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Volumn 59, Issue 5-6, 1996, Pages 365-366

Bacterial 3α-hydroxysteroid dehydrogenase is homologous to a fusion of bacterial ribosomal L10 and L7/12 genes

Author keywords

[No Author keywords available]

Indexed keywords

3ALPHA HYDROXYSTEROID DEHYDROGENASE; HYBRID PROTEIN; RIBOSOME PROTEIN; 3 ALPHA HYDROXYSTEROID DEHYDROGENASE (B SPECIFIC); 3(OR 17)BETA HYDROXYSTEROID DEHYDROGENASE; BACTERIAL PROTEIN; RIBOSOMAL PROTEIN L10; RIBOSOMAL PROTEIN L7 L12; RIBOSOMAL PROTEIN L7-L12;

EID: 0030300129     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-0760(96)00141-0     Document Type: Article
Times cited : (2)

References (6)
  • 1
    • 0028802303 scopus 로고
    • Cloning, sequencing and expression of Pseudomonas testosteroni gene encoding 3α-hydroxysteroid dehydrogenase
    • 1. Abalain J. H., Di Stefane S., Abalain-Collac M. L. and Floch H. H.: Cloning, sequencing and expression of Pseudomonas testosteroni gene encoding 3α-hydroxysteroid dehydrogenase. J. Steroid Biochem. Molec. Biol. 55 (1995) 233-238.
    • (1995) J. Steroid Biochem. Molec. Biol. , vol.55 , pp. 233-238
    • Abalain, J.H.1    Di Stefane, S.2    Abalain-Collac, M.L.3    Floch, H.H.4
  • 2
    • 0001572325 scopus 로고
    • Purification and properties of a 3α-hydroxysteroid dehydrogenase from Pseudomonas testosteroni
    • 2. Boyer J., Baron D. N. and Talalay P.: Purification and properties of a 3α-hydroxysteroid dehydrogenase from Pseudomonas testosteroni. Biochemistry 4 (1965) 1825-1833.
    • (1965) Biochemistry , vol.4 , pp. 1825-1833
    • Boyer, J.1    Baron, D.N.2    Talalay, P.3
  • 4
    • 0026184024 scopus 로고
    • Genealogy of regulation of human sex and adrenal function, prostaglandin action, snapdragon and petunia flower colors, antibiotics, and nitrogen fixation: Functional diversity from two ancestral dehydrogenases
    • 4. Baker M. E.: Genealogy of regulation of human sex and adrenal function, prostaglandin action, snapdragon and petunia flower colors, antibiotics, and nitrogen fixation: functional diversity from two ancestral dehydrogenases. Steroids 56 (1991) 354-360.
    • (1991) Steroids , vol.56 , pp. 354-360
    • Baker, M.E.1
  • 5
    • 0030059256 scopus 로고    scopus 로고
    • Unusual evolution of mammalian 11β-and 17β-hydroxysteroid and retinol dehydrogenases
    • 5. Baker M. E.: Unusual evolution of mammalian 11β-and 17β-hydroxysteroid and retinol dehydrogenases. Bioessays 18 (1996) 63-70.
    • (1996) Bioessays , vol.18 , pp. 63-70
    • Baker, M.E.1
  • 6
    • 0026786288 scopus 로고
    • The C-terminal domain of Escherichia coli ribosomal protein L7/ L12 can occupy a location near the factor-binding domain of the 50S subunit as shown by cross-linking with N-[4-(p-Azidosalicylamido)butyl]-3-(2′-pyridyldithio)propionamide
    • 6. Zecherle G. N., Oleinikov A. and Traut R. R.: The C-terminal domain of Escherichia coli ribosomal protein L7/ L12 can occupy a location near the factor-binding domain of the 50S subunit as shown by cross-linking with N-[4-(p-Azidosalicylamido)butyl]-3-(2′-pyridyldithio)propionamide. Biochemistry 31 (1992) 9526-9532.
    • (1992) Biochemistry , vol.31 , pp. 9526-9532
    • Zecherle, G.N.1    Oleinikov, A.2    Traut, R.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.