메뉴 건너뛰기




Volumn 1764, Issue 6, 2006, Pages 1054-1062

Caldesmon freezes the structure of actin filaments during the actomyosin ATPase cycle

Author keywords

Caldesmon; Conformational change; F actin; Fluorescence polarization; Ghost muscle fiber; Myosin subfragment S1

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CALDESMON; MYOSIN ADENOSINE TRIPHOSPHATASE;

EID: 33745201819     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2006.04.001     Document Type: Article
Times cited : (12)

References (53)
  • 1
    • 0026082863 scopus 로고
    • The dynamics of actin and myosin association and the crossbridge model of muscle contraction
    • Geeves M.A. The dynamics of actin and myosin association and the crossbridge model of muscle contraction. Biochem. J. 274 (1991) 1-14
    • (1991) Biochem. J. , vol.274 , pp. 1-14
    • Geeves, M.A.1
  • 2
    • 0019544621 scopus 로고
    • Mechanism of the actomyosin ATPase: effect of actin on the ATP hydrolysis step
    • Stein L.A., Chock P.B., and Eisenberg E. Mechanism of the actomyosin ATPase: effect of actin on the ATP hydrolysis step. Proc. Natl. Acad. Sci. U. S. A. 78 (1981) 1346-1350
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 1346-1350
    • Stein, L.A.1    Chock, P.B.2    Eisenberg, E.3
  • 3
    • 0020806081 scopus 로고
    • Crosslinked myosin subfragment 1: a stable analogue of the subfragment-1.ATP complex
    • Chalovich J.M., Greene L.E., and Eisenberg E. Crosslinked myosin subfragment 1: a stable analogue of the subfragment-1.ATP complex. Proc. Natl. Acad. Sci. U. S. A. 80 (1983) 4909-4913
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 4909-4913
    • Chalovich, J.M.1    Greene, L.E.2    Eisenberg, E.3
  • 4
    • 0019013686 scopus 로고
    • Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex
    • Greene L.E., and Eisenberg E. Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex. Proc. Natl. Acad. Sci. U. S. A. 77 (1980) 2616-2620
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 2616-2620
    • Greene, L.E.1    Eisenberg, E.2
  • 5
    • 0021894617 scopus 로고
    • The function of myosin and myosin light chain kinase phosphorylation in smooth muscle
    • Kamm K.E., and Stull J.T. The function of myosin and myosin light chain kinase phosphorylation in smooth muscle. Annu. Rev. Pharmacol. Toxicol. 25 (1985) 593-620
    • (1985) Annu. Rev. Pharmacol. Toxicol. , vol.25 , pp. 593-620
    • Kamm, K.E.1    Stull, J.T.2
  • 6
    • 0032836236 scopus 로고    scopus 로고
    • Thin-filament linked regulation of smooth muscle myosin
    • Haeberle J.R. Thin-filament linked regulation of smooth muscle myosin. J. Muscle Res. Cell Motil. 20 (1999) 363-370
    • (1999) J. Muscle Res. Cell Motil. , vol.20 , pp. 363-370
    • Haeberle, J.R.1
  • 7
    • 0025799684 scopus 로고
    • The molecular anatomy of caldesmon
    • Marston S.B., and Redwood C.S. The molecular anatomy of caldesmon. Biochem. J. 279 (1991) 1-16
    • (1991) Biochem. J. , vol.279 , pp. 1-16
    • Marston, S.B.1    Redwood, C.S.2
  • 8
    • 0025881953 scopus 로고
    • Electron microscopic studies of chicken gizzard caldesmon and its complex with calmodulin
    • Mabuchi K., and Wang C.L. Electron microscopic studies of chicken gizzard caldesmon and its complex with calmodulin. J. Muscle Res. Cell Motil. 12 (1991) 145-151
    • (1991) J. Muscle Res. Cell Motil. , vol.12 , pp. 145-151
    • Mabuchi, K.1    Wang, C.L.2
  • 9
    • 0031555487 scopus 로고    scopus 로고
