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Publications - Original Research

1.      Pomerat, C.M., Rounds, D.E., Raiborn, C.W. and Pollard, T.D. (1964) Observations on newborn ratdorsal root ganglia in vitro following gamma irradiation. In: "Response of the nervous system to ionizingirradiation" (Haley and Snider, eds.), Little, Brown and Company, pp. 175-200.

2.      Ito, S., Shihman Chang, R. and Pollard, T.D. (1969) Cytoplasmic distribution of DNA in a strain of Hartmannellid amoeba. J. Protozool. 16:638-645.

3.      Pollard, T.D., Shelton, E., Weihing, R.R. and Korn, E.D. (1970) Ultrastructural characterization of F-actin isolated from Acanthamoeba castellanii and identification of cytoplasmic filaments as F-actin by reaction with rabbit muscle heavy meromyosin. J. Mol. Biol. 51:91-97.

4.      Pollard, T.D. and Ito, S. (1970) Cytoplasmic filaments of Amoeba proteus. I. The role of filaments in consistency changes and movements. J. Cell Biol. 46:267-289.

5.      Pollard, T.D. and Weiss, I.W. (1970) Acute tubular necrosis in a patient with march hemoglobinuria. New Eng. J. Med. 283:803.

6.      Pollard, T.D. and Korn, E.D. (1971) Filaments of Amoeba proteus. II. Binding of heavy meromyosin by thin filaments in motile cytoplasmic extracts. J. Cell Biol. 48:216-219.

7.      Stossel, T.P., Pollard, T.D., Mason, R.J. and Vaughan, M. (1971) Isolation and properties of phagocytic vesicles from polymorphonuclear leukocytes. J. Clin. Invest. 50:1745-1757.

8.      Adelstein, R.S., Pollard, T.D. and Kuehl, W.M. (1971) Isolation and characterization of myosin and two myosin fragments from human blood platelets. Proc. Natl. Acad. Sci. USA 68:2703-2707.

9.     Stossel, T.P., Mason, R.J., Pollard, T.D. and Vaughan, M. (1972) Isolation and properties of phagocytic vesicles. II. Alveolar macrophages. J. Clin. Invest. 50:605-614.

10.    Adelstein, R.S., Conti, M.A., Johnson, G.S., Pastan, I. and Pollard, T.D. (1972) Isolation and characterization of myosin from cloned mouse fibroblasts. Proc. Natl. Acad. Sci. USA 69:3693-3697.

11.    Pollard, T.D. and Korn, E.D. (1973) The contractile proteins of Acanthamoeba castellanii. Cold Spring Harbor Symposium on Quantitative Biology 37:573-583.

12.    Pollard, T.D. and Korn, E.D. (1973) Electron microscopic identification of actin associated with isolated amoeba membranes. J. Biol. Chem. 248:448-450.

13.    Pollard, T.D., Eisenberg, E., Korn, E.D. and Kielley, W.W. (1973) Inhibition of Mg++‑ATPase of actin-activated Acanthamoeba myosin by muscle troponin tropomyosin: implications for the mechanism of control of amoeba motility and muscle contraction. Biochem. Biophys. Res. Comm. 51:693-698.

14.    Pollard, T.D. and Korn, E.D. (1973) Acanthamoeba myosin. I. Isolation from Acanthamoeba castellanii of an enzyme similar to muscle myosin. J. Biol. Chem. 248:4682-4690.

15.    Pollard, T.D. and Korn, E.D. (1973) Acanthamoeba myosin. II. Interaction with actin and with a new cofactor protein required for actin activation of Mg++ATPase activity. J. Biol. Chem. 248:4691-4697.

16.    Stossel, T.P. and Pollard, T.D. (1973) Myosin in polymorphonuclear leukocytes. J. Biol. Chem. 248:8288-8294.

17.    Orkin, R.W., Pollard, T.D. and Hay, E.D. (1973) SDS gel analysis of muscle proteins in embryonic cells. Devel. Biol. 35:388-394.

18.    Burns, R.G. and Pollard, T.D. (1974) A dynein-like protein from brain. FEBS Letters 40:274-280.

19.    Pollard, T.D., Thomas, S.M. and Niederman, R. (1974) Human platelet myosin. I. Purification by  a rapid method applicable to other non-muscle cells,  Anal. Biochem. 60:258-266.

20.    Niederman, R. and Pollard, T.D. (1975) Human platelet myosin. II. In vitro assembly of myosin and structure of myosin filaments. J. Cell Biol. 67:72-92.

21.    Pollard, T.D. (1975) Electron microscopy of synthetic myosin filaments. Evidence for cross-bridge flexibility and copolymer formation. J. Cell Biol. 67:93-104.

22.    Woodrum, D.T., Rich, S.A. and Pollard, T.D. (1975) Evidence for biased bidirectional polymerization of actin using heavy meromyosin prepared by an improved method. J. Cell Biol. 67:231-237.

23.    Pollard, T.D. (1976) The role of actin in the temperature dependent gelation and contraction of extracts of Acanthamoeba. J. Cell Biol. 68:579-601.

24.    Fujiwara, K. and Pollard, T.D. (1976) Fluorescent antibody localization of myosin in the cytoplasmic, cleavage furrow and mitotic spindle of human cells. J. Cell Biol. 71:848-875.

25.    Pollard, T.D., Fujiwara, K., Handin, R. and Weiss, G. (1976) Contractile proteins in platelet activation and contraction. Annals N.Y. Acad. Sci. 283:218-236.

26.    Schreiner, G.F., Fujiwara, K., Pollard, T.D. and Unanue, E.R. (1977) Redistribution of myosin accompanying capping of surface Ig. J. Exp. Med. 145:1393-1398.

27.    Fujiwara, K. and Pollard, T.D. (1978) Simultaneous localization of myosin and tubulin in human tissue culture cells by double antibody staining. J. Cell Biol. 77:182-195.

28.    Maupin-Szamier, P. and Pollard, T.D. (1978)  Actin filament destruction by osmium tetroxide. J. Cell Biol. 77:837-852.

29.    Herman, I. and Pollard, T.D. (1978) Actin localization in fixed, dividing cells stained with fluorescent heavy meromyosin. Exp. Cell Research 114:15-25.

30.    Pollard, T.D., Stafford, W.F., III and Porter, M.E. (1978) Characterization of a second myosin from Acanthamoeba castellanii. J. Biol. Chem. 253:4798-4808.

31.    Griffith, L.M. and Pollard, T.D. (1978) Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins. J. Cell Biol. 78:958-965.

32.    Fujiwara, K., Porter, M.E. and Pollard, T.D. (1978) Alpha-actinin localization in the cleavage furrow during cytokinesis. J. Cell Biol. 79:268-275.

33.    Braun, J., Fujiwara, K., Pollard, T.D. and Unanue, E.R. (1978) Two distinct mechanisms for redistribution of lymphocyte surface macromolecules. I. Relationship to cytoplasmic myosin. J. Cell Biol. 79:408-418.

34.    Braun, J., Fujiwara, K., Pollard, T.D. and Unanue, E.R. (1978) Two distinct mechanisms for redistribution of lymphocyte surface macromolecules. II. Contrasting effects of local anesthetics and a calcium ionophore. J. Cell Biol. 79:419-426.

