Contact Information
Primary Office: 1-324 Bowen Science Building
51 Newton Road
Iowa City, IA 52242
319-335-8101
Education
BA, Science, University of Tokyo, Tokyo, Japan
Physiology Course, Marine Biological Laboratory
PhD, Biology, Princeton University
Postdoctoral Fellow, Columbia University
Education/Training Program Affiliations
Department of Cell and Developmental Graduate ProgramResearch Summary
Molecular mechanisms of contraction in striated muscles, and the mechanisms of hypertrophic and dilated cardiomyopathy (HCM, DCM).
To study the molecular mechanisms of contraction, it is essential that force can be measured, hence “skinned” single muscle fibers are used, in which the plasma membrane is chemically removed. To learn the function of individual amino acid residues in a contractile protein, it is necessary to replace it with a recombinant protein. We developed a system, in which the thin filament of cardiac fibers is selectively removed by gelsolin, and reconstituted by actin monomers, followed by regulatory proteins tropomyosin (Tpm) and troponin (Tn). Because this procedure does not require any adverse conditions (extreme ionic strength, pH, temperature, etc), the reproducibility of active tension is 104±3%; similarly, the reproducibility of other contractile parameters are excellent. This technique has numerous applications. One can study the actin-myosin interaction without Tpm/Tn; we found that Tpm/Tn increases force/cross-bridge by 50% indicating that the actin-Tpm interaction allosterically activates the actin-myosin interaction. This technique has also been used to study mutant proteins to establish the structure-function relationships. It was further used to learn molecular pathogenesis based on thin filament proteins (actin, Tpm, Tn) that are known to cause HCM and DCM in humans. The technique makes it possible to obtain information on early events of pathogenesis, ie, before complex signaling cascades ensue. In Tpm mutations that cause HCM, we found that tension at pCa 8 increases from 10% (WT) to 30% to cause diastolic problem, whereas in Tpm mutations that cause DCM, tension at pCa 8 and pCa 4.5 both decrease to cause systolic problem.
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Publications
Wang, L., Bai, F., Zhang, Q., Song, W., Messer, A. & Kawai, M. (2018). Development of apical hypertrophic cardiomyopathy with age in a transgenic mouse model carrying the cardiac actin E99K mutation. Journal of Muscle Research and Cell Motility, [Epub ahead of print]. PMID: 29582353.
Ishii, S., Kawai, M., Ishiwata, S. & Suzuki, M. (2018). Estimation of actomyosin active force maintained by tropomyosin and troponin complex under vertical forces in the in vitro motility assay system. PLoS One(eCollection 2018), 13(2), e0192558. PMID: 29420610.
Kawai, M. (2018). Biomechanics, Muscle Fibers, and How to Interface Experimental Apparatus to a Computer. Cham: Springer International Publishing AG. DOI: https://doi.org/10.1007/978-3-319-72036-4.
Kawai, M., Lamb, G. & Galler, S. (2015). Editorial on EMC 2014 special issue. (Vols. 36). (1), pp. 1-3. J Muscle Res Cell Motil. PMID: 25452123.
Bai, F., Caster, H. H., Dawson, J. F. & Kawai, M. (2015). The immediate effect of HCM causing actin mutants E99K and A230V on actin-Tm-myosin interaction in thin-filament reconstituted myocardium. (Vols. 79). pp. 123-132. J Mol Cell Cardiol. PMID: 25451174.
Wang, L., Bahadir, A. & Kawai, M. (2015). High ionic strength depresses muscle contractility by decreasing both force per cross-bridge and the number of strongly attached cross-bridges. (Vols. 36). (3), pp. 227-241. J Muscle Res Cell Motil. PMID: 25836331.
Wang, L., Sadayappan, S. & Kawai, M. (2014). Cardiac Myosin Binding Protein C Phosphorylation Affects Cross-bridge Cycle’s Elementary Steps in a Site-specific Manner. (Vols. 9). (11), pp. e113417. PLos One. PMID: 25420047.
