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Volumn 24, Issue 4-6, 2003, Pages 315-321

Probing nucleotide dissociation from myosin in vitro using microgram quantities of myosin

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; COUMARIN; MYOSIN II; MYOSIN SUBFRAGMENT 1; NUCLEOTIDE;

EID: 0142156181     PISSN: 01424319     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Conference Paper
Times cited : (9)

References (26)
  • 1
    • 0016233229 scopus 로고
    • The characterization of myosin-product complexes and of product-release steps during the magnesium ion-dependent adenosine triphosphatase reaction
    • Bagshaw CR and Trentham DR (1974) The characterization of myosin-product complexes and of product-release steps during the magnesium ion-dependent adenosine triphosphatase reaction. Biochem J 141: 331-349.
    • (1974) Biochem J , vol.141 , pp. 331-349
    • Bagshaw, C.R.1    Trentham, D.R.2
  • 2
    • 0033545955 scopus 로고    scopus 로고
    • Kinetic analysis of Dictyostelium discoideum myosin motor domains with glycine-to-alanine mutations in the reactive thiol region
    • Batra R, Geeves MA and Manstein DJ (1999) Kinetic analysis of Dictyostelium discoideum myosin motor domains with glycine-to-alanine mutations in the reactive thiol region. Biochemistry 38: 6126-6134.
    • (1999) Biochemistry , vol.38 , pp. 6126-6134
    • Batra, R.1    Geeves, M.A.2    Manstein, D.J.3
  • 3
    • 0035968217 scopus 로고    scopus 로고
    • ADP binding induces an asymmetry between the heads of unphosphorylated myosin
    • Berger CE, Fagnant PM, Heizmann S, Trybus KM and Geeves MA (2001) ADP binding induces an asymmetry between the heads of unphosphorylated myosin. J Biol Chem 276: 23240-23245.
    • (2001) J Biol Chem , vol.276 , pp. 23240-23245
    • Berger, C.E.1    Fagnant, P.M.2    Heizmann, S.3    Trybus, K.M.4    Geeves, M.A.5
  • 4
    • 0033618274 scopus 로고    scopus 로고
    • Transient kinetic analysis of the 130-kDa myosin I (MYR-1 gene product) from rat liver. A myosin I designed for maintenance of tension?
    • Coluccio LM and Geeves MA (1999) Transient kinetic analysis of the 130-kDa myosin I (MYR-1 gene product) from rat liver. A myosin I designed for maintenance of tension? J Biol Chem 274: 21575-21580.
    • (1999) J Biol Chem , vol.274 , pp. 21575-21580
    • Coluccio, L.M.1    Geeves, M.A.2
  • 5
    • 0032539594 scopus 로고    scopus 로고
    • Interaction of actin and ADP with the head domain of smooth muscle myosin: Implications for strain-dependent ADP release in smooth muscle
    • Cremo CR and Geeves MA (1998) Interaction of actin and ADP with the head domain of smooth muscle myosin: implications for strain-dependent ADP release in smooth muscle. Biochemistry 37: 1969-1978.
    • (1998) Biochemistry , vol.37 , pp. 1969-1978
    • Cremo, C.R.1    Geeves, M.A.2
  • 7
    • 0020674810 scopus 로고
    • New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes
    • Hiratsuka T (1983) New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes. Biochim Biophys Acta 742: 496-508.
    • (1983) Biochim Biophys Acta , vol.742 , pp. 496-508
    • Hiratsuka, T.1
  • 8
    • 0029562245 scopus 로고
    • A 32 degree tail swing in brush border myosin I on ADP release
    • Jontes JD, Wilson-Kubalek EM and Milligan RA (1995) A 32 degree tail swing in brush border myosin I on ADP release. Nature 378: 751-753.
    • (1995) Nature , vol.378 , pp. 751-753
    • Jontes, J.D.1    Wilson-Kubalek, E.M.2    Milligan, R.A.3
  • 9
    • 0030472486 scopus 로고    scopus 로고
    • A novel stopped-flow method for measuring the affinity of actin for myosin head fragments using microgram quantities of protein
    • Kurzawa SE and Geeves MA (1996) A novel stopped-flow method for measuring the affinity of actin for myosin head fragments using microgram quantities of protein. J Muscle Res Cell Motil 17: 669-676.
    • (1996) J Muscle Res Cell Motil , vol.17 , pp. 669-676
    • Kurzawa, S.E.1    Geeves, M.A.2
  • 10
    • 0029055358 scopus 로고
    • Overexpression of myosin motor domains in Dictyostelium: Screening of transformants and purification of the affinity tagged protein
    • Manstein DJ and Hunt DM (1995) Overexpression of myosin motor domains in Dictyostelium: screening of transformants and purification of the affinity tagged protein. J Muscle Res Cell Motil 16: 325-332.
    • (1995) J Muscle Res Cell Motil , vol.16 , pp. 325-332
    • Manstein, D.J.1    Hunt, D.M.2
  • 11
    • 0020021291 scopus 로고
    • Preparation of myosin and its subfragments from rabbit skeletal muscle
    • Margossian SS and Lowey S (1982) Preparation of myosin and its subfragments from rabbit skeletal muscle. Methods Enzymol 85: 55-71.