35.    Mooseker, M.S., Pollard, T.D. and Fujiwara, K. (1978) Characterization and localization of myosin in the brush border of intestinal epithelial cells. J. Cell Biol. 79:444-453.

36.    Herman, I.M. and Pollard, T.D. (1979) Comparison of purified anti-actin and fluorescent-heavy meromyosin staining patterns in dividing cells. J. Cell Biol. 80:509-520.

37.    MacLean-Fletcher, S. and Pollard, T.D. (1980) Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors. J. Cell Biol. 85:414-428.

38.   MacLean-Fletcher, S. and Pollard, T.D. (1980) Mechanism of action of cytochalasin B on actin. Cell 20:329-341.

39.    MacLean-Fletcher, S. and Pollard, T.D. (1980) Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association. Biochem. Biophys. Res. Comm. 96:18-27.

40.    Isenberg, G.H., Aebi, U. and Pollard, T.D. (1980) An actin binding protein from Acanthamoeba regulates actin filament polymerization and interactions. Nature 288:455-459.

41.    Aebi, U., Smith, P.R., Isenberg, G.H. and Pollard, T.D. (1980) Structure of crystalline actin sheets. Nature 288:296-298.

42.    Herman, I.M. and Pollard, T.D. (1981) Electron microscopic localization of cytoplasmic myosin with ferritin-labeled antibodies. J. Cell Biol. 88:346-351.

43.    Pollard, T.D. and Mooseker, M.S. (1981) Direct measurement of actin polymerization rate constants by electron microscopy of actin filaments nucleated by isolated microvillus cores. J. Cell Biol. 88:654-659.

44.   Pollard, T.D. (1981) Purification of a calcium-sensitive actin gelation protein from Acanthamoeba. J. Biol. Chem. 256:7666-7670.

45.    Herman, I.M., Crisona, N.J. and Pollard, T.D. (1981) Relation between cell activity and the distribution of cytoplasmic actin and myosin. J. Cell Biol. 90:84-91.

46.    Aebi, U., Fowler, W.E., Isenberg, G.H., Pollard, T.D. and Smith, P.R. (1981) Crystalline actin sheets: their structure and polymorphism. J. Cell Biol. 91:340-351.

47.    Tseng, P.C.-H. and Pollard, T.D. (1982) Mechanism of action of Acanthamoeba profilin. Demonstration of actin species specificity and regulation of micromolar concentrations of MgCl2. J. Cell Biol. 94:213-218.

48.    Griffith, L.M. and Pollard, T.D. (1982) Cross-linking of actin filament networks by self-association and actin-binding macromolecules. J. Biol. Chem. 257:9135-9142.

49.    Griffith, L.M. and Pollard, T.D. (1982) The interaction of actin filaments with microtubules and microtubule-associated proteins. J. Biol. Chem. 257:9143-9151.

50.    Mooseker, M.S., Pollard, T.D. and Wharton, K.A. (1982) Nucleated polymerization of actin from the membrane-associated ends of microvillar filaments in the intestinal brush border. J. Cell Biol. 95:223-233.

51.    Pollard, T.D. (1982)  Structure and polymerization of Acanthamoeba myosin-II filaments. J. Cell Biol. 95:816-825.

52.    Maupin, P. and Pollard, T.D. (1983) Improved preservation and staining of HeLa cell actin filaments, clathrin-coated membranes, and other cytoplasmic structures by tannic acid-glutaraldehyde-saponin fixation. J. Cell Biol. 96:51-62.

53.    Wong, A.J., Pollard, T.D. and Herman, I.M. (1983) Actin filament stress fibers in vascular endothelial cells in vivo. Science 219:867-869.

54.    Dang, C.V., Yang, D.C.H. and Pollard, T.D. (1983) Association of methionyl-tRNA synthetase with detergent-insoluble components of the rough endoplasmic reticulum. J. Cell Biol. 96:1138-1147.

55.    Cooper, J.A., Buhle, E.L., Jr., Walker, S.B., Tsong, T.Y. and Pollard, T.D. (1983) Kinetic evidence for a monomer activation step in actin polymerization. Biochemistry 22:2193-2202.

56.    Cooper, J.A., Walker, S.B. and Pollard, T.D. (1983) Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization. J. Muscle Res. & Cell Motility 4:253-262.

57.    Selden, S.C. and Pollard, T.D. (1983)  Phosphorylation of microtubule-associated proteins regulates their interaction with actin filaments. J. Biol. Chem. 258:7064-7071.

58.    Smith, P.R., Fowler, W.E., Pollard, T.D. and Aebi, U. (1983) Structure of the actin molecule determined from electron micrographs of crystalline actin sheets with a tentative alignment of the molecule in the actin filament. J. Mol. Biol. 167:641-660.

59.    Pollard, T.D. (1983) Measurement of rate constants for actin filament elongation in solution. Anal. Biochem. 134:406-412.

60.    Tseng, P.C.-H., Runge, M.S., Cooper, J.A., Williams, J.C., Jr. and Pollard, T.D. (1984) Physical, immunochemical, and functional properties of Acanthamoeba profilin. J. Cell Biol. 98:214-221.

61.    Pollard, T.D. and Weeds, A.G. (1984) The rate constant for ATP hydrolysis by polymerized actin. FEBS Lett. 170:94-98.

62.    Kiehart, D.P. and Pollard, T.D. (1984) Stimulation of Acanthamoeba actomyosin ATPase activity by myosin-II polymerization. Nature 308:864-866.

63.    Cooper, J.A., Blum, J.D. and Pollard, T.D. (1984) Acanthamoeba castellanii capping protein: Properties, mechanism of action, immunologic cross-reactivity, and localization. J. Cell Biol. 99:217-225.

64.    Kiehart, D.P., Kaiser, D. and Pollard, T.D. (1984) Monoclonal antibodies demonstrate limited structural homology between myosin isozymes from Acanthamoeba. J. Cell Biol. 99:1002-1014.

65.    Kiehart, D.P., Kaiser, D. and Pollard, T.D. (1984) 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. J. Cell Biol. 99:1015-1023.

66.    Kiehart, D.P. and Pollard, T.D. (1984) Inhibition of Acanthamoeba actomyosin-II ATPase activity and mechanochemical function by monoclonal antibodies. J. Cell Biol. 99:1024-1033.

67.    Pollard, T.D. (1984) Polymerization of ADP-actin. J. Cell Biol. 99:769-777.

68.    Pollard, T.D. and Cooper, J.A. (1984) Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation. Biochemistry 23:6631-6641.

69.    Pollard, T.D. (1984) Purification of a high molecular weight actin filament gelation protein from Acanthamoeba that shares antigenic determinants with vertebrate spectrins. J. Cell Biol. 99:1970-1980.

70.    Wong, A.J., Kiehart, D.P. and Pollard, T.D. (1985) Myosin from human erythrocytes. J. Biol. Chem. 260:46-49.

71.    Cooper, J.A. and Pollard, T.D. (1985) Effect of capping protein on the kinetics of actin polymerization. Biochemistry: 24:793-799.