Wang, L., Ji, X., Barefield, D., Sadayappan, S. & Kawai, M. (2014). Phosphorylation of cMyBP-C affects contractile mechanisms in a site specific manner. (Vols. 106). pp. 1112-1122. Biophys J.
Bai, F., Caster, H. M., Rubenstein, P. A., Dawson, J. F. & Kawai, M. (2014). Using baculovirus/insect cell expressed recombinant actin to study the molecular pathogenesis of HCM caused by actin mutation A331P. (Vols. 74). pp. 64-75. J Mol Cell Cardiol.
Wang, L., Muthu, P., Szczesna-Cordary, D. & Kawai, M. (2013). Diversity and similarity of motor function and cross-bridge kinetics in papillary muscles of transgenic mice carrying myosin regulatory light chain mutations D166V and R58Q. (Vols. 62). (153-163) J Molec Cell Cardiol. PMID: http://dx.doi.org/10.1016.
Bai, F., Caster, H. M., Pinto, J. R. & Kawai, M. (2013). Analysis of the molecular pathogenesis of cardiomyopathy-causing cTnT mutants I79N, ?E96, and ?K210. (Vols. 104). (9), pp. 1979-1988. Bethesda, MD: Biophys J.
Wang, L., Muthu, P. P., Szczesna-Cordary, D. & Kawai, M. (2013). Characterizations of myosin essential light chain's N-terminal truncation mutant ?43 in transgenic mouse papillary muscles by using tension transients in response to sinusoidal length alterations. (Vols. 34). (9), pp. 93-105. J Muscle Res Cell Motil. PMID: http://dx.doi.org/10.1007/s10974-013-9337.
Bai, F., Wang, L. & Kawai, M. (2013). A study of tropomyosin’s role in cardiac function and disease using thin-filament reconstituted myocardium. (Vols. 34). pp. 295-310. London, UK: J Muscle Res Cell Motil. PMID: http://dx.doi.org/10.1007/s10974-013-9343.
Wang, L., Kawai, M. (2013). A re-interpretation of the rate of tension redevelopment (kTR) in active muscle. (Vols. 34). pp. 407-415. J Muscle Res Cell Motil. PMID: http://dx.doi.org/10.1007/s10974-013-9366-5.
Iorga, B., Wang, L., Stehle, R., Pfitzer, G. & Kawai, M. (2012). ATP binding and cross-bridge detachment steps during full Ca2+ activation: Comparison of myofibril and muscle fibre mechanics by sinusoidal analysis. (Vols. 590.14). pp. 3361–3373. J Physiol (Lond). PMID: 10.1113/jphysiol.2012.228379.
Bai, F., Groth, H. L. & Kawai, M. (2012). DCM-related tropomyosin mutants E40K/E54K over-inhibit the actomyosin interaction and lead to a decrease in the number of cycling cross-bridges. (Vols. 7). pp. (e4741) 1-12. PLoS ONE. PMID: 10.1371, 10.1371/journal.pone.0047471.
Oguchi, Y., Ishizuka, J., Hitchcock-DeGregori, S. E., Ishiwata, S. & Kawai, M. (2011). The role of tropomyosin domains in cooperative activation of the actin-myosin interaction. (Vols. 414). pp. 667-680. J Mol Biol. PMID: http://dx.doi.org/10.1016/j.jmb.2011.10.026.
Candau, R., Kawai, M. (2011). Correlation between cross-bridge kinetics obtained from Trp fluorescence of myofibril suspensions and mechanical studies of single muscle fibers in rabbit psoas. (Vols. 32). pp. 315-326. J Muscle Res Cell Motil. PMID: http://dx.doi.org/10.1007/s10974-011-9264-7.
Muthus, P., Wang, L., Yuan, C., Kazmierczak, K., Huang, W., Hernandez, O., Kawai, M., Irving, T. & Szczesna-Cordary, D. (2011). Structural and functional aspects of myosin ELC-mediated cardiac muscle contraction. (Vols. 11-191973). pp. 1-12. FASEB J . PMID: http://dx.doi.org/10.1096/fj.11-191973.