    • Visualization of caldesmon on smooth muscle thin filaments
    • Lehman W., Vibert P., and Craig R. Visualization of caldesmon on smooth muscle thin filaments. J. Mol. Biol. 274 (1997) 310-317
    • (1997) J. Mol. Biol. , vol.274 , pp. 310-317
    • Lehman, W.1    Vibert, P.2    Craig, R.3
  • 10
    • 0042429156 scopus 로고    scopus 로고
    • Visualization of caldesmon binding to synthetic filaments of smooth muscle myosin
    • Kulikova N., Podlubnaya Z., Makuch R., and Dabrowska R. Visualization of caldesmon binding to synthetic filaments of smooth muscle myosin. J. Muscle Res. Cell Motil. 24 (2003) 7-13
    • (2003) J. Muscle Res. Cell Motil. , vol.24 , pp. 7-13
    • Kulikova, N.1    Podlubnaya, Z.2    Makuch, R.3    Dabrowska, R.4
  • 11
    • 0022400733 scopus 로고
    • Caldesmon-induced inhibition of ATPase activity of actomyosin and contraction of skinned fibres of chicken gizzard smooth muscle
    • Szpacenko A., Wagner J., Dabrowska R., and Ruegg J.C. Caldesmon-induced inhibition of ATPase activity of actomyosin and contraction of skinned fibres of chicken gizzard smooth muscle. FEBS Lett. 192 (1985) 9-12
    • (1985) FEBS Lett. , vol.192 , pp. 9-12
    • Szpacenko, A.1    Wagner, J.2    Dabrowska, R.3    Ruegg, J.C.4
  • 12
    • 0023945560 scopus 로고
    • Effect of caldesmon on the ATPase activity and the binding of smooth and skeletal myosin subfragments to actin
    • Hemric M.E., and Chalovich J.M. Effect of caldesmon on the ATPase activity and the binding of smooth and skeletal myosin subfragments to actin. J. Biol. Chem. 263 (1988) 1878-1885
    • (1988) J. Biol. Chem. , vol.263 , pp. 1878-1885
    • Hemric, M.E.1    Chalovich, J.M.2
  • 13
    • 0038182972 scopus 로고    scopus 로고
    • Influence of ionic strength, actin state, and caldesmon construct size on the number of actin monomers in a caldesmon binding site
    • Fredricksen S., Cai A., Gafurov B., Resetar A., and Chalovich J.M. Influence of ionic strength, actin state, and caldesmon construct size on the number of actin monomers in a caldesmon binding site. Biochemistry 42 (2003) 6136-6148
    • (2003) Biochemistry , vol.42 , pp. 6136-6148
    • Fredricksen, S.1    Cai, A.2    Gafurov, B.3    Resetar, A.4    Chalovich, J.M.5
  • 14
    • 0021925951 scopus 로고
    • The influence of caldesmon on ATPase activity of the skeletal muscle actomyosin and bundling of actin filaments
    • Dabrowska R., Goch A., Galazkiewicz B., and Osinska H. The influence of caldesmon on ATPase activity of the skeletal muscle actomyosin and bundling of actin filaments. Biochim. Biophys. Acta 842 (1985) 70-75
    • (1985) Biochim. Biophys. Acta , vol.842 , pp. 70-75
    • Dabrowska, R.1    Goch, A.2    Galazkiewicz, B.3    Osinska, H.4
  • 15
    • 0023664281 scopus 로고
    • Caldesmon inhibits skeletal actomyosin subfragment-1 ATPase activity and the binding of myosin subfragment-1 to actin
    • Chalovich J.M., Cornelius P., and Benson C.E. Caldesmon inhibits skeletal actomyosin subfragment-1 ATPase activity and the binding of myosin subfragment-1 to actin. J. Biol. Chem. 262 (1987) 5711-5716
    • (1987) J. Biol. Chem. , vol.262 , pp. 5711-5716
    • Chalovich, J.M.1    Cornelius, P.2    Benson, C.E.3
  • 16
    • 0033864963 scopus 로고    scopus 로고
    • Actin and the smooth muscle regulatory proteins: a structural perspective
    • Hodgkinson J.L. Actin and the smooth muscle regulatory proteins: a structural perspective. J. Muscle Res. Cell Motil. 21 (2000) 115-130