72.    Sato, M., Leimbach, G., Schwarz, W.H. and Pollard, T.D. (1985) Mechanical properties of actin. J. Biol. Chem. 260:8585-8592.

73.    Cooper, J.A., Blum, J.D., Williams, R.C., Jr. and Pollard, T.D. (1986) Purification and characterization of actophorin, a new 15,000-dalton actin binding protein from Acanthamoeba castellanii. J. Biol. Chem. 261:477-485.

74.    Kaiser, D.P., Sato, M.D., Ebert, R. and Pollard, T.D. (1986) Purification and characterization of two isoforms of Acanthamoeba profilin. J. Cell Biol. 102:221-226.

75.    Selden, S.C. and Pollard, T.D. (1986) Interaction of actin filaments with microtubules is mediated by microtubule associated proteins and regulated by phosphorylation. Ann. New York Acad. Sci. 466:803-812.

76.    Sato, M., Schwarz, W.H. and Pollard, T.D. (1986) Acanthamoeba profilin affects the mechanical properties of nonfilamentous actin. J. Biol. Chem. 261:10701-10706.

77.    Adams, R.J. and Pollard, T.D. (1986) Propulsion of organelles isolated from Acanthamoeba along actin filaments by myosin-I. Nature 322:754-756.

78.    Drenckhahn, D. and Pollard, T.D. (1986) Elongation of actin filaments is a diffusion-limited reaction at the barbed end and is accelerated by inert macromolecules. J. Biol. Chem. 261:12754-12758.

79.    Magnus, K.A., Lattman, E.E., Sato, M. and Pollard, T.D. (1986) Crystallization of Acanthamoeba profilin-I. J. Biol. Chem. 261:13360-13361.

80.    Maupin, P. and Pollard, T.D. (1986) Arrangement of actin filaments and myosin-like filaments in the contractile ring and actin-like filaments in the mitotic spindle of dividing HeLa cells. J. Ultrastruct. Res. 94:92-103.

81.    Hagen, S.J., Kiehart, D.P., Kaiser, D.A. and Pollard, T.D. (1986) Characterization of monoclonal antibodies to Acanthamoeba myosin-I that cross-react with both myosin-II and low molecular weight nuclear proteins. J. Cell Biol. 103:2121-2128.

82.    Pollard, T.D. (1986) Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. J. Cell Biol. 103:2747-2754.

83.    Pollard, T.D., Tseng, P.C.-H., Rimm, D.L. , Bichell, D.P., Williams, R.C., Jr., Sinard, J. and Sato, M. (1986) Characterization of alpha-actinin from Acanthamoeba. Cell Motil. Cytoskel. 6:649-661.

84.    Earnshaw, W.C., Sullivan, K.F., Machlin, P.S., Cooke, C.A., Kaiser, D.A., Pollard, T.D., Rothfield, N.F. and Cleveland, D.W. (1987) Molecular cloning of cDNA for CENP‑B, the major human centromere autoantigen. J. Cell Biol. 104:817-829.

85.    Sato, M., Schwarz, W.H. and Pollard, T.D. (1987) Dependence of the mechanical properties of actin/alpha-actinin gels on deformation rate. Nature 325:828-830.

86.    Aebi, U. and Pollard, T.D. (1987) A glow discharge unit to render electron microscope grids and other surfaces hydrophilic. J. Electron Microscopic Technique 7:29-33.

87.    Sellers, H.S., Schwarz, W.H., Sato, M. and Pollard, T.D. (1987) Boundary effects on the drag of an oscillating sphere: applications to the magnetic sphere rheometer. J. Non-Newtonian Fluid Mech. 26:43-55.

88.    Ampe, C., Sato, M., Pollard, T.D. and Vandekerckhove, J. (1988) The primary structure of the basic isoform of Acanthamoeba profilin. Eur. J. Biochem. 170:597-601.

89.    Lee, S., Li, M. and Pollard, T.D. (1988) Evaluation of the binding of Acanthamoeba profilin to pyrene-labeled actin by fluorescence enhancement. Anal. Biochem. 168:148-155.

90.    Sato, M., Schwarz, W.H., Selden, S.C. and Pollard, T.D. (1988) Mechanical properties of brain tubulin and microtubules. J. Cell Biol. 106:1205-1211.

91.    Murphy, D.B., Gray, R.V., Grasser, W.A. and Pollard, T.D. (1988) Direct demonstration of actin filament annealing in vitro. J. Cell Biol. 106:1947-1954.

92.    Carboni, J.M., Conzelman, K.A., Adams, R.A., Kaiser, D.A., Pollard, T.D. and Mooseker, M.S. (1988) 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. J. Cell Biol. 107:1749-1757.

93.    Rimm, D.L., Pollard, T.D. and Hieter, P. (1988) Resolution of Acanthamoeba castellanii chromosomes by pulsed field gel electrophoresis and construction of the initial linkage map. Chromosoma 97:219-223.

94.    Magnus, K.A., Maciver, S.K. and Pollard, T.D. (1988) Crystallization of actophorin, an actin filament severing protein from Acanthamoeba. J. Biol. Chem. 263:18143-18144.

95.    Hitchcock-DeGregori, S.E., Sampath, P. and Pollard, T.D. (1988) Tropomyosin inhibits the rate of actin polymerization by stabilizing actin filaments. Biochemistry 27:9182-9185.

96.    Sinard, J.H. and Pollard, T.D. (1989) Microinjection into Acanthamoeba castellanii of monoclonal antibodies to myosin-II slows but does not stop cell locomotion. Cell Motil. Cytoskel. 12:42-52.

97.    Rimm, D.L. and Pollard, T.D. (1989) New plasmid vectors for high level synthesis of eukaryotic fusion proteins in Escherichia coli. Gene 75:323-327.

98.    Rimm, D.L., Sinard, J.H. and Pollard, T.D. (1989) Location of the head-tail junction of myosin. J. Cell Biol. 108:1783-1789.

99.    Vandekerckhove, J.S., Kaiser, D.A. and Pollard, T.D. (1989) Acanthamoeba actin and profilin can be crosslinked between glutamic acid 364 of actin and lysine 115 of profilin. J. Cell Biol. 109:619-626.

100.  Adams, R.J. and Pollard, T.D (1989)  Binding of myosin I to membrane lipids. Nature 340:565-568.

101.  Rimm, D.L. and Pollard, T.D.. (1989) Purification and characterization of an Acanthamoeba nuclear actin-binding protein. J. Cell Biol. 109:585-591.

102.  Sinard, J.H. and Pollard, T.D. (1989) The effect of heavy chain phosphorylation and solution conditions on the assembly of Acanthamoeba myosin-II. J. Cell Biol. 109:1529-1535.

103.  Sinard, J.H., Stafford, W.F. and Pollard, T.D. (1989) The mechanism of assembly of Acanthamoeba myosin-II minifilaments: minifilaments assemble by three successive dimerization steps. J. Cell Biol. 109:1537-1547.

104.  Kaiser, D.A., Goldschmidt-Clermont, P.J., Levine, B. and Pollard, T.D. (1989) Characterization of renatured profilin purified by urea elution from poly-L-proline agarose columns. Cell Motil. Cytoskel. 14:251-262.