Bai, F., Weis, A., Takeda, A. K., Chase, B. P. & Kawai, M. (2011). Enhanced active cross-bridges during diastole: molecular pathogenesis of tropomyosin’s HCM mutations. (Vols. 100). pp. 1014-1023. Biophys J. PMID: 10.1016/j.bpj.2011.01.001.
Lu, X., Heeley, D. H., Smillie, L. B. & Kawai, M. (2010). The role of tropomyosin isoforms and phosphorylation in force generation in thin-filament reconstituted bovine cardiac muscle fibres. (Vols. 31). pp. 93–109. J Muscle Res Cell Motil. PMID: http://dx.doi.org/10.1007/s10974-010-9213.
Kawai, M., Candau, R. (2010). Muscle contraction and supplying ATP to muscle cells. In P. Connes , O. Hue , S. Perrey (Eds.) Handbook of Exercise Physiology – From a cellular to an integrative approach. pp. 3-26. Amsterdam, The Netherlands: IOS Press.
Kawai, M., Lu, X., Hitchcock-DeGregori, S. E., Stanton, K. J. & Wandling, M. W. (2009). Tropomyosin period 3 is essential for enhancement of isometric tension in thin filament-reconstituted bovine myocardium. (Vols. 2009). pp. 1-17. J Biophysics. PMID: http://dx.doi.org/10.1155/2009/380967.
Kawai, M., Halvorson, H. R. (2007). Force transients and minimum cross-bridge models in muscular contraction. (Vols. 28). pp. 371-395. J Muscle Res Cell Motil. PMID: http://dx.doi.org/10.1007/s10974-008-9131-3.
Kawai, M., Ishiwata, S. (2006). Use of thin filament reconstituted muscle fibres to probe the mechanism of force generation. (Vols. 27). pp. 455-468. London, UK: J Muscle Res Cell Motil. PMID: 10.1007/s10974-006-9075-4.
Kawai, M., Kido, T., Vogel, M., Fink, R. H. & Ishiwata, S. (2006). Temperature change does not affect force between regulated actin filaments and HMM in single molecule experiments. (Vols. 574.3). pp. 877–887. J Physiol (Lond). PMID: 10.1113/jphysiol.2006.111708.
Lu, X., Tobacman, L. S. & Kawai, M. (2006). Temperature dependence of isometric tension and cross-bridge kinetics of cardiac muscle fibers reconstituted with a tropomyosin internal deletion mutant. (Vols. 91). (11), pp. 4230-4240. Biophys J. PMID: 10.1529/biophysj.106.084608.
Lu, X., Bryant, M. K., Bryan, K., Rubenstein, P. A. & Kawai, M. (2005). Role of the N-terminal negative charge of actin in cross-bridge kinetics and force generation in reconstituted bovine myocardium. (Vols. 564.1). pp. 65-82. J Physiol (Lond). PMID: http://dx.doi.org/10.1113/jphysiol.2004.078055.
Galler, S., Wang, B. G. & Kawai, M. (2005). Elementary steps of the cross-bridge cycle in fast-twitch fiber types from rabbit skeletal muscles. (Vols. 89). pp. 3248-3260. Biophys J. PMID: http://dx.doi.org/10.1529/biophysj.104.056614.
Fujita, H., Lu, X., Suzuki, M., Ishiwata, S. & Kawai, M. (2004). The effect of tropomyosin on force and elementary steps of the cross-bridge cycle in bovine myocardium. (Vols. 556.2). pp. 637-649. J Physiol (Lond). PMID: http://dx.doi.org/10.1113/jphysiol.2003.059956.
Lu, X., Tobacman, L. S. & Kawai, M. (2003). Effects of tropomyosin internal deletion ?23Tm on isometric tension and the cross-bridge kinetics in bovine myocardium. (Vols. 553.2). pp. 457-471. J Physiol (Lond). PMID: http://dx.doi.org/10.1113/jphysiol.2003.053694.
Kawai, M. (2003). What do we learn by studying the temperature effect on isometric tension and tension transients in mammalian striated muscle fibres?. (Vols. 24). pp. 127-138. J Muscle Res Cell Motil. PMID: http://dx.doi.org/10.1023/A:1026093212111.
