메뉴 건너뛰기




Volumn 20, Issue 2, 2014, Pages 262-277

Charge deficient analogues of the natural polyamines

Author keywords

Cell organelles; Charge deficient; Ornithine decarboxylase; Polyamine; Polyamine analog; Reactive oxygen species

Indexed keywords

ACYLTRANSFERASE; AMINE; CARBON; FLUORINE; HYDROGEN; HYDROGEN PEROXIDE; HYDROXYLAMINE; METHYLAMINE; POLYAMINE; PUTRESCINE; REACTIVE OXYGEN METABOLITE; SPERMIDINE; SPERMINE;

EID: 84892956577     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/13816128113199990037     Document Type: Review
Times cited : (11)

References (234)
  • 3
    • 84870372431 scopus 로고    scopus 로고
    • The role of B lymphocytes in the progression from autoimmunity to autoimmune disease
    • Salinas GF, Braza F, Brouard S, Tak PP, Baeten D. The role of B lymphocytes in the progression from autoimmunity to autoimmune disease. Clin Immunol 2012; 146: 34-45.
    • (2012) Clin Immunol , vol.146 , pp. 34-45
    • Salinas, G.F.1    Braza, F.2    Brouard, S.3    Tak, P.P.4    Baeten, D.5
  • 5
    • 79952068436 scopus 로고    scopus 로고
    • Cell and tissue interactions in carcinogenesis and metastasis and their clinical significance
    • Tarin D. Cell and tissue interactions in carcinogenesis and metastasis and their clinical significance. Semin Cancer Biol 2011; 21: 72-82.
    • (2011) Semin Cancer Biol , vol.21 , pp. 72-82
    • Tarin, D.1
  • 6
    • 77956095537 scopus 로고    scopus 로고
    • Mitochondria and cell death: Outer membrane permeabilization and beyond
    • Tait SW, Green DR. Mitochondria and cell death: outer membrane permeabilization and beyond. Nat Rev Mol Cell Biol 2010; 11: 621-32.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 621-632
    • Tait, S.W.1    Green, D.R.2
  • 7
    • 84872444027 scopus 로고    scopus 로고
    • Clearing the final hurdles to mitochondrial apoptosis: Regulation post cytochrome C release
    • Monian P, Jiang X. Clearing the final hurdles to mitochondrial apoptosis: regulation post cytochrome C release. Exp Oncol 2012; 34: 185-91.
    • (2012) Exp Oncol , vol.34 , pp. 185-191
    • Monian, P.1    Jiang, X.2
  • 9
    • 84868197448 scopus 로고    scopus 로고
    • Programmed cell death pathways in cancer: A review of apoptosis, autophagy and programmed necrosis
    • Ouyang L, Shi Z, Zhao S, et al. Programmed cell death pathways in cancer: a review of apoptosis, autophagy and programmed necrosis. Cell Prolif 2012; 45: 487-98.
    • (2012) Cell Prolif , vol.45 , pp. 487-498
    • Ouyang, L.1    Shi, Z.2    Zhao, S.3
  • 10
    • 65349191918 scopus 로고    scopus 로고
    • Programmed cell death and cancer
    • Sun Y, Peng ZL. Programmed cell death and cancer. Postgrad Med J 2009; 85: 134-40.
    • (2009) Postgrad Med J , vol.85 , pp. 134-140
    • Sun, Y.1    Peng, Z.L.2
  • 11
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine B, Kroemer G. Autophagy in the pathogenesis of disease. Cell 2008; 132: 27-42.
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 12
    • 84865544952 scopus 로고    scopus 로고
    • Mitochondrial fission, fusion, and stress
    • Youle RJ, van der Bliek AM. Mitochondrial fission, fusion, and stress. Science 2012; 337: 1062-5.
    • (2012) Science , vol.337 , pp. 1062-1065
    • Youle, R.J.1    van der Bliek, A.M.2
  • 13
    • 83555169408 scopus 로고    scopus 로고
    • Crosstalk between mitochondrial (dys)function and mitochondrial abundance
    • Michel S, Wanet A, De Pauw A, et al. Crosstalk between mitochondrial (dys)function and mitochondrial abundance. J Cell Physiol 2012; 227: 2297-310.
    • (2012) J Cell Physiol , vol.227 , pp. 2297-2310
    • Michel, S.1    Wanet, A.2    De Pauw, A.3
  • 14
    • 84864304711 scopus 로고    scopus 로고
    • Mitochondrial DNA damage and its consequences for mitochondrial gene expression
    • Cline SD. Mitochondrial DNA damage and its consequences for mitochondrial gene expression. Biochim Biophys Acta 2012; 1819: 979-91.
    • (2012) Biochim Biophys Acta , vol.1819 , pp. 979-991
    • Cline, S.D.1
  • 15
    • 44849128599 scopus 로고    scopus 로고
    • Expression and maintenance of mitochondrial DNA: New insights into human disease pathology