105.  Sinard, J.H. and Pollard, T.D. (1990)  Acanthamoeba myosin-II minifilaments assemble on a millisecond time scale with rate constants greater than those expected for a diffusion limited reaction. J. Biol. Chem. 265:3654-3660.

106.  Goldschmidt-Clermont, P.J., Machesky, L.M., Baldassare, J.J. and Pollard, T.D. (1990)  The actin-binding protein profilin binds to PIP2 and inhibits its hydrolysis by phospholipase C. Science 247:1575-1578.

107.  Pollard, T.D., Maupin, P., Sinard, J. and Huxley, H.E. (1990) A stopped-flow/rapid-freezing machine with millisecond time resolution to prepare intermediates in biochemical reactions for electron microscopy. J. Electron Microscopic Technique 16:160-166.

108.  Rimm, D.L., Kaiser, D.A., Bhandari, D., Maupin, P., Kiehart, D.P. and Pollard, T.D. (1990)  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. J. Cell Biol. 111:2405-2416.

109.  Sinard, J.H., Rimm, D.L. and Pollard, T.D. (1990)  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. J. Cell Biol. 111:2417-2426.

110.  Machesky, L.M., Goldschmidt-Clermont, P.J. and Pollard, T.D. (1990) The affinities of human platelet and Acanthamoeba profilin isoforms for polyphosphoinositides account for their relative abilities to inhibit phospholipase C. Cell Regulation 1:937-950.

111.  Sampath, P. and Pollard, T.D. (1991)  Effects of cytochalasin, phalloidin and pH on the elongation of actin filaments. Biochemistry 30:1973-1980.

112.  Goldschmidt-Clermont, P.J., Kim, J.W., Machesky, L.M., Rhee, S.G. and Pollard, T.D. (1991)  Regulation of phospholipase C-gamma l by profilin and tyrosine phosphorylation. Science 251:1231-1233.

113.  Goldschmidt-Clermont, P.J., Machesky, L.M., Doberstein, S.K. and Pollard, T.D. (1991)  Mechanism of the interaction of human platelet profilin with actin. J. Cell Biol. 113:1081-1089.

114.  Vojtek, A., Haarer, B., Field, J., Gerst, J., Pollard, T.D., Brown, S. and Wigler, M. (1991)  Evidence for a functional link between profilin and CAP in the yeast Saccharomyces cerevisiae. Cell 66:497-505.

115.  Pollard, T.D. and Rimm, D.L. (1991)  Analysis of cDNA clones for Acanthamoeba profilin-I and profilin-II shows end to end homology with vertebrate profilins and a family of profilin genes. Cell Motil. Cytoskel. 20:169-177.

116.  Bremer, A., Millonig, R.C., Sutterlin, R., Engel, A., Pollard, T.D. and Aebi, U. (1991)  The structural basis for the intrinsic disorder of the actin filament: the 'lateral slipping' model. J. Cell Biol. 115:689-703.

117.  Kobayashi, T., Zot, H.G., Pollard, T.D. and Collins, J.H. (1991)  Functional implications of the unusual amino acid sequence of the regulatory light chain of Acanthamoeba castellanii myosin‑II. J. Muscle Res. Cell Motil. 12:553-559.

118.  Maciver, S.K., Zot, H.G. and Pollard, T.D. (1991)  Characterization of actin filament severing by actophorin from Acanthamoeba castellanii. J. Cell Biol. 115:1611-1620.

119.  Maciver, S.K., Wachsstock, D., Schwarz, W.H. and Pollard, T.D. (1991)  The actin filament severing protein actophorin catalyzes the formation of rigid bundles of actin filaments crosslinked with alpha-actinin. J. Cell Biol. 115:1621-1628.

120.  Zot, H.G., Doberstein, S.K. and Pollard, T.D. (1991)  Myosin-I moves actin filaments on a phospholipid substrate: implications for membrane targeting. J. Cell Biol. 116:367-376.

121.  Doberstein, S.K. and Pollard, T.D. (1992)  Localization and specificity of the phospholipid and actin binding sites on the tail of Acanthamoeba myosin-IC. J. Cell Biol. 117:1241-1249.

122.  Yonemura, S. and Pollard, T.D. (1992)  The localization of actin, myosin-I and myosin-II in Acanthamoeba by fluorescence microscopy. J. Cell Sci. 102:629-642.

123.  Satterwhite, L.L., Lohka, M.L., Wilson, K., Cisek, L.J., Corden, J.L. and Pollard, T.D. (1992)  Phosphorylation of myosin regulatory light chain by cyclin-p34 kinase. J. Cell Biol. 118:595-605.

124.  Goldschmidt-Clermont, P.J., Furman, M.I., Wachsstock, D., Safer, D., Nachmias, V.T. and Pollard, T.D. (1992)  Regulation of actin nucleotide exchange by thymosinß4 and profilin. Molec. Biol. Cell 3:1015-1024.

125.  Pollard, T.D., Goldberg, I. and Schwarz, W.H. (1992)  Nucleotide exchange, structure and mechanical properties of filaments assembled from ATP-actin and ADP-actin. J. Biol. Chem. 267:20339-20345.

126.  Pollard, T.D., Bhandari, D., Maupin, P., Weeds, A.G. and Zot, H.G. (1993)  Direct visualization by electron microscopy of the weakly-bound intermediates in the actomyosin ATPase cycle. Biophys. J. 64:454-471.

127.  Archer, S.J., Vinson, V.K., Pollard, T.D. and Torchia, D.A. (1993)  Secondary structure and topology of Acanthamoeba  profilin-I as determined by heteronuclear magnetic resonance spectroscopy. Biochemistry. 32:6680-6687.

128.  Wachsstock, D.H., Schwarz, W.H. and Pollard, T.D. (1993)  Affinity of alpha-actinin for actin filaments determines the structure and mechanical properties of actin filament gels. Biophys. J. 65:205-214.

129.  Quirk, S., Maciver, S.K., Ampe, C., Doberstein, S.K., Kaiser, D.A., VanDamme, J., Vandekerckhove, J.S. and Pollard, T.D. (1993)  Primary structure and studies of Acanthamoeba actophorin. Biochemistry 32:8525-8533.

130.  Vinson, V.K., Archer, S.J., Lattman, E.E., Pollard, T.D. and Torchia, D.A. (1993)  Three dimensional solution structure of Acanthamoeba  profilin-I  J. Cell Biol. 122:1277-1283.

131.  Doberstein, S.K., Baines, I., Weigand, G., Korn, E.D. and Pollard, T.D. (1993)  Inhibition of contractile vacuole function in vivo  by myosin-I antibodies. Nature 365: 841-843.

132.  Porter, J., Yu, M., Doberstein, S.K., Pollard, T.D. and Montell, C. (1993)  Dependence of calmodulin localization in the retina on the NINAC unconventional myosin. Science  262:1038-1042.

133.  Archer, S.J., Vinson, V.K., Pollard, T.D. and Torchia, D.A. (1994)  Elucidation of the poly-L-proline binding site in Acanthamoeba profilin-I by NMR spectroscopy. FEBS Lett. 337:145-151.

134.  Almo, S.C., Pollard, T.D., Way, M. and Lattman, E.E. (1994)  Purification, characterization and crystallization of Acanthamoeba profilin expressed in Escherichia coli. J. Mol. Biol. 236:950-952.