Ding, W., Fujita, H. & Kawai, M. (2002). The length of cooperative units on the thin filament in rabbit psoas muscle fibres. (Vols. 87.6). pp. 691-697. Experimental Physiology. PMID: http://dx.doi.org/10.1113/eph8702448.
Fujita, H., Sasaki, D., Ishiwata, S. & Kawai, M. (2002). Elementary steps of the cross-bridge cycle in bovine myocardium with and without regulatory proteins. (Vols. 82). (2), pp. 915-928. Biophys J.
Fujita, H., Kawai, M. (2002). Temperature effect on isometric tension is mediated by regulatory proteins tropomyosin and troponin in bovine myocardium. (Vols. 539.1). pp. 267-276. J Physiol (Lond).
Wang, G., Kawai, M. (2001). Effect of temperature on elementary steps of the cross-bridge cycle in rabbit soleus slow-twitch muscle fibers. (Vols. 531). (1), pp. 219-234. J Phys.
Kawai, M., Kawaguchi, K., Saito, M. & Ishiwata, S. (2000). Temperature change does not affect force between single actin filaments and HMM from rabbit muscles. (Vols. 78). pp. 3112-3119. Biophys J.
Wang, G., Ding, W. & Kawai, M. (1999). Does thin filament compliance diminish the cross-bridge kinetics? A study in rabbit psoas fibers. (Vols. 76). pp. 978-984. Biophys J.
Kawai, M. (1998). Comments on the paper by Dr. David Smith entitled, "A strain-dependent ratchet model for [phosphate]-and [ATP]-dependent muscle contraction. (Vols. 19). pp. 713-715. J Muscle Res Cell Mot.
Kawai, M. (1997). Force generation and phosphate release steps in skinned rabbit soleus slow-twitch muscle fibres. (Vols. 73). pp. 878-894. Biophys J. DOI: http://dx.doi.org/10.1016/S0006-3495(97)78121-9.
Murphy, K. P., Zhao, Y. & Kawai, M. (1996). Molecular forces involved in force generation during skeletal muscle contraction. (Vols. 199). pp. 2565-2571. J Exptl Biol.
Zhao, Y., Swamy, P., Humphries, K. A. & Kawai, M. (1996). The effect of partial extraction of troponin C on the elementary steps of the cross-bridge cycle in rabbit psoas fibers. (Vols. 71). pp. 2759-2773. Biophys J.
Zhao, Y., Kawai, M. (1996). Inotropic agent EMD-53998 weakens nucleotide and phosphate binding to cross-bridges in porcine myocardium. (Vols. 271). (4), pp. H1394-1406. Heart Circ Physiol. PMID: 8897933.
Wang, G., Kawai, M. (1996). Effects of MgATP and MgADP on the cross-bridge kinetics of rabbit soleus slow-twitch muscle fibers. (Vols. 71). pp. 1450-1461. Biophys J. DOI: http://dx.soi.org/10.1016/S0006-3495(96)79346-3.
Zhao, Y., Kawai, M. (1995). The hydrophobic interaction between actin and myosin underlies the mechanism of force generation by cross-bridges. (Vols. 68 (4 Suppl)). pp. 332s. Biophys J.
Kawai, M., Zhao, Y. (1995). Nucleotide binding site of myosin head is under the influence of thin filament proteins. (Vols. 68 (4 Suppl)). pp. 216s. Biophys J.
Raucher, D., Fajer, E. A., Sar, C., Hideg, K., Zhao, Y., Kawai, M. & Fajer, P. G. (1995). A novel electron paramagnetic resonance spin label and its application to study the cross-bridge cycle. Biophys J.
Schraeger, J. A., Canby, C. A., Rongish, B. J., Kawai, M. & Tomanek, R. J. (1994). Normal left ventricular diastolic compliance following regression of hypertrophy. (Vols. 23). (3), pp. 349-357. J Cardiovasc Pharm. PMID: 7515976.
Zhao, Y., Kawai, M. (1994). BDM affects nucleotide binding and force generation steps of the cross-bridge cycle in rabbit psoas muscle fibers. (Vols. 266). (35), pp. C437-C447. Am Physiol (Cell Physiol). PMID: 8141258.
