Full Text
The Full Text of this article is available as a PDF (2.7 MB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- AEvarsson A., Brazhnikov E., Garber M., Zheltonosova J., Chirgadze Y., al-Karadaghi S., Svensson L. A., Liljas A. Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus. EMBO J. 1994 Aug 15;13(16):3669–3677. doi: 10.1002/j.1460-2075.1994.tb06676.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Amor J. C., Harrison D. H., Kahn R. A., Ringe D. Structure of the human ADP-ribosylation factor 1 complexed with GDP. Nature. 1994 Dec 15;372(6507):704–708. doi: 10.1038/372704a0. [DOI] [PubMed] [Google Scholar]
- Berliner E., Young E. C., Anderson K., Mahtani H. K., Gelles J. Failure of a single-headed kinesin to track parallel to microtubule protofilaments. Nature. 1995 Feb 23;373(6516):718–721. doi: 10.1038/373718a0. [DOI] [PubMed] [Google Scholar]
- Berstein G., Blank J. L., Jhon D. Y., Exton J. H., Rhee S. G., Ross E. M. Phospholipase C-beta 1 is a GTPase-activating protein for Gq/11, its physiologic regulator. Cell. 1992 Aug 7;70(3):411–418. doi: 10.1016/0092-8674(92)90165-9. [DOI] [PubMed] [Google Scholar]
- Block S. M., Goldstein L. S., Schnapp B. J. Bead movement by single kinesin molecules studied with optical tweezers. Nature. 1990 Nov 22;348(6299):348–352. doi: 10.1038/348348a0. [DOI] [PubMed] [Google Scholar]
- Bourne H. R., Sanders D. A., McCormick F. The GTPase superfamily: a conserved switch for diverse cell functions. Nature. 1990 Nov 8;348(6297):125–132. doi: 10.1038/348125a0. [DOI] [PubMed] [Google Scholar]
- Bourne H. R., Sanders D. A., McCormick F. The GTPase superfamily: conserved structure and molecular mechanism. Nature. 1991 Jan 10;349(6305):117–127. doi: 10.1038/349117a0. [DOI] [PubMed] [Google Scholar]
- Brownbridge G. G., Lowe P. N., Moore K. J., Skinner R. H., Webb M. R. Interaction of GTPase activating proteins (GAPs) with p21ras measured by a novel fluorescence anisotropy method. Essential role of Arg-903 of GAP in activation of GTP hydrolysis on p21ras. J Biol Chem. 1993 May 25;268(15):10914–10919. [PubMed] [Google Scholar]
- Coleman D. E., Berghuis A. M., Lee E., Linder M. E., Gilman A. G., Sprang S. R. Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis. Science. 1994 Sep 2;265(5177):1405–1412. doi: 10.1126/science.8073283. [DOI] [PubMed] [Google Scholar]
- Coppin C. M., Finer J. T., Spudich J. A., Vale R. D. Detection of sub-8-nm movements of kinesin by high-resolution optical-trap microscopy. Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):1913–1917. doi: 10.1073/pnas.93.5.1913. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Czworkowski J., Wang J., Steitz T. A., Moore P. B. The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution. EMBO J. 1994 Aug 15;13(16):3661–3668. doi: 10.1002/j.1460-2075.1994.tb06675.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dantzig J. A., Hibberd M. G., Trentham D. R., Goldman Y. E. Cross-bridge kinetics in the presence of MgADP investigated by photolysis of caged ATP in rabbit psoas muscle fibres. J Physiol. 1991 Jan;432:639–680. doi: 10.1113/jphysiol.1991.sp018405. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Eisenberg E., Hill T. L. Muscle contraction and free energy transduction in biological systems. Science. 1985 Mar 1;227(4690):999–1006. doi: 10.1126/science.3156404. [DOI] [PubMed] [Google Scholar]
