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77
Referenced
47
-
Atkinson, M. A. L. &Korn, E. D. (1986) The purification and characterization of a globular subfragment ofAcanthamoeba Myosin II that is fully active when cross-linked to F-actin.J. biol. Chem. 261, 3382–8.
(
10.1016/S0021-9258(17)35794-0
) / J. biol. Chem. by M. A. L. Atkinson (1986) -
Audemard, E., Bertrand, R., Bonet, A., Chaussepied, P. &Mornet, D. (1988) Pathway for the communication between the ATPase and actin sites in myosin.J. Musc. Res. Cell Motility,9, 197–218.
(
10.1007/BF01773891
) / J. Musc. Res. Cell Motility by E. Audemard (1988) - Bertrand, R., Chaussepied, P., Kassab, R., Boyer, M., Benyamin, Y. &Roustan, C. (1987) Crosslinking of the skeletal myosin subfragment-1 heavy chain to the NH2-terminal region of actin within residues 40–113.J. Musc. Res. Cell Motility 8, 70. / J. Musc. Res. Cell Motility by R. Bertrand (1987)
-
Biosca, J. A., Barman, T. E. &Travers, F. (1984) Transient kinetics of the binding of ATP to acto-myosin subfragment-1: Evidence that the dissociation of actomyosin subfragment-1 by ATP leads to a new conformation of subfragment-1.Biochemistry 23, 2428–36.
(
10.1021/bi00306a017
) / Biochemistry by J. A. Biosca (1984) -
Bonet, A., Mornet, D., Audemard, E., Bertrand, R. &Kassab, R. (1987) Comparative structure of the protease-sensitive regions of the subfragment-1 heavy chain from smooth and skeletal myosin.J. biol. Chem. 262, 16524–30.
(
10.1016/S0021-9258(18)49287-3
) / J. biol. Chem. by A. Bonet (1987) -
Bonet, A., Audemard, E. &Mornet, D. (1988) The actin-myosin subfragment-1 complex stabilized by phenyldiglyoxalJ. biol. Chem. 263, 14115–21.
(
10.1016/S0021-9258(18)68192-X
) / J. biol. Chem. by A. Bonet (1988) -
Botts, J., Takashi, R., Torgerson, P., Hozumi, T., Muhlrad, A., Mornet, D. &Morales, M. F. (1984) On the mechanism of energy transduction in myosin subfragment-1Proc. natn. Acad. Sci. U.S.A. 81, 2060–4.
(
10.1073/pnas.81.7.2060
) / Proc. natn. Acad. Sci. U.S.A. by J. Botts (1984) -
Castellani, L., Elliot, B. W., Winkelmann, D. A., Vibert, P. &Cohen, C. (1987) Myosin binding to actin, structural analysis using myosin fragments.J. molec. Biol. 196, 955–60.
(
10.1016/0022-2836(87)90420-7
) / J. molec. Biol. by L. Castellani (1987) -
Chaussepied, P., Mornet, D., Audemard, E., Derancourt, J. &Kassab, R. (1986a) Abolition of ATPase activities of skeletal myosin subfragment-1 by a new selective proteolytic cleavage within the 50 kilodalton heavy chain segment.Biochemistry 25, 1134–40.
(
10.1021/bi00353a028
) / Biochemistry by P. Chaussepied (1986) -
Chaussepied, P., Mornet, D., Barman, T. E., Travers, F. &Kassab, R. (1986b) Alteration of the ATP hydrolysis and actin binding properties of thrombin-cut myosin subfragment-1.Biochemistry,25, 1141–9.
(
10.1021/bi00353a029
) / Biochemistry by P. Chaussepied (1986) -
Chaussepied, P., Morales, M. F. &Kassab, R. (1988) The myosin (SH2-50 kilodalton fragment) cross-link: location and consequences.Biochemistry 27, 1778–85.
(
10.1021/bi00405a059
) / Biochemistry by P. Chaussepied (1988) -
Cross, R. L., Cunningham, D., Miller, C. G., Xue, Z., Zhou, Z. M. &Boyer, P. D. (1987) Adenine nucleotide binding sites on beef heart F1 ATPase.Proc. natn. Acad. Sci. U.S.A. 84, 5715–9.