    • (2000) J. Muscle Res. Cell Motil. , vol.21 , pp. 115-130
    • Hodgkinson, J.L.1
  • 17
    • 0032917668 scopus 로고    scopus 로고
    • Conformational changes of contractile proteins and their role in muscle contraction
    • Borovikov Y.S. Conformational changes of contractile proteins and their role in muscle contraction. Int. Rev. Cyt. 189 (1999) 267-301
    • (1999) Int. Rev. Cyt. , vol.189 , pp. 267-301
    • Borovikov, Y.S.1
  • 18
    • 0026101786 scopus 로고
    • Troponin I and caldesmon restrict alterations in actin structure occurring on binding of myosin subfragment 1
    • Nowak E., Borovikov Y.S., Khoroshev M.I., and Dabrowska R. Troponin I and caldesmon restrict alterations in actin structure occurring on binding of myosin subfragment 1. FEBS Lett. 281 (1991) 51-54
    • (1991) FEBS Lett. , vol.281 , pp. 51-54
    • Nowak, E.1    Borovikov, Y.S.2    Khoroshev, M.I.3    Dabrowska, R.4
  • 19
    • 0026048670 scopus 로고
    • Polarization microfluorimetry study of interaction between myosin head and F-actin in muscle fibers
    • Borovikov Yu S., Kuleva N.V., and Khoroshev M.I. Polarization microfluorimetry study of interaction between myosin head and F-actin in muscle fibers. Gen. Physiol. Biophys. 10 (1991) 441-459
    • (1991) Gen. Physiol. Biophys. , vol.10 , pp. 441-459
    • Borovikov Yu, S.1    Kuleva, N.V.2    Khoroshev, M.I.3
  • 20
    • 0023659154 scopus 로고
    • The effect of caldesmon on actin-myosin interaction in skeletal muscle fibers
    • Galazkiewicz B., Borovikov Y.S., and Dabrowska R. The effect of caldesmon on actin-myosin interaction in skeletal muscle fibers. Biochim. Biophys. Acta 916 (1987) 368-375
    • (1987) Biochim. Biophys. Acta , vol.916 , pp. 368-375
    • Galazkiewicz, B.1    Borovikov, Y.S.2    Dabrowska, R.3
  • 21
    • 0024804676 scopus 로고
    • Caldesmon weakens the bonding between myosin heads and actin in ghost fibers
    • Nowak E., Borovikov Y.S., and Dabrowska R. Caldesmon weakens the bonding between myosin heads and actin in ghost fibers. Biochim. Biophys. Acta 999 (1989) 289-292
    • (1989) Biochim. Biophys. Acta , vol.999 , pp. 289-292
    • Nowak, E.1    Borovikov, Y.S.2    Dabrowska, R.3
  • 23
    • 0040137496 scopus 로고
    • Comparative studies of chicken gizzard and rabbit skeletal tropomyosin
    • Dabrowska R., Nowak E., and Drabikowski W. Comparative studies of chicken gizzard and rabbit skeletal tropomyosin. Comp. Biochem. Physiol. 65B (1980) 75-83
    • (1980) Comp. Biochem. Physiol. , vol.65 B , pp. 75-83
    • Dabrowska, R.1    Nowak, E.2    Drabikowski, W.3
  • 24
    • 0021686984 scopus 로고
    • Smooth muscle caldesmon. Rapid purification and F-actin cross-linking properties
    • Bretscher A. Smooth muscle caldesmon. Rapid purification and F-actin cross-linking properties. J. Biol. Chem. 259 (1984) 12873-12880
    • (1984) J. Biol. Chem. , vol.259 , pp. 12873-12880
    • Bretscher, A.1
  • 25
    • 0017336444 scopus 로고
    • Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility
    • Weeds A.G., and Pope B. Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility. J. Mol. Biol. 111 (1977) 129-157
    • (1977) J. Mol. Biol. , vol.111 , pp. 129-157
    • Weeds, A.G.1    Pope, B.2
  • 26
    • 0017346888 scopus 로고
    • Polarization of fluorescence from single skinned glycerinated rabbit psoas fibers in rigor and relaxation