- Finer J. T., Simmons R. M., Spudich J. A. Single myosin molecule mechanics: piconewton forces and nanometre steps. Nature. 1994 Mar 10;368(6467):113–119. doi: 10.1038/368113a0. [DOI] [PubMed] [Google Scholar]
- Fisher A. J., Smith C. A., Thoden J. B., Smith R., Sutoh K., Holden H. M., Rayment I. X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-. Biochemistry. 1995 Jul 18;34(28):8960–8972. doi: 10.1021/bi00028a004. [DOI] [PubMed] [Google Scholar]
- Funatsu T., Harada Y., Tokunaga M., Saito K., Yanagida T. Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution. Nature. 1995 Apr 6;374(6522):555–559. doi: 10.1038/374555a0. [DOI] [PubMed] [Google Scholar]
- Gilbert S. P., Webb M. R., Brune M., Johnson K. A. Pathway of processive ATP hydrolysis by kinesin. Nature. 1995 Feb 23;373(6516):671–676. doi: 10.1038/373671a0. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Goldstein L. S. With apologies to scheherazade: tails of 1001 kinesin motors. Annu Rev Genet. 1993;27:319–351. doi: 10.1146/annurev.ge.27.120193.001535. [DOI] [PubMed] [Google Scholar]
- Hackney D. D. Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis. Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):6865–6869. doi: 10.1073/pnas.91.15.6865. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hackney D. D. Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains. Nature. 1995 Oct 5;377(6548):448–450. doi: 10.1038/377448a0. [DOI] [PubMed] [Google Scholar]
- Hackney D. D. The kinetic cycles of myosin, kinesin, and dynein. Annu Rev Physiol. 1996;58:731–750. doi: 10.1146/annurev.ph.58.030196.003503. [DOI] [PubMed] [Google Scholar]
- Harrington W. F. A mechanochemical mechanism for muscle contraction. Proc Natl Acad Sci U S A. 1971 Mar;68(3):685–689. doi: 10.1073/pnas.68.3.685. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hinshaw J. E., Schmid S. L. Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding. Nature. 1995 Mar 9;374(6518):190–192. doi: 10.1038/374190a0. [DOI] [PubMed] [Google Scholar]
- Hoenger A., Sablin E. P., Vale R. D., Fletterick R. J., Milligan R. A. Three-dimensional structure of a tubulin-motor-protein complex. Nature. 1995 Jul 20;376(6537):271–274. doi: 10.1038/376271a0. [DOI] [PubMed] [Google Scholar]
- Howard J., Hudspeth A. J., Vale R. D. Movement of microtubules by single kinesin molecules. Nature. 1989 Nov 9;342(6246):154–158. doi: 10.1038/342154a0. [DOI] [PubMed] [Google Scholar]
- Howard J. The movement of kinesin along microtubules. Annu Rev Physiol. 1996;58:703–729. doi: 10.1146/annurev.ph.58.030196.003415. [DOI] [PubMed] [Google Scholar]
- Huxley A. F., Simmons R. M. Proposed mechanism of force generation in striated muscle. Nature. 1971 Oct 22;233(5321):533–538. doi: 10.1038/233533a0. [DOI] [PubMed] [Google Scholar]
- Ishijima A., Harada Y., Kojima H., Funatsu T., Higuchi H., Yanagida T. Single-molecule analysis of the actomyosin motor using nano-manipulation. Biochem Biophys Res Commun. 1994 Mar 15;199(2):1057–1063. doi: 10.1006/bbrc.1994.1336. [DOI] [PubMed] [Google Scholar]
- Jacquet E., Baouz S., Parmeggiani A. Characterization of mammalian C-CDC25Mm exchange factor and kinetic properties of the exchange reaction intermediate p21.C-CDC25Mm. Biochemistry. 1995 Sep 26;34(38):12347–12354. doi: 10.1021/bi00038a031. [DOI] [PubMed] [Google Scholar]
