메뉴 건너뛰기




Volumn 6, Issue 5, 2011, Pages

In silico and in vitro investigations of the mutability of disease-causing missense mutation sites in spermine synthase

Author keywords

[No Author keywords available]

Indexed keywords

RNA; SPERMINE SYNTHASE;

EID: 79957582046     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0020373     Document Type: Article
Times cited : (53)

References (39)
  • 1
    • 4944242891 scopus 로고    scopus 로고
    • Polyamines and cancer: old molecules, new understanding
    • Gerner EW, Meyskens FL Jr, (2004) Polyamines and cancer: old molecules, new understanding. Nat Rev Cancer 4: 781-792.
    • (2004) Nat Rev Cancer , vol.4 , pp. 781-792
    • Gerner, E.W.1    Meyskens Jr., F.L.2
  • 2
    • 32944472945 scopus 로고    scopus 로고
    • Aminopropyltransferases: function, structure and genetics
    • Ikeguchi Y, Bewley MC, Pegg AE, (2006) Aminopropyltransferases: function, structure and genetics. J Biochem 139: 1-9.
    • (2006) J Biochem , vol.139 , pp. 1-9
    • Ikeguchi, Y.1    Bewley, M.C.2    Pegg, A.E.3
  • 3
    • 70350780368 scopus 로고    scopus 로고
    • Mammalian polyamine metabolism and function
    • Pegg AE, (2009) Mammalian polyamine metabolism and function. IUBMB Life 61: 880-894.
    • (2009) IUBMB Life , vol.61 , pp. 880-894
    • Pegg, A.E.1
  • 4
    • 77949905958 scopus 로고    scopus 로고
    • The polyamine metabolism genes ornithine decarboxylase and antizyme 2 predict aggressive behavior in neuroblastomas with and without MYCN amplification
    • Geerts D, Koster J, Albert D, Koomoa DL, Feith DJ, et al. The polyamine metabolism genes ornithine decarboxylase and antizyme 2 predict aggressive behavior in neuroblastomas with and without MYCN amplification. Int J Cancer 126: 2012-2024.
    • Int J Cancer , vol.126 , pp. 2012-2024
    • Geerts, D.1    Koster, J.2    Albert, D.3    Koomoa, D.L.4    Feith, D.J.5
  • 5
    • 0036163891 scopus 로고    scopus 로고
    • Essential role of S-adenosylmethionine decarboxylase in mouse embryonic development
    • Nishimura K, Nakatsu F, Kashiwagi K, Ohno H, Saito T, et al. (2002) Essential role of S-adenosylmethionine decarboxylase in mouse embryonic development. Genes Cells 7: 41-47.
    • (2002) Genes Cells , vol.7 , pp. 41-47
    • Nishimura, K.1    Nakatsu, F.2    Kashiwagi, K.3    Ohno, H.4    Saito, T.5
  • 6
    • 0034809529 scopus 로고    scopus 로고
    • The ornithine decarboxylase gene is essential for cell survival during early murine development
    • Pendeville H, Carpino N, Marine JC, Takahashi Y, Muller M, et al. (2001) The ornithine decarboxylase gene is essential for cell survival during early murine development. Mol Cell Biol 21: 6549-6558.
    • (2001) Mol Cell Biol , vol.21 , pp. 6549-6558
    • Pendeville, H.1    Carpino, N.2    Marine, J.C.3    Takahashi, Y.4    Muller, M.5
  • 7
    • 0034667601 scopus 로고    scopus 로고
    • Effect of spermine synthase deficiency on polyamine biosynthesis and content in mice and embryonic fibroblasts, and the sensitivity of fibroblasts to 1,3-bis-(2-chloroethyl)-N-nitrosourea
    • Mackintosh CA, Pegg AE, (2000) Effect of spermine synthase deficiency on polyamine biosynthesis and content in mice and embryonic fibroblasts, and the sensitivity of fibroblasts to 1,3-bis-(2-chloroethyl)-N-nitrosourea. Biochem J 351 (Pt 2): 439-447.
    • (2000) Biochem J , vol.351 , Issue.Pt 2 , pp. 439-447
    • Mackintosh, C.A.1    Pegg, A.E.2
  • 8
    • 34547654456 scopus 로고    scopus 로고
    • Targeting the polyamine biosynthetic enzymes: a promising approach to therapy of African sleeping sickness, Chagas' disease, and leishmaniasis
    • Heby O, Persson L, Rentala M, (2007) Targeting the polyamine biosynthetic enzymes: a promising approach to therapy of African sleeping sickness, Chagas' disease, and leishmaniasis. Amino Acids 33: 359-366.
    • (2007) Amino Acids , vol.33 , pp. 359-366
    • Heby, O.1    Persson, L.2    Rentala, M.3
  • 9