135.  Wachsstock, D.H., Schwarz, W.H. and Pollard, T.D. (1994)  Crosslinker dynamics determine the mechanical properties of actin gels. Biophys. J. 66:801-809.

136.  Smith, K.J., Levy, D.B., Maupin, P., Pollard, T.D., Vogelstein, B. and Kinzler, K.W. (1994)  Wild-type but not mutant APC associates with the microtubule cytoskeleton. Cancer Res. 54:3672-3675.

137.  Wachsstock, D.H. and Pollard, T.D. (1994)  Transient state kinetics tutorial using KINSIM. Biophys. J. 67:1260-1273.

138.  Fedorov, A.A., Magnus, K.A., Graupe, H., Lattman, E.E., Pollard, T.D., and Almo, S.C. (1994)  Crystal structures of two Acanthamoeba profilins that differ in their affinity for polyphosphoinosides. Proc. Nat. Acad. Sci. USA. 91.8636-8640.

139.  Machesky, L.M., Cole, N.B., Moss, B. and Pollard, T.D. (1994)  Vaccinia virus expresses a novel profilin with a higher affinity for polyphosphoinositides than for actin. Biochemistry 33:10815-10824.

140.  Machesky, L.M., Atkinson, S.J., Ampe, C., Vandekerckhove, J. and Pollard, T.D. (1994)  A cortical complex of seven Acanthamoeba  polypeptides including two unconventional actins binds to profilin. J. Cell Biol. 127:107-115.

141.  Maupin, P., Phillips, C.L., Adelstein, R.S. and Pollard, T.D. (1994)  Differential localization of myosin‑II isozymes in human cultured cells and blood cells. J. Cell Sci. 107:3077-3090.

142.  De La Cruz, E. and Pollard, T.D. (1994)  Transient kinetic analysis of rhodamine phalloidin binding to actin filaments. Biochemistry 33:14387-14392.

143.  De La Cruz, E.M. and Pollard, T.D. (1995)  Nucleotide and divalent cation-free actin:  Stabilization by sucrose and nucleotide binding kinetics. Biochemistry 34:5452-5461.

144.  Doberstein, S.K., Wiegand, G., Machesky, L.M. and Pollard, T.D. (1995)  Fluorescent erythrocyte ghosts as standards for quantitative flow cytometry. Cytometry 20:14-18.

145.  Kelleher, J.F., Atkinson, S.J. and Pollard, T.D. (1995)  Sequences, structural models and cellular localization of the actin-related proteins Arp2 and Arp3 from Acanthamoeba.. J. Cell Biol. 131:385-397.

146.  Bresnick, A., Wolff-Long, V., Baumann, O. and Pollard, T.D. (1995)  Phosphorylation on threonine-18 of the regulatory light chain dissociates the ATPase and motor properties of smooth muscle myosin-II. Biochemistry 34:12576-12583.

147.  Kaiser, D.A. and Pollard, T.D. (1996)  Characterization of the actin and poly-L-proline binding sites of Acanthamoeba profilin with monoclonal antibodies and mutagenesis. J. Mol. Biol. 255:89-107.

148.  Ostap, E. M. and Pollard, T.D. (1996)  Biochemical kinetic characterization of the Acanthamoeba myosin‑I ATPase. J. Cell Biol. 132:1053-1060.

149.  De La Cruz, E.M. and Pollard, T.D. (1996)  Kinetics and thermodynamics of phalloidin binding to actin from three divergent species. Biochemistry 35:14054-14061.

150.  Petrella, E.C., Machesky, L.M., Kaiser, D.A. and Pollard, T.D. (1996)  Structural requirements and thermodynamics of the interaction of proline peptides with profilin. Biochemistry 35:16535-16543.

151.  Mullins, R.D., Stafford, W.F. and Pollard, T.D. (1997)  Structure, subunit topology and actin-binding activity of the Arp2/3 complex from Acanthamoeba. J. Cell Biol. 136: 331-343.

152.  Turbedsky, K., Pollard, T.D. and Bresnick, A.R. (1997)  A subset of protein kinase C phosphorylation sites on myosin II regulatory light chain inhibit phosphorylation by myosin light chain kinase. Biochemistry 36: 2063-2067.

153.  Leonard, S.A., Gittis, A.G., Petrella, E.C., Pollard, T.D. and Lattman, E.E. (1997)  Crystal structure of the actin-binding protein actophorin from Acanthamoeba. Nature Struct. Biol. 4:369-373.

154.  Bezanilla, M., Forsburg, S.L. and Pollard, T.D. (1997)  Identification of a second myosin-II in S. pombe:  Myp2p is conditionally required for cytokinesis. Molec. Biol. Cell 8:2693-2705.

155.  Jontes, J.D., Milligan, R.A., Pollard, T.D. and Ostap, E.M. (1997) Kinetic characterization of brush border myosin-I ATPase. Proc. Nat. Acad. Sci. USA 94:14332-14337.

156.  Xu, J., Wirtz, D. and Pollard, T.D. (1998)  Dynamic crosslinking by alpha-actinin determines the mechanical properties of actin filament networks. J. Biol. Chem. 273:9570-9576.

157.  Xu, J., Schwarz, W.H., Kas, J.A., Stossel, T.A., Janmey, P.A. and Pollard, T.D. (1998)  Mechanical properties of actin filament networks depend on preparation, polymerization conditions and storage of G-actin. Biophys. J. 74:2731-2740.

158.  Mullins, R.D., Kelleher, J.F., Xu, J. and Pollard, T.D. (1998) Arp2/3 complex from Acanthamoeba binds profilin and crosslinks actin filaments. Molec. Biol. Cell 9:841-852.

159.  Jontes, J.D., Ostap, E.M., Pollard, T.D. and Milligan, R.A. (1998) Three-dimensional structure of Acanthamoeba myosin-IB determined by cryo-electron microscopy of decorated actin filaments. J. Cell Biol. 141:155-162.

160.  Mullins, R.D., Heuser, J.A. and Pollard, T.D. (1998)  The interaction of the Arp2/3 complex with actin:  nucleation, high affinity pointed end capping and formation of branching networks of filaments. Proc. Nat. Acad. Sci. USA 95:6181-6186.

161.  Vinson*, V.K., De La Cruz*, E.M., Higgs, H. and Pollard, T.D. (1998)  Interactions of Acanthamoeba profilin with actin and nucleotides bound to actin. Biochemistry 37:10871-10880.* co-first authors.

162.  Freeman, J.L.R., De La Cruz, E.M., Pollard, T.D., Lefkowitz, R.J. and Pitcher, J.A. (1998)  Regulation of G-protein coupled receptor kinase 5 (GRK5) by actin. J. Biol. Chem. 273:20653-20657.

163.  Blanchoin, L. and Pollard, T.D. (1998)  Interaction of actin monomers with actophorin (ADF/cofilin) and profilin. J. Biol. Chem. 273:25106-25111.

164.  Liu, S., Fedorov, A.A., Pollard, T.D., Lattman, E.E., Almo, S.C. and Magnus, K.A. (1998)  Crystal packing induces a conformational change in profilin-I from Acanthamoeba castellanii. J. Struct. Biol. 123:22-29.