- John J., Rensland H., Schlichting I., Vetter I., Borasio G. D., Goody R. S., Wittinghofer A. Kinetic and structural analysis of the Mg(2+)-binding site of the guanine nucleotide-binding protein p21H-ras. J Biol Chem. 1993 Jan 15;268(2):923–929. [PubMed] [Google Scholar]
- Jontes J. D., Wilson-Kubalek E. M., Milligan R. A. A 32 degree tail swing in brush border myosin I on ADP release. Nature. 1995 Dec 14;378(6558):751–753. doi: 10.1038/378751a0. [DOI] [PubMed] [Google Scholar]
- Kawashima T., Berthet-Colominas C., Wulff M., Cusack S., Leberman R. The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution. Nature. 1996 Feb 8;379(6565):511–518. doi: 10.1038/379511a0. [DOI] [PubMed] [Google Scholar]
- Kjeldgaard M., Nyborg J. Refined structure of elongation factor EF-Tu from Escherichia coli. J Mol Biol. 1992 Feb 5;223(3):721–742. doi: 10.1016/0022-2836(92)90986-t. [DOI] [PubMed] [Google Scholar]
- Kull F. J., Sablin E. P., Lau R., Fletterick R. J., Vale R. D. Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. Nature. 1996 Apr 11;380(6574):550–555. doi: 10.1038/380550a0. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lambright D. G., Noel J. P., Hamm H. E., Sigler P. B. Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein. Nature. 1994 Jun 23;369(6482):621–628. doi: 10.1038/369621a0. [DOI] [PubMed] [Google Scholar]
- Lambright D. G., Sondek J., Bohm A., Skiba N. P., Hamm H. E., Sigler P. B. The 2.0 A crystal structure of a heterotrimeric G protein. Nature. 1996 Jan 25;379(6563):311–319. doi: 10.1038/379311a0. [DOI] [PubMed] [Google Scholar]
- Lee E., Taussig R., Gilman A. G. The G226A mutant of Gs alpha highlights the requirement for dissociation of G protein subunits. J Biol Chem. 1992 Jan 15;267(2):1212–1218. [PubMed] [Google Scholar]
- Ma Y. Z., Taylor E. W. Kinetic mechanism of kinesin motor domain. Biochemistry. 1995 Oct 10;34(40):13233–13241. doi: 10.1021/bi00040a039. [DOI] [PubMed] [Google Scholar]
- Ma Y. Z., Taylor E. W. Mechanism of microtubule kinesin ATPase. Biochemistry. 1995 Oct 10;34(40):13242–13251. doi: 10.1021/bi00040a040. [DOI] [PubMed] [Google Scholar]
- McDonald H. B., Stewart R. J., Goldstein L. S. The kinesin-like ncd protein of Drosophila is a minus end-directed microtubule motor. Cell. 1990 Dec 21;63(6):1159–1165. doi: 10.1016/0092-8674(90)90412-8. [DOI] [PubMed] [Google Scholar]
- Meyhöfer E., Howard J. The force generated by a single kinesin molecule against an elastic load. Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):574–578. doi: 10.1073/pnas.92.2.574. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Milburn M. V., Tong L., deVos A. M., Brünger A., Yamaizumi Z., Nishimura S., Kim S. H. Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins. Science. 1990 Feb 23;247(4945):939–945. doi: 10.1126/science.2406906. [DOI] [PubMed] [Google Scholar]
- Miller R. T., Masters S. B., Sullivan K. A., Beiderman B., Bourne H. R. A mutation that prevents GTP-dependent activation of the alpha chain of Gs. Nature. 1988 Aug 25;334(6184):712–715. doi: 10.1038/334712a0. [DOI] [PubMed] [Google Scholar]
