Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving transferase
Reexamination Certificate
2007-05-08
2007-05-08
Gitomer, Ralph (Department: 1657)
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
Involving transferase
C435S019000, C435S021000, C424S548000
Reexamination Certificate
active
11102237
ABSTRACT:
The present invention provides high throughput screening methods for characterizing compounds that modulate the biological activity of a biochemically functional sarcomere. Compounds characterized by such methods are useful for treating congestive heart failure.
REFERENCES:
patent: 5439883 (1995-08-01), Karsanov et al.
patent: 6194632 (2001-02-01), Leiden
patent: 6410254 (2002-06-01), Finer et al.
patent: 6440684 (2002-08-01), Beraud et al.
patent: 6495337 (2002-12-01), Hartman et al.
patent: 6509167 (2003-01-01), Hartman et al.
patent: 6573061 (2003-06-01), Hartman et al.
patent: 6759240 (2004-07-01), Hartman et al.
patent: 6762043 (2004-07-01), Beraud
patent: 2002/0022716 (2002-02-01), Hartman et al.
patent: 2003/0203835 (2003-10-01), Hartman et al.
patent: 2005/0148638 (2005-07-01), Malik et al.
patent: 2006/0014761 (2006-01-01), Morgan et al.
patent: WO 01/02598 (2001-01-01), None
Brenner, B.; Thin Filament Activation Probed by Fluorescence . . . ; Biophysical Journal; 77(5)2677-91; Nov. 1999.
Cooper, J.A., et al.; Methods to Measure Actin Polymerization; Methods Enzymol; 1982; pp. 182-210; vol. 85, Pt. B.
De La Cruz, E., et al.; Transient kinetic analysis of rhodamine phalloidin binding to actin filaments; Biochemistry; Dec. 6, 1994; pp. 14387-14392; vol. 33, No. 48.
Ebashi, S.; A New Simple Method of Preparing Actin from Chicken Gizzard; J. Biochem; 97(2)693-695; 1985.
Finer, J.T., et al.; Characterization of single actin-myosin interactions; Biophys J; Apr. 1995; pp. 291S-296S; vol. 68, No. 4 Suppl.
Friedman, A.L., et al.; Kinetic characterization of myosin head fragments with long-lived myosin ATP states; Biochemistry; Jul. 7, 1998; pp. 9679-9687; vol. 37, No. 27.
Giese, K.C., et al.; Phenotypically selected mutations in myosin's actin binding domain demonstrate intermolecular contacts important for motor function; Jul. 15, 1997; pp. 8465-8473; vol. 36, No. 28.
Gonsior, S.; A Six Module Human Nebulin Fragment Bundles Actin Filaments and Induces Actin Polymerization; J of Muscle Res and Cell Motility; 19(3)225-235; 1998.
Goodson, H.V., et al.; Specialized conservation of surface loops of myosin: evidence that loops are involved in determining functional characteristics; Mol Biol; Mar. 19, 1999; pp. 173-185; vol. 287, No. 1.
Kiehart, D.P., et al.; Inhibition of acanthamoeba actomyosin-II ATPase activity and mechanochemical function by specific monoclonal antibodies; J Cell Biol; Sep. 1984; pp. 1024-1033; vol. 99, No. 3.
Kobayashi, R.; Purification and Characterization of Tropomyosin from Bovine Thyroid; Biochimica et Biophysica Acta; 702(2)220-232; 1982.
Kron, S.J., et al.; Assays for actin sliding movement over myosin-coated surfaces; Methods Enzymol; 1991; pp. 399-416; vol. 196.
Kron, S.J., et al.; Fluorescent actin filaments move on myosin fixed to a glass surface; Proc Natl Acad Sci USA; Sep. 1986; pp. 6272-6276; vol. 83, No. 17.
Murphy, C.T., et al.; Dictyostelium myosin 27-50K loop substitutions specifically affect ADP release rates; Biochemistry; May 12, 1998; pp. 6738-6744; vol. 37, No. 19.
Murphy, C.T., et al.; The sequence of the myosin 50-20K loop affects Myosin's affinity for actin throughout the actin-myosin ATPase cycle and its maximum ATPase activity; Biochemistry; Mar. 23, 1999; pp. 3785-3792; vol. 38, No. 12.
Pardee, J.D., et al.; Purification of muscle actin; Methods Cell Biol; 1982; pp. 271-289; vol. 24.
Pardee, J.D., et al.; Purification of muscle actin; Methods Enzymol; 1982; pp. 164-181; vol. 85, Pt. B.
Pollard, T.D.; Assays for Myosin; Methods Enzymol.; 1982; pp. 123-130; vol. 85, Pt. B.
Pollard, T.D., et al.; Methods to Characterize Actin Filament Networks; Methods Enzymol; 1982; pp. 211-233; vol. 85, Pt. B.
Pollard, T.D.; Purification of Nonmuscle Myosins; Methods Enzymol.; 1982; pp. 331-356; vol. 85, Pt. B.
Pollard, T.D., et al.; The Rate Constant for ATP Hydrolysis by Polymerized Actin; FEBS Lett; May 7, 1984; pp. 94-98; vol. 170, No. 1.
Rock, R.S., et al.; In vitro assays of processive myosin motors; Methods; Dec. 2000; pp. 373-381; vol. 22.
Ruppel, K.M., et al.; Structure-function analysis of the motor domain of myosin; Annu Rev Cell Dev Biol; 1996; pp. 543-573; vol. 12.
Sanger, J.; Use of Fluorescent Probes to Study Myofibrillogenesis; Cellular and Molecular Biology; 93:221-235, 1988.
Sheetz, M.P., et al.; ATP-dependent movement of myosin in vitro: characterization of a quantitative assay; J Cell Biol; Nov. 1984; pp. 1867-1871; vol. 99, No. 5.
Sheetz, M.P., et al.; Myosin movement in vitro: a quantitative assay using oriented actin cables from Nitella; Methods Enzymol; 1986; pp. 531-544; vol. 134.
Spudich, J.A., et al.; Movement of myosin-coated beads on oriented filaments reconstituted from purified actin; Nature; Jun. 13-19, 1985; pp. 584-586; vol. 315, No. 6020.
Toyoshima, Y.Y., et al.; The myosin step size: measurement of the unit displacement per ATP hydrolyzed in an in vitro assay; Proc Natl Acad Sci USA; Sep. 1990; pp. 7130-7134; vol. 87, No. 18.
Toyoshima, Y.Y., et al.; Myosin subfragment-1 is sufficient to move actin filaments in vitro; Nature; Aug. 6-12, 1987; pp. 536-539; vol. 328, No. 6130.
Uyeda, T.Q., et al.; Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin; Nature; Apr. 7, 1994; pp. 567-569; vol. 368, No. 6471.
Warrick, H.M., et al.; In vitro methods for measuring force and velocity of the actin-myosin interaction using purified proteins; Methods Cell Biol; 1993; pp. 1-21; vol. 39.
Xu, J., et al.; Mechanical properties of actin filament networks depend on preparation, polymerization conditions, and storage of actin monomers; Biophys J; May 1998; pp. 2731-2740; vol. 74, No. 5.
Office Action of Oct. 7, 2004 (including Form 892) in abandoned U.S. Appl. No. 10/417,470.
Finer Jeffrey T.
Hartman James J.
Malik Fady
Sakowicz Roman
Cytokinetics Inc.
Gitomer Ralph
Townsend and Townsend / and Crew LLP
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