(
10.1073/pnas.84.16.5715
) / Proc. natn. Acad. Sci. U.S.A. by R. L. Cross (1987) -
Doi, Y., Higashida, M. &Kido, S. (1987) Plasma-gelsolin-binding sites on the actin sequence.Eur. J. Biochem. 164, 89–94.
(
10.1111/j.1432-1033.1987.tb10997.x
) / Eur. J. Biochem. by Y. Doi (1987) -
Dos Remedios, C., Miki, M. &Barden, J. A. (1987) Fluorescence resonance energy transfer measurement of distances in actin and myosin. A critical evaluation.J. Musc. Res. Cell Motility 8, 97–117.
(
10.1007/BF01753986
) / J. Musc. Res. Cell Motility by C. Dos Remedios (1987) -
Eccleston, J. F. (1980) Fluorescence changes associated with the binding of ribose-5′-triphosphate and myosin subfragment-1: Evidence for a second triphosphate binding site.FEBS Lett. 113, 55–7.
(
10.1016/0014-5793(80)80493-5
) / FEBS Lett. by J. F. Eccleston (1980) -
Fowler, W. E., Buhle, E. L. &Aebi, V. (1984) Tubular arrays of the actin-DNase I Complex induced by gadolinium.Proc. natn. Acad. Sci. U.S.A. 81, 1669–73.
(
10.1073/pnas.81.6.1669
) / Proc. natn. Acad. Sci. U.S.A. by W. E. Fowler (1984) -
Griffiths, A. J., Levine, B. A. &Trayer, I. P. (1987) The interaction of the SH1/SH2 region of the myosin heavy chain with actin.Biochem. Soc. Trans. 15, 874–5.
(
10.1042/bst0150874
) / Biochem. Soc. Trans. by A. J. Griffiths (1987) -
Harrington, W. F. (1979) On the origin of the contractile force in skeletal muscle.Proc. natn. Acad. Sci. U.S.A. 68, 685–9.
(
10.1073/pnas.68.3.685
) / Proc. natn. Acad. Sci. U.S.A. by W. F. Harrington (1979) -
Highsmith, S. &Eden, D. (1987) Limited trypsinolysis changes the dynamics of myosin subfragment-1.Biochemistry 26, 2747–50.
(
10.1021/bi00384a014
) / Biochemistry by S. Highsmith (1987) - Highsmith, S. &Jardetsky, O. (1980) Actomyosin energetics.Fedn Proc. Fed. Am. Soc. Exp. Biol. 39, 1881. / Fedn Proc. Fed. Am. Soc. Exp. Biol. by S. Highsmith (1980)
-
Hirono, M., Endo, H., Okada, N., Numata, O. &Watanabe, Y. (1987) Tetrahymena actin. Cloning and sequencing of the Tetrahymena actin gene and its identification of its gene product.J. molec. Biol. 194, 181–92.
(
10.1016/0022-2836(87)90367-6
) / J. molec. Biol. by M. Hirono (1987) -
Hoshimaru, M. &Nakanishi, S. (1987) Identification of a new type of mammalian myosin heavy chain by molecular cloning.J. biol. Chem. 262, 14625–32.
(
10.1016/S0021-9258(18)47842-8
) / J. biol. Chem. by M. Hoshimaru (1987) -
Hozumi, T. (1983) Structure and function of myosin subfragment-1 as studied by tryptic digestion.Biochemistry 22, 799–804.
(
10.1021/bi00273a014
) / Biochemistry by T. Hozumi (1983) -
Hynes, T. R., Block, S. M., White, B. T. &Spudich, J. A. (1987) Movement of myosin fragments in vitro: Domains involved in force production.Cell,48, 953–63.
(
10.1016/0092-8674(87)90704-5
) / Cell by T. R. Hynes (1987) -
Jacobson, G. R. &Rosenbusch, J. P. (1976) ATP binding to a protease-resistant core of action.Proc. natn. Acad. Sci. U.S.A. 73, 2742–6.
(
10.1073/pnas.73.8.2742
) / Proc. natn. Acad. Sci. U.S.A. by G. R. Jacobson (1976) -
Johnson, P., Wester, P. J. &Hikida, R. S. (1979) Protein-protein interactions of proteolytic fragments of actin.Biochim. Biophys. Acta 578, 253–7.