165.  Xu, J., Casella, J.F. and Pollard, T.D. (1999)  Effect of capping protein, CapZ, on the length of actin filaments and mechanical properties of actin filament networks. J. Cell Motility Cytoskeleton 42:73-81.

166.  Machesky, L.M., Mullins, R.D., Higgs, H.N., Kaiser, D.A., Blanchoin, L., May, R.C., Hall, M.E. and Pollard, T.D. (1999)  WASp-related protein Scar activates dendritic nucleation of actin filaments by Arp2/3 complex. Proc. Nat. Acad Sci. USA 96: 3739-3744.

167.  Mullins, R.D. and Pollard, T.D. (1999)  Rho-family GTPases require Arp2/3 complex to stimulate actin polymerization in Acanthamoeba extracts. Current Biol. 9:405-415.

168.  Blanchoin, L. and Pollard, T.D. (1999)  Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments. J. Biol. Chem. 274:15538-15546.

169.  May, R.C., Hall, M.E., Higgs, H.N., Pollard, T.D., Chakraborty, T., Wehland, J., Machesky, L.M. and Sechi, A.S. (1999)  The Arp2/3 complex is essential for the actin-based motility of Listeria monocytogenes. Current Biol. 9:759-762.

170.  Kaiser, D.A., Vinson, V.K., Murphy, D.B. and Pollard, T.D. (1999) Profilin is predominantly associated with monomeric actin in Acanthamoeba.. J. Cell Science 112:3769-3777.

171. Higgs, H.N., Blanchoin, L. and Pollard, T.D. (1999) Influence of the Wiskott-Aldrich syndrome protein (WASp) C terminus and Arp2/3 complex on actin polymerization. Biochemistry 38:15212-15222.

172.  Lee, W.-L., Ostap, E.M., Zot, H.G. and Pollard, T.D. (1999) Organization and ligand binding properties of the tail of Acanthamoeba myosin-IA:  Identification of an actin binding site in the basic (TH-1) domain. J. Biol. Chem. 274: 35159-15171.

173.  Sept, D., Xu, J., Pollard, T.D. and McCammon, J.A. (1999) Annealing accounts for the length of actin filaments formed by spontaneous polymerization. Biophys. J. 77:2911-2919.

174.  Blanchoin, L., Robinson, R.C., Choe, S. and Pollard, T.D. (2000) Phosphorylation of Acanthamoeba actophorin (ADF/cofilin) blocks interaction with actin without a change in atomic structure. J. Molec. Biol. 295:203-211.

175.  De La Cruz, E.M., Mandinova, A., Steinmetz, M.O., Stoffler, D., Aebi, U. and Pollard, T.D. (2000) Polymerization and structure of nucleotide-free actin filaments. J. Molec. Biol. 295:517-526.

176.  Bezanilla, M. and Pollard, T.D. (2000) Myosin-II tails confer unique functions in S. pombe:  characterization of a novel myosin-II tail. Molec. Biol. Cell 11:79-91.

177.  Bezanilla, M., Wilson, J.M. and Pollard, T.D. (2000)  Fission yeast myosin-II isoforms assemble into contractile rings at distinct times during mitosis. Current Biology 10:397-400.

178.  Blanchoin*, L., Amann*, K. J., Higgs, H.N., Marchand, J.-B., Kaiser, D.A. and Pollard, T.D. (2000) Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASp/Scar proteins. Nature 404:1007-1011. * co-first authors.

179.  Higgs, H. N. and Pollard, T. D. (2000) Activation by Cdc42 and PIP2 of Wiskott-Aldrich Syndrome protein (WASp) stimulates actin nucleation by  Arp2/3 complex. J. Cell Biol. 150: 1311-1320.

180. Blanchoin, L., Pollard, T.D. and Mullins, R.D. (2000) Interactions of actophorin (ADF/cofilin), Arp2/3 complex, capping protein and profilin in the remodeling and disassembly of branched actin filament networks. Current Biology. 10:1273-1282.

181.  Kim, Y.J., Kaiser, D.A., Pollard, T.D. and Ichikawa, Y. (2000) Synthesis of (3R)-carboxy pyrrolidine (a ß-proline analog) and its oligomer. Bioorg. Med. Chem. Lett. 10:2417-2419.

182.  Lee, W.-L., Bezanilla, M. and Pollard, T.D. (2000) Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex and shares functions with WASp. J. Cell Biol. 151:789-800.

183.  Marchand, J.-B., Kaiser, D. A., Pollard, T. D. and Higgs, H. N. (2001) Interaction of WASp/Scar proteins with actin and vertebrate Arp2/3 complex. Nature Cell Biol. 3:76-82.

184.  Amann, K.J. and Pollard, T.D. (2001) The Arp2/3 complex nucleates filament branches from the sides of pre-existing actin filaments. Nature Cell Biol. 3:306-310.

185.  Pollard, T.D. (2001) Genomics, the cytoskeleton and motility. Nature 409:842-843.

186.  Lu, J. and Pollard, T.D. (2001) Profilin binding to poly-L-proline and actin monomers along with ability to catalyze actin nucleotide exchange are required for viability of fission yeast. Molec. Biol. Cell. 12:1161-1175.

187.  Heufner, K., Higgs, H.N., Pollard, T.D., Jacobi, C., Aepfelbacher, M. and Linder, S. (2001) The VC region of Wiskott-Aldrich syndrome protein induces Arp2/3 complex-dependent actin nucleation. J. Biol. Chem. 276:35761-35767.

188.  Volkmann, N., Amann, K.J., Stoilova-McPhie, S., Egile, C., Winter, D.C., Hazelwood, L., Heuser, J.E., Li, R., Pollard, T.D. and Hanein, D. (2001) Structure of Arp2/3 complex in its activated state and in actin filament branch junctions. Science 293:2456-2459.

189.  Blanchoin. L., Pollard, T.D. and Hitchcock-DeGregori, S.E. (2001) Inhibition of Arp2/3 Complex-Nucleated Actin Polymerization and Branch Formation by Tropomyosin. Current Biol. 11:1300-1304.

190.  Andrianantoandro, E., Blanchoin, L., Sept, D., McCammon, J.A. and Pollard, T.D. (2001) Kinetic mechanism of end to end annealing of actin filaments. J. Molec. Biol. 312:721-730.

191.  Robinson*, R.C., Turbedsky*, K., Kaiser, D.A., Higgs, H.N., Marchand, J.-B., Choe, S. and Pollard, T.D. (2001) Crystal structure of Arp2/3 complex. Science 294:1679-1684. * co-first authors.

192.  Amann, K.J. and Pollard, T.D. (2001) Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection microscopy. Proc. Nat. Acad. Sci. (U.S.A.) 98:15009-15013.

193.  Blanchoin, L. and Pollard, T.D. (2002) Hydrolysis of bound ATP by polymerized actin depends on the bound divalent cation but not profilin. Biochemistry 41:597-602.

