메뉴 건너뛰기




Volumn 42, Issue 2-3, 2012, Pages 725-731

Do mammalian amine oxidases and the mitochondrial polyamine transporter have similar protein structures?

Author keywords

Amine oxidases; Mitochondrial polyamines uniporter; Polyamines

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING); BOVINE SERUM ALBUMIN; CARRIER PROTEIN; POLYAMINE; PUTRESCINE; SPERMIDINE; SPERMINE; AMINE OXIDASE (COPPER CONTAINING);

EID: 84861657189     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-011-0988-x     Document Type: Article
Times cited : (2)

References (22)
  • 2
    • 79551593168 scopus 로고    scopus 로고
    • Plasma amine oxidases in various clinical conditions and in apoptosis
    • Floris G, Mondovì B (eds) CRC Press, Boca Raton
    • Boomsma F, van der Meiracker AH, Toninello A (2009) Plasma amine oxidases in various clinical conditions and in apoptosis. In: Floris G, Mondovì B (eds) Copper amine oxidases. CRC Press, Boca Raton, pp 143-158
    • (2009) Copper Amine Oxidases. , pp. 143-158
    • Boomsma, F.1    Van Der Meiracker, A.H.2    Toninello, A.3
  • 6
    • 0037626151 scopus 로고    scopus 로고
    • Electrostatic compared with hydrophobic interactions between bovine serum amine oxidase and its substrates
    • DOI 10.1042/BJ20021055
    • Di Paolo ML, Stevanato R, Corazza A, Vianello F, Lunelli L, Scarpa M, Rigo A (2003) Electrostatic versus hydrophobic interactions between bovine serum amine oxidase and its substrates. Biochem J 371:549-556 (Pubitemid 36547639)
    • (2003) Biochemical Journal , vol.371 , Issue.2 , pp. 549-556
    • Di Paolo, M.L.1    Stevanato, R.2    Corazza, A.3    Vianello, F.4    Lunelli, L.5    Scarpa, M.6    Rigo, A.7
  • 7
    • 0028071662 scopus 로고
    • Gibbs free energy of adsorption for biomolecules in ion-exchange systems
    • DOI 10.1016/0301-4622(94)00006-9
    • Gerstner JA, Bell JA, Cramer SM (1994) Gibbs free energy of adsorption for biomolecules in ion-exchange systems. Biophys Chem 52:97-106 (Pubitemid 24300337)
    • (1994) Biophysical Chemistry , vol.52 , Issue.2 , pp. 97-106
    • Gerstner, J.A.1    Bell, J.A.2    Cramer, S.M.3
  • 8
    • 0025374783 scopus 로고
    • A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase
    • Janes SM, Mu D, Wemmer D, Smith AJ, Kaur S, Maltby D, Burlingame AL, Klinman JP (1990) A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase. Science 248:981-987
    • (1990) Science , vol.248 , pp. 981-987
    • Janes, S.M.1    Mu, D.2    Wemmer, D.3    Smith, A.J.4    Kaur, S.5    Maltby, D.6    Burlingame, A.L.7    Klinman, J.P.8
  • 11
    • 84862690511 scopus 로고    scopus 로고
    • Mechanism of TPQ biogenesis in prokaryotic copper amine oxidase
    • Floris G, Mondovì B (eds) CRC Press, Boca Raton
    • Okajima T, Tanizawa K (2009) Mechanism of TPQ biogenesis in prokaryotic copper amine oxidase. In: Floris G, Mondovì B (eds) Copper amine oxidases. CRC Press, Boca Raton, pp 103-118
    • (2009) Copper Amine Oxidases , pp. 103-118
    • Okajima, T.1    Tanizawa, K.2
  • 13
    • 0000370657 scopus 로고
    • Electrostatic and Van der Waals contributions to protein adsorption: Computation of equilibrium constants
    • Roth CM, Lenhoff AM (1993) Electrostatic and Van der Waals contributions to protein adsorption: computation of equilibrium constants. Langmuir 9:962-972
    • (1993) Langmuir , vol.9 , pp. 962-972
    • Roth, C.M.1    Lenhoff, A.M.2
  • 14
    • 77955070990 scopus 로고    scopus 로고
    • Structural organization of mammalian copper-containing amine oxidase genes
    • Schwelberger HG (2010) Structural organization of mammalian copper-containing amine oxidase genes. Inflamm Res 59:223-225
    • (2010) Inflamm Res , vol.59 , pp. 223-225
    • Schwelberger, H.G.1
  • 15
    • 0028258569 scopus 로고
    • Electrostatic control of oxidative deamination catalysed by bovine serum amine oxidase
    • Stevanato R, Mondovì B, Befani O, Scarpa M, Rigo A (1994) Electrostatic control of oxidative deamination catalysed by bovine serum amine oxidase. Biochem J 299:317-320 (Pubitemid 24106325)
    • (1994) Biochemical Journal , vol.299 , Issue.1 , pp. 317-320
    • Stevanato, R.1    Mondovi, B.2    Befani, O.3    Scarpa, M.4    Rigo, A.5
  • 18
    • 0026686432 scopus 로고
    • Evidence that spermine, spermidine and putrescine are transported electrophoretically in mitochondria by a specific polyamine uniporter
    • Toninello A, Dalla Via L, Siliprandi D, Garlid KD (1992) Evidence that spermine, spermidine and putrescine are transported electrophoretically in mitochondria by a specific polyamine uniporter. J Biol Chem 267:18393-18397
    • (1992) J Biol Chem , vol.267 , pp. 18393-18397
    • Toninello, A.1    Dalla Via, L.2    Siliprandi, D.3    Garlid, K.D.4
  • 19
    • 0039007970 scopus 로고    scopus 로고
    • Kinetics and free energy profiles of spermine transport in liver mitochondria
    • DOI 10.1021/bi991217c
    • Toninello A, Dalla Via L, Stevanato R, Yagisawa S (2000) Kinetics and free Energy profiles of spermine tran sport in liver mitochondria. Biochemistry 39:324-331 (Pubitemid 30056466)
    • (2000) Biochemistry , vol.39 , Issue.2 , pp. 324-331
    • Toninello, A.1    Dalla Via, L.2    Stevanato, R.3    Yagisawa, S.4
  • 20
    • 0026934588 scopus 로고
    • Isolation of amine oxidase from bovine plasma by a two-step procedures
    • Vianello F, Di Paolo ML, Stevanato R, Rigo A (1992) Isolation of amine oxidase from bovine plasma by a two-step procedures. Protein Expr Purif 3:362-367
    • (1992) Protein Expr Purif , vol.3 , pp. 362-367
    • Vianello, F.1    Di Paolo, M.L.2    Stevanato, R.3    Rigo, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.