(
10.1016/0005-2795(79)90133-8
) / Biochim. Biophys. Acta by P. Johnson (1979) -
Jung, G., Korn, E. D. &Hammer, J. A. III (1987) The heavy chain ofAcanthamoeba myosin IB is a fusion of a myosin-like and non-myosin like sequences.Proc. natn. Acad. Sci. U.S.A. 84, 6720–4.
(
10.1073/pnas.84.19.6720
) / Proc. natn. Acad. Sci. U.S.A. by G. Jung (1987) -
Knight, P. &Offer, G. (1978) p-NN′-phenylene-bismaleimide, a specific cross-linking for F-actin.Biochem. J. 175, 1023–32.
(
10.1042/bj1751023
) / Biochem. J. by P. Knight (1978) -
Konno, K. (1988) G-actin structure revealed by chymotryptic digestion.J. Biochem. (Tokyo) 103, 386–92.
(
10.1093/oxfordjournals.jbchem.a122279
) / J. Biochem. (Tokyo) by K. Konno (1988) -
Korn, E. D. (1982) Actin polymerization and its regulation by protein from nonmuscle cells.Physiol. Rev. 62, 672–737.
(
10.1152/physrev.1982.62.2.672
) / Physiol. Rev. by E. D. Korn (1982) - Labbe, J. P. (1985) Etude structurale et fonctionnelle du complexe de rigueur F-actine-tête globulaires de myosine de muscle squelettique.Thesis of Dr Ingenieur Montpellier.
-
Lehrer, S. S. (1981) Damage of actin filaments by glutharaldehyde: protection by tropomyosin.J. cell. Biol. 90, 459–66.
(
10.1083/jcb.90.2.459
) / J. cell. Biol. by S. S. Lehrer (1981) -
Lu, R. C. &Wong, A. (1988) Topography of myosin S1: identification of sites on the 25 kDa domain that are close to SH1 by intramolecular crosslinking.Biophys. J. 53, 175a.
(
10.1016/S0006-3495(88)83079-0
) / Biophys. J. by R. C. Lu (1988) -
Lynch, J. T., Albanesi, J. P., Korn, E. D., Robinson, E. A., Bowers, B. &Fujisaki, H. (1986) ATPase activities and actin binding properties of subfragments ofAcanthamoeba myosin LA.J. biol. Chem. 261, 17156–62.
(
10.1016/S0021-9258(19)76012-8
) / J. biol. Chem. by J. T. Lynch (1986) - Lynch, T. J., Brzeska, H. &Korn, E. D. (1987) Actin-binding domains of myosin I.J. cell. Biol. 105, 115a. / J. cell. Biol. by T. J. Lynch (1987)
-
Mejean, C., Boyer, M., Labbe, J. P., Derancourt, J., Benyamin, Y. &Roustan, C. (1986) Antigenic probes locate the myosin subfragment-1 interaction site on the N-terminal part of actin.Biosci. Rep. 6, 493–9.
(
10.1007/BF01116141
) / Biosci. Rep. by C. Mejean (1986) -
Mejean, C., Boyer, M., Labbe, J. P., Marlier, L., Benyamin, Y. &Roustan, C. (1987) Anti-actin antibodies, an immunological approach to the myosin actin and the tropomyosin-actin interface.Biochem. J. 244, 571–7.
(
10.1042/bj2440571
) / Biochem. J. by C. Mejean (1987) -
Millar, N. C. &Geeves, M. A. (1988) Protein fluorescence changes associated with ATP and adenosine 5′-(γ-thio)-triphosphate binding to skeletal muscle myosin subfragment 1 and actomyosin subfragment 1.Biochem. J. 249, 735–43.
(
10.1042/bj2490735
) / Biochem. J. by N. C. Millar (1988) -
Miller, L., Kalnoski, M., Yunossi, Z., Bulinski, J. C. &Reisler, E. (1987) Antibodies directed against N-terminal residues on actin do not block acto-myosin binding.Biochemistry 26, 6064–70.
(
10.1021/bi00393a018
) / Biochemistry by L. Miller (1987) -
Miller, L., Phillips, M. &Reisler, E. (1988) Polymerization of G-actin by myosin subfragment-1.J. biol. Chem. 263, 1996–2002.