- Mixon M. B., Lee E., Coleman D. E., Berghuis A. M., Gilman A. G., Sprang S. R. Tertiary and quaternary structural changes in Gi alpha 1 induced by GTP hydrolysis. Science. 1995 Nov 10;270(5238):954–960. doi: 10.1126/science.270.5238.954. [DOI] [PubMed] [Google Scholar]
- Molloy J. E., Burns J. E., Kendrick-Jones J., Tregear R. T., White D. C. Movement and force produced by a single myosin head. Nature. 1995 Nov 9;378(6553):209–212. doi: 10.1038/378209a0. [DOI] [PubMed] [Google Scholar]
- Mooseker M. S., Cheney R. E. Unconventional myosins. Annu Rev Cell Dev Biol. 1995;11:633–675. doi: 10.1146/annurev.cb.11.110195.003221. [DOI] [PubMed] [Google Scholar]
- Nassar N., Horn G., Herrmann C., Scherer A., McCormick F., Wittinghofer A. The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. Nature. 1995 Jun 15;375(6532):554–560. doi: 10.1038/375554a0. [DOI] [PubMed] [Google Scholar]
- Neal S. E., Eccleston J. F., Hall A., Webb M. R. Kinetic analysis of the hydrolysis of GTP by p21N-ras. The basal GTPase mechanism. J Biol Chem. 1988 Dec 25;263(36):19718–19722. [PubMed] [Google Scholar]
- Nixon A. E., Brune M., Lowe P. N., Webb M. R. Kinetics of inorganic phosphate release during the interaction of p21ras with the GTPase-activating proteins, p120-GAP and neurofibromin. Biochemistry. 1995 Nov 28;34(47):15592–15598. doi: 10.1021/bi00047a026. [DOI] [PubMed] [Google Scholar]
- Noel J. P., Hamm H. E., Sigler P. B. The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S. Nature. 1993 Dec 16;366(6456):654–663. doi: 10.1038/366654a0. [DOI] [PubMed] [Google Scholar]
- Pai E. F., Kabsch W., Krengel U., Holmes K. C., John J., Wittinghofer A. Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation. Nature. 1989 Sep 21;341(6239):209–214. doi: 10.1038/341209a0. [DOI] [PubMed] [Google Scholar]
- Pai E. F., Krengel U., Petsko G. A., Goody R. S., Kabsch W., Wittinghofer A. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 1990 Aug;9(8):2351–2359. doi: 10.1002/j.1460-2075.1990.tb07409.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Patterson B., Spudich J. A. Cold-sensitive mutations of Dictyostelium myosin heavy chain highlight functional domains of the myosin motor. Genetics. 1996 Jun;143(2):801–810. doi: 10.1093/genetics/143.2.801. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Peskin C. S., Oster G. Coordinated hydrolysis explains the mechanical behavior of kinesin. Biophys J. 1995 Apr;68(4 Suppl):202S–211S. [PMC free article] [PubMed] [Google Scholar]
- Rayment I., Holden H. M., Whittaker M., Yohn C. B., Lorenz M., Holmes K. C., Milligan R. A. Structure of the actin-myosin complex and its implications for muscle contraction. Science. 1993 Jul 2;261(5117):58–65. doi: 10.1126/science.8316858. [DOI] [PubMed] [Google Scholar]
- Rayment I., Rypniewski W. R., Schmidt-Bäse K., Smith R., Tomchick D. R., Benning M. M., Winkelmann D. A., Wesenberg G., Holden H. M. Three-dimensional structure of myosin subfragment-1: a molecular motor. Science. 1993 Jul 2;261(5117):50–58. doi: 10.1126/science.8316857. [DOI] [PubMed] [Google Scholar]
- Rickard J. E., Kreis T. E. CLIPs for organelle-microtubule interactions. Trends Cell Biol. 1996 May;6(5):178–183. doi: 10.1016/0962-8924(96)10017-9. [DOI] [PubMed] [Google Scholar]
- Sablin E. P., Kull F. J., Cooke R., Vale R. D., Fletterick R. J. Crystal structure of the motor domain of the kinesin-related motor ncd. Nature. 1996 Apr 11;380(6574):555–559. doi: 10.1038/380555a0. [DOI] [PubMed] [Google Scholar]
