92. PMID 22918943 DOI: 10.1091/Mbc.E12-07-0535 |
0.591 |
|
2012 |
Yang Q, Zhang XF, Pollard TD, Forscher P. Arp2/3 complex-dependent actin networks constrain myosin II function in driving retrograde actin flow. The Journal of Cell Biology. 197: 939-56. PMID 22711700 DOI: 10.1083/Jcb.201111052 |
0.492 |
|
2012 |
Courtemanche N, Pollard TD. Determinants of Formin Homology 1 (FH1) domain function in actin filament elongation by formins. The Journal of Biological Chemistry. 287: 7812-20. PMID 22247555 DOI: 10.1074/Jbc.M111.322958 |
0.464 |
|
2012 |
Pfaendtner J, Volkmann N, Hanein D, Dalhaimer P, Pollard TD, Voth GA. Key structural features of the actin filament Arp2/3 complex branch junction revealed by molecular simulation. Journal of Molecular Biology. 416: 148-61. PMID 22206989 DOI: 10.1016/J.Jmb.2011.12.025 |
0.391 |
|
2012 |
Chen Q, Nag S, Pollard TD. Formins filter modified actin subunits during processive elongation. Journal of Structural Biology. 177: 32-9. PMID 22056467 DOI: 10.1016/J.Jsb.2011.10.005 |
0.567 |
|
2012 |
Xu XP, Rouiller I, Slaughter BD, Egile C, Kim E, Unruh JR, Fan X, Pollard TD, Li R, Hanein D, Volkmann N. Three-dimensional reconstructions of Arp2/3 complex with bound nucleation promoting factors. The Embo Journal. 31: 236-47. PMID 21934650 DOI: 10.1038/Emboj.2011.343 |
0.533 |
|
2012 |
Stachowiak MR, Laplante C, Pollard TD, O'Shaughnessy B. The Role of the Contractile Ring during Cytokinesis Biophysical Journal. 102: 219a. DOI: 10.1016/J.Bpj.2011.11.1202 |
0.577 |
|
2011 |
Chen Q, Pollard TD. Actin filament severing by cofilin is more important for assembly than constriction of the cytokinetic contractile ring. The Journal of Cell Biology. 195: 485-98. PMID 22024167 DOI: 10.1083/Jcb.201103067 |
0.492 |
|
2011 |
Arasada R, Pollard TD. Distinct roles for F-BAR proteins Cdc15p and Bzz1p in actin polymerization at sites of endocytosis in fission yeast. Current Biology : Cb. 21: 1450-9. PMID 21885283 DOI: 10.1016/J.Cub.2011.07.046 |
0.445 |
|
2011 |
Ti SC, Jurgenson CT, Nolen BJ, Pollard TD. Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex. Proceedings of the National Academy of Sciences of the United States of America. 108: E463-71. PMID 21676862 DOI: 10.1073/Pnas.1100125108 |
0.725 |
|
2011 |
Pollard TD. Cell biology. Formin tip tracking. Science (New York, N.Y.). 331: 39-41. PMID 21212345 DOI: 10.1126/Science.1200773 |
0.502 |
|
2011 |
Ti SC, Pollard TD. Purification of actin from fission yeast Schizosaccharomyces pombe and characterization of functional differences from muscle actin. The Journal of Biological Chemistry. 286: 5784-92. PMID 21148484 DOI: 10.1074/Jbc.M110.199794 |
0.749 |
|
2011 |
Stachowiak MR, Laplante C, Guirao B, Garcia P, Pollard TD, O'Shaughnessy B. Mechanisms of Cytokinetic Ring Constriction in Fission Yeast Biophysical Journal. 100: 443a. DOI: 10.1016/J.Bpj.2010.12.2612 |
0.64 |
|
2010 |
Pollard TD. A guide to simple and informative binding assays. Molecular Biology of the Cell. 21: 4061-7. PMID 21115850 DOI: 10.1091/Mbc.E10-08-0683 |
0.336 |
|
2010 |
Dalhaimer P, Pollard TD. Molecular dynamics simulations of Arp2/3 complex activation. Biophysical Journal. 99: 2568-76. PMID 20959098 DOI: 10.1016/J.Bpj.2010.08.027 |
0.467 |
|
2010 |
Wu JQ, Ye Y, Wang N, Pollard TD, Pringle JR. Cooperation between the septins and the actomyosin ring and role of a cell-integrity pathway during cell division in fission yeast. Genetics. 186: 897-915. PMID 20739711 DOI: 10.1534/Genetics.110.119842 |
0.33 |
|
2010 |
Sirotkin V, Berro J, Macmillan K, Zhao L, Pollard TD. Quantitative analysis of the mechanism of endocytic actin patch assembly and disassembly in fission yeast. Molecular Biology of the Cell. 21: 2894-904. PMID 20587778 DOI: 10.1091/Mbc.E10-02-0157 |
0.85 |
|
2010 |
Berro J, Sirotkin V, Pollard TD. Mathematical modeling of endocytic actin patch kinetics in fission yeast: disassembly requires release of actin filament fragments. Molecular Biology of the Cell. 21: 2905-15. PMID 20587776 DOI: 10.1091/Mbc.E10-06-0494 |
0.864 |
|
2010 |
Gleick PH, Adams RM, Amasino RM, Anders E, Anderson DJ, Anderson WW, Anselin LE, Arroyo MK, Asfaw B, Ayala FJ, Bax A, Bebbington AJ, Bell G, Bennett MV, Bennetzen JL, ... ... Pollard TD, et al. Climate change and the integrity of science. Science (New York, N.Y.). 328: 689-90. PMID 20448167 DOI: 10.1126/Science.328.5979.689 |
0.464 |
|
2010 |
Miller MM, Lapetina S, MacGrath SM, Sfakianos MK, Pollard TD, Koleske AJ. Regulation of actin polymerization and adhesion-dependent cell edge protrusion by the Abl-related gene (Arg) tyrosine kinase and N-WASp. Biochemistry. 49: 2227-34. PMID 20146487 DOI: 10.1021/Bi901721U |
0.406 |
|
2010 |
Pollard TD, Wu JQ. Understanding cytokinesis: lessons from fission yeast. Nature Reviews. Molecular Cell Biology. 11: 149-55. PMID 20094054 DOI: 10.1038/Nrm2834 |
0.441 |
|
2010 |
Pollard TD. Mechanics of cytokinesis in eukaryotes. Current Opinion in Cell Biology. 22: 50-6. PMID 20031383 DOI: 10.1016/J.Ceb.2009.11.010 |
0.485 |
|
2010 |
Pfaendtner J, Lyman E, Pollard TD, Voth GA. Structure and dynamics of the actin filament. Journal of Molecular Biology. 396: 252-63. PMID 19931282 DOI: 10.1016/J.Jmb.2009.11.034 |
0.497 |
|
2010 |
Pollard TD. Mechanism of actin filament self-assembly and regulation of the process by actin-binding proteins. Biophysical Journal. 49: 149-51. PMID 19431625 DOI: 10.1016/S0006-3495(86)83630-X |
0.496 |
|
2010 |
Anderson K, Beck F, Eibauer M, Rouiller I, Xu X, Li R, Pollard T, Nickell S, Volkmann N, Hanein D. Three-Dimensional Structure of the Arp2/3 –Mediated Actin-Branch Junction Microscopy and Microanalysis. 16: 1056-1057. DOI: 10.1017/S1431927610057508 |
0.427 |
|
2009 |
Pollard TD, Cooper JA. Actin, a central player in cell shape and movement. Science (New York, N.Y.). 326: 1208-12. PMID 19965462 DOI: 10.1126/Science.1175862 |
0.726 |
|
2009 |
Nolen BJ, Tomasevic N, Russell A, Pierce DW, Jia Z, McCormick CD, Hartman J, Sakowicz R, Pollard TD. Characterization of two classes of small molecule inhibitors of Arp2/3 complex. Nature. 460: 1031-4. PMID 19648907 DOI: 10.1038/Nature08231 |
0.838 |
|
2009 |
Pfaendtner J, Branduardi D, Parrinello M, Pollard TD, Voth GA. Nucleotide-dependent conformational states of actin. Proceedings of the National Academy of Sciences of the United States of America. 106: 12723-8. PMID 19620726 DOI: 10.1073/Pnas.0902092106 |
0.404 |
|
2009 |
Paul AS, Pollard TD. Review of the mechanism of processive actin filament elongation by formins. Cell Motility and the Cytoskeleton. 66: 606-17. PMID 19459187 DOI: 10.1002/Cm.20379 |
0.762 |
|
2009 |
Chan C, Beltzner CC, Pollard TD. Cofilin dissociates Arp2/3 complex and branches from actin filaments. Current Biology : Cb. 19: 537-45. PMID 19362000 DOI: 10.1016/J.Cub.2009.02.060 |
0.855 |
|
2009 |
Zencheck WD, Xiao H, Nolen BJ, Angeletti RH, Pollard TD, Almo SC. Nucleotide- and activator-dependent structural and dynamic changes of arp2/3 complex monitored by hydrogen/deuterium exchange and mass spectrometry. Journal of Molecular Biology. 390: 414-27. PMID 19298826 DOI: 10.1016/J.Jmb.2009.03.028 |
0.491 |
|
2009 |
Paul AS, Pollard TD. Energetic requirements for processive elongation of actin filaments by FH1FH2-formins. The Journal of Biological Chemistry. 284: 12533-40. PMID 19251693 DOI: 10.1074/Jbc.M808587200 |
0.73 |
|
2009 |
Ezezika OC, Younger NS, Lu J, Kaiser DA, Corbin ZA, Nolen BJ, Kovar DR, Pollard TD. Incompatibility with formin Cdc12p prevents human profilin from substituting for fission yeast profilin: insights from crystal structures of fission yeast profilin. The Journal of Biological Chemistry. 284: 2088-97. PMID 19028693 DOI: 10.1074/Jbc.M807073200 |
0.67 |
|
2009 |
Pollard TD, Berro J. Mathematical models and simulations of cellular processes based on actin filaments. The Journal of Biological Chemistry. 284: 5433-7. PMID 18940808 DOI: 10.1074/Jbc.R800043200 |
0.752 |
|
2009 |
Saha S, Pollard TD. Towards Mapping Domain Boundaries of Proteins Biophysical Journal. 96: 6a-7a. DOI: 10.1016/J.Bpj.2008.12.928 |
0.507 |
|
2009 |
Dalhaimer P, Pollard TD. Conformational Changes Of Arp2/3 Complex During Activation Biophysical Journal. 96: 129a. DOI: 10.1016/J.Bpj.2008.12.582 |
0.488 |
|
2009 |
