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Volumn 42, Issue C, 1997, Pages 15-18

The Effect of Phosphorylation at Ser-40 on the Structure and Thermal Stability of Tyrosine Hydroxylase

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EID: 77956740077     PISSN: 10543589     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1054-3589(08)60683-3     Document Type: Article
Times cited : (8)

References (5)
  • 1
    • 0025212130 scopus 로고
    • PH-dependent release of catecholamines from tyrosine hydroxylase and the effect of phosphorylation of Ser-40
    • Haavik J., Martínez A., and Flatmark T. PH-dependent release of catecholamines from tyrosine hydroxylase and the effect of phosphorylation of Ser-40. FEBS Lett. 262 (1990) 363-365
    • (1990) FEBS Lett. , vol.262 , pp. 363-365
    • Haavik, J.1    Martínez, A.2    Flatmark, T.3
  • 2
    • 0027354020 scopus 로고
    • Quantitative studies of the structure of proteins in solution by Fourier-transformed infrared spectroscopy
    • Arrondo J.L.R., Muga A., Castresana J., and Goñi F.M. Quantitative studies of the structure of proteins in solution by Fourier-transformed infrared spectroscopy. Prog. Biophys. Mol. Biol. 59 (1993) 23-56
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 23-56
    • Arrondo, J.L.R.1    Muga, A.2    Castresana, J.3    Goñi, F.M.4
  • 3
    • 0029810874 scopus 로고    scopus 로고
    • Conformational properties and stability of tyrosine hydroxylase studied by infrared spectroscopy
    • Martinez A., Haavik J., Flatmark T., Arrondo J.L.R., and Muga A. Conformational properties and stability of tyrosine hydroxylase studied by infrared spectroscopy. J. Biol. Chem. 271 (1996) 19737-19742
    • (1996) J. Biol. Chem. , vol.271 , pp. 19737-19742
    • Martinez, A.1    Haavik, J.2    Flatmark, T.3    Arrondo, J.L.R.4    Muga, A.5
  • 4
    • 0027987495 scopus 로고
    • Structure and thermal denaturation of crystalline and noncrystalline cytochrome oxidase as studied by infrared spectroscopy
    • Arrondo J.L.R., Castresana J., Valpuesta J.M., and Goñi F.M. Structure and thermal denaturation of crystalline and noncrystalline cytochrome oxidase as studied by infrared spectroscopy. Biochemistry 33 (1994) 11650-11655
    • (1994) Biochemistry , vol.33 , pp. 11650-11655
    • Arrondo, J.L.R.1    Castresana, J.2    Valpuesta, J.M.3    Goñi, F.M.4
  • 5
    • 0023813556 scopus 로고
    • Predicted amino acid sequence of bovine tyrosine hydroxylase and its similarity to tyrosine hydroxylases from other species
    • Saadat S., Stehle A.D., Lamouroux A., Mallet J., and Thoenen H. Predicted amino acid sequence of bovine tyrosine hydroxylase and its similarity to tyrosine hydroxylases from other species. J. Neurochem. 51 (1988) 572-578
    • (1988) J. Neurochem. , vol.51 , pp. 572-578
    • Saadat, S.1    Stehle, A.D.2    Lamouroux, A.3    Mallet, J.4    Thoenen, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.