Zhao, Y., Kawai, M. (1994). Kinetic and thermodynamic studies of the cross-bridge cycle in rabbit psoas muscle fibers. (Vols. 67). pp. 1655-1668. Biophys J. PMID: 7819497.
Kawai, M., Wray, J. S. & Zhao, Y. (1993). The effect of the lattice spacing change on cross-bridge kinetics in chemically skinned rabbit psoas muscle fibers. I. Proportionality between the lattice spacing and the fiber width. (Vols. 64). pp. 187-196. Biophys J. PMID: 7679296.
Zhao, Y., Kawai, M. (1993). The effect of the lattice spacing change on cross-bridge kinetics in chemically skinned rabbit psoas muscle fibers. Elementary steps affected by the spacing change. (Vols. 64). (1), pp. 197-210. Biophys J. DOI: 10.1016/S0006-3495(93)81357-2.
Zhao, Y., Kawai, M. & Wray, J. (1993). The effect of lattice spacing change on cross-bridge kinetics in rabbit psoas fibers. In H. Sugi , G. Pollack (Eds.) Mechanisms of Myofilament Sliding in Muscle Contraction. pp. 581-592. New York, New York: Plenum Press. PMID: 8109370.
Kawai, M. (1993). Kawai's response to Horiuti and Sakoda. (Vols. 65). pp. 2263-2264. Biophys J.
Kawai, M., Saeki, Y. & Zhao, Y. (1993). Cross-bridge scheme and kinetic constants of elementary steps deduced from chemically skinned papillary and trabecular muscles of the ferret. (Vols. 73). pp. 35-50. Circ Res. PMID: 8508533.
Kawai, M., Zhao, Y. & Halvorson, H. R. (1993). Elementary steps of contraction probed by sinusoidal analysis technique in rabbit psoas fibers. In H. Sugi , G. J. Pollack (Eds.) Mechanisms of Myofilament Sliding in Muscle Contraction. pp. 567-577. New York, New York: Plenum Press. PMID: 8109368.
Kawai, M., Zhao, Y. (1993). Cross-bridge scheme and force per cross-bridge state in skinned rabbit psoas muscle fibers. (Vols. 65). (2), pp. 638-651. Biophys J. PMID: 8218893.
Saeki, Y., Kawai, M. & Zhao, Y. (1991). Comparison of cross-bridge dynamics between intact and skinned myocardium from ferret right ventricles. (Vols. 68). (3), pp. 772-781. Circ Res. PMID: 1742866.
Kawai, M., Halvorson, H. R. (1991). Two step mechanism of phosphate release and the mechanism of force generation in chemically skinned rabbit psoas muscle. (Vols. 59). (2), pp. 329-342. Biophys J. PMID: 2009356.
Marcussen, B. L., Kawai, M. (1990). Role of MgATP and inorganic phosphate ions in cross-bridge kinetics in insect (Lethocerus Colossicus) flight muscle. In N. Sperelakis , J. D. Wood (Eds.) Frontiers in Smooth Muscle Research. pp. 805-813. New York, New York: Wiley-Liss. PMID: 2138792.
Kawai, M., Wray, J. S. & Guth, K. (1990). Effect of ionic strength on cross-bridge kinetics as studied by sinusoidal analysis, ATP hydrolysis rate, and X-ray diffraction techniques in chemically skinned rabbit psoas fibers. (Vols. 11). (5), pp. 392-402. J Muscle Res Cell Motil. PMID: 2266166.
Tawada, K., Kawai, M. (1990). Covalent cross-linking of single muscle fibers from rabbit psoas increases oscillatory power. (Vols. 57). (3), pp. 643-647. Biophys J. DOI: 10.1016/S0006-3495(90)82582-0.
Kawai, M., Halvorson, H. R. (1989). Role of MgATP in the crossbridge kinetics in chemically skinned rabbit psoas fibers. Study of a fast exponential process (C). (Vols. 55). pp. 595-603. Biophys J. PMID: 2785822.