(
10.1016/S0021-9258(19)77976-9
) / J. biol. Chem. by L. Miller (1988) -
Mimura, N. &Asano, A. (1987) Further characterization of a conserved actin-binding 27 kDa fragment of actinogelin and alpha actinins and mapping of their binding sites cm the actin molecule by chemical cross-linking.J. biol. Chem. 262, 4717–23.
(
10.1016/S0021-9258(18)61254-2
) / J. biol. Chem. by N. Mimura (1987) -
Miyata, M., Arata, T. &Inoue, A. (1988) Reaction of the two heads of gizzard myosin with ATP.J. Biochem. 103, 336–41.
(
10.1093/oxfordjournals.jbchem.a122271
) / J. Biochem. by M. Miyata (1988) -
Mockrin, S. C. &Korn, E. D. (1981) Isolation and characterization of covalently cross-linked actin dimer.J. biol. Chem. 256, 8228–33.
(
10.1016/S0021-9258(18)43413-8
) / J. biol. Chem. by S. C. Mockrin (1981) - Moir, A. J. G. &Levine, B. A. (1986) Protein cognitive sites on the surface of actin. A proton NMR studyJ. Inorganic Chem. 27, 271–8. / J. Inorganic Chem. by A. J. G. Moir (1986)
-
Morales, M. F. &Botts, J. (1979) On the molecular basis for chemomechanical energy transduction in muscle.Proc. natn. Acad. Sci. U.S.A. 76, 3857–9.
(
10.1073/pnas.76.8.3857
) / Proc. natn. Acad. Sci. U.S.A. by M. F. Morales (1979) -
Mornet, D., Bertrand, R., Pantel, P., Audemard, E. &Kassab, R. (1981) Structure of the actin interface.Nature 292, 301–6.
(
10.1038/292301a0
) / Nature by D. Mornet (1981) -
Mornet, D., Der Terrossian, E., Pradel, L. A., Kassab, R. &Barman, T. E. (1977) The reaction of myosin with a bromoalkyl analog of adenosine triphosphate.FEBS Lett. 84, 362–6.
(
10.1016/0014-5793(77)80725-4
) / FEBS Lett. by D. Mornet (1977) -
Mornet, D., &Ue, K. (1985) Proteolysis and structure of skeletal muscle actin.Proc. natn. Acad. Sci. U.S.A. 81, 3680–4.
(
10.1073/pnas.81.12.3680
) / Proc. natn. Acad. Sci. U.S.A. by D. Mornet (1985) -
Mornet, D., Ue, K. &Morales, M. F. (1985) Stabilization of a primary loop in myosin subfragment-1 using fluorescent crosslinker.Proc. natn. Acad. Sci. U.S.A. 82, 1658–62.
(
10.1073/pnas.82.6.1658
) / Proc. natn. Acad. Sci. U.S.A. by D. Mornet (1985) -
Muhlrad, A. &Morales, M. F. (1984) Isolation and partial renaturation of proteolytic fragments of the myosin head.Proc. natn. Acad. Sci. U.S.A. 81, 1003–7.
(
10.1073/pnas.81.4.1003
) / Proc. natn. Acad. Sci. U.S.A. by A. Muhlrad (1984) -
Mumeyuki, E., Nishida, E., Sutoh, K. &Sakai, H. (1985) Purification of cofilin, a 21,000 molecular weight actin binding protein from porcine kidney and identification of the cofilin-binding site in the actin sequence.J. Biochem. (Tokyo) 97, 563–8.
(
10.1093/oxfordjournals.jbchem.a135091
) / J. Biochem. (Tokyo) by E. Mumeyuki (1985) -
Muszbek, L. &Laki, K. (1975) Cleavage of actin by thrombin.Proc. natn. Acad. Sci. U.S.A. 71, 2208–11.
(
10.1073/pnas.71.6.2208
) / Proc. natn. Acad. Sci. U.S.A. by L. Muszbek (1975) -
Oharra, O., Takahashi, S., Ooi, T. &Fujiyoshi, Y. (1982) Crosslinking study on skeletal muscle actin: Properties of suberimidate treated actin.J. Biochem. (Tokyo) 91, 1999–2012.
(
10.1093/oxfordjournals.jbchem.a133893
) / J. Biochem. (Tokyo) by O. Oharra (1982) -
Okamoto, Y. &Sekine, T. (1987) A new, smaller actin-activable myosin subfragment-1 which lacks the 20kDa, SH1 and SH2 peptide.J. biol. Chem. 262, 7951–4.