Ti S, Pollard TD. Interactions of WASp Nucleation Promoting Factors with Fission Yeast Arp2/3 Complex Biophysical Journal. 96: 386a. DOI: 10.1016/J.Bpj.2008.12.2890 |
0.737 |
|
2008 |
Wu JQ, McCormick CD, Pollard TD. Chapter 9: Counting proteins in living cells by quantitative fluorescence microscopy with internal standards. Methods in Cell Biology. 89: 253-73. PMID 19118678 DOI: 10.1016/S0091-679X(08)00609-2 |
0.775 |
|
2008 |
Nolen BJ, Pollard TD. Structure and biochemical properties of fission yeast Arp2/3 complex lacking the Arp2 subunit. The Journal of Biological Chemistry. 283: 26490-8. PMID 18640983 DOI: 10.1074/Jbc.M802607200 |
0.44 |
|
2008 |
Lord M, Sladewski TE, Pollard TD. Yeast UCS proteins promote actomyosin interactions and limit myosin turnover in cells. Proceedings of the National Academy of Sciences of the United States of America. 105: 8014-9. PMID 18523008 DOI: 10.1073/Pnas.0802874105 |
0.514 |
|
2008 |
Mahaffy RE, Pollard TD. Influence of phalloidin on the formation of actin filament branches by Arp2/3 complex. Biochemistry. 47: 6460-7. PMID 18489122 DOI: 10.1021/Bi702484H |
0.51 |
|
2008 |
Pollard TD. Progress towards understanding the mechanism of cytokinesis in fission yeast. Biochemical Society Transactions. 36: 425-30. PMID 18481973 DOI: 10.1042/Bst0360425 |
0.483 |
|
2008 |
Chereau D, Boczkowska M, Skwarek-Maruszewska A, Fujiwara I, Hayes DB, Rebowski G, Lappalainen P, Pollard TD, Dominguez R. Leiomodin is an actin filament nucleator in muscle cells. Science (New York, N.Y.). 320: 239-43. PMID 18403713 DOI: 10.1126/Science.1155313 |
0.458 |
|
2008 |
Baum J, Tonkin CJ, Paul AS, Rug M, Smith BJ, Gould SB, Richard D, Pollard TD, Cowman AF. A malaria parasite formin regulates actin polymerization and localizes to the parasite-erythrocyte moving junction during invasion. Cell Host & Microbe. 3: 188-98. PMID 18329618 DOI: 10.1016/J.Chom.2008.02.006 |
0.671 |
|
2008 |
Rouiller I, Xu XP, Amann KJ, Egile C, Nickell S, Nicastro D, Li R, Pollard TD, Volkmann N, Hanein D. The structural basis of actin filament branching by the Arp2/3 complex. The Journal of Cell Biology. 180: 887-95. PMID 18316411 DOI: 10.1083/Jcb.200709092 |
0.83 |
|
2008 |
Beltzner CC, Pollard TD. Pathway of actin filament branch formation by Arp2/3 complex. The Journal of Biological Chemistry. 283: 7135-44. PMID 18165685 DOI: 10.1074/Jbc.M705894200 |
0.843 |
|
2008 |
Paul AS, Paul A, Pollard TD, Pollard T. The role of the FH1 domain and profilin in formin-mediated actin-filament elongation and nucleation. Current Biology : Cb. 18: 9-19. PMID 18160294 DOI: 10.1016/J.Cub.2007.11.062 |
0.716 |
|
2008 |
Dalhaimer P, Pollard TD, Nolen BJ. Nucleotide-mediated conformational changes of monomeric actin and Arp3 studied by molecular dynamics simulations. Journal of Molecular Biology. 376: 166-83. PMID 18155236 DOI: 10.1016/J.Jmb.2007.11.068 |
0.477 |
|
2008 |
Vavylonis D, Wu JQ, Hao S, O'Shaughnessy B, Pollard TD. Assembly mechanism of the contractile ring for cytokinesis by fission yeast. Science (New York, N.Y.). 319: 97-100. PMID 18079366 DOI: 10.1126/Science.1151086 |
0.774 |
|
2008 |
Rouiller I, Xu XP, Amann KJ, Egile C, Nicastro D, Nickell S, Li R, Pollard TD, Volkmann N, Hanein D. Insights into the mechanism of formation of Arp2/3 induced actin branches from electron microscopy and electron tomography studies Microscopy and Microanalysis. 14: 1580-1581. DOI: 10.1017/S1431927608084249 |
0.767 |
|
2008 |
Paul AS, Pollard TD. The Role of the FH1 Domain and Profilin in Formin-Mediated Actin-Filament Elongation and Nucleation (DOI:10.1016/j.cub.2007.11.062) Current Biology. 18: 233. DOI: 10.1016/j.cub.2008.01.043 |
0.672 |
|
2007 |
Kuhn JR, Pollard TD. Single molecule kinetic analysis of actin filament capping. Polyphosphoinositides do not dissociate capping proteins. The Journal of Biological Chemistry. 282: 28014-24. PMID 17656356 DOI: 10.1074/Jbc.M705287200 |
0.49 |
|
2007 |
Fujiwara I, Vavylonis D, Pollard TD. Polymerization kinetics of ADP- and ADP-Pi-actin determined by fluorescence microscopy. Proceedings of the National Academy of Sciences of the United States of America. 104: 8827-32. PMID 17517656 DOI: 10.1073/Pnas.0702510104 |
0.728 |
|
2007 |
Nolen BJ, Pollard TD. Insights into the influence of nucleotides on actin family proteins from seven structures of Arp2/3 complex. Molecular Cell. 26: 449-57. PMID 17499050 DOI: 10.1016/J.Molcel.2007.04.017 |
0.489 |
|
2007 |
Pollard TD. Regulation of actin filament assembly by Arp2/3 complex and formins. Annual Review of Biophysics and Biomolecular Structure. 36: 451-77. PMID 17477841 DOI: 10.1146/Annurev.Biophys.35.040405.101936 |
0.559 |
|
2007 |
Ali MY, Krementsova EB, Kennedy GG, Mahaffy R, Pollard TD, Trybus KM, Warshaw DM. Myosin Va maneuvers through actin intersections and diffuses along microtubules. Proceedings of the National Academy of Sciences of the United States of America. 104: 4332-6. PMID 17360524 DOI: 10.1073/Pnas.0611471104 |
0.461 |
|
2007 |
Kiselar JG, Mahaffy R, Pollard TD, Almo SC, Chance MR. Visualizing Arp2/3 complex activation mediated by binding of ATP and WASp using structural mass spectrometry. Proceedings of the National Academy of Sciences of the United States of America. 104: 1552-7. PMID 17251352 DOI: 10.1073/Pnas.0605380104 |
0.457 |
|
2007 |
Rouiller I, Xu X, Amann K, Egile C, Nickell S, Nicastro D, Li R, Pollard T, Volkmann N, Hanein D. Three-Dimensional Structure of the Arp2/3 Branch Junction Microscopy and Microanalysis. 13. DOI: 10.1017/S1431927607079111 |
0.758 |
|
2006 |
Andrianantoandro E, Pollard TD. Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin. Molecular Cell. 24: 13-23. PMID 17018289 DOI: 10.1016/J.Molcel.2006.08.006 |
0.798 |
|
2006 |
Mahaffy RE, Pollard TD. Kinetics of the formation and dissociation of actin filament branches mediated by Arp2/3 complex. Biophysical Journal. 91: 3519-28. PMID 16905606 DOI: 10.1529/Biophysj.106.080937 |
0.543 |
|
2006 |
Wu JQ, Sirotkin V, Kovar DR, Lord M, Beltzner CC, Kuhn JR, Pollard TD. Assembly of the cytokinetic contractile ring from a broad band of nodes in fission yeast. The Journal of Cell Biology. 174: 391-402. PMID 16864655 DOI: 10.1083/Jcb.200602032 |
0.816 |
|
2006 |
Moseley JB, Okada K, Balcer HI, Kovar DR, Pollard TD, Goode BL. Twinfilin is an actin-filament-severing protein and promotes rapid turnover of actin structures in vivo. Journal of Cell Science. 119: 1547-57. PMID 16569665 DOI: 10.1242/Jcs.02860 |
0.743 |
|
2006 |
Haviv L, Brill-Karniely Y, Mahaffy R, Backouche F, Ben-Shaul A, Pollard TD, Bernheim-Groswasser A. Reconstitution of the transition from lamellipodium to filopodium in a membrane-free system. Proceedings of the National Academy of Sciences of the United States of America. 103: 4906-11. PMID 16549794 DOI: 10.1073/Pnas.0508269103 |
0.497 |
|
2006 |
Vavylonis D, Kovar DR, O'Shaughnessy B, Pollard TD. Model of formin-associated actin filament elongation. Molecular Cell. 21: 455-66. PMID 16483928 DOI: 10.1016/J.Molcel.2006.01.016 |
0.838 |
|
2006 |
Kovar DR, Harris ES, Mahaffy R, Higgs HN, Pollard TD. Control of the assembly of ATP- and ADP-actin by formins and profilin. Cell. 124: 423-35. PMID 16439214 DOI: 10.1016/J.Cell.2005.11.038 |
0.728 |
|
2005 |
Wu JQ, Pollard TD. Counting cytokinesis proteins globally and locally in fission yeast. Science (New York, N.Y.). 310: 310-4. PMID 16224022 DOI: 10.1126/Science.1113230 |
0.359 |
|
2005 |
Lord M, Laves E, Pollard TD. Cytokinesis depends on the motor domains of myosin-II in fission yeast but not in budding yeast. Molecular Biology of the Cell. 16: 5346-55. PMID 16148042 DOI: 10.1091/Mbc.E05-07-0601 |
0.389 |
|
2005 |
Sirotkin V, Beltzner CC, Marchand JB, Pollard TD. Interactions of WASp, myosin-I, and verprolin with Arp2/3 complex during actin patch assembly in fission yeast. The Journal of Cell Biology. 170: 637-48. PMID 16087707 DOI: 10.1083/Jcb.200502053 |
0.842 |
|
2005 |
Kovar DR, Wu JQ, Pollard TD. Profilin-mediated competition between capping protein and formin Cdc12p during cytokinesis in fission yeast. Molecular Biology of the Cell. 16: 2313-24. PMID 15743909 DOI: 10.1091/Mbc.E04-09-0781 |
0.721 |
|
2005 |
Turbedsky K, Pollard TD, Yeager M. Assembly of Acanthamoeba myosin-II minifilaments. Model of anti-parallel dimers based on EM and X-ray diffraction of 2D and 3D crystals. Journal of Molecular Biology. 345: 363-73. PMID 15571728 DOI: 10.1016/J.Jmb.2004.10.048 |