Feit, H., Kawai, M. & Mostafapour, A. S. (1989). The role of collagen crosslinking in the increased stiffness of avian dystrophic muscle. (Vols. 12). pp. 486-492. Muscle and Nerve. PMID: 2725576.
Feit, H., Kawai, M. & Mostafapour, A. S. (1989). Increased resistance of the collagen in avian dystrophic muscle to collagenolytic attack. Evidence for increased crosslinking. (Vols. 12). (6), pp. 476-485. Muscle and Nerve. PMID: 2542788.
Kawai, M., Halvorson, H. R. (1989). Effect of MgATP and MgADP on the cross-bridge kinetics in chemically skinned rabbit psoas fibers: An interpretation of a fast exponential process (C). In R. J. Paul , H. Yamada , G. Elzinga (Eds.) Muscle Energetics (Prog Clin Biol Res 315:51-62). New York, New York: Alan R Liss.
Kawai, M., Guth, K. & Cornacchia, T. W. (1988). The role of monovalent phosphate anions in the cross-bridge kinetics of chemically skinned rabbit psoas fibers. In H. Sugi , G. Pollack (Eds.) Molecular Mechanism of Muscle Contraction. pp. 203-214. New York, New York: Plenum Publishing Co..
Kawai, M., Guth, K., Winnikes, K., Haist, C. & Ruegg, J. C. (1987). The effect of inorganic phosphate on the ATP hydrolysis rate and the tension transients in chemically skinned rabbit psoas fibers. (Vols. 408). (1), pp. 1-9. Pflugers Archiv. PMID: 3822768.
Kawai, M. (1986). The role of orthophosphate in cross-bridge kinetics in chemically skinned rabbit psoas fibers as detected with sinusoidal and step length alterations. (Vols. 7). (5), pp. 421-434. J Muscle Res Cell Mot.
Diamond, M. S., Brandt, P. W. & Kawai, M. (1986). Comments on the "Critical dependence of calcium-activated force on width in highly compressed fibers of the frog.". (Vols. 50). pp. 1215-1216. Biophys J.
Feit, H., Kawai, M. (1985). Physiological and biochemical characterization of avian dystrophic muscle reveals alterations of collagen. (Vols. 460). pp. 431-433. Annals of the New York Academy of Sciences. DOI: 10.1111/j.1749-6632.1985.tb51201.x.
Feit, H., Kawai, M. & Schulman, M. I. (1985). Stiffness and contractile properties of avian normal and dystrophic muscle bundles as measured by sinusoidal length perturbations. (Vols. 8). pp. 503-510. Muscle and Nerve. PMID: 16758574.
Feit, H., Hammon, K. & Kawai, M. (1985). Collagen in chemically skinned, extracted dystrophic myofibers. (Vols. 8). (9), pp. 806-807. Muscle and Nerve. PMID: 4079959.
Kawai, M., Schulman, M. I. (1985). Cross-bridge kinetics in chemically skinned rabbit psoas fibers when the actin-myosin lattice spacing is altered by dextran T-500. (Vols. 6). (3), pp. 313-332. J Muscle Res Cell Mot. DOI: 10.1007/BF00713172.
Kawai, M. (1985). The mechanism of muscular contraction: Frequency response function of skinned fibers and an interpretation. In H. R. Lang (Eds.) 20 Years of The Department of Pure and Applied Science. pp. 121-127. Tokyo, Japan: Special Publication by the Anniversary Committee, Tokyo University.
Kawai, M., Brandt, P. W. & Cox, R. N. (1984). The role of Ca2+ in cross-bridge kinetics in chemically skinned rabbit psoas fibers. In G. J. Pollack , H. Sugi (Eds.) Advances in Experimental Medicine and Biology: Vol. 170. Contractile Mechanism in Muscle. pp. 657-672. New York, New York: Plenum Press.
Brandt, P. W., Diamond, M. S., Gluck, B., Kawai, M. & Schachat, F. H. (1984). Molecular basis of cooperativity in vertebrate muscle thin filaments. (Vols. 49). pp. 155-167. Carlsberg Research Communication (Copenhagen).