    • Shadel GS. Expression and maintenance of mitochondrial DNA: new insights into human disease pathology. Am J Pathol 2008; 172: 1445-56.
    • (2008) Am J Pathol , vol.172 , pp. 1445-1456
    • Shadel, G.S.1
  • 16
    • 80052266526 scopus 로고    scopus 로고
    • Cross talk between mitochondria and NADPH oxidases
    • Dikalov S. Cross talk between mitochondria and NADPH oxidases. Free Radic Biol Med 2011; 51: 1289-301.
    • (2011) Free Radic Biol Med , vol.51 , pp. 1289-1301
    • Dikalov, S.1
  • 17
    • 79959541505 scopus 로고    scopus 로고
    • Acetylation of MnSOD directs enzymatic activity responding to cellular nutrient status or oxidative stress
    • Ozden O, Park SH, Kim HS, et al. Acetylation of MnSOD directs enzymatic activity responding to cellular nutrient status or oxidative stress. Aging (Albany NY) 2011; 3: 102-7.
    • (2011) Aging (Albany NY) , vol.3 , pp. 102-107
    • Ozden, O.1    Park, S.H.2    Kim, H.S.3
  • 18
    • 77953612373 scopus 로고    scopus 로고
    • Maillard reaction, mitochondria and oxidative stress: Potential role of antioxidants
    • Edeas M, Attaf D, Mailfert AS, Nasu M, Joubet R. Maillard reaction, mitochondria and oxidative stress: potential role of antioxidants. Pathol Biol (Paris) 2010; 58: 220-5.
    • (2010) Pathol Biol (Paris) , vol.58 , pp. 220-225
    • Edeas, M.1    Attaf, D.2    Mailfert, A.S.3    Nasu, M.4    Joubet, R.5
  • 19
    • 79958152853 scopus 로고    scopus 로고
    • Superoxide dismutase in redox biology: The roles of superoxide and hydrogen peroxide
    • Buettner GR. Superoxide dismutase in redox biology: the roles of superoxide and hydrogen peroxide. Anticancer Agents Med Chem 2011; 11: 341-6.
    • (2011) Anticancer Agents Med Chem , vol.11 , pp. 341-346
    • Buettner, G.R.1
  • 20
    • 70350780368 scopus 로고    scopus 로고
    • Mammalian polyamine metabolism and function
    • Pegg AE. Mammalian polyamine metabolism and function. IUBMB Life 2009; 61: 880-94.
    • (2009) IUBMB Life , vol.61 , pp. 880-894
    • Pegg, A.E.1
  • 21
    • 69249245459 scopus 로고    scopus 로고
    • Polyamine catabolism and disease
    • Casero RA, Pegg AE. Polyamine catabolism and disease. Biochem J 2009; 421: 323-38.
    • (2009) Biochem J , vol.421 , pp. 323-338
    • Casero, R.A.1    Pegg, A.E.2
  • 22
    • 34247099261 scopus 로고    scopus 로고
    • Polyamines and neoplastic growth
    • Pegg AE, Feith DJ. Polyamines and neoplastic growth. Biochem Soc Trans 2007; 35: 295-9.
    • (2007) Biochem Soc Trans , vol.35 , pp. 295-299
    • Pegg, A.E.1    Feith, D.J.2
  • 23
    • 30944463252 scopus 로고    scopus 로고
    • Animal disease models generated by genetic engineering of polyamine metabolism
    • Jänne J, Alhonen L, Keinänen TA, et al. Animal disease models generated by genetic engineering of polyamine metabolism. J Cell Mol Med 2005; 9: 865-82.
    • (2005) J Cell Mol Med , vol.9 , pp. 865-882
    • Jänne, J.1    Alhonen, L.2    Keinänen, T.A.3
  • 26
    • 0020479292 scopus 로고
    • Effect of androgens in turnover of ornithine decarboxylase in mouse kidney. Studies using labeling of the enzyme by reaction with (14C)alpha-difluoromethylornithine
    • Seely JE, Pösö H, Pegg AE. Effect of androgens in turnover of ornithine decarboxylase in mouse kidney. Studies using labeling of the enzyme by reaction with (14C)alpha-difluoromethylornithine. J Biol Chem 1982; 257: 7549-53.
    • (1982) J Biol Chem , vol.257 , pp. 7549-7553
    • Seely, J.E.1    Pösö, H.2    Pegg, A.E.3
  • 27
    • 0015524977 scopus 로고
    • Polyamine synthesis in the regenerating rat liver: Stimulation of S-adenosylmethionine decarboxylase, and spermidine and spermine synthases after partial hepatectomy
    • Hannonen P, Raina A, Jänne J. Polyamine synthesis in the regenerating rat liver: stimulation of S-adenosylmethionine decarboxylase, and spermidine and spermine synthases after partial hepatectomy. Biochim Biophys Acta 1972; 273: 84-90.
    • (1972) Biochim Biophys Acta , vol.273 , pp. 84-90
    • Hannonen, P.1    Raina, A.2    Jänne, J.3
  • 28
    • 0018391720 scopus 로고
    • Investigation of the turnover of rat liver Sadenosylmethionine decarboxylase using a specific antibody
    • Pegg AE. Investigation of the turnover of rat liver Sadenosylmethionine decarboxylase using a specific antibody. J Biol Chem 1979; 254: 3249-53.