(
10.1016/S0021-9258(18)47509-6
) / J. biol. Chem. by Y. Okamoto (1987) -
Rajasekharan, K. N., Sivaramakrishnan, M. &Burke, M. (1987) Proximity and ligand-induced movement of inter domain residues in myosin subfragment-1 containing trapped MgATP and MgPPi probed by multifunctional crosslinking.J. biol. Chem. 262, 11207–14.
(
10.1016/S0021-9258(18)60945-7
) / J. biol. Chem. by K. N. Rajasekharan (1987) -
Rouayrenc, J. F., Fattoum, A., Mejean, C. &Kassab, R. (1986) Characterization of the calcium-induced conformational changes in gelsolin and identification of interaction regions between actin and gelsolin.Biochemistry 25, 3859–67.
(
10.1021/bi00361a018
) / Biochemistry by J. F. Rouayrenc (1986) -
Shriver, J. W. (1986) The structure of myosin and its role in energy transduction in muscle.Biochem. Cell Biol. 64, 265–76.
(
10.1139/o86-038
) / Biochem. Cell Biol. by J. W. Shriver (1986) -
Shuckla, K. K., Levy, H. M., Ramirez, F., Marecek, J. F., Meyerson, S. &Kuhn, E. S. (1980) Distribution of18OPi species from γ18O ATP hydrolysis by myosin and heavy meromyosin.J. biol. Chem. 255, 11344–50.
(
10.1016/S0021-9258(19)70298-1
) / J. biol. Chem. by K. K. Shuckla (1980) -
Shuckla, K. K., Ramirez, J., Marecek, J. F. &Levy, H. M. (1979) A mechanism for the hydrolysis of MgATP by actomyosin of skeletal muscle.J. theor. Biol. 76, 359–67.
(
10.1016/0022-5193(79)90318-7
) / J. theor. Biol. by K. K. Shuckla (1979) -
Sutoh, K. (1982) Identification of myosin-binding sites on the actin sequence.Biochemistry 21, 3654–61.
(
10.1021/bi00258a020
) / Biochemistry by K. Sutoh (1982) -
Sutoh, K. (1987) A short hydrophobic segment next to trp 130 in the myosin heavy chain is close to the ribose of ADP bound in the ATPase site.Biochemistry 26, 7648–54.
(
10.1021/bi00398a018
) / Biochemistry by K. Sutoh (1987) -
Sutoh, K. &Hatano, S. (1986) Actin-fragmin interactions as revealed by chemical crosslinking.Biochemistry 25, 435–40.
(
10.1021/bi00350a024
) / Biochemistry by K. Sutoh (1986) -
Sutoh, K. &Hiratsuka, T. (1988) Spatial proximity of the glycine-rich loop and the SH2 thiol in myosin subfragment-1.Biochemistry 27, 2964–9.
(
10.1021/bi00408a045
) / Biochemistry by K. Sutoh (1988) -
Sutoh, K. &Mabuchi, I. (1984) N-terminal and C-terminal segments of actin participate in binding depactin, an actin-depolymerizing protein from star-fish oocytes.Biochemistry,23, 6757–61.
(
10.1021/bi00321a073
) / Biochemistry by K. Sutoh (1984) -
Sutoh, K. &Lu, R. C. (1987) Identification of two segments, separated by 45 kilodaltons, of the myosin subfragment-1 heavy chain that can be crosslinked to the SH1 thiol.Biochemistry 26, 4511–6.
(
10.1021/bi00388a051
) / Biochemistry by K. Sutoh (1987) -
Sutoh, K., Yamamoto, K. &Wakabayashi, T. (1984) Electron microscopic visualization of the SH1 thiol of myosin by the use of an avidin-biotin system.J. molec. Biol. 178, 323–39.
(
10.1016/0022-2836(84)90147-5
) / J. molec. Biol. by K. Sutoh (1984) -
Suzuki, R., Nishi, N., Tokura, S. &Morita, F. (1987) F-actin binding synthetic heptapeptide having the amino acid sequence around the SH1 cysteinyl residue of myosin.J. biol. Chem. 262, 11410–2.