- Scheffzek K., Klebe C., Fritz-Wolf K., Kabsch W., Wittinghofer A. Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form. Nature. 1995 Mar 23;374(6520):378–381. doi: 10.1038/374378a0. [DOI] [PubMed] [Google Scholar]
- Schweins T., Langen R., Warshel A. Why have mutagenesis studies not located the general base in ras p21. Nat Struct Biol. 1994 Jul;1(7):476–484. doi: 10.1038/nsb0794-476. [DOI] [PubMed] [Google Scholar]
- Shimizu T., Sablin E., Vale R. D., Fletterick R., Pechatnikova E., Taylor E. W. Expression, purification, ATPase properties, and microtubule-binding properties of the ncd motor domain. Biochemistry. 1995 Oct 10;34(40):13259–13266. doi: 10.1021/bi00040a042. [DOI] [PubMed] [Google Scholar]
- Smith C. A., Rayment I. Active site comparisons highlight structural similarities between myosin and other P-loop proteins. Biophys J. 1996 Apr;70(4):1590–1602. doi: 10.1016/S0006-3495(96)79745-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Smith C. A., Rayment I. X-ray structure of the magnesium(II)-pyrophosphate complex of the truncated head of Dictyostelium discoideum myosin to 2.7 A resolution. Biochemistry. 1995 Jul 18;34(28):8973–8981. doi: 10.1021/bi00028a005. [DOI] [PubMed] [Google Scholar]
- Smith C. A., Rayment I. X-ray structure of the magnesium(II).ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 A resolution. Biochemistry. 1996 Apr 30;35(17):5404–5417. doi: 10.1021/bi952633+. [DOI] [PubMed] [Google Scholar]
- Sondek J., Lambright D. G., Noel J. P., Hamm H. E., Sigler P. B. GTPase mechanism of Gproteins from the 1.7-A crystal structure of transducin alpha-GDP-AIF-4. Nature. 1994 Nov 17;372(6503):276–279. doi: 10.1038/372276a0. [DOI] [PubMed] [Google Scholar]
- Sprinzl M. Elongation factor Tu: a regulatory GTPase with an integrated effector. Trends Biochem Sci. 1994 Jun;19(6):245–250. doi: 10.1016/0968-0004(94)90149-x. [DOI] [PubMed] [Google Scholar]
- Spudich J. A. How molecular motors work. Nature. 1994 Dec 8;372(6506):515–518. doi: 10.1038/372515a0. [DOI] [PubMed] [Google Scholar]
- Stewart R. J., Thaler J. P., Goldstein L. S. Direction of microtubule movement is an intrinsic property of the motor domains of kinesin heavy chain and Drosophila ncd protein. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5209–5213. doi: 10.1073/pnas.90.11.5209. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Story R. M., Steitz T. A. Structure of the recA protein-ADP complex. Nature. 1992 Jan 23;355(6358):374–376. doi: 10.1038/355374a0. [DOI] [PubMed] [Google Scholar]
- Sung Y. J., Carter M., Zhong J. M., Hwang Y. W. Mutagenesis of the H-ras p21 at glycine-60 residue disrupts GTP-induced conformational change. Biochemistry. 1995 Mar 14;34(10):3470–3477. doi: 10.1021/bi00010a040. [DOI] [PubMed] [Google Scholar]
- Svoboda K., Schmidt C. F., Schnapp B. J., Block S. M. Direct observation of kinesin stepping by optical trapping interferometry. Nature. 1993 Oct 21;365(6448):721–727. doi: 10.1038/365721a0. [DOI] [PubMed] [Google Scholar]
- Sweeney H. L., Holzbaur E. L. Mutational analysis of motor proteins. Annu Rev Physiol. 1996;58:751–792. doi: 10.1146/annurev.ph.58.030196.003535. [DOI] [PubMed] [Google Scholar]