0.785 |
|
2005 |
Turbedsky K, Pollard TD. Assembly of Acanthamoeba myosin-II minifilaments. Definition of C-terminal residues required to form coiled-coils, dimers, and octamers. Journal of Molecular Biology. 345: 351-61. PMID 15571727 DOI: 10.1016/J.Jmb.2004.10.049 |
0.8 |
|
2005 |
Kuhn JR, Pollard TD. Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy. Biophysical Journal. 88: 1387-402. PMID 15556992 DOI: 10.1529/Biophysj.104.047399 |
0.487 |
|
2004 |
Kovar DR, Pollard TD. Progressing actin: Formin as a processive elongation machine. Nature Cell Biology. 6: 1158-9. PMID 15573095 DOI: 10.1038/Ncb1204-1158 |
0.68 |
|
2004 |
Pollard TD. John Heuser's contributions to the visualization of the actin cytoskeleton by electron microscopy. European Journal of Cell Biology. 83: 253-5. PMID 15511082 DOI: 10.1078/0171-9335-00376 |
0.353 |
|
2004 |
Nolen BJ, Littlefield RS, Pollard TD. Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP. Proceedings of the National Academy of Sciences of the United States of America. 101: 15627-32. PMID 15505213 DOI: 10.1073/Pnas.0407149101 |
0.518 |
|
2004 |
Lord M, Pollard TD. UCS protein Rng3p activates actin filament gliding by fission yeast myosin-II. The Journal of Cell Biology. 167: 315-25. PMID 15504913 DOI: 10.1083/Jcb.200404045 |
0.455 |
|
2004 |
Kovar DR, Pollard TD. Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces. Proceedings of the National Academy of Sciences of the United States of America. 101: 14725-30. PMID 15377785 DOI: 10.1073/Pnas.0405902101 |
0.75 |
|
2004 |
Pollard TD. Formins coming into focus. Developmental Cell. 6: 312-4. PMID 15030751 DOI: 10.1016/S1534-5807(04)00073-5 |
0.437 |
|
2004 |
Beltzner CC, Pollard TD. Identification of functionally important residues of Arp2/3 complex by analysis of homology models from diverse species. Journal of Molecular Biology. 336: 551-65. PMID 14757065 DOI: 10.1016/J.Jmb.2003.12.017 |
0.811 |
|
2004 |
Golemi-Kotra D, Mahaffy R, Footer MJ, Holtzman JH, Pollard TD, Theriot JA, Schepartz A. High affinity, paralog-specific recognition of the Mena EVH1 domain by a miniature protein. Journal of the American Chemical Society. 126: 4-5. PMID 14709031 DOI: 10.1021/Ja037954K |
0.336 |
|
2004 |
Pollard TD. Ray Rappaport chronology: Twenty-five years of seminal papers on cytokinesis in the Journal of Experimental Zoology. Journal of Experimental Zoology. Part a, Comparative Experimental Biology. 301: 9-14. PMID 14695684 DOI: 10.1002/Jez.A.20000 |
0.316 |
|
2003 |
Wu JQ, Kuhn JR, Kovar DR, Pollard TD. Spatial and temporal pathway for assembly and constriction of the contractile ring in fission yeast cytokinesis. Developmental Cell. 5: 723-34. PMID 14602073 DOI: 10.1016/S1534-5807(03)00324-1 |
0.689 |
|
2003 |
Pollard TD. Functional genomics of cell morphology using RNA interference: pick your style, broad or deep. Journal of Biology. 2: 25. PMID 14527346 DOI: 10.1186/1475-4924-2-25 |
0.3 |
|
2003 |
Panchal SC, Kaiser DA, Torres E, Pollard TD, Rosen MK. A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex. Nature Structural Biology. 10: 591-8. PMID 12872157 DOI: 10.1038/Nsb952 |
0.405 |
|
2003 |
Kovar DR, Kuhn JR, Tichy AL, Pollard TD. The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin. The Journal of Cell Biology. 161: 875-87. PMID 12796476 DOI: 10.1083/Jcb.200211078 |
0.757 |
|
2003 |
Pollard TD. The cytoskeleton, cellular motility and the reductionist agenda. Nature. 422: 741-5. PMID 12700767 DOI: 10.1038/Nature01598 |
0.364 |
|
2003 |
Pollard TD, Borisy GG. Cellular motility driven by assembly and disassembly of actin filaments. Cell. 112: 453-65. PMID 12600310 DOI: 10.1016/S0092-8674(03)00120-X |
0.55 |
|
2003 |
Maul RS, Song Y, Amann KJ, Gerbin SC, Pollard TD, Chang DD. EPLIN regulates actin dynamics by cross-linking and stabilizing filaments. The Journal of Cell Biology. 160: 399-407. PMID 12566430 DOI: 10.1083/Jcb.200212057 |
0.835 |
|
2003 |
Ostap EM, Maupin P, Doberstein SK, Baines IC, Korn ED, Pollard TD. Dynamic localization of myosin-I to endocytic structures in Acanthamoeba. Cell Motility and the Cytoskeleton. 54: 29-40. PMID 12451593 DOI: 10.1002/Cm.10081 |
0.756 |
|
2002 |
Pollard TD. Cellular motility powered by actin filament assembly and disassembly. Harvey Lectures. 98: 1-17. PMID 16033155 |
0.351 |
|
2002 |
Pollard TD, Beltzner CC. Structure and function of the Arp2/3 complex. Current Opinion in Structural Biology. 12: 768-74. PMID 12504682 DOI: 10.1016/S0959-440X(02)00396-2 |
0.841 |
|
2002 |
Kong HH, Pollard TD. Intracellular localization and dynamics of myosin-II and myosin-IC in live Acanthamoeba by transient transfection of EGFP fusion proteins. Journal of Cell Science. 115: 4993-5002. PMID 12432085 DOI: 10.1242/Jcs.00159 |
0.456 |
|
2002 |
Pollard TD. Formins initiate new actin filaments. Nature Cell Biology. 4: E191. PMID 12149629 DOI: 10.1038/Ncb0802-E191A |
0.48 |
|
2002 |
Okada K, Blanchoin L, Abe H, Chen H, Pollard TD, Bamburg JR. Xenopus actin-interacting protein 1 (XAip1) enhances cofilin fragmentation of filaments by capping filament ends. The Journal of Biological Chemistry. 277: 43011-6. PMID 12055192 DOI: 10.1074/Jbc.M203111200 |
0.539 |
|
2002 |
Blanchoin L, Pollard TD. Hydrolysis of ATP by polymerized actin depends on the bound divalent cation but not profilin. Biochemistry. 41: 597-602. PMID 11781099 DOI: 10.1021/Bi011214B |
0.503 |
|
2001 |
Amann KJ, Pollard TD. Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy. Proceedings of the National Academy of Sciences of the United States of America. 98: 15009-13. PMID 11742068 DOI: 10.1073/Pnas.211556398 |
0.829 |
|
2001 |
Gillespie PG, Albanesi JP, Bahler M, Bement WM, Berg JS, Burgess DR, Burnside B, Cheney RE, Corey DP, Coudrier E, de Lanerolle P, Hammer JA, Hasson T, Holt JR, Hudspeth AJ, ... ... Pollard TD, et al. Myosin-I nomenclature. The Journal of Cell Biology. 155: 703-4. PMID 11724811 DOI: 10.1083/Jcb.200110032 |
0.764 |
|
2001 |
Robinson RC, Turbedsky K, Kaiser DA, Marchand JB, Higgs HN, Choe S, Pollard TD. Crystal structure of Arp2/3 complex. Science (New York, N.Y.). 294: 1679-84. PMID 11721045 DOI: 10.1126/Science.1066333 |
0.817 |
|
2001 |
Andrianantoandro E, Blanchoin L, Sept D, McCammon JA, Pollard TD. Kinetic mechanism of end-to-end annealing of actin filaments. Journal of Molecular Biology. 312: 721-30. PMID 11575927 DOI: 10.1006/Jmbi.2001.5005 |
0.781 |
|
2001 |
Volkmann N, Amann KJ, Stoilova-McPhie S, Egile C, Winter DC, Hazelwood L, Heuser JE, Li R, Pollard TD, Hanein D. Structure of Arp2/3 complex in its activated state and in actin filament branch junctions. Science (New York, N.Y.). 293: 2456-9. PMID 11533442 DOI: 10.1126/Science.1063025 |
0.839 |
|
2001 |
Blanchoin L, Pollard TD, Hitchcock-DeGregori SE. Inhibition of the Arp2/3 complex-nucleated actin polymerization and branch formation by tropomyosin. Current Biology : Cb. 11: 1300-4. PMID 11525747 DOI: 10.1016/S0960-9822(01)00395-5 |
0.561 |
|
2001 |
De La Cruz EM, Pollard TD. Structural biology. Actin' up. Science (New York, N.Y.). 293: 616-8. PMID 11474090 DOI: 10.1126/science.1063558 |
0.645 |
|
2001 |
Hüfner K, Higgs HN, Pollard TD, Jacobi C, Aepfelbacher M, Linder S. The verprolin-like central (vc) region of Wiskott-Aldrich syndrome protein induces Arp2/3 complex-dependent actin nucleation. The Journal of Biological Chemistry. 276: 35761-7. PMID 11459849 DOI: 10.1074/Jbc.M106520200 |
0.492 |
|
2001 |
Higgs HN, Pollard TD. Regulation of actin filament network formation through Arp2/3 complex: Activation by a diverse array of proteins Annual Review of Biochemistry. 70: 649-676. PMID 11395419 DOI: 10.1146/Annurev.Biochem.70.1.649 |
0.545 |
|
2001 |
Lu J, Pollard TD. Profilin binding to poly-L-proline and actin monomers along with ability to catalyze actin nucleotide exchange is required for viability of fission yeast. Molecular Biology of the Cell. 12: 1161-75. PMID 11294914 DOI: 10.1091/Mbc.12.4.1161 |
0.417 |
|
2001 |
Amann KJ, Pollard TD. The Arp2/3 complex nucleates actin filament branches from the sides of pre-existing filaments Nature Cell Biology. 3: 306-310. PMID 11231582 DOI: 10.1038/35060104 |
0.845 |
|
2001 |