    • Borejdo J., and Putnam S. Polarization of fluorescence from single skinned glycerinated rabbit psoas fibers in rigor and relaxation. Biochim. Biophys. Acta 459 (1977) 578-595
    • (1977) Biochim. Biophys. Acta , vol.459 , pp. 578-595
    • Borejdo, J.1    Putnam, S.2
  • 27
    • 0018530414 scopus 로고
    • Active site trapping of nucleotides by crosslinking two sulfhydryls in myosin subfragment 1
    • Wells J.A., and Yount R.G. Active site trapping of nucleotides by crosslinking two sulfhydryls in myosin subfragment 1. Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 4966-4970
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 4966-4970
    • Wells, J.A.1    Yount, R.G.2
  • 28
    • 0020023995 scopus 로고
    • Sulfhydryl modification and labeling of myosin
    • Reisler E. Sulfhydryl modification and labeling of myosin. Methods Enzymol. 85 Pt B (1982) 84-93
    • (1982) Methods Enzymol. , vol.85 , Issue.PART B , pp. 84-93
    • Reisler, E.1
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0021066205 scopus 로고
    • Effect of troponin-tropomyosin complex and Ca2+ on conformational changes in F-actin induced by myosin subfragment-1
    • Borovikov Y.S., and Gusev N.B. Effect of troponin-tropomyosin complex and Ca2+ on conformational changes in F-actin induced by myosin subfragment-1. Eur. J. Biochem. 136 (1983) 363-369
    • (1983) Eur. J. Biochem. , vol.136 , pp. 363-369
    • Borovikov, Y.S.1    Gusev, N.B.2
  • 32
    • 0032999729 scopus 로고    scopus 로고
    • Backward movements of cross-bridges by application of stretch and by binding of MgADP to skeletal muscle fibers in the rigor state as studied by x-ray diffraction
    • Takezawa Y., Kim D.S., Ogino M., Sugimoto Y., Kobayashi T., Arata T., and Wakabayashi K. Backward movements of cross-bridges by application of stretch and by binding of MgADP to skeletal muscle fibers in the rigor state as studied by x-ray diffraction. Biophys. J. 76 (1999) 1770-1783
    • (1999) Biophys. J. , vol.76 , pp. 1770-1783
    • Takezawa, Y.1    Kim, D.S.2    Ogino, M.3    Sugimoto, Y.4    Kobayashi, T.5    Arata, T.6    Wakabayashi, K.7
  • 33
    • 0018975627 scopus 로고
    • Stereochemical aspects of the interaction of myosin and actomyosin with nucleotides
    • Goody R.S., and Hofmann W. Stereochemical aspects of the interaction of myosin and actomyosin with nucleotides. J. Muscle Res. Cell Motil. 1 (1980) 101-115
    • (1980) J. Muscle Res. Cell Motil. , vol.1 , pp. 101-115
    • Goody, R.S.1    Hofmann, W.2
  • 34
    • 0029884381 scopus 로고    scopus 로고
    • Orientation of intermediate nucleotide states of indane dione spin-labeled myosin heads in muscle fibers
    • Roopnarine O., and Thomas D.D. Orientation of intermediate nucleotide states of indane dione spin-labeled myosin heads in muscle fibers. Biophys. J. 70 (1996) 2795-2806
    • (1996) Biophys. J. , vol.70 , pp. 2795-2806
    • Roopnarine, O.1    Thomas, D.D.2
  • 36
    • 0020327766 scopus 로고
    • Cross-bridge orientation in skeletal muscle measured by linear dichroism of an extrinsic chromophore
    • Borejdo J., Assulin O., Ando T., and Putnam S. Cross-bridge orientation in skeletal muscle measured by linear dichroism of an extrinsic chromophore. J. Mol. Biol. 158 (1982) 391-414
    • (1982) J. Mol. Biol. , vol.158 , pp. 391-414
    • Borejdo, J.1    Assulin, O.2    Ando, T.3    Putnam, S.4
  • 37
    • 0016756968 scopus 로고
    • Polarization from a helix of fluorophores and its relation to that obtained from muscle