(
10.1016/S0021-9258(18)60821-X
) / J. biol. Chem. by R. Suzuki (1987) -
Tokunaga, M., Sutoh, K., Toyoshima, C. &Wakabayashi, T. (1987) Location of the ATPase site of myosin determined by three-dimensional electron microscopy.Nature 329, 635–8.
(
10.1038/329635a0
) / Nature by M. Tokunaga (1987) -
Toyoshima, C. &Wakabayashi, T. (1985) Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle.J. Biochem. (Tokyo) 97, 245–63.
(
10.1093/oxfordjournals.jbchem.a135049
) / J. Biochem. (Tokyo) by C. Toyoshima (1985) -
Toyoshima, Y. Y., Kron, S. J., Mc-Nally, E. M., Niebling, K. R., Toyoshima, C. &Spudich, J. A. (1987) Myosin subfragment-1 is sufficient to move actin filamentsin vitro.Nature 328, 536–9.
(
10.1038/328536a0
) / Nature by Y. Y. Toyoshima (1987) -
Ue, K. (1987) Intramolecular crosslinking of myosin subfragment-1 with bimane.Biochemistry 26, 1889–94.
(
10.1021/bi00381a016
) / Biochemistry by K. Ue (1987) -
Wakabayashi, T. &Toyoshima, C. (1981) Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle. the multi-domain structure of actin-myosin-Sl complex.J. Biochem. (Tokyo) 90, 683–701.
(
10.1093/oxfordjournals.jbchem.a133523
) / J. Biochem. (Tokyo) by T. Wakabayashi (1981) -
Walker, J. E., Saraste, M., Runswick, M. J. &Gay, N. J. (1982) Distantly related sequences in the alpha and beta subunits of ATP synthetase, myosin, kinases, and other ATP-requiring enzymes and a common nucleotide binding fold.EMBO. J. 1, 945–51.
(
10.1002/j.1460-2075.1982.tb01276.x
) / EMBO. J. by J. E. Walker (1982) -
Wells, J. A. &Yount, R. G. (1982) Chemical modification of myosin by active site trapping of metal-nucleotide with crosslinking reagents.Meth. Enzymol. 85, 93–123.
(
10.1016/0076-6879(82)85013-1
) / Meth. Enzymol. by J. A. Wells (1982) -
Yanagisawa, M., Hamada, Y., Katsuragawa, Y. Imamura, M., Mikawa, T. &Masaki, T. (1987) Complete primary structure of vertebrate smooth muscle myosin heavy chain deduced from its complementary DNA sequence.J. molec. Biol. 198, 143–57.
(
10.1016/0022-2836(87)90302-0
) / J. molec. Biol. by M. Yanagisawa (1987) - Yee, D., Wiedner, H. &Eckstein, F. (1980) Biphasic steady-state kinetics of myosin adenosine triphosphatase.Eur. J. Biochem. 133, 85–90. / Eur. J. Biochem. by D. Yee (1980)
-
Yount, R. G., Frye, R. &O'Keefe, K. (1972) Inhibition of heavy meromyosin by purine disulfide analogs of adenosine triphosphate.Cold Spring. Harb. Symp. quant. Biol. 37, 113–20.
(
10.1101/SQB.1973.037.01.017
) / Cold Spring. Harb. Symp. quant. Biol. by R. G. Yount (1972)
Dates
Type | When |
---|---|
Created | 20 years, 2 months ago (June 17, 2005, 4:07 a.m.) |
Deposited | 4 years, 1 month ago (July 11, 2021, 7:28 p.m.) |
Indexed | 1 year, 5 months ago (March 17, 2024, 6:12 p.m.) |
Issued | 36 years, 7 months ago (Feb. 1, 1989) |
Published | 36 years, 7 months ago (Feb. 1, 1989) |
Published Print | 36 years, 7 months ago (Feb. 1, 1989) |
@article{Mornet_1989, title={Functional sequences of the myosin head}, volume={10}, ISSN={1573-2657}, url={http://dx.doi.org/10.1007/bf01739853}, DOI={10.1007/bf01739853}, number={1}, journal={Journal of Muscle Research and Cell Motility}, publisher={Springer Science and Business Media LLC}, author={Mornet, Dominique and Bonet, Armelle and Audemard, Etienne and Bonicel, Jacques}, year={1989}, month=feb, pages={10–24} }