Marchand JB, Kaiser DA, Pollard TD, Higgs HN. Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex Nature Cell Biology. 3: 76-82. PMID 11146629 DOI: 10.1038/35050590 |
0.488 |
|
2001 |
Pollard TD. Reflections on a quarter century of research on contractile systems. Trends in Biochemical Sciences. 25: 607-11. PMID 11116187 DOI: 10.1016/S0968-0004(00)01719-9 |
0.385 |
|
2001 |
Pollard TD, Blanchoin L, Mullins RD. Actin dynamics. Journal of Cell Science. 114: 3-4. PMID 11112680 |
0.654 |
|
2000 |
Lee WL, Bezanilla M, Pollard TD. Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex and shares functions with WASp. The Journal of Cell Biology. 151: 789-800. PMID 11076964 DOI: 10.1083/Jcb.151.4.789 |
0.828 |
|
2000 |
Blanchoin L, Pollard TD, Mullins RD. Interactions of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks. Current Biology : Cb. 10: 1273-82. PMID 11069108 DOI: 10.1016/S0960-9822(00)00749-1 |
0.771 |
|
2000 |
Amann KJ, Pollard TD. Cellular regulation of actin network assembly Current Biology. 10. PMID 11069094 DOI: 10.1016/S0960-9822(00)00751-X |
0.812 |
|
2000 |
Higgs HN, Pollard TD. Activation by Cdc42 and PIP2 of Wiskott-Aldrich Syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex Journal of Cell Biology. 150: 1311-1320. PMID 10995437 DOI: 10.1083/Jcb.150.6.1311 |
0.477 |
|
2000 |
Pollard TD, Blanchoin L, Mullins RD. Molecular mechanisms controlling actin filament dynamics in nonmuscle cells. Annual Review of Biophysics and Biomolecular Structure. 29: 545-76. PMID 10940259 DOI: 10.1146/Annurev.Biophys.29.1.545 |
0.752 |
|
2000 |
Blancholn L, Amann KJ, Higgs HN, Marchand JB, Kaiser DA, Pollard TD. Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins Nature. 404: 1007-1011. PMID 10801131 DOI: 10.1038/35010008 |
0.833 |
|
2000 |
Bezanilla M, Wilson JM, Pollard TD. Fission yeast myosin-II isoforms assemble into contractile rings at distinct times during mitosis. Current Biology : Cb. 10: 397-400. PMID 10753748 DOI: 10.1016/S0960-9822(00)00420-6 |
0.706 |
|
2000 |
Bezanilla M, Pollard TD. Myosin-II tails confer unique functions in Schizosaccharomyces pombe: characterization of a novel myosin-II tail. Molecular Biology of the Cell. 11: 79-91. PMID 10637292 DOI: 10.1091/Mbc.11.1.79 |
0.682 |
|
2000 |
De La Cruz EM, Mandinova A, Steinmetz MO, Stoffler D, Aebi U, Pollard TD. Polymerization and structure of nucleotide-free actin filaments. Journal of Molecular Biology. 295: 517-26. PMID 10623543 DOI: 10.1006/Jmbi.1999.3390 |
0.736 |
|
2000 |
Blanchoin L, Robinson RC, Choe S, Pollard TD. Phosphorylation of Acanthamoeba actophorin (ADF/cofilin) blocks interaction with actin without a change in atomic structure. Journal of Molecular Biology. 295: 203-11. PMID 10623520 DOI: 10.1006/Jmbi.1999.3336 |
0.444 |
|
1999 |
Sept D, Xu J, Pollard TD, McCammon JA. Annealing accounts for the length of actin filaments formed by spontaneous polymerization Biophysical Journal. 77: 2911-2919. PMID 10585915 DOI: 10.1016/S0006-3495(99)77124-9 |
0.534 |
|
1999 |
Lee WL, Ostap EM, Zot HG, Pollard TD. Organization and ligand binding properties of the tail of Acanthamoeba myosin-IA. Identification of an actin-binding site in the basic (tail homology-1) domain. The Journal of Biological Chemistry. 274: 35159-71. PMID 10574999 DOI: 10.1074/Jbc.274.49.35159 |
0.77 |
|
1999 |
Higgs HN, Blanchoin L, Pollard TD. Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization Biochemistry. 38: 15212-15222. PMID 10563804 DOI: 10.1021/Bi991843+ |
0.514 |
|
1999 |
Higgs HN, Pollard TD. Regulation of actin polymerization by Arp2/3 complex and WASp/Scar proteins Journal of Biological Chemistry. 274: 32531-32534. PMID 10551802 DOI: 10.1074/Jbc.274.46.32531 |
0.481 |
|
1999 |
May RC, Hall ME, Higgs HN, Pollard TD, Chakraborty T, Wehland J, Machesky LM, Sechi AS. The Arp2/3 complex is essential for the actin-based motility of Listeria monocytogenes Current Biology. 9: 759-762. PMID 10421578 DOI: 10.1016/S0960-9822(99)80337-6 |
0.515 |
|
1999 |
Blanchoin L, Pollard TD. Mechanism of interaction of Acanthamoeba actophorin (ADF/Cofilin) with actin filaments. The Journal of Biological Chemistry. 274: 15538-46. PMID 10336448 DOI: 10.1074/Jbc.274.22.15538 |
0.527 |
|
1999 |
Mullins RD, Pollard TD. Structure and function of the Arp2/3 complex. Current Opinion in Structural Biology. 9: 244-9. PMID 10322212 |
0.727 |
|
1999 |
Mullins RD, Pollard TD. Rho-family GTPases require the Arp2/3 complex to stimulate actin polymerization in Acanthamoeba extracts. Current Biology : Cb. 9: 405-15. PMID 10226024 DOI: 10.1016/S0960-9822(99)80187-0 |
0.738 |
|
1999 |
Machesky LM, Mullins RD, Higgs HN, Kaiser DA, Blanchoin L, May RC, Hall ME, Pollard TD. Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex. Proceedings of the National Academy of Sciences of the United States of America. 96: 3739-44. PMID 10097107 DOI: 10.1073/pnas.96.7.3739 |
0.719 |
|
1999 |
Xu J, Casella JF, Pollard TD. Effect of capping protein, CapZ, on the length of actin filaments and mechanical properties of actin filament networks. Cell Motility and the Cytoskeleton. 42: 73-81. PMID 9915586 DOI: 10.1002/(Sici)1097-0169(1999)42:1<73::Aid-Cm7>3.0.Co;2-Z |
0.541 |
|
1998 |
Liu S, Fedorov AA, Pollard TD, Lattman EE, Almo SC, Magnus KA. Crystal packing induces a conformational change in profilin-I from Acanthamoeba castellanii Journal of Structural Biology. 123: 22-29. PMID 9774541 DOI: 10.1006/Jsbi.1998.4009 |
0.327 |
|
1998 |
Kelleher JF, Mullins RD, Pollard TD. Purification and assay of the Arp2/3 complex from Acanthamoeba castellanii. Methods in Enzymology. 298: 42-51. PMID 9751870 |
0.582 |
|
1998 |
Blanchoin L, Pollard TD. Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin. The Journal of Biological Chemistry. 273: 25106-11. PMID 9737968 DOI: 10.1074/Jbc.273.39.25106 |
0.547 |
|
1998 |
Vinson VK, De La Cruz EM, Higgs HN, Pollard TD. Interactions of Acanthamoeba profilin with actin and nucleotides bound to actin. Biochemistry. 37: 10871-80. PMID 9692980 DOI: 10.1021/Bi980093L |
0.717 |
|
1998 |
Freeman JL, De La Cruz EM, Pollard TD, Lefkowitz RJ, Pitcher JA. Regulation of G protein-coupled receptor kinase 5 (GRK5) by actin. The Journal of Biological Chemistry. 273: 20653-7. PMID 9685424 DOI: 10.1074/Jbc.273.32.20653 |
0.675 |
|
1998 |
Mullins RD, Heuser JA, Pollard TD. The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proceedings of the National Academy of Sciences of the United States of America. 95: 6181-6. PMID 9600938 |
0.741 |
|
1998 |
Xu J, Schwarz WH, Käs JA, Stossel TP, Janmey PA, Pollard TD. Mechanical properties of actin filament networks depend on preparation, polymerization conditions, and storage of actin monomers. Biophysical Journal. 74: 2731-40. PMID 9591697 DOI: 10.1016/S0006-3495(98)77979-2 |
0.474 |
|
1998 |
Xu J, Wirtz D, Pollard TD. Dynamic cross-linking by α-actinin determines the mechanical properties of actin filament networks Journal of Biological Chemistry. 273: 9570-9576. PMID 9545287 DOI: 10.1074/Jbc.273.16.9570 |
0.497 |
|
1998 |
Jontes JD, Ostap EM, Pollard TD, Milligan RA. Three-dimensional structure of Acanthamoeba castellanii myosin-IB (MIB) determined by cryoelectron microscopy of decorated actin filaments. The Journal of Cell Biology. 141: 155-62. PMID 9531555 DOI: 10.1083/Jcb.141.1.155 |
0.705 |
|
1998 |
Mullins RD, Kelleher JF, Xu J, Pollard TD. Arp2/3 complex from Acanthamoeba binds profilin and cross-links actin filaments. Molecular Biology of the Cell. 9: 841-52. PMID 9529382 DOI: 10.1091/Mbc.9.4.841 |
0.758 |
|
1997 |
Jontes JD, Milligan RA, Pollard TD, Ostap EM. Kinetic characterization of brush border myosin-I ATPase. Proceedings of the National Academy of Sciences of the United States of America. 94: 14332-7. PMID 9405612 DOI: 10.1073/pnas.94.26.14332 |
0.597 |
|
1997 |
Bezanilla M, Forsburg SL, Pollard TD. Identification of a second myosin-II in Schizosaccharomyces pombe: Myp2p is conditionally required for cytokinesis. Molecular Biology of the Cell. 8: 2693-705. PMID 9398685 DOI: 10.1091/Mbc.8.12.2693 |
0.718 |
|
1997 |
Leonard SA, Gittis AG, Petrella EC, Pollard TD, Lattman EE. Crystal structure of the actin-binding protein actophorin from Acanthamoeba. Nature Structural Biology. 4: 369-73. PMID 9145107 DOI: 10.1038/Nsb0597-369 |
0.496 |
|
1997 |
