메뉴 건너뛰기




Volumn 79, Issue 3, 2000, Pages 1524-1529

ADP inhibition of myosin V ATPase activity

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; MYOSIN;

EID: 0033850082     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76403-4     Document Type: Article
Times cited : (123)

References (12)
  • 1
    • 0033618274 scopus 로고    scopus 로고
    • Transient kinetic analysis of the 130-kDa myosin-I (MYR-1 gene product) from rat liver
    • Coluccio, L. M., and M. A. Geeves. 1999. Transient kinetic analysis of the 130-kDa myosin-I (MYR-1 gene product) from rat liver. J. Biol. Chem. 274:21575-21580.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21575-21580
    • Coluccio, L.M.1    Geeves, M.A.2
  • 3
    • 0032485859 scopus 로고    scopus 로고
    • Modulation of actin affinity and actomyosin adenosine triphosphatase by charge changes in the myosin motor domain
    • Furch, M., M. Geeves, and D. J. Manstein. 1998. Modulation of actin affinity and actomyosin adenosine triphosphatase by charge changes in the myosin motor domain. Biochemistry. 37:6317-6326.
    • (1998) Biochemistry , vol.37 , pp. 6317-6326
    • Furch, M.1    Geeves, M.2    Manstein, D.J.3
  • 5
    • 0019135186 scopus 로고
    • Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association
    • MacLean-Fletcher, S., and T. D. Pollard. 1980. Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association. Biochem. Biophys. Res. Commun. 96:18-27.
    • (1980) Biochem. Biophys. Res. Commun. , vol.96 , pp. 18-27
    • MacLean-Fletcher, S.1    Pollard, T.D.2
  • 8
    • 0015834603 scopus 로고
    • Acanthamoeba myosin. I. Isolation from Acanthamoeba castellanii of an enzyme similar to muscle myosin
    • Pollard, T. D., and E. D. Korn. 1973. Acanthamoeba myosin. I. Isolation from Acanthamoeba castellanii of an enzyme similar to muscle myosin. J. Biol. Chem. 248:4682-4690.
    • (1973) J. Biol. Chem. , vol.248 , pp. 4682-4690
    • Pollard, T.D.1    Korn, E.D.2
  • 9
    • 0031149266 scopus 로고    scopus 로고
    • Motor proteins: Myosin V - The multi-purpose transport motor
    • Titus, M. A. 1997. Motor proteins: myosin V - the multi-purpose transport motor. Curr. Biol. 7:R301-R304.
    • (1997) Curr. Biol. , vol.7
    • Titus, M.A.1
  • 10
    • 0033600904 scopus 로고    scopus 로고
    • Kinetic characterization of a monomeric unconventional myosin V construct
    • Trybus, K. M., E. Krementsova, and Y. Freyzon. 1999. Kinetic characterization of a monomeric unconventional myosin V construct. J. Biol. Chem. 274:27448-27456.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27448-27456
    • Trybus, K.M.1    Krementsova, E.2    Freyzon, Y.3
  • 11
    • 0034635409 scopus 로고    scopus 로고
    • Effect of ADP and ionic strength on the kinetic and motile properties of recombinant mouse myosin V
    • Wang, F., L. Chen, O. Arcucci, E. V. Harvey, B. Bowers, Y. Xu, J. A. Hammer, and J. Sellers. 2000. Effect of ADP and ionic strength on the kinetic and motile properties of recombinant mouse myosin V. J. Biol. Chem. 275:4329-4335.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4329-4335
    • Wang, F.1    Chen, L.2    Arcucci, O.3    Harvey, E.V.4    Bowers, B.5    Xu, Y.6    Hammer, J.A.7    Sellers, J.8
  • 12
    • 0020013525 scopus 로고
    • Special instrumentation and techniques for kinetic studies of contractile systems
    • White, H. D. 1982. Special instrumentation and techniques for kinetic studies of contractile systems. Methods Enzymol. 85:698-708.
    • (1982) Methods Enzymol. , vol.85 , pp. 698-708
    • White, H.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.