194.  Okada, K., Blanchoin, L., Abe, H., Chen, H., Pollard, T.D. and Bamburg, J.R. (2002) Xenopus actin interacting protein 1 (XAip1) enhances cofilin fragmentation of filaments by capping filament ends. J. Biol. Chem. 277: 43011-43016

195.  Kong, H.-H. and Pollard, T.D. (2002) Intracellular localization of myosin-II and myosin-IC in live Acanthamoeba by transient transfection of EGFP fusion proteins. J. Cell Sci. 115:4993-5002.

196.  Jahng, A.W., Strang, C., Kaiser, D.A., Pollard, T.D., Pfaffinger, P. and Choe, S. (2003) Zinc mediates assembly of the T1 domain of the voltage-gated K channel 4.2. J. Biol. Chem. 278: 47885- 47890.

197.  Ostap, E.M., Maupin, P., Doberstein, S.K., Baines, I.C., Korn, E.D. and Pollard, T.D. (2003) Dynamic localization of myosin-I to endocytic structures in Acanthamoeba. Cell Motil. Cytoskel. 54:29-40.

198.  Maul,R.S., Song, Y., Amann, K.J., Gerbin, S.C., Pollard, T.D. and Chang, D.D. (2003) EPLIN regulates actin dynamics by crosslinking and stabilizing filaments. J. Cell Biol. 160:399-407.

199.  Kovar, D.R., Kuhn, J.R., Tichy, A. and Pollard, T.D. (2003) The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin. J. Cell Biol. 161:875-887.

200.  Panchal, S.C., Kaiser, D.A., Torres, E., Pollard, T.D. and Rosen, M.K. (2003) A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex. Nature Struct. Biol. 10:591-598.

201.  Wu, J.-Q., Kuhn, J.R., Kovar, D.R. and Pollard, T.D. (2003) Spatial and temporal pathway for assembly and constriction of the contractile ring in fission yeast cytokinesis. Devel. Cell 5:723-734.

202.  Beltzner, C.C. and Pollard, T.D. (2004) Identification of functionally important residues of Arp2/3 complex by analysis of homology models from diverse species. J. Molec. Biol. 336:551-565.

203.  Golemi-Kotra, D., Mahaffy, R., Footer, M.J., Holtzman, J.H., Pollard, T.D., Theriot, J.A. and Schepartz, A. (2004) High affinity, paralog-specific recognition of the Mena EVH1 domain by a miniature protein. J. Amer. Chem. Soc. 126:4-5.

204,  Kovar, D.R. and Pollard, T.D. (2004) Insertional assembly of actin in association with formins produces piconewton forces. Proc. Nat. Acad. Sci. USA 101:14725-14730.

205.    Lord, M. and Pollard, T.D. (2004) UCS protein Rng3 activates actin filament gliding by fission yeast myosin-II. J. Cell Biol. 167:315-325.

206.    Nolen, B., Littlefield, R.S. and Pollard, T.D. (2004) Crystal structures of bovine Arp2/3 complex with bound ATP or ADP. Proc. Nat. Acad. Sci. USA 101:15627-15632.

207.    Turbedsky, K. and Pollard, T.D. (2005) Assembly of Acanthamoeba myosin-II minifilaments. I. Definition of C-terminal residues required to form coiled-coils, dimers and octamers J. Molec. Biol. 345:351-361.

208.    Turbedsky, K., Pollard, T.D. and Yeager, M. (2005) Assembly of Acanthamoeba Myosin-II minifilaments. II. Model of anti-parallel dimers based on EM and X-ray diffraction of 2D and 3D crystals. J. Mol. Biol. 345:363-373.

209.  Kuhn, J.R. and Pollard, T.D. (2005) Analysis of actin filament dynamics by total internal reflection fluorescence microscopy. Biophysical J. 88:1387-1402.

210.  Kovar, D.R., Wu, J.-Q. and Pollard, T.D. (2005) Profilin-mediated competition between capping protein and formin Cdc12p during cytokinesis in fission yeast. Molec. Biol. Cell, 16:2313-2324.

211.  Sirotkin, V., Beltzner, C.C., Marchand, J.B. and Pollard, T.D. (2005) Interactions of WASp, myosin-I, and verprolin with Arp2/3 complex during actin patch assembly in fission yeast. J. Cell Biol. 170:637-648.

212.  Wu, J.-Q. and Pollard, T.D. (2005) Counting cytokinesis proteins globally and locally in fission yeast. Science 310:310-314.

213.  Lord, M., Laves, E. and Pollard, T.D. (2005) Cytokinesis depends on the motor domains of myosin-II in fission yeast but not in budding yeast. Molec. Biol. Cell 16:5346-5355.

214.  Kovar, D.R., Harris, E.S., Mahaffy, R.E. Higgs, H.N. and Pollard, T.D. (2006) Control of the assembly of ATP- and ADP-actin by formins and profilin. Cell 724:423-435.

215.  Vavylonis, D., Kovar, D.R., O'Shaughnessy, B. and Pollard, T.D. (2006) Mathematical model of the assembly of ATP- and ADP-actin by formins and profilin. Molec. Cell 21:455-466.

216.  Haviv, L., Brill-Karniely, Y., Mahaffy, R., Backouche, F., Ben-Shaul, A., Pollard, T.D. and Bernheim-Groswasser, A. (2006) Reconstitution of the transition from lamellipodium to filopodium in a membrane free system. Proc. Nat. Acad. Sci. USA 103:4906-4911.

217.  Moseley, J.B., Okada, K., Balcer, H.I., Kovar, D.R., Pollard, T.D. and Goode, B.L. (2006) Twinfilin is an actin filament severing protein and promotes rapid turnover of actin structures in vivo. J. Cell Sci. 119:1547-1557.

218.  Wu, J.-Q., Sirotkin, V., Kovar, D., Lord, M., Beltzner, C., Kuhn, J.R. and Pollard, T.D.  (2006) Assembly of the cytokinetic contractile ring from a broad band of nodes in fission yeast. J. Cell Biol. 174:391-402.

219.  Andrianantoandro, E. and Pollard, T.D. (2006) Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilins. Molec. Cell 24:13-23.

220.  Mahaffy, R.E. and Pollard, T.D. (2006) Kinetics of the formation and dissociation of actin filament branches  by Arp2/3 complex. Biophys. J. 91, 3519-28.

221.  Kiselar, J.G, Mahaffy, R., Pollard, T.D., Almo, S.C. and Chance, M.R. (2007) Local and global conformational rearrangements of Arp2/3 complex mediated by binding of nucleotides and WASp. Proc. Nat. Acad. Sci. USA. In press.

222.  Ali, M.Y., Krementsova, E.B., Kennedy, G.G., Mahaffy, R., Pollard, T.D., Trybus, K.M. and Warshaw, D.M. (2007) Myosin V maneuvers through actin intersections and diffuses along microtubules. Proc. Nat. Acad. Sci. USA. In press.

Publications - Reviews and Invited Chapters

1.      Pollard, T.D. (1972) Motile cytoplasmic extracts of Amoeba proteus. Acta Protozool. 11:55-58.

2.      Pollard, T.D., Adelstein, R.S. and Korn, E.D. (1972)  Isolation of myosin from Acanthamoeba castellanii and human platelets. Acta Protozool. 11:59-66.