Turbedsky K, Pollard TD, Bresnick AR. A subset of protein kinase C phosphorylation sites on the myosin II regulatory light chain inhibits phosphorylation by myosin light chain kinase. Biochemistry. 36: 2063-7. PMID 9047304 DOI: 10.1021/Bi9624651 |
0.62 |
|
1997 |
Mullins RD, Stafford WF, Pollard TD. Structure, subunit topology, and actin-binding activity of the Arp2/3 complex from Acanthamoeba. The Journal of Cell Biology. 136: 331-43. PMID 9015304 DOI: 10.1083/Jcb.136.2.331 |
0.695 |
|
1996 |
Mullins RD, Kelleher JF, Pollard TD. Actin' like actin? Trends in Cell Biology. 6: 208-12. PMID 15157457 DOI: 10.1016/0962-8924(96)20017-0 |
0.766 |
|
1996 |
Pollard TD, Ostap EM. The chemical mechanism of myosin-I: implications for actin-based motility and the evolution of the myosin family of motor proteins. Cell Structure and Function. 21: 351-6. PMID 9118240 DOI: 10.1247/Csf.21.351 |
0.721 |
|
1996 |
De La Cruz EM, Pollard TD. Kinetics and thermodynamics of phalloidin binding to actin filaments from three divergent species. Biochemistry. 35: 14054-61. PMID 8916890 DOI: 10.1021/Bi961047T |
0.698 |
|
1996 |
Kaiser DA, Pollard TD. Characterization of actin and poly-L-proline binding sites of Acanthamoeba profilin with monoclonal antibodies and by mutagenesis. Journal of Molecular Biology. 256: 89-107. PMID 8609617 DOI: 10.1006/Jmbi.1996.0070 |
0.394 |
|
1996 |
Ostap EM, Pollard TD. Overlapping functions of myosin-I isoforms? The Journal of Cell Biology. 133: 221-4. PMID 8609156 DOI: 10.1083/Jcb.133.2.221 |
0.612 |
|
1996 |
Ostap EM, Pollard TD. Biochemical kinetic characterization of the Acanthamoeba myosin-I ATPase. The Journal of Cell Biology. 132: 1053-60. PMID 8601584 DOI: 10.1083/Jcb.132.6.1053 |
0.708 |
|
1995 |
De La Cruz EM, Pollard TD. Nucleotide-free actin: stabilization by sucrose and nucleotide binding kinetics. Biochemistry. 34: 5452-61. PMID 7727403 DOI: 10.1021/Bi00016A016 |
0.691 |
|
1995 |
Kelleher JF, Atkinson SJ, Pollard TD. Sequences, structural models, and cellular localization of the actin-related proteins Arp2 and Arp3 from Acanthamoeba Journal of Cell Biology. 131: 385-397. PMID 7593166 DOI: 10.1083/Jcb.131.2.385 |
0.519 |
|
1995 |
Pollard TD. Actin cytoskeleton. Missing link for intracellular bacterial motility? Current Biology : Cb. 5: 837-40. PMID 7583135 DOI: 10.1016/S0960-9822(95)00167-9 |
0.452 |
|
1995 |
Bresnick AR, Wolff-Long VL, Baumann O, Pollard TD. Phosphorylation on threonine-18 of the regulatory light chain dissociates the ATPase and motor properties of smooth muscle myosin II. Biochemistry. 34: 12576-83. PMID 7548006 DOI: 10.1021/Bi00039A012 |
0.682 |
|
1994 |
Archer SJ, Vinson VK, Pollard TD, Torchia DA. Elucidation of the poly-L-proline binding site in Acanthamoeba profilin I by NMR spectroscopy. Febs Letters. 337: 145-51. PMID 8287969 DOI: 10.1016/0014-5793(94)80262-9 |
0.4 |
|
1994 |
Zot HG, Pollard TD. Motility of myosin I on planar lipid surfaces. Methods in Cell Biology. 39: 51-63. PMID 8246805 DOI: 10.1016/S0091-679X(08)60160-0 |
0.392 |
|
1994 |
Fedorov AA, Magnus KA, Graupe MH, Lattman EE, Pollard TD, Almo SC. X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates Proceedings of the National Academy of Sciences of the United States of America. 91: 8636-8640. PMID 8078936 DOI: 10.1073/Pnas.91.18.8636 |
0.401 |
|
1994 |
Machesky LM, Cole NB, Moss B, Pollard TD. Vaccinia virus expresses a novel profilin with a higher affinity for polyphosphoinositides than actin. Biochemistry. 33: 10815-24. PMID 8075084 DOI: 10.1021/Bi00201A032 |
0.45 |
|
1994 |
Wachsstock DH, Schwarz WH, Pollard TD. Cross-linker dynamics determine the mechanical properties of actin gels. Biophysical Journal. 66: 801-9. PMID 8011912 DOI: 10.1016/S0006-3495(94)80856-2 |
0.386 |
|
1994 |
De La Cruz EM, Pollard TD. Transient kinetic analysis of rhodamine phalloidin binding to actin filaments. Biochemistry. 33: 14387-92. PMID 7981198 DOI: 10.1021/Bi00252A003 |
0.715 |
|
1994 |
Machesky LM, Atkinson SJ, Ampe C, Vandekerckhove J, Pollard TD. Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose Journal of Cell Biology. 127: 107-115. PMID 7929556 DOI: 10.1083/Jcb.127.1.107 |
0.452 |
|
1994 |
Pollard TD, Almo S, Quirk S, Vinson V, Lattman EE. Structure of actin binding proteins: insights about function at atomic resolution. Annual Review of Cell Biology. 10: 207-49. PMID 7888177 DOI: 10.1146/Annurev.Cb.10.110194.001231 |
0.477 |
|
1994 |
Schroer TA, Fyrberg E, Cooper JA, Waterston RH, Helfman D, Pollard TD, Meyer DI. Actin-related protein nomenclature and classification. The Journal of Cell Biology. 127: 1777-8. PMID 7806557 DOI: 10.1083/Jcb.127.6.1777 |
0.612 |
|
1993 |
Pollard TD, Bhandari D, Maupin P, Wachsstock D, Weeds AG, Zot HG. Direct visualization by electron microscopy of the weakly bound intermediates in the actomyosin adenosine triphosphatase cycle Biophysical Journal. 64: 454-471. PMID 8457671 DOI: 10.1016/S0006-3495(93)81387-0 |
0.526 |
|
1993 |
Doberstein SK, Baines IC, Wiegand G, Korn ED, Pollard TD. Inhibition of contractile vacuole function in vivo by antibodies against myosin-I. Nature. 365: 841-3. PMID 8413668 DOI: 10.1038/365841A0 |
0.638 |
|
1993 |
Vinson VK, Archer SJ, Lattman EE, Pollard TD, Torchia DA. Three-dimensional solution structure of Acanthamoeba profilin-I. The Journal of Cell Biology. 122: 1277-83. PMID 8397216 DOI: 10.1083/Jcb.122.6.1277 |
0.41 |
|
1993 |
Wachsstock DH, Schwartz WH, Pollard TD. Affinity of alpha-actinin for actin determines the structure and mechanical properties of actin filament gels. Biophysical Journal. 65: 205-14. PMID 8369430 DOI: 10.1016/S0006-3495(93)81059-2 |
0.485 |
|
1993 |
Quirk S, Maciver SK, Ampe C, Doberstein SK, Kaiser DA, VanDamme J, Vandekerckhove JS, Pollard TD. Primary structure of and studies on Acanthamoeba actophorin. Biochemistry. 32: 8525-33. PMID 8357799 DOI: 10.1021/Bi00084A019 |
0.463 |
|
1993 |
Archer SJ, Vinson VK, Pollard TD, Torchia DA. Secondary structure and topology of Acanthamoeba profilin I as determined by heteronuclear nuclear magnetic resonance spectroscopy. Biochemistry. 32: 6680-7. PMID 8329394 DOI: 10.1021/Bi00077A022 |
0.364 |
|
1993 |
Porter JA, Yu M, Doberstein SK, Pollard TD, Montell C. Dependence of calmodulin localization in the retina on the NINAC unconventional myosin. Science (New York, N.Y.). 262: 1038-42. PMID 8235618 DOI: 10.1126/Science.8235618 |
0.367 |
|
1993 |
Pollard TD, Goldman RD. Cytoplasm and cell motility Current Opinion in Cell Biology. 5: 1-2. DOI: 10.1016/S0955-0674(05)80001-8 |
0.335 |
|
1992 |
Kobayashi T, Zot HG, Pollard TD, Collins JH. Functional implications of the unusual amino acid sequence of the regulatory light chain of Acanthamoeba castellanii myosin-II. Journal of Muscle Research and Cell Motility. 12: 553-9. PMID 1791194 DOI: 10.1007/Bf01738443 |
0.324 |
|
1992 |
Maciver SK, Wachsstock DH, Schwarz WH, Pollard TD. The actin filament severing protein actophorin promotes the formation of rigid bundles of actin filaments crosslinked with alpha-actinin. The Journal of Cell Biology. 115: 1621-8. PMID 1757466 DOI: 10.1083/Jcb.115.6.1621 |
0.504 |
|
1992 |
Maciver SK, Zot HG, Pollard TD. Characterization of actin filament severing by actophorin from Acanthamoeba castellanii. The Journal of Cell Biology. 115: 1611-20. PMID 1757465 DOI: 10.1083/Jcb.115.6.1611 |
0.537 |
|
1992 |
Doberstein SK, Pollard TD. Localization and specificity of the phospholipid and actin binding sites on the tail of Acanthamoeba myosin IC. The Journal of Cell Biology. 117: 1241-9. PMID 1607386 DOI: 10.1083/Jcb.117.6.1241 |
0.393 |
|
1992 |
Zot HG, Doberstein SK, Pollard TD. Myosin-I moves actin filaments on a phospholipid substrate: implications for membrane targeting. The Journal of Cell Biology. 116: 367-76. PMID 1530945 DOI: 10.1083/Jcb.116.2.367 |
0.452 |
|
1992 |
Satterwhite LL, Lohka MJ, Wilson KL, Scherson TY, Cisek LJ, Corden JL, Pollard TD. Phosphorylation of myosin-II regulatory light chain by cyclin-p34cdc2: a mechanism for the timing of cytokinesis. The Journal of Cell Biology. 118: 595-605. PMID 1386367 DOI: 10.1083/Jcb.118.3.595 |
0.366 |
|
1992 |
Goldschmidt-Clermont PJ, Furman MI, Wachsstock D, Safer D, Nachmias VT, Pollard TD. The control of actin nucleotide exchange by thymosin beta 4 and profilin. A potential regulatory mechanism for actin polymerization in cells. Molecular Biology of the Cell. 3: 1015-24. PMID 1330091 DOI: 10.1091/Mbc.3.9.1015 |