    • 0037396384 scopus 로고    scopus 로고
    • Polyamine biosynthetic enzymes as drug targets in parasitic protozoa
    • Heby O, Roberts SC, Ullman B, (2003) Polyamine biosynthetic enzymes as drug targets in parasitic protozoa. Biochem Soc Trans 31: 415-419.
    • (2003) Biochem Soc Trans , vol.31 , pp. 415-419
    • Heby, O.1    Roberts, S.C.2    Ullman, B.3
  • 10
    • 61749092136 scopus 로고    scopus 로고
    • A missense mutation, p.V132G, in the X-linked spermine synthase gene (SMS) causes Snyder-Robinson syndrome
    • Becerra-Solano LE, Butler J, Castaneda-Cisneros G, McCloskey DE, Wang X, et al. (2009) A missense mutation, p.V132G, in the X-linked spermine synthase gene (SMS) causes Snyder-Robinson syndrome. Am J Med Genet A 149A: 328-335.
    • (2009) Am J Med Genet A , vol.149 A , pp. 328-335
    • Becerra-Solano, L.E.1    Butler, J.2    Castaneda-Cisneros, G.3    McCloskey, D.E.4    Wang, X.5
  • 11
    • 0348077408 scopus 로고    scopus 로고
    • X-linked spermine synthase gene (SMS) defect: the first polyamine deficiency syndrome
    • Cason AL, Ikeguchi Y, Skinner C, Wood TC, Holden KR, et al. (2003) X-linked spermine synthase gene (SMS) defect: the first polyamine deficiency syndrome. Eur J Hum Genet 11: 937-944.
    • (2003) Eur J Hum Genet , vol.11 , pp. 937-944
    • Cason, A.L.1    Ikeguchi, Y.2    Skinner, C.3    Wood, T.C.4    Holden, K.R.5
  • 12
    • 50049128469 scopus 로고    scopus 로고
    • New SMS mutation leads to a striking reduction in spermine synthase protein function and a severe form of Snyder-Robinson X-linked recessive mental retardation syndrome
    • de Alencastro G, McCloskey DE, Kliemann SE, Maranduba CM, Pegg AE, et al. (2008) New SMS mutation leads to a striking reduction in spermine synthase protein function and a severe form of Snyder-Robinson X-linked recessive mental retardation syndrome. J Med Genet 45: 539-543.
    • (2008) J Med Genet , vol.45 , pp. 539-543
    • de Alencastro, G.1    McCloskey, D.E.2    Kliemann, S.E.3    Maranduba, C.M.4    Pegg, A.E.5
  • 13
    • 77957102925 scopus 로고    scopus 로고
    • The impact of spermine synthase (SMS) mutations on brain morphology
    • Kesler SR, Schwartz C, Stevenson RE, Reiss AL, (2009) The impact of spermine synthase (SMS) mutations on brain morphology. Neurogenetics 10: 299-305.
    • (2009) Neurogenetics , vol.10 , pp. 299-305
    • Kesler, S.R.1    Schwartz, C.2    Stevenson, R.E.3    Reiss, A.L.4
  • 14
    • 59449106100 scopus 로고    scopus 로고
    • Spermine synthase deficiency leads to deafness and a profound sensitivity to alpha-difluoromethylornithine
    • Wang X, Levic S, Gratton MA, Doyle KJ, Yamoah EN, et al. (2009) Spermine synthase deficiency leads to deafness and a profound sensitivity to alpha-difluoromethylornithine. J Biol Chem 284: 930-937.
    • (2009) J Biol Chem , vol.284 , pp. 930-937
    • Wang, X.1    Levic, S.2    Gratton, M.A.3    Doyle, K.J.4    Yamoah, E.N.5
  • 15
    • 47049102867 scopus 로고    scopus 로고
    • Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism
    • Wu H, Min J, Zeng H, McCloskey DE, Ikeguchi Y, et al. (2008) Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism. J Biol Chem 283: 16135-16146.
    • (2008) J Biol Chem , vol.283 , pp. 16135-16146
    • Wu, H.1    Min, J.2    Zeng, H.3    McCloskey, D.E.4    Ikeguchi, Y.5
  • 16
    • 77956276773 scopus 로고    scopus 로고
    • Computational analysis of missense mutations causing Snyder-Robinson syndrome
    • Zhang Z, Teng S, Wang L, Schwartz CE, Alexov E, (2010) Computational analysis of missense mutations causing Snyder-Robinson syndrome. Hum Mutat 31: 1043-1049.
    • (2010) Hum Mutat , vol.31 , pp. 1043-1049
    • Zhang, Z.1    Teng, S.2    Wang, L.3    Schwartz, C.E.4    Alexov, E.5
  • 17
    • 41949118839 scopus 로고    scopus 로고
    • Approaches and resources for prediction of the effects of non-synonymous single nucleotide polymorphism on protein function and interactions