Kawai, M., Schachat, F. H. (1984). Differences in the transient response to fast and slow skeletal muscle fibers: correlations between complex modulus and myosin light chains. (Vols. 45). (6), pp. 1145-1151. Biophys J. DOI: 10.1016/S0006-3495(84)84262-9.
Brandt, P. W., Cox, R. N., Kawai, M. & Robinson, T. (1982). Regulation of tension in skinned muscle fibers: effect of cross-bridge rate constants on apparent Ca2+sensitivity. (Vols. 79). (6), pp. 997-1016. J Gen Physiol.
Kawai, M. (1982). Correlation between exponential processes and cross-bridge kinetics. In B. M. Twarog , R. J. Levine , M. M. Dewey (Eds.) Basic Biology of Muscles: A Comparative Approach. pp. 109-130. New York, New York: Raven Press.
Cox, R. N., Kawai, M. (1981). Alternate energy transduction routes in chemically skinned rabbit psoas muscle fibers: a further study of the effect of MgATP over a wide concentration range. (Vols. 2). (2), pp. 203-214. J Muscle Res Cell Motil. DOI: 10.1007/BF00711870.
Kawai, M., Cox, R. N. & Brandt, P. W. (1981). Effect of Ca ion concentration on cross-bridge kinetics in rabbit psoas fibers. Evidence for the presence of two Ca-activated states of thin filament. (Vols. 35). (2), pp. 375-384. Biophys J. PMID: 6791720.
Brandt, P. W., Cox, R. N. & Kawai, M. (1980). Can the binding Ca2+ to two regulatory sites on troponin C determine the steep pCa/tension of relationship of skeletal muscle?. (Vols. 77). (8), pp. 4717-4720. Proc Natl Acad Sci USA.
Kawai, M., Brandt, P. W. (1980). Sinusoidal analysis: a high resolution method for correlating biochemical reactions with physiological processes in activated skeletal muscles of rabbit, frog, and crayfish. (Vols. 1). (3), pp. 279-303. J Muscle Res Cell Motil. PMID: 6971874.
Kawai, M., Brandt, P. W. (1979). Mechanochemistry of actin-myosin interaction. In F. A. Pepe , J. W. Sanger , V. T. Nachmias (Eds.) Motility in Cell Function. pp. 411-414. New York, New York: Academic Press.
Cox, R. N., Kawai, M., Karlin, A. & Brandt, P. W. (1979). Voltage fluctuations at the frog sartorius motor endplate produced by a covalently attached activator. (Vols. 51). (2), pp. 145-159. J Membrane Biol. PMID: 316828.
Kawai, M. (1979). Effect of MgATP on cross-bridge kinetics in chemically skinned rabbit psoas fibers as measured by sinusoidal analysis technique. In H. Sugi , G. H. Pollack (Eds.) Cross-bridge Mechanism in Muscle Contraction. pp. 149-169. Tokoyo, Japan: University of Tokyo Press.
Kawai, M., Brandt, P. W. (1978). Studies of cross-bridge behavior when the muscle length is changed in a sinusoidal manner.
Kawai, M. (1978). Head rotation or dissociation? A study of exponential rate processes in chemically skinned rabbit muscle fibers when MgATP concentration is changed. (Vols. 22). (1), pp. 97-103. Biophys J. PMID: 638228.
Kawai, M., Brandt, P. W. & Orentlicher, M. (1977). Dependence of energy transduction in intact skeletal muscles on the time in tension. DOI: 10.1016/S0006-3495(77)85605-1.
Kawai, M., Brandt, P. W. (1977). Effect of MgATP on stiffness measured at two frequencies in Ca activated muscle fibers. (Vols. 74). (9), pp. 4073-4075. Proc Natl Acad Sci USA.
Kawai, M., Brandt, P. W. (1976). Two rigor states in skinned crayfish single muscle fibers. (Vols. 68). (3), pp. 267-280. J Gen Physiol. PMID: 821913.
Kawai, M., Kuntz, I. D. (1973). Optical diffraction studies of muscle fibers. (Vols. 13). (9), pp. 857-876. Biophys J. DOI: 10.1016/S0006-3495(73)86031-X.