0.526 |
|
1992 |
Satterwhite LL, Pollard TD. Cytokinesis Current Biology. 2: 93. DOI: 10.1016/0960-9822(92)90221-U |
0.329 |
|
1992 |
Pollard TD, Goldman RD. Cytoplasm and cell motility Editorial overview Current Opinion in Cell Biology. 4: 1-3. DOI: 10.1016/0955-0674(92)90050-M |
0.332 |
|
1991 |
Sinard JH, Rimm DL, Pollard TD. Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. II. Assembly properties of tails with NH2- and COOH-terminal deletions. The Journal of Cell Biology. 111: 2417-26. PMID 2177477 DOI: 10.1083/Jcb.111.6.2417 |
0.421 |
|
1991 |
Machesky LM, Goldschmidt-Clermont PJ, Pollard TD. The affinities of human platelet and Acanthamoeba profilin isoforms for polyphosphoinositides account for their relative abilities to inhibit phospholipase C. Cell Regulation. 1: 937-50. PMID 1966040 DOI: 10.1091/Mbc.1.12.937 |
0.341 |
|
1991 |
Bremer A, Millonig RC, Sütterlin R, Engel A, Pollard TD, Aebi U. The structural basis for the intrinsic disorder of the actin filament: the "lateral slipping" model. The Journal of Cell Biology. 115: 689-703. PMID 1918159 DOI: 10.1083/Jcb.115.3.689 |
0.481 |
|
1991 |
Sampath P, Pollard TD. Effects of cytochalasin, phalloidin, and pH on the elongation of actin filaments. Biochemistry. 30: 1973-80. PMID 1899622 DOI: 10.1021/Bi00221A034 |
0.488 |
|
1991 |
Vojtek A, Haarer B, Field J, Gerst J, Pollard TD, Brown S, Wigler M. Evidence for a functional link between profilin and CAP in the yeast S. cerevisiae. Cell. 66: 497-505. PMID 1868547 DOI: 10.1016/0092-8674(81)90013-1 |
0.43 |
|
1991 |
Goldschmidt-Clermont PJ, Machesky LM, Doberstein SK, Pollard TD. Mechanism of the interaction of human platelet profilin with actin. The Journal of Cell Biology. 113: 1081-9. PMID 1645736 DOI: 10.1083/Jcb.113.5.1081 |
0.552 |
|
1991 |
Pollard TD, Machesky L, Goldschmidt-Clermont P. Chapter 13 Interaction of Profilins with Membrane Lipids Current Topics in Membranes. 38: 217-225. DOI: 10.1016/S0070-2161(08)60790-X |
0.364 |
|
1990 |
Pollard TD, Satterwhite L, Cisek L, Corden J, Sato M, Maupin P. Actin and myosin biochemistry in relation to cytokinesis. Annals of the New York Academy of Sciences. 582: 120-30. PMID 2192589 DOI: 10.1111/J.1749-6632.1990.Tb21673.X |
0.495 |
|
1990 |
Goldschmidt-Clermont PJ, Machesky LM, Baldassare JJ, Pollard TD. The actin-binding protein profilin binds to PIP2 and inhibits its hydrolysis by phospholipase C. Science (New York, N.Y.). 247: 1575-8. PMID 2157283 DOI: 10.1126/Science.2157283 |
0.446 |
|
1990 |
Rimm DL, Kaiser DA, Bhandari D, Maupin P, Kiehart DP, Pollard TD. Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. I. High resolution epitope mapping and characterization of monoclonal antibody binding sites. The Journal of Cell Biology. 111: 2405-16. PMID 1703536 DOI: 10.1083/Jcb.111.6.2405 |
0.664 |
|
1989 |
Hitchcock-DeGregori SE, Sampath P, Pollard TD. Tropomyosin inhibits the rate of actin polymerization by stabilizing actin filaments. Biochemistry. 27: 9182-5. PMID 3242622 DOI: 10.1021/Bi00426A016 |
0.461 |
|
1989 |
Sinard JH, Stafford WF, Pollard TD. The mechanism of assembly of Acanthamoeba myosin-II minifilaments: minifilaments assemble by three successive dimerization steps. The Journal of Cell Biology. 109: 1537-47. PMID 2793933 DOI: 10.1083/Jcb.109.4.1537 |
0.433 |
|
1989 |
Sinard JH, Pollard TD. The effect of heavy chain phosphorylation and solution conditions on the assembly of Acanthamoeba myosin-II. The Journal of Cell Biology. 109: 1529-35. PMID 2793932 DOI: 10.1083/Jcb.109.4.1529 |
0.406 |
|
1989 |
Adams RJ, Pollard TD. Binding of myosin I to membrane lipids Nature. 340: 565-568. PMID 2770861 DOI: 10.1038/340565A0 |
0.413 |
|
1989 |
Rimm DL, Pollard TD. Purification and characterization of an Acanthamoeba nuclear actin-binding protein. The Journal of Cell Biology. 109: 585-91. PMID 2760108 DOI: 10.1083/Jcb.109.2.585 |
0.428 |
|
1989 |
Rimm DL, Sinard JH, Pollard TD. Location of the head-tail junction of myosin. The Journal of Cell Biology. 108: 1783-9. PMID 2715178 DOI: 10.1083/Jcb.108.5.1783 |
0.414 |
|
1989 |
Adams RJ, Pollard TD. Membrane-bound myosin-I provides new mechanisms in cell motility Cell Motility and the Cytoskeleton. 14: 178-182. PMID 2692839 DOI: 10.1002/Cm.970140203 |
0.343 |
|
1989 |
Kaiser DA, Goldschmidt-Clermont PJ, Levine BA, Pollard TD. Characterization of renatured profilin purified by urea elution from poly-L-proline agarose columns. Cell Motility and the Cytoskeleton. 14: 251-62. PMID 2611892 DOI: 10.1002/Cm.970140211 |
0.384 |
|
1989 |
Vandekerckhove JS, Kaiser DA, Pollard TD. Acanthamoeba actin and profilin can be cross-linked between glutamic acid 364 of actin and lysine 115 of profilin. The Journal of Cell Biology. 109: 619-26. PMID 2569469 DOI: 10.1083/Jcb.109.2.619 |
0.405 |
|
1989 |
Sinard JH, Pollard TD. Microinjection into Acanthamoeba castellanii of monoclonal antibodies to myosin-II slows but does not stop cell locomotion. Cell Motility and the Cytoskeleton. 12: 42-52. PMID 2523248 DOI: 10.1002/Cm.970120106 |
0.343 |
|
1988 |
Murphy DB, Gray RO, Grasser WA, Pollard TD. Direct demonstration of actin filament annealing in vitro. The Journal of Cell Biology. 106: 1947-54. PMID 3384850 DOI: 10.1083/Jcb.106.6.1947 |
0.517 |
|
1988 |
Lee S, Li M, Pollard TD. Evaluation of the binding of Acanthamoeba profilin to pyrene-labeled actin by fluorescence enhancement. Analytical Biochemistry. 168: 148-55. PMID 3364709 DOI: 10.1016/0003-2697(88)90022-X |
0.421 |
|
1988 |
Sato M, Schwartz WH, Selden SC, Pollard TD. Mechanical properties of brain tubulin and microtubules Journal of Cell Biology. 106: 1205-1211. PMID 3360851 DOI: 10.1083/Jcb.106.4.1205 |
0.426 |
|
1988 |
Carboni JM, Conzelman KA, Adams RA, Kaiser DA, Pollard TD, Mooseker MS. Structural and immunological characterization of the myosin-like 110-kD subunit of the intestinal microvillar 110K-calmodulin complex: evidence for discrete myosin head and calmodulin-binding domains. The Journal of Cell Biology. 107: 1749-57. PMID 2460467 DOI: 10.1083/Jcb.107.5.1749 |
0.637 |
|
1987 |
Sato M, Schwarz WH, Pollard TD. Dependence of the mechanical properties of actin/alpha-actinin gels on deformation rate. Nature. 325: 828-30. PMID 3821871 DOI: 10.1038/325828A0 |
0.47 |
|
1987 |
Pollard TD. Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. The Journal of Cell Biology. 103: 2747-54. PMID 3793756 DOI: 10.1083/Jcb.103.6.2747 |
0.452 |
|
1986 |
Kaiser DA, Sato M, Ebert RF, Pollard TD. Purification and characterization of two isoforms of Acanthamoeba profilin. The Journal of Cell Biology. 102: 221-6. PMID 3941153 DOI: 10.1083/Jcb.102.1.221 |
0.355 |
|
1986 |
Cooper JA, Blum JD, Williams RC, Pollard TD. Purification and characterization of actophorin, a new 15,000-dalton actin-binding protein from Acanthamoeba castellanii. The Journal of Biological Chemistry. 261: 477-85. PMID 3941084 |
0.732 |
|
1986 |
Kiehart DP, Kaiser DA, Pollard TD. Antibody inhibitors of nonmuscle myosin function and assembly. Methods in Enzymology. 134: 423-53. PMID 3821574 DOI: 10.1016/0076-6879(86)34109-0 |
0.62 |
|
1986 |
Maupin P, Pollard TD. Arrangement of actin filaments and myosin-like filaments in the contractile ring and of actin-like filaments in the mitotic spindle of dividing HeLa cells. Journal of Ultrastructure and Molecular Structure Research. 94: 92-103. PMID 3772181 DOI: 10.1016/0889-1605(86)90055-8 |
0.558 |
|
1986 |
Adams RJ, Pollard TD. Propulsion of organelles isolated from Acanthamoeba along actin filaments by myosin-I Nature. 322: 754-756. PMID 3748157 DOI: 10.1038/322754A0 |
0.505 |
|
1986 |
Pollard TD, Cooper JA. Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Annual Review of Biochemistry. 55: 987-1035. PMID 3527055 DOI: 10.1146/Annurev.Bi.55.070186.005011 |
0.71 |
|
1986 |
Pollard TD. Assembly and dynamics of the actin filament system in nonmuscle cells. Journal of Cellular Biochemistry. 31: 87-95. PMID 3525579 DOI: 10.1002/Jcb.240310202 |
0.551 |
|
1986 |
Selden SC, Pollard TD. Interaction of actin filaments with microtubules is mediated by microtubule-associated proteins and regulated by phosphorylation Annals of the New York Academy of Sciences. 803-812. PMID 3460455 DOI: 10.1111/J.1749-6632.1986.Tb38464.X |