3.      Pollard, T.D. (1973) Progress in understanding amoeboid movement at the molecular level. In: "The Biology of the Amoeba" (K. Jeon, ed.), Academic Press, Inc., New York, pp. 291-317.

4.      Pollard, T.D. and Weihing, R.R. (1974) Actin and myosin and cell movement. CRC Critical Reviews in Biochemistry 2:1-65.

5.      Pollard, T.D. (1975) Functional implications of the biochemical and structural properties of cytoplasmic contractile proteins. In: "Molecules and Cell Movement" (S. Inoue and R.E. Stephens, eds.), Raven Press, New York, pp. 259-269.

6.      Pollard, T.D. (1976) The properties of actin, myosin and associated proteins from nonmuscle cells. In: "Handbook of Biochemistry and Molecular Biology", Proteins II, (G. Fasman, ed.), CRC Press, Cleveland, Ohio; pp. 307-324.

7.      Pollard, T.D., Fujiwara, K., Niederman, R. and Maupin-Szamier, P. (1976) Evidence for the role of cytoplasmic actin and myosin in cellular structure and motility. In: "Cell Motility" (R. Goldman,  T.D. Pollard and J. Rosenbaum, eds.), Cold Spring Harbor Laboratory Press, New York, pp. 689-724.

8.      Pollard, T.D. and Fujiwara, K. (1976) Participation of contractile proteins in cytoplasmic structure and cell division. Current Topics in Intracellular Regulation. In: "Contractile Systems in Non-muscle Tissues", (S.V. Perry, A. Margreth and R.S. Adelstein, eds.), Elsevier/North-Holland Biomedical Press, Amsterdam, pp. 23-28.

9.      Pollard, T.D. (1976) Cytoskeletal functions of cytoplasmic contractile proteins. J. Supramolec. Str. 5:317-334.

10.    Pollard, T.D. (1977) Cytoplasmic contractile proteins. In: "International Cell Biology 1976-1977" (B.R. Brinkley and K.R. Porter, eds.), Rockefeller University Press, New York, pp. 378-387.

11.    Pollard, T.D. and Maupin, P. (1978) Electron microscopy of cytoplasmic contractile proteins. In: "Electron Microscopy", Vol. 3, (G.W. Bailey, ed.), Claitor's Publ. Co. Baton, Rouge, LA, pp. 606-614.

12.    Adelstein, R.S. and Pollard, T.D. (1978) Platelet contractile proteins. In: "Progress in Hemostasis and Thrombosis", (T.H. Spaet, ed.), Grune & Stratton Press, New York, pp. 37-58.

13.    Pollard, T.D. (1978) Contractile proteins and cell surface dynamics. In: "Transport of Macromolecules in Cellular Systems", (S.C. Silverstein, ed.), Dahlem Konferenzen Publications, Berlin, pp. 489-502.

14.    Pollard, T.D. (1979) Cytoplasmic myosin filaments. In: "Motility in Cell Function", (F.A. Pepe, J.W. Sanger and V.T. Nachmias, eds.), Academic Press, Inc., New York, pp. 117-125.

15.    Pollard, T.D. (1980) Platelet contractile proteins. In: "Thrombosis and Haemostasis" 42:1634-1637.

16.    Fujiwara, K. and Pollard, T.D. (1980) Techniques for localizing contractile proteins with fluorescent antibodies. In: "Current Topics in Developmental Biology", Vol. 14, Academic Press, Inc., New York, pp. 271-296.

17.    Pollard, T.D. (1981) Cytoplasmic contractile proteins. In: "Discovery in Cell Biology", J. Cell Biol. 91:156s-165s.

18.    Paranko, J., Pelliniemi, L.J., Dym, M., Fujiwara, K. and Pollard, T.D. (1981) Postnatal development of myosin containing cells in the male rat reproductive tract. In: "International Congress Series No. 559, Development and Function of Reproductive Organs", Proceedings of the Vth Workshop on the Development and Function of the Reproductive Organs, Copenhagen, (A.G. Byskov and H. Peters, eds.), Excerpta Medica, Elsevier North-Holland, Amsterdam, pp. 191-198.

19.    Pollard, T.D. and Craig, S.W. (1982) Mechanism of actin polymerization. Trends in Biochem. Sci. 7:55-58.

20.    Craig, S.W. and Pollard, T.D. (1982) Actin-binding proteins. Trends in Biochem. Sci. 7:88-92.

21.    Pollard, T.D., Aebi, U., Cooper, J.A., Elzinga, M., Fowler, W.E., Griffith, L.M., Herman, I.M., Heuser, J., Isenberg, G., Kiehart, D.P., Levy, J., MacLean-Fletcher, S., Maupin, P., Mooseker, M.S., Runge, M., Smith, P.R. and Tseng, P. (1982)  The mechanism of actin-filament assembly and cross-linking. In: "Cell and Muscle Motility", (R.W. Dowben and J.W. Shay, eds.), Plenum Publ. Corp., New York, 2:15-44.

22.    Pollard, T.D. (1982) A falling ball apparatus to measure filament cross-linking. In: "Methods in Cell Biology", Vol. 24, Academic Press, Inc., New York, pp. 301-311.

23.    Pollard, T.D. (1982) Myosin purification and characterization. In: "Methods in Cell Biology", Vol. 24, Academic Press, Inc., New York, pp. 333-371.

24.    Pollard, T.D., Aebi, U., Cooper, J.A., Fowler, W.E. and Tseng, P. (1982) Actin structure, polymerization and gelation. Cold Spring Harbor Symposia on Quantitative Biology, Vol. 46, Cold Spring Harbor Laboratory Press,  New York, pp. 513-524.

25.    Pollard, T.D., Griffith, L.M. and Herman, I.M. (1982) Actin filament-microtubule interactions. In: "Proceedings of the ICN-UCLA Symposia. Differentiation and Function of Hemapoietic Cell Surfaces", (V.T. Marchesi and R.C. Gallo, eds.), Alan R. Liss, Inc., New York, pp. 183-192.

26.    Pollard, T.D. (1982) Assays for myosin. In: "Methods in Enzymology" (L.W. Cunningham and D.W. Frederiksen, eds.), Vol. 85, Academic Press, Inc., New York, pp. 123-130.

27.    Cooper, J.A. and Pollard, T.D. (1982) Methods to measure actin polymerization. In: "Methods in Enzymology", (L.W. Cunningham and D.W. Frederiksen, eds.), Vol. 85, Academic Press, Inc., New York, pp. 182-210.

28.    Pollard, T.D. and Cooper, J.A. (1982) Methods to characterize actin filament networks. In: "Methods in Enzymology", (L.W. Cunningham and D.W. Frederiksen, eds.), Vol. 85, Academic Press, Inc., New York, pp. 211-233.

29.    Pollard, T.D. (1982) Purification of nonmuscle myosins. In: "Methods in Enzymology, (L.W. Cunningham and D.W. Frederiksen, eds.), Vol. 85, Academic Press, Inc., New York, pp. 331-356.

30.    Pollard, T.D., Aebi, U., Cooper, J.A., Fowler, W.E., Kiehart, D.P., Smith, P.R. and Tseng, P.C.-H. (1982) Actin and myosin function in Acanthamoeba. Phil. Trans. Royal Soc. London B 299:237-245.