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Volumn 85, Issue 4, 2003, Pages 2073-2074

Solution properties of TMR-actin: When biochemical and crystal data agree

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; F ACTIN; G ACTIN; MALEIMIDE DERIVATIVE; TETRAMETHYLRHODAMINE 5 MALEIMIDE; UNCLASSIFIED DRUG;

EID: 0141865627     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74635-9     Document Type: Note
Times cited : (7)

References (11)
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    • Belmont, L. D., A. Orlova, D. G. Drubin, and E. H. Egelman. 1999. A change in actin conformation associated with filament instability after Pi release. Proc. Natl. Acad. Sci. USA. 96:29-34.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 29-34
    • Belmont, L.D.1    Orlova, A.2    Drubin, D.G.3    Egelman, E.H.4
  • 2
    • 0034870406 scopus 로고    scopus 로고
    • Actin allostery again?
    • Egelman, E. H. 2001. Actin allostery again? Nat. Struct. Biol. 8:735-736.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 735-736
    • Egelman, E.H.1
  • 3
    • 0141445972 scopus 로고    scopus 로고
    • Crystal structure of monomeric actin in the ATP state. Structural basis of nucleotide-dependent actin dynamics
    • Graceffa, P., and R. Dominguez. 2003. Crystal structure of monomeric actin in the ATP state. Structural basis of nucleotide-dependent actin dynamics. J. Biol. Chem. 278:34172-34180.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34172-34180
    • Graceffa, P.1    Dominguez, R.2
  • 4
    • 0028871340 scopus 로고
    • Conformational changes in subdomain 2 of G-actin: Fluorescence probing by dansyl ethylenediamine attached to Gln-41
    • Kim, E., M. Motoki, K. Seguro, A. Muhlrad, and E. Reisler. 1995. Conformational changes in subdomain 2 of G-actin: fluorescence probing by dansyl ethylenediamine attached to Gln-41. Biophys. J. 69:2024-2032.
    • (1995) Biophys. J. , vol.69 , pp. 2024-2032
    • Kim, E.1    Motoki, M.2    Seguro, K.3    Muhlrad, A.4    Reisler, E.5
  • 5
    • 0141707869 scopus 로고    scopus 로고
    • Solution properties of tetramethylrhodamine modified G-actin
    • Kudryashov, D. S., and E. Reisler. 2003. Solution properties of tetramethylrhodamine modified G-actin. Biophys. J. 85:2466-2475.
    • (2003) Biophys. J. , vol.85 , pp. 2466-2475
    • Kudryashov, D.S.1    Reisler, E.2
  • 6
    • 0035958757 scopus 로고    scopus 로고
    • The crystal structure of uncomplexed actin in the ADP state
    • Otterbein, L. R., P. Graceffa, and R. Dominguez. 2001. The crystal structure of uncomplexed actin in the ADP state. Science. 293:708-711.
    • (2001) Science , vol.293 , pp. 708-711
    • Otterbein, L.R.1    Graceffa, P.2    Dominguez, R.3
  • 7
    • 0033895234 scopus 로고    scopus 로고
    • Molecular mechanisms controlling actin filament dynamics in nonmuscle cells
    • Pollard, T. D., L. Blanchoin, and R. D. Mullins. 2000. Molecular mechanisms controlling actin filament dynamics in nonmuscle cells. Annu. Rev. Biophys. Biomol. Struct. 29:545-576.
    • (2000) Annu. Rev. Biophys. Biomol. Struct. , vol.29 , pp. 545-576
    • Pollard, T.D.1    Blanchoin, L.2    Mullins, R.D.3
  • 9
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    • Thermal unfolding of G-actin monitored with the DNase I-inhibition assay stabilities of actin isoforms
    • Schuler, H., U. Lindberg, C. E. Schutt, and R. Karlsson. 2000. Thermal unfolding of G-actin monitored with the DNase I-inhibition assay stabilities of actin isoforms. Eur. J. Biochem. 267:476-486.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 476-486
    • Schuler, H.1    Lindberg, U.2    Schutt, C.E.3    Karlsson, R.4
  • 11
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    • Localization of the tightly bound divalentcation-dependent and nucleotide-dependent conformation changes in G-actin using limited proteolytic digestion
    • Strzelecka-Golaszewska, H., J. Moraczewska, S. Y. Khaitlina, and M. Mossakowska. 1993. Localization of the tightly bound divalentcation-dependent and nucleotide-dependent conformation changes in G-actin using limited proteolytic digestion. Eur. J. Biochem. 211:731-742.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.