    • Tregear G.W., and Mendelson R.A. Polarization from a helix of fluorophores and its relation to that obtained from muscle. Biophys. J. 15 (1975) 455-467
    • (1975) Biophys. J. , vol.15 , pp. 455-467
    • Tregear, G.W.1    Mendelson, R.A.2
  • 38
    • 0018326091 scopus 로고
    • On the molecular basis for chemomechanical energy transduction in muscle
    • Morales M.F., and Botts J. On the molecular basis for chemomechanical energy transduction in muscle. Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 3857-3859
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 3857-3859
    • Morales, M.F.1    Botts, J.2
  • 39
    • 0029118087 scopus 로고
    • Fluorescence polarization study of the rigor complexes formed at different degrees of saturation of actin filaments with myosin subfragment-1
    • Andreev O.A., Takashi R., and Borejdo J. Fluorescence polarization study of the rigor complexes formed at different degrees of saturation of actin filaments with myosin subfragment-1. J. Muscle Res. Cell Motil. 16 (1995) 353-367
    • (1995) J. Muscle Res. Cell Motil. , vol.16 , pp. 353-367
    • Andreev, O.A.1    Takashi, R.2    Borejdo, J.3
  • 40
    • 0015948545 scopus 로고
    • Use of fluorescence polarization to observe changes in attitude of S-1 moieties in muscle fibers
    • Nichei T., Mendelson R., and Botts J. Use of fluorescence polarization to observe changes in attitude of S-1 moieties in muscle fibers. Biophys. J. 14 (1974) 236-242
    • (1974) Biophys. J. , vol.14 , pp. 236-242
    • Nichei, T.1    Mendelson, R.2    Botts, J.3
  • 41
    • 0035312384 scopus 로고    scopus 로고
    • Myosin motors: missing structures and hidden springs
    • Houdusse A., and Sweeney H.L. Myosin motors: missing structures and hidden springs. Curr. Opin. Struck. Biol. 11 (2001) 182-194
    • (2001) Curr. Opin. Struck. Biol. , vol.11 , pp. 182-194
    • Houdusse, A.1    Sweeney, H.L.2
  • 42
    • 0035901520 scopus 로고    scopus 로고
    • Conformation of myosin interdomain interactions during contraction: deductions from muscle fibers using polarized fluorescence
    • Burghardt T.P., Cruz-Walker A.R., Park S., and Ajtai K. Conformation of myosin interdomain interactions during contraction: deductions from muscle fibers using polarized fluorescence. Biochemistry 40 (2001) 4821-4833
    • (2001) Biochemistry , vol.40 , pp. 4821-4833
    • Burghardt, T.P.1    Cruz-Walker, A.R.2    Park, S.3    Ajtai, K.4
  • 43
    • 0019003415 scopus 로고
    • Exchange between inorganic phosphate and adenosine 5′-triphosphate in the medium by actomyosin subfragment 1
    • Sleep J.A., and Hutton R.L. Exchange between inorganic phosphate and adenosine 5′-triphosphate in the medium by actomyosin subfragment 1. Biochemistry 19 (1980) 1276-1283
    • (1980) Biochemistry , vol.19 , pp. 1276-1283
    • Sleep, J.A.1    Hutton, R.L.2
  • 44
    • 0022393454 scopus 로고
    • Suppression of muscle contraction by vanadate. Mechanical and ligand binding studies on glycerol-extracted rabbit fibers
    • Dantzig J.A., and Goldman Y.E. Suppression of muscle contraction by vanadate. Mechanical and ligand binding studies on glycerol-extracted rabbit fibers. J. Gen. Physiol. 86 (1985) 305-327
    • (1985) J. Gen. Physiol. , vol.86 , pp. 305-327
    • Dantzig, J.A.1    Goldman, Y.E.2
  • 45
    • 0037303089 scopus 로고    scopus 로고
    • An x-ray diffraction study on the ADP-induced conformational change in skeletal muscle myosin