    • Teng S, Michonova-Alexova E, Alexov E, (2008) Approaches and resources for prediction of the effects of non-synonymous single nucleotide polymorphism on protein function and interactions. Curr Pharm Biotechnol 9: 123-133.
    • (2008) Curr Pharm Biotechnol , vol.9 , pp. 123-133
    • Teng, S.1    Michonova-Alexova, E.2    Alexov, E.3
  • 18
    • 32044453591 scopus 로고    scopus 로고
    • Identification and analysis of deleterious human SNPs
    • Yue P, Moult J, (2006) Identification and analysis of deleterious human SNPs. J Mol Biol 356: 1263-1274.
    • (2006) J Mol Biol , vol.356 , pp. 1263-1274
    • Yue, P.1    Moult, J.2
  • 19
    • 33645764714 scopus 로고    scopus 로고
    • SNPs3D: candidate gene and SNP selection for association studies
    • Yue P, Melamud E, Moult J, (2006) SNPs3D: candidate gene and SNP selection for association studies. BMC Bioinformatics 7: 166.
    • (2006) BMC Bioinformatics , vol.7 , pp. 166
    • Yue, P.1    Melamud, E.2    Moult, J.3
  • 20
    • 36348992229 scopus 로고    scopus 로고
    • Modeling and analyzing three-dimensional structures of human disease proteins
    • Ye Y, Li Z, Godzik A, (2006) Modeling and analyzing three-dimensional structures of human disease proteins. Pac Symp Biocomput pp. 439-450.
    • (2006) Pac Symp Biocomput , pp. 439-450
    • Ye, Y.1    Li, Z.2    Godzik, A.3
  • 21
    • 27544469800 scopus 로고    scopus 로고
    • Predicting protein stability changes from sequences using support vector machines
    • Capriotti E, Fariselli P, Calabrese R, Casadio R, (2005) Predicting protein stability changes from sequences using support vector machines. Bioinformatics 21 (Suppl 2): ii54-ii58.
    • (2005) Bioinformatics , vol.21 , Issue.SUPPL. 2
    • Capriotti, E.1    Fariselli, P.2    Calabrese, R.3    Casadio, R.4
  • 22
    • 20844461337 scopus 로고    scopus 로고
    • LS-SNP: large-scale annotation of coding non-synonymous SNPs based on multiple information sources
    • Karchin R, Diekhans M, Kelly L, Thomas DJ, Pieper U, et al. (2005) LS-SNP: large-scale annotation of coding non-synonymous SNPs based on multiple information sources. Bioinformatics 21: 2814-2820.
    • (2005) Bioinformatics , vol.21 , pp. 2814-2820
    • Karchin, R.1    Diekhans, M.2    Kelly, L.3    Thomas, D.J.4    Pieper, U.5
  • 23
    • 0035065485 scopus 로고    scopus 로고
    • SNPs, protein structure, and disease
    • Wang Z, Moult J, (2001) SNPs, protein structure, and disease. Hum Mutat 17: 263-270.
    • (2001) Hum Mutat , vol.17 , pp. 263-270
    • Wang, Z.1    Moult, J.2
  • 24
    • 0242362185 scopus 로고    scopus 로고
    • Three-dimensional structural location and molecular functional effects of missense SNPs in the T cell receptor Vbeta domain
    • Wang Z, Moult J, (2003) Three-dimensional structural location and molecular functional effects of missense SNPs in the T cell receptor Vbeta domain. Proteins 53: 748-757.
    • (2003) Proteins , vol.53 , pp. 748-757
    • Wang, Z.1    Moult, J.2
  • 25
    • 0036713510 scopus 로고    scopus 로고
    • Human non-synonymous SNPs: server and survey
    • Ramensky V, Bork P, Sunyaev S, (2002) Human non-synonymous SNPs: server and survey. Nucleic Acids Res 30: 3894-3900.
    • (2002) Nucleic Acids Res , vol.30 , pp. 3894-3900
    • Ramensky, V.1    Bork, P.2    Sunyaev, S.3
  • 26
    • 66149102833 scopus 로고    scopus 로고
    • Modeling effects of human single nucleotide polymorphisms on protein-protein interactions
    • Teng S, Madej T, Panchenko A, Alexov E, (2009) Modeling effects of human single nucleotide polymorphisms on protein-protein interactions. Biophys J 96: 2178-2188.
    • (2009) Biophys J , vol.96 , pp. 2178-2188
    • Teng, S.1    Madej, T.2    Panchenko, A.3    Alexov, E.4
  • 27
    • 42949163017 scopus 로고    scopus 로고
    • Single nucleotide polymorphisms that cause structural changes in the cyclic AMP receptor protein transcriptional regulator of the tuberculosis vaccine strain Mycobacterium bovis BCG alter global gene expression without attenuating growth