0.503 |
|
1986 |
Pollard TD, Tseng PC, Rimm DL, Bichell DP, Williams RC, Sinard J, Sato M. Characterization of alpha-actinin from Acanthamoeba. Cell Motility and the Cytoskeleton. 6: 649-61. PMID 2948678 DOI: 10.1002/Cm.970060613 |
0.426 |
|
1986 |
Hagen SJ, Kiehart DP, Kaiser DA, Pollard TD. Characterization of monoclonal antibodies to Acanthamoeba myosin-I that cross-react with both myosin-II and low molecular mass nuclear proteins. The Journal of Cell Biology. 103: 2121-8. PMID 2946703 DOI: 10.1083/Jcb.103.6.2121 |
0.643 |
|
1985 |
Pollard TD. Actin-binding protein evolution. Nature. 312: 403. PMID 6504153 DOI: 10.1038/312403A0 |
0.449 |
|
1985 |
Pollard TD. Purification of a high molecular weight actin filament gelation protein from Acanthamoeba that shares antigenic determinants with vertebrate spectrins. The Journal of Cell Biology. 99: 1970-80. PMID 6209283 DOI: 10.1083/Jcb.99.6.1970 |
0.405 |
|
1985 |
Cooper JA, Pollard TD. Effect of capping protein on the kinetics of actin polymerization. Biochemistry. 24: 793-9. PMID 3994986 DOI: 10.1021/Bi00324A039 |
0.707 |
|
1985 |
Pollard TD. Myosin filaments in cytoplasm. Nature. 314: 321. PMID 3885044 DOI: 10.1038/314321A0 |
0.539 |
|
1984 |
Kiehart DP, Pollard TD. Stimulation of Acanthamoeba actomyosin ATPase activity by myosin-II polymerization. Nature. 308: 864-6. PMID 21510101 DOI: 10.1038/308864A0 |
0.704 |
|
1984 |
Tseng PC, Runge MS, Cooper JA, Williams RC, Pollard TD. Physical, immunochemical, and functional properties of Acanthamoeba profilin. The Journal of Cell Biology. 98: 214-21. PMID 6707086 DOI: 10.1083/Jcb.98.1.214 |
0.682 |
|
1984 |
Pollard TD. Measurement of rate constants for actin filament elongation in solution. Analytical Biochemistry. 134: 406-12. PMID 6650826 DOI: 10.1016/0003-2697(83)90316-0 |
0.442 |
|
1984 |
Pollard TD, Cooper JA. Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation. Biochemistry. 23: 6631-41. PMID 6543322 DOI: 10.1021/Bi00321A054 |
0.738 |
|
1984 |
Pollard TD. Polymerization of ADP-actin. The Journal of Cell Biology. 99: 769-77. PMID 6540783 DOI: 10.1083/Jcb.99.3.769 |
0.451 |
|
1984 |
Pollard TD, Selden SC, Maupin P. Interaction of actin filaments with microtubules. The Journal of Cell Biology. 99: 33s-37s. PMID 6430911 DOI: 10.1083/Jcb.99.1.33S |
0.493 |
|
1984 |
Cooper JA, Blum JD, Pollard TD. Acanthamoeba castellanii capping protein: properties, mechanism of action, immunologic cross-reactivity, and localization. The Journal of Cell Biology. 99: 217-25. PMID 6429155 DOI: 10.1083/Jcb.99.1.217 |
0.72 |
|
1984 |
Pollard TD, Weeds AG. The rate constant for ATP hydrolysis by polymerized actin. Febs Letters. 170: 94-8. PMID 6427006 DOI: 10.1016/0014-5793(84)81376-9 |
0.427 |
|
1984 |
Kiehart DP, Pollard TD. Inhibition of acanthamoeba actomyosin-II ATPase activity and mechanochemical function by specific monoclonal antibodies. The Journal of Cell Biology. 99: 1024-33. PMID 6206075 DOI: 10.1083/Jcb.99.3.1024 |
0.672 |
|
1984 |
Kiehart DP, Kaiser DA, Pollard TD. Direct localization of monoclonal antibody-binding sites on Acanthamoeba myosin-II and inhibition of filament formation by antibodies that bind to specific sites on the myosin-II tail. The Journal of Cell Biology. 99: 1015-23. PMID 6206074 DOI: 10.1083/Jcb.99.3.1015 |
0.667 |
|
1984 |
Kiehart DP, Kaiser DA, Pollard TD. Monoclonal antibodies demonstrate limited structural homology between myosin isozymes from Acanthamoeba. The Journal of Cell Biology. 99: 1002-14. PMID 6206073 DOI: 10.1083/Jcb.99.3.1002 |
0.656 |
|
1983 |
Pollard TD. Structure and polymerization of Acanthamoeba myosin-II filaments. The Journal of Cell Biology. 95: 816-25. PMID 7153247 DOI: 10.1083/Jcb.95.3.816 |
0.436 |
|
1983 |
Herman IM, Pollard TD, Wong AJ. Contractile proteins in endothelial cells. Annals of the New York Academy of Sciences. 401: 50-60. PMID 6963126 DOI: 10.1111/J.1749-6632.1982.Tb25706.X |
0.606 |
|
1983 |
Cooper JA, Walker SB, Pollard TD. Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization. Journal of Muscle Research and Cell Motility. 4: 253-62. PMID 6863518 DOI: 10.1007/Bf00712034 |
0.702 |
|
1983 |
Cooper JA, Buhle EL, Walker SB, Tsong TY, Pollard TD. Kinetic evidence for a monomer activation step in actin polymerization. Biochemistry. 22: 2193-202. PMID 6860660 DOI: 10.1021/Bi00278A021 |
0.66 |
|
1983 |
Smith PR, Fowler WE, Pollard TD, Aebi U, Huxley HE. Structure of the actin molecule determined from electron micrographs of crystalline actin sheets with a tentative alignment of the molecule in the actin filament Journal of Molecular Biology. 167: 641-660. PMID 6683760 DOI: 10.1016/S0022-2836(83)80103-X |
0.508 |
|
1983 |
Wong AJ, Pollard TD, Herman IM. Actin filament stress fibers in vascular endothelial cells in vivo. Science (New York, N.Y.). 219: 867-9. PMID 6681677 DOI: 10.1126/Science.6681677 |
0.639 |
|
1983 |
Dang CV, Yang DCH, Pollard TD. Association of methionyl-tRNA synthetase with detergent-insoluble components of the rough endoplasmic reticulum Journal of Cell Biology. 96: 1138-1147. PMID 6339526 DOI: 10.1083/Jcb.96.4.1138 |
0.358 |
|
1983 |
Maupin P, Pollard TD. Improved preservation and staining of HeLa cell actin filaments, clathrin-coated membranes, and other cytoplasmic structures by tannic acid-glutaraldehyde-saponin fixation. The Journal of Cell Biology. 96: 51-62. PMID 6186673 DOI: 10.1083/Jcb.96.1.51 |
0.368 |
|
1982 |
Aebi U, Fowler WE, Isenberg G, Pollard TD, Smith PR. Crystalline actin sheets: their structure and polymorphism. The Journal of Cell Biology. 91: 340-51. PMID 7309785 DOI: 10.1083/Jcb.91.2.340 |
0.484 |
|
1982 |
Tseng PC, Pollard TD. Mechanism of action of Acanthamoeba profilin: demonstration of actin species specificity and regulation by micromolar concentrations of MgCl2. The Journal of Cell Biology. 94: 213-8. PMID 7119015 DOI: 10.1083/JCB.94.1.213 |
0.381 |
|
1982 |
Pollard TD. A falling ball apparatus to measure filament cross-linking. Methods in Cell Biology. 24: 301-11. PMID 7048020 DOI: 10.1016/S0091-679X(08)60663-9 |
0.367 |
|
1982 |
Pollard TD, Aebi U, Cooper JA, Fowler WE, Tseng P. Actin structure, polymerization, and gelation. Cold Spring Harbor Symposia On Quantitative Biology. 46: 513-24. PMID 6955097 DOI: 10.1101/Sqb.1982.046.01.048 |
0.699 |
|
1982 |
Mooseker MS, Pollard TD, Wharton KA. Nucleated polymerization of actin from the membrane-associated ends of microvillar filaments in the intestinal brush border. The Journal of Cell Biology. 95: 223-33. PMID 6890554 DOI: 10.1083/Jcb.95.1.223 |
0.666 |
|
1982 |
Pollard TD, Cooper JA. Methods to characterize actin filament networks. Methods in Enzymology. 85: 211-33. PMID 6889670 DOI: 10.1016/0076-6879(82)85022-2 |
0.698 |
|
1982 |
Cooper JA, Pollard TD. Methods to measure actin polymerization. Methods in Enzymology. 85: 182-210. PMID 6889668 DOI: 10.1016/0076-6879(82)85021-0 |
0.701 |
|
1982 |
Pollard TD. Cytoplasmic contractile proteins. The Journal of Cell Biology. 91: 156s-165s. PMID 6459328 DOI: 10.1083/Jcb.91.3.156S |
0.331 |
|
1982 |
Pollard TD. Purification of nonmuscle myosins. Methods in Enzymology. 331-56. PMID 6289044 DOI: 10.1016/0076-6879(82)85033-7 |
0.499 |
|
1982 |
Pollard TD. Assays for myosin. Methods in Enzymology. 123-30. PMID 6214689 DOI: 10.1016/0076-6879(82)85015-5 |
0.387 |
|
1982 |
Pollard TD. Myosin purification and characterization. Methods in Cell Biology. 24: 333-71. PMID 6212751 DOI: 10.1016/S0091-679X(08)60665-2 |
0.488 |
|
1982 |
Pollard TD, Aebi U, Cooper JA, Fowler WE, Kiehart DP, Smith PR, Tseng PC. Actin and myosin function in acanthamoeba. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 299: 237-45. PMID 6129659 DOI: 10.1098/Rstb.1982.0129 |
0.824 |
|
1982 |
Craig SW, Pollard TD. Actin-binding proteins Trends in Biochemical Sciences. 7: 88-92. DOI: 10.1016/0968-0004(82)90153-0 |
0.673 |
|
1982 |
Pollard TD, Craig SW. Mechanism of actin polymerization Trends in Biochemical Sciences. 7: 55-58. DOI: 10.1016/0968-0004(82)90076-7 |
0.617 |
|
1981 |
Herman IM, Pollard TD. Electron microscopic localization of cytoplasmic myosin with ferritin-labeled antibodies. The Journal of Cell Biology. 88: 346-51. PMID 7193682 DOI: 10.1083/Jcb.88.2.346 |
0.668 |
|
1981 |