    • Horiuti K., Yagi N., Takemori S., and Yamaguchi M. An x-ray diffraction study on the ADP-induced conformational change in skeletal muscle myosin. J. Biochem. (Tokyo) 133 (2003) 207-210
    • (2003) J. Biochem. (Tokyo) , vol.133 , pp. 207-210
    • Horiuti, K.1    Yagi, N.2    Takemori, S.3    Yamaguchi, M.4
  • 46
    • 0017837968 scopus 로고
    • Cross bridge slippage induced by the ATP analogue AMP-PNP and stretch in glycerol-extracted fibrillar muscle fibres
    • Kuhn H.J. Cross bridge slippage induced by the ATP analogue AMP-PNP and stretch in glycerol-extracted fibrillar muscle fibres. Biophys. Struct. Mech. 4 (1978) 159-168
    • (1978) Biophys. Struct. Mech. , vol.4 , pp. 159-168
    • Kuhn, H.J.1
  • 47
    • 0018938480 scopus 로고
    • Divalent metal ion binding and subunit interactions in myosins: a critical review
    • Bagshaw C.R. Divalent metal ion binding and subunit interactions in myosins: a critical review. J. Muscle Res. Cell Motil. 1 (1980) 255-277
    • (1980) J. Muscle Res. Cell Motil. , vol.1 , pp. 255-277
    • Bagshaw, C.R.1
  • 48
    • 0021015221 scopus 로고
    • Studies on conformation of F-actin in muscle fibers in the relaxed state, rigor, and during contraction using fluorescent phalloidin
    • Prochniewicz-Nakayama E., Yanagida T., and Oosawa F. Studies on conformation of F-actin in muscle fibers in the relaxed state, rigor, and during contraction using fluorescent phalloidin. J. Cell Biol. 97 (1983) 1663-1667
    • (1983) J. Cell Biol. , vol.97 , pp. 1663-1667
    • Prochniewicz-Nakayama, E.1    Yanagida, T.2    Oosawa, F.3
  • 49
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm
    • Lorenz M., Popp D., and Holmes K.C. Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234 (1993) 826-836
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 51
    • 0036099064 scopus 로고    scopus 로고
    • Regulatory and essential light chains of myosin rotate equally during contraction of skeletal muscle
    • Borejdo J., Ushakov D.S., and Akopova I. Regulatory and essential light chains of myosin rotate equally during contraction of skeletal muscle. Biophys. J. 82 (2002) 3150-3159
    • (2002) Biophys. J. , vol.82 , pp. 3150-3159
    • Borejdo, J.1    Ushakov, D.S.2    Akopova, I.3
  • 52
    • 0025267475 scopus 로고
    • Dissociation of the effect of caldesmon on the ATPase activity and on the binding of smooth heavy meromyosin to actin by partial digestion of caldesmon
    • Velaz L., Ingraham R.H., and Chalovich J.M. Dissociation of the effect of caldesmon on the ATPase activity and on the binding of smooth heavy meromyosin to actin by partial digestion of caldesmon. J. Biol. Chem. 265 (1990) 2929-2934
    • (1990) J. Biol. Chem. , vol.265 , pp. 2929-2934
    • Velaz, L.1    Ingraham, R.H.2    Chalovich, J.M.3
  • 53
    • 11144230917 scopus 로고    scopus 로고
    • Modes of caldesmon binding to actin: sites of caldesmon contact and modulation of interactions by phosphorylation
    • Foster D.B., Huang R., Hatch V., Craig R., Graceffa P., Lehman W., and Wang C.L. Modes of caldesmon binding to actin: sites of caldesmon contact and modulation of interactions by phosphorylation. J. Biol. Chem. 279 (2004) 53387-53394
    • (2004) J. Biol. Chem. , vol.279 , pp. 53387-53394
    • Foster, D.B.1    Huang, R.2    Hatch, V.3    Craig, R.4    Graceffa, P.5    Lehman, W.6    Wang, C.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.