- Takei K., McPherson P. S., Schmid S. L., De Camilli P. Tubular membrane invaginations coated by dynamin rings are induced by GTP-gamma S in nerve terminals. Nature. 1995 Mar 9;374(6518):186–190. doi: 10.1038/374186a0. [DOI] [PubMed] [Google Scholar]
- Thompson R. C., Dix D. B., Karim A. M. The reaction of ribosomes with elongation factor Tu.GTP complexes. Aminoacyl-tRNA-independent reactions in the elongation cycle determine the accuracy of protein synthesis. J Biol Chem. 1986 Apr 15;261(11):4868–4874. [PubMed] [Google Scholar]
- Tong L. A., de Vos A. M., Milburn M. V., Kim S. H. Crystal structures at 2.2 A resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP. J Mol Biol. 1991 Feb 5;217(3):503–516. doi: 10.1016/0022-2836(91)90753-s. [DOI] [PubMed] [Google Scholar]
- Uyeda T. Q., Abramson P. D., Spudich J. A. The neck region of the myosin motor domain acts as a lever arm to generate movement. Proc Natl Acad Sci U S A. 1996 Apr 30;93(9):4459–4464. doi: 10.1073/pnas.93.9.4459. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Uyeda T. Q., Ruppel K. M., Spudich J. A. Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin. Nature. 1994 Apr 7;368(6471):567–569. doi: 10.1038/368567a0. [DOI] [PubMed] [Google Scholar]
- Vale R. D., Funatsu T., Pierce D. W., Romberg L., Harada Y., Yanagida T. Direct observation of single kinesin molecules moving along microtubules. Nature. 1996 Apr 4;380(6573):451–453. doi: 10.1038/380451a0. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Walker J. E., Saraste M., Runswick M. J., Gay N. J. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1982;1(8):945–951. doi: 10.1002/j.1460-2075.1982.tb01276.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Walker R. A., Salmon E. D., Endow S. A. The Drosophila claret segregation protein is a minus-end directed motor molecule. Nature. 1990 Oct 25;347(6295):780–782. doi: 10.1038/347780a0. [DOI] [PubMed] [Google Scholar]
- Wall M. A., Coleman D. E., Lee E., Iñiguez-Lluhi J. A., Posner B. A., Gilman A. G., Sprang S. R. The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2. Cell. 1995 Dec 15;83(6):1047–1058. doi: 10.1016/0092-8674(95)90220-1. [DOI] [PubMed] [Google Scholar]
- Webb M. R. The role of nucleoside triphosphate hydrolysis in transducing systems: p21ras and muscle. Philos Trans R Soc Lond B Biol Sci. 1992 Apr 29;336(1276):19–24. doi: 10.1098/rstb.1992.0039. [DOI] [PubMed] [Google Scholar]
- Wells J. A., Yount R. G. Active site trapping of nucleotides by crosslinking two sulfhydryls in myosin subfragment 1. Proc Natl Acad Sci U S A. 1979 Oct;76(10):4966–4970. doi: 10.1073/pnas.76.10.4966. [DOI] [PMC free article] [PubMed] [Google Scholar]
- White H. D., Taylor E. W. Energetics and mechanism of actomyosin adenosine triphosphatase. Biochemistry. 1976 Dec 28;15(26):5818–5826. doi: 10.1021/bi00671a020. [DOI] [PubMed] [Google Scholar]
- Whittaker M., Wilson-Kubalek E. M., Smith J. E., Faust L., Milligan R. A., Sweeney H. L. A 35-A movement of smooth muscle myosin on ADP release. Nature. 1995 Dec 14;378(6558):748–751. doi: 10.1038/378748a0. [DOI] [PubMed] [Google Scholar]
- Yang J. T., Saxton W. M., Stewart R. J., Raff E. C., Goldstein L. S. Evidence that the head of kinesin is sufficient for force generation and motility in vitro. Science. 1990 Jul 6;249(4964):42–47. doi: 10.1126/science.2142332. [DOI] [PubMed] [Google Scholar]