    • (1982) Methods Enzymol , vol.85 , pp. 55-71
    • Margossian, S.S.1    Lowey, S.2
  • 12
    • 0036713581 scopus 로고    scopus 로고
    • A novel pressure-jump apparatus for the microvolume analysis of protein-ligand and protein-protein interactions: Its application to nucleotide binding to skeletal-muscle and smooth-muscle myosin subfragment-1
    • Pearson DS, Holtermann G, Ellison P, Cremo C and Geeves MA (2002) A novel pressure-jump apparatus for the microvolume analysis of protein-ligand and protein-protein interactions: its application to nucleotide binding to skeletal-muscle and smooth-muscle myosin subfragment-1. Biochem J 366: 643-651.
    • (2002) Biochem J , vol.366 , pp. 643-651
    • Pearson, D.S.1    Holtermann, G.2    Ellison, P.3    Cremo, C.4    Geeves, M.A.5
  • 14
    • 0010083875 scopus 로고
    • ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle
    • Siemankowski RF, Wiseman MO and White HD (1985) ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle. Proc Natl Acad Sci USA 82: 658-662.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 658-662
    • Siemankowski, R.F.1    Wiseman, M.O.2    White, H.D.3
  • 15
    • 0942268804 scopus 로고    scopus 로고
    • Isolation and kinetic characterisation of myosin and myosin S1 from the Drosophila indirect flight muscles
    • in press
    • Silva R, Sparrow JC and Geeves MA (in press) Isolation and kinetic characterisation of myosin and myosin S1 from the Drosophila indirect flight muscles. J Muscle Res Cell Motil.
    • J Muscle Res Cell Motil
    • Silva, R.1    Sparrow, J.C.2    Geeves, M.A.3
  • 16
    • 0028227181 scopus 로고
    • Inhibition of ATP binding to myofibrils and acto-myosin subfragment 1 by caged ATP
    • Sleep J, Herrmann C, Barman T and Travers F (1994) Inhibition of ATP binding to myofibrils and acto-myosin subfragment 1 by caged ATP. Biochemistry 33: 6038-6042.
    • (1994) Biochemistry , vol.33 , pp. 6038-6042
    • Sleep, J.1    Herrmann, C.2    Barman, T.3    Travers, F.4
  • 17
    • 0027724301 scopus 로고
    • Myosin isoforms in smooth muscle: How may they affect function and structure?
    • Somlyo AP (1993) Myosin isoforms in smooth muscle: how may they affect function and structure? J Muscle Res Cell Motil 14: 557-563.
    • (1993) J Muscle Res Cell Motil , vol.14 , pp. 557-563
    • Somlyo, A.P.1
  • 20
    • 0034870958 scopus 로고    scopus 로고
    • Fluorescent coumarin-labeled nucleotides to measure ADP release from actomyosin
    • Webb MR and Corrie JE (2001) Fluorescent coumarin-labeled nucleotides to measure ADP release from actomyosin. Biophys J 81: 1562-1569.
    • (2001) Biophys J , vol.81 , pp. 1562-1569
    • Webb, M.R.1    Corrie, J.E.2
  • 21
    • 0016752124 scopus 로고
    • Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin
    • Weeds AG and Taylor RS (1975) Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin. Nature 257: 54-56.
    • (1975) Nature , vol.257 , pp. 54-56
    • Weeds, A.G.1    Taylor, R.S.2
  • 22
    • 0033709850 scopus 로고    scopus 로고
    • A flash photolysis fluorescence/light scattering apparatus for use with sub microgram quantities of muscle proteins
    • Weiss S, Chizhov I and Geeves MA (2000) A flash photolysis fluorescence/light scattering apparatus for use with sub microgram quantities of muscle proteins. J Muscle Res Cell Motil 21: 423-432.
    • (2000) J Muscle Res Cell Motil , vol.21 , pp. 423-432
    • Weiss, S.1    Chizhov, I.2    Geeves, M.A.3
  • 23
    • 0035824536 scopus 로고    scopus 로고
    • Differing ADP release rates from myosin heavy chain isoforms define the shortening velocity of skeletal muscle fibers
    • Weiss S, Rossi R, Pellegrino MA, Bottinelli R and Geeves MA (2001) Differing ADP release rates from myosin heavy chain isoforms define the shortening velocity of skeletal muscle fibers. J Biol Chem 276: 45902-45908.
    • (2001) J Biol Chem , vol.276 , pp. 45902-45908
    • Weiss, S.1    Rossi, R.2    Pellegrino, M.A.3    Bottinelli, R.4    Geeves, M.A.5
  • 26
    • 0026018966 scopus 로고
    • Kinetics of the interaction of 2′(3′)-O-(N- methylanthraniloyl)-ATP with myosin subfragment 1 and actomyosin subfragment 1: Characterization of two acto-S1-ADP complexes
    • Woodward SK, Eccleston JF and Geeves MA (1991) Kinetics of the interaction of 2′(3′)-O-(N-methylanthraniloyl)-ATP with myosin subfragment 1 and actomyosin subfragment 1: characterization of two acto-S1-ADP complexes. Biochemistry 30: 422-430.
    • (1991) Biochemistry , vol.30 , pp. 422-430
    • Woodward, S.K.1    Eccleston, J.F.2    Geeves, M.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.