The size and shape of caldesmon and its fragments in solution studied by dynamic light scattering and hydrodynamic model calculations
Czurylo EA, Hellweg T, Eimer W, Dabrowska R (1997)
Biophysical Journal 72(2): 835-842.
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The size and the shape of caldesmon as well as its 50-kDa central and 19-kDa C-terminal fragments were investigated by photon correlation spectroscopy. The hydrodynamic radii, which have been calculated from the experimentally obtained translational diffusion coefficients, are 9.8 nm, 6.0 nm, and 2.9 nm, respectively. Moreover, the experimental values for the translational diffusion coefficients are compared with results obtained from hydrodynamic model calculations. Detailed models for the structure of caldesmon in solution are derived. The contour length is about 64 nm for all of the models used for caldesmon.
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Czurylo EA, Hellweg T, Eimer W, Dabrowska R. The size and shape of caldesmon and its fragments in solution studied by dynamic light scattering and hydrodynamic model calculations. Biophysical Journal. 1997;72(2):835-842.
Czurylo, E. A., Hellweg, T., Eimer, W., & Dabrowska, R. (1997). The size and shape of caldesmon and its fragments in solution studied by dynamic light scattering and hydrodynamic model calculations. Biophysical Journal, 72(2), 835-842.
Czurylo, E. A., Hellweg, T., Eimer, W., and Dabrowska, R. (1997). The size and shape of caldesmon and its fragments in solution studied by dynamic light scattering and hydrodynamic model calculations. Biophysical Journal 72, 835-842.
Czurylo, E.A., et al., 1997. The size and shape of caldesmon and its fragments in solution studied by dynamic light scattering and hydrodynamic model calculations. Biophysical Journal, 72(2), p 835-842.
E.A. Czurylo, et al., “The size and shape of caldesmon and its fragments in solution studied by dynamic light scattering and hydrodynamic model calculations”, Biophysical Journal, vol. 72, 1997, pp. 835-842.
Czurylo, E.A., Hellweg, T., Eimer, W., Dabrowska, R.: The size and shape of caldesmon and its fragments in solution studied by dynamic light scattering and hydrodynamic model calculations. Biophysical Journal. 72, 835-842 (1997).
Czurylo, EA, Hellweg, Thomas, Eimer, W, and Dabrowska, R. “The size and shape of caldesmon and its fragments in solution studied by dynamic light scattering and hydrodynamic model calculations”. Biophysical Journal 72.2 (1997): 835-842.
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Data provided by Europe PubMed Central.
Hyphenated analytical techniques for multidimensional characterisation of submicron particles: a review.
Lespes G, Gigault J., Anal. Chim. Acta 692(1-2), 2011
PMID: 21501709
Lespes G, Gigault J., Anal. Chim. Acta 692(1-2), 2011
PMID: 21501709
43 References
Data provided by Europe PubMed Central.
What is latch? New ideas about tonic contraction in smooth muscle.
Marston SB., J. Muscle Res. Cell. Motil. 10(2), 1989
PMID: 2668329
Marston SB., J. Muscle Res. Cell. Motil. 10(2), 1989
PMID: 2668329
The molecular anatomy of caldesmon.
Marston SB, Redwood CS., Biochem. J. 279 ( Pt 1)(), 1991
PMID: 1930128
Marston SB, Redwood CS., Biochem. J. 279 ( Pt 1)(), 1991
PMID: 1930128
Inhibition of actin-tropomyosin activation of myosin MgATPase activity by the smooth muscle regulatory protein caldesmon.
Marston SB, Redwood CS., J. Biol. Chem. 267(24), 1992
PMID: 1387396
Marston SB, Redwood CS., J. Biol. Chem. 267(24), 1992
PMID: 1387396
Caldesmon and the structure of smooth muscle thin filaments: electron microscopy of isolated thin filaments.
Moody C, Lehman W, Craig R., J. Muscle Res. Cell. Motil. 11(2), 1990
PMID: 2351755
Moody C, Lehman W, Craig R., J. Muscle Res. Cell. Motil. 11(2), 1990
PMID: 2351755
Landmark mapping: a general method for localizing cysteine residues within a protein.
Nefsky B, Bretscher A., Proc. Natl. Acad. Sci. U.S.A. 86(10), 1989
PMID: 2726736
Nefsky B, Bretscher A., Proc. Natl. Acad. Sci. U.S.A. 86(10), 1989
PMID: 2726736
The calmodulin and F-actin binding sites of smooth muscle caldesmon lie in the carboxyl-terminal domain whereas the molecular weight heterogeneity lies in the middle of the molecule.