    • Hunt DM, Saldanha JW, Brennan JF, Benjamin P, Strom M, et al. (2008) Single nucleotide polymorphisms that cause structural changes in the cyclic AMP receptor protein transcriptional regulator of the tuberculosis vaccine strain Mycobacterium bovis BCG alter global gene expression without attenuating growth. Infect Immun 76: 2227-2234.
    • (2008) Infect Immun , vol.76 , pp. 2227-2234
    • Hunt, D.M.1    Saldanha, J.W.2    Brennan, J.F.3    Benjamin, P.4    Strom, M.5
  • 28
    • 0034897806 scopus 로고    scopus 로고
    • Missense polymorphism in the human carboxypeptidase E gene alters enzymatic activity
    • Chen H, Jawahar S, Qian Y, Duong Q, Chan G, et al. (2001) Missense polymorphism in the human carboxypeptidase E gene alters enzymatic activity. Hum Mutat 18: 120-131.
    • (2001) Hum Mutat , vol.18 , pp. 120-131
    • Chen, H.1    Jawahar, S.2    Qian, Y.3    Duong, Q.4    Chan, G.5
  • 30
    • 0035838974 scopus 로고    scopus 로고
    • Extending the Accuracy Limits of Prediction for Side-chain Conformations
    • Xiang Z, Honig B, (2001) Extending the Accuracy Limits of Prediction for Side-chain Conformations. J Mol Biol 311: 421-430.
    • (2001) J Mol Biol , vol.311 , pp. 421-430
    • Xiang, Z.1    Honig, B.2
  • 32
    • 0344778061 scopus 로고
    • Semianalytical Treatment of Solvation for Molecular Mechanics and Dynamics
    • Still WC, Tempczyk A, Hawley RC, Hendrickson T, (1990) Semianalytical Treatment of Solvation for Molecular Mechanics and Dynamics. J Am Chem Soc 112: 6127-6129.
    • (1990) J Am Chem Soc , vol.112 , pp. 6127-6129
    • Still, W.C.1    Tempczyk, A.2    Hawley, R.C.3    Hendrickson, T.4
  • 35
    • 33645941402 scopus 로고
    • The OPLS potential function for proteins
    • Jorgensen WL, Tirado-Rives J, (1988) The OPLS potential function for proteins. J Am Chem Soc 110: 1657-1666.
    • (1988) J Am Chem Soc , vol.110 , pp. 1657-1666
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 36
    • 34347402439 scopus 로고    scopus 로고
    • Structural and functional consequences of single amino acid substitutions in the pyrimidine base binding pocket of Escherichia coli CMP kinase
    • Ofiteru A, Bucurenci N, Alexov E, Bertrand T, Briozzo P, et al. (2007) Structural and functional consequences of single amino acid substitutions in the pyrimidine base binding pocket of Escherichia coli CMP kinase. Febs J 274: 3363-3373.
    • (2007) Febs J , vol.274 , pp. 3363-3373
    • Ofiteru, A.1    Bucurenci, N.2    Alexov, E.3    Bertrand, T.4    Briozzo, P.5
  • 37
    • 0033614791 scopus 로고    scopus 로고
    • Calculated Protein and Proton Motions Coupled to Electron Transfer: Electron Transfer from QA- to QB in Bacterial Photosynthetic Reaction Centers
    • Alexov E, Gunner M, (1999) Calculated Protein and Proton Motions Coupled to Electron Transfer: Electron Transfer from QA- to QB in Bacterial Photosynthetic Reaction Centers. Biochemistry 38: 8253-8270.
    • (1999) Biochemistry , vol.38 , pp. 8253-8270
    • Alexov, E.1    Gunner, M.2
  • 38
    • 0036787760 scopus 로고    scopus 로고
    • Combining Conformational Flexibility and Continuum Electrostatics for Calculating Residue pKa's in Proteins
    • Georgescu R, Alexov E, Gunner M, (2002) Combining Conformational Flexibility and Continuum Electrostatics for Calculating Residue pKa's in Proteins. Biophys J 83: 1731-1748.
    • (2002) Biophys J , vol.83 , pp. 1731-1748
    • Georgescu, R.1    Alexov, E.2    Gunner, M.3
  • 39
    • 62749167980 scopus 로고    scopus 로고
    • MCCE2: Improving Protein pKa Calculations with Extensive Side Chain Rotamer Sampling
    • Song Y, Mao J, Gunner MR, (2009) MCCE2: Improving Protein pKa Calculations with Extensive Side Chain Rotamer Sampling. Comp Chem 30: 2231-2247.
    • (2009) Comp Chem , vol.30 , pp. 2231-2247
    • Song, Y.1    Mao, J.2    Gunner, M.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.