Herman IM, Crisona NJ, Pollard TD. Relation between cell activity and the distribution of cytoplasmic actin and myosin. The Journal of Cell Biology. 90: 84-91. PMID 7019223 DOI: 10.1083/Jcb.90.1.84 |
0.698 |
|
1981 |
Pollard TD, Mooseker MS. Direct measurement of actin polymerization rate constants by electron microscopy of actin filaments nucleated by isolated microvillus cores Journal of Cell Biology. 88: 654-659. PMID 6894301 DOI: 10.1083/Jcb.88.3.654 |
0.648 |
|
1981 |
Isenberg G, Aebi U, Pollard TD. An actin-binding protein from Acanthamoeba regulates actin filament polymerization and interactions. Nature. 288: 455-9. PMID 6893736 DOI: 10.1038/288455A0 |
0.551 |
|
1981 |
MacLean-Fletcher S, Pollard TD. Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association. Biochemical and Biophysical Research Communications. 96: 18-27. PMID 6893667 DOI: 10.1016/0006-291X(80)91175-4 |
0.51 |
|
1981 |
Aebi U, Smith PR, Isenberg G, Pollard TD. Structure of crystalline actin sheets. Nature. 288: 296-8. PMID 6893623 DOI: 10.1038/288296A0 |
0.466 |
|
1980 |
MacLean-Fletcher S, Pollard TD. Mechanism of action of cytochalasin B on actin. Cell. 20: 329-41. PMID 6893016 DOI: 10.1016/0092-8674(80)90619-4 |
0.506 |
|
1980 |
MacLean-Fletcher SD, Pollard TD. Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors. The Journal of Cell Biology. 85: 414-28. PMID 6892818 DOI: 10.1083/Jcb.85.2.414 |
0.349 |
|
1979 |
Braun J, Fujiwara K, Pollard TD, Unanue ER. Two distinct mechanisms for redistribution of lymphocyte surface macromolecules. II. Contrasting effects of local anesthetics and a calcium ionophore. The Journal of Cell Biology. 79: 419-26. PMID 363728 DOI: 10.1083/Jcb.79.2.419 |
0.345 |
|
1979 |
Braun J, Fujiwara K, Pollard TD, Unanue ER. Two distinct mechanisms for redistribution of lymphocyte surface macromolecules. I. Relationship to cytoplasmic myosin. The Journal of Cell Biology. 79: 409-18. PMID 309887 DOI: 10.1083/Jcb.79.2.409 |
0.339 |
|
1979 |
Herman IM, Pollard TD. Comparison of purified anti-actin and fluorescent-heavy meromyosin staining patterns in dividing cells. The Journal of Cell Biology. 80: 509-20. PMID 110816 DOI: 10.1083/Jcb.80.3.509 |
0.69 |
|
1978 |
Griffith LM, Pollard TD. Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins. The Journal of Cell Biology. 78: 958-65. PMID 568144 DOI: 10.1083/Jcb.78.3.958 |
0.485 |
|
1978 |
Fujiwara K, Porter ME, Pollard TD. Alpha-actinin localization in the cleavage furrow during cytokinesis Journal of Cell Biology. 79: 268-275. PMID 359574 DOI: 10.1083/Jcb.79.1.268 |
0.346 |
|
1978 |
Fujiwara K, Pollard TD. Simultaneous localization of myosin and tubulin in human tissue culture cells by double antibody staining. The Journal of Cell Biology. 77: 182-95. PMID 350890 DOI: 10.1083/Jcb.77.1.182 |
0.369 |
|
1978 |
Mooseker MS, Pollard TD, Fujiwara K. Characterization and localization of myosin in the brush border of intestinal epithelial cells Journal of Cell Biology. 79: 444-453. PMID 152766 DOI: 10.1083/Jcb.79.2.444 |
0.651 |
|
1978 |
Herman IM, Pollard TD. Actin localization in fixed dividing cells stained with fluorescent heavy meromyosin. Experimental Cell Research. 114: 15-25. PMID 77785 DOI: 10.1016/0014-4827(78)90030-7 |
0.629 |
|
1978 |
Maupin-Szamier P, Pollard TD. Actin filament destruction by osmium tetroxide. The Journal of Cell Biology. 77: 837-52. PMID 28332 DOI: 10.1083/Jcb.77.3.837 |
0.541 |
|
1977 |
Pollard TD. The role of actin in the temperature-dependent gelation and contraction of extracts of Acanthamoeba. The Journal of Cell Biology. 68: 579-601. PMID 1030705 DOI: 10.1083/Jcb.68.3.579 |
0.46 |
|
1977 |
Pollard TD. Cytoskeletal functions of cytoplasmic contractile proteins. Journal of Supramolecular Structure. 5: 317-34. PMID 799215 DOI: 10.1002/Jss.400050306 |
0.515 |
|
1977 |
Schreiner GF, Fujiwara K, Pollard TD, Unanue ER. Redistribution of myosin accompanying capping of surface Ig. The Journal of Experimental Medicine. 145: 1393-8. PMID 323408 DOI: 10.1084/Jem.145.5.1393 |
0.314 |
|
1977 |
Fujiwara K, Pollard TD. Fluorescent antibody localization of myosin in the cytoplasm, cleavage furrow, and mitotic spindle of human cells. The Journal of Cell Biology. 71: 848-75. PMID 62755 DOI: 10.1083/Jcb.71.3.848 |
0.352 |
|
1975 |
Pollard TD. Electron microscopy of synthetic myosin filaments. Evidence for cross-bridge. Flexibility and copolymer formation. The Journal of Cell Biology. 67: 93-104. PMID 1236853 DOI: 10.1083/Jcb.67.1.93 |
0.465 |
|
1975 |
Niederman R, Pollard TD. Human platelet myosin. II. In vitro assembly and structure of myosin filaments. The Journal of Cell Biology. 67: 72-92. PMID 240861 DOI: 10.1083/Jcb.67.1.72 |
0.469 |
|
1975 |
Woodrum DT, Rich SA, Pollard TD. Evidence for biased bidirectional polymerization of actin filaments using heavy meromyosin prepared by an improved method. The Journal of Cell Biology. 67: 231-7. PMID 240859 DOI: 10.1083/JCB.67.1.231 |
0.39 |
|
1974 |
Pollard TD, Thomas SM, Niederman R. Human platelet myosin. I. Purification by a rapid method applicable to other nonmuscle cells Analytical Biochemistry. 60: 258-266. PMID 4277511 DOI: 10.1016/0003-2697(74)90152-3 |
0.345 |
|
1974 |
Burns RG, Pollard TD. A dynein-like protein from brain. Febs Letters. 40: 274-80. PMID 4277332 DOI: 10.1016/0014-5793(74)80243-7 |
0.363 |
|
1974 |
Pollard TD, Weihing RR. Actin and myosin and cell movement. Crc Critical Reviews in Biochemistry. 2: 1-65. PMID 4273099 DOI: 10.3109/10409237409105443 |
0.309 |
|
1973 |
Orkin RW, Pollard TD, Hay ED. SDS gel analysis of muscle proteins in embryonic cells. Developmental Biology. 35: 388-94. PMID 4788228 DOI: 10.1016/0012-1606(73)90035-3 |
0.427 |
|
1973 |
Pollard TD, Korn ED. Electron microscopic identification of actin associated with isolated amoeba plasma membranes. The Journal of Biological Chemistry. 248: 448-50. PMID 4567783 |
0.518 |
|
1973 |
Pollard TD, Korn ED. Acanthamoeba myosin. II. Interaction with actin and with a new cofactor protein required for actin activation of Mg 2+ adenosine triphosphatase activity. The Journal of Biological Chemistry. 248: 4691-7. PMID 4268864 |
0.619 |
|
1973 |
Pollard TD, Korn ED. Acanthamoeba myosin. I. Isolation from Acanthamoeba castellanii of an enzyme similar to muscle myosin. The Journal of Biological Chemistry. 248: 4682-90. PMID 4268863 |
0.504 |
|
1973 |
Pollard TD, Eisenberg E, Korn ED, Kielley WW. Inhibition of Mg ++ ATPase activity of actin-activated Acanthamoeba myosin by muscle troponin-tropomyosin: implications for the mechanism of control of amoeba motility and muscle contraction. Biochemical and Biophysical Research Communications. 51: 693-8. PMID 4267405 DOI: 10.1016/0006-291X(73)91370-3 |
0.587 |
|
1973 |
Pollard TD, Korn ED. The "Contractile" Proteins of Acanthamoeba castellanii Cold Spring Harbor Symposia On Quantitative Biology. 37: 573-583. DOI: 10.1101/Sqb.1973.037.01.068 |
0.557 |
|
1972 |
Adelstein RS, Conti MA, Johnson GS, Pastan I, Pollard TD. Isolation and characterization of myosin from cloned mouse fibroblasts. Proceedings of the National Academy of Sciences of the United States of America. 69: 3693-7. PMID 4264772 DOI: 10.1073/Pnas.69.12.3693 |
0.392 |
|
1971 |
Pollard TD, Korn ED. Filaments of Amoeba proteus. II. Binding of heavy meromyosin by thin filaments in motile cytoplasmic extracts. The Journal of Cell Biology. 48: 216-9. PMID 5545110 DOI: 10.1083/Jcb.48.1.216 |
0.641 |
|
1971 |
Adelstein RS, Pollard TD, Kuehl WM. Isolation and characterization of myosin and two myosin fragments from human blood platelets. Proceedings of the National Academy of Sciences of the United States of America. 68: 2703-7. PMID 4256552 DOI: 10.1073/Pnas.68.11.2703 |
0.375 |
|
1970 |
Pollard TD, Ito S. Cytoplasmic filaments of Amoeba proteus. I. The role of filaments in consistency changes and movement. The Journal of Cell Biology. 46: 267-89. PMID 4915451 DOI: 10.1083/Jcb.46.2.267 |
0.41 |
|
1970 |
Pollard TD, Shelton E, Weihing RR, Korn ED. Ultrastructural characterization of F-actin isolated from Acanthamoeba castellanii and identification of cytoplasmic filaments as F-actin by reaction with rabbit heavy meromyosin. Journal of Molecular Biology. 50: 91-7. PMID 4318206 DOI: 10.1016/0022-2836(70)90106-3 |
0.661 |
|
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