Riseman VM, Lynch WP, Nefsky B, Bretscher A., J. Biol. Chem. 264(5), 1989
PMID: 2914935
Riseman VM, Lynch WP, Nefsky B, Bretscher A., J. Biol. Chem. 264(5), 1989
PMID: 2914935
The mechanism of Ca2+ regulation of vascular smooth muscle thin filaments by caldesmon and calmodulin.
Smith CW, Pritchard K, Marston SB., J. Biol. Chem. 262(1), 1987
PMID: 2947901
Smith CW, Pritchard K, Marston SB., J. Biol. Chem. 262(1), 1987
PMID: 2947901
Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin.
Sobue K, Muramoto Y, Fujita M, Kakiuchi S., Proc. Natl. Acad. Sci. U.S.A. 78(9), 1981
PMID: 6946503
Sobue K, Muramoto Y, Fujita M, Kakiuchi S., Proc. Natl. Acad. Sci. U.S.A. 78(9), 1981
PMID: 6946503
Caldesmon, a novel regulatory protein in smooth muscle and nonmuscle actomyosin systems.
Sobue K, Sellers JR., J. Biol. Chem. 266(19), 1991
PMID: 2061300
Sobue K, Sellers JR., J. Biol. Chem. 266(19), 1991
PMID: 2061300
Turkey gizzard caldesmon molecular weight and shape.
Stafford WF, Chalovich JM, Graceffa P., Arch. Biochem. Biophys. 313(1), 1994
PMID: 8053685
Stafford WF, Chalovich JM, Graceffa P., Arch. Biochem. Biophys. 313(1), 1994
PMID: 8053685
Phosphorylation of caldesmon by smooth-muscle casein kinase II.
Sutherland C, Renaux BS, McKay DJ, Walsh MP., J. Muscle Res. Cell. Motil. 15(4), 1994
PMID: 7806638
Sutherland C, Renaux BS, McKay DJ, Walsh MP., J. Muscle Res. Cell. Motil. 15(4), 1994
PMID: 7806638
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 RH, Chalovich JM., J. Biol. Chem. 265(5), 1990
PMID: 2137453
Velaz L, Ingraham RH, Chalovich JM., J. Biol. Chem. 265(5), 1990
PMID: 2137453
Three-dimensional reconstruction of caldesmon-containing smooth muscle thin filaments.
Vibert P, Craig R, Lehman W., J. Cell Biol. 123(2), 1993
PMID: 8408215
Vibert P, Craig R, Lehman W., J. Cell Biol. 123(2), 1993
PMID: 8408215
Phosphorylation of aorta caldesmon by endogenous proteolytic fragments of protein kinase C.
Vorotnikov AV, Gusev NB, Hua S, Collins JH, Redwood CS, Marston SB., J. Muscle Res. Cell. Motil. 15(1), 1994
PMID: 8182108
Vorotnikov AV, Gusev NB, Hua S, Collins JH, Redwood CS, Marston SB., J. Muscle Res. Cell. Motil. 15(1), 1994
PMID: 8182108
The Ayerst Award Lecture 1990. Calcium-dependent mechanisms of regulation of smooth muscle contraction.
Walsh MP., Biochem. Cell Biol. 69(12), 1991
PMID: 1818584
Walsh MP., Biochem. Cell Biol. 69(12), 1991
PMID: 1818584
A long helix from the central region of smooth muscle caldesmon.
Wang CL, Chalovich JM, Graceffa P, Lu RC, Mabuchi K, Stafford WF., J. Biol. Chem. 266(21), 1991
PMID: 1856225
Wang CL, Chalovich JM, Graceffa P, Lu RC, Mabuchi K, Stafford WF., J. Biol. Chem. 266(21), 1991
PMID: 1856225
Localization of the calmodulin- and the actin-binding sites of caldesmon.
Wang CL, Wang LW, Xu SA, Lu RC, Saavedra-Alanis V, Bryan J., J. Biol. Chem. 266(14), 1991
PMID: 2026616
Wang CL, Wang LW, Xu SA, Lu RC, Saavedra-Alanis V, Bryan J., J. Biol. Chem. 266(14), 1991
PMID: 2026616
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