    • (1979) J Biol Chem , vol.254 , pp. 3249-3253
    • Pegg, A.E.1
  • 29
    • 0022410537 scopus 로고
    • Regulation of S-adenosylmethionine decarboxylase activity in rat liver and prostate
    • Shirahata A, Pegg AE. Regulation of S-adenosylmethionine decarboxylase activity in rat liver and prostate. J Biol Chem 1985; 260: 9583-8.
    • (1985) J Biol Chem , vol.260 , pp. 9583-9588
    • Shirahata, A.1    Pegg, A.E.2
  • 30
    • 33744951504 scopus 로고    scopus 로고
    • Regulation of ornithine decarboxylase
    • Pegg AE. Regulation of ornithine decarboxylase. J Biol Chem 2006; 281: 14529-32.
    • (2006) J Biol Chem , vol.281 , pp. 14529-14532
    • Pegg, A.E.1
  • 31
    • 77449159833 scopus 로고    scopus 로고
    • S-Adenosylmethionine decarboxylase
    • Pegg AE. S-Adenosylmethionine decarboxylase. Essays Biochem 2009; 46: 25-45.
    • (2009) Essays Biochem , vol.46 , pp. 25-45
    • Pegg, A.E.1
  • 32
    • 77449090048 scopus 로고    scopus 로고
    • Regulation of cellular polyamine levels and cellular proliferation by antizyme and antizyme inhibitor
    • Kahana C. Regulation of cellular polyamine levels and cellular proliferation by antizyme and antizyme inhibitor. Essays Biochem 2009; 46: 47-61.
    • (2009) Essays Biochem , vol.46 , pp. 47-61
    • Kahana, C.1
  • 33
    • 0028598524 scopus 로고
    • Antizyme protects against abnormal accumulation and toxicity of polyamines in ornithine decarboxylase-overproducing cells
    • Suzuki T, He Y, Kashiwagi K, et al. Antizyme protects against abnormal accumulation and toxicity of polyamines in ornithine decarboxylase-overproducing cells. Proc Natl Acad Sci USA 1994; 91: 8930-4.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8930-8934
    • Suzuki, T.1    He, Y.2    Kashiwagi, K.3
  • 34
    • 0028296140 scopus 로고
    • Feedback repression of polyamine transport is mediated by antizyme in mammalian tissue-culture cells
    • Mitchell JLA, Judd GG, Bareyal-Leyser A, Ling SY. Feedback repression of polyamine transport is mediated by antizyme in mammalian tissue-culture cells. Biochem J 1994; 299: 19-22.
    • (1994) Biochem J , vol.299 , pp. 19-22
    • Mitchell, J.L.A.1    Judd, G.G.2    Bareyal-Leyser, A.3    Ling, S.Y.4
  • 36
    • 0028831608 scopus 로고
    • Autoregulatory frameshifting in decoding mammalian ornithine decarboxylase antizyme
    • Matsufuji S, Matsufuji T, Miyazaki Y, et al. Autoregulatory frameshifting in decoding mammalian ornithine decarboxylase antizyme. Cell 1995; 80: 51-60.
    • (1995) Cell , vol.80 , pp. 51-60
    • Matsufuji, S.1    Matsufuji, T.2    Miyazaki, Y.3
  • 37
    • 67650815445 scopus 로고    scopus 로고
    • Antizyme and antizyme inhibitor, a regulatory tango
    • Kahana C. Antizyme and antizyme inhibitor, a regulatory tango. Cell Mol Life Sci 2009; 66: 2479-88.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 2479-2488
    • Kahana, C.1
  • 38
    • 0027510121 scopus 로고
    • Cell-specific translational regulation of Sadenosylmethionine decarboxylase mRNA. Dependence on translation and codin capacity of the cis-acting upstream open reading frame
    • Hill JR, Morris DR. Cell-specific translational regulation of Sadenosylmethionine decarboxylase mRNA. Dependence on translation and codin capacity of the cis-acting upstream open reading frame. J Biol Chem 1993; 268: 726-31.
    • (1993) J Biol Chem , vol.268 , pp. 726-731
    • Hill, J.R.1    Morris, D.R.2
  • 39
    • 0029909265 scopus 로고    scopus 로고
    • The upstream open reading frame of the mRNA encoding S-adenosylmethionine decarboxylase is a polyamine-responsive translational control element
    • Ruan H, Shantz LM, Pegg AE, Morris DR. The upstream open reading frame of the mRNA encoding S-adenosylmethionine decarboxylase is a polyamine-responsive translational control element. J Biol Chem 1996; 271: 29576-82.
    • (1996) J Biol Chem , vol.271 , pp. 29576-29582
    • Ruan, H.1    Shantz, L.M.2    Pegg, A.E.3    Morris, D.R.4
  • 40
    • 47549106852 scopus 로고    scopus 로고
    • Spermidine/spermine-N(1)-acetyltransferase: A key metabolic regulator
    • Pegg AE. Spermidine/spermine-N(1)-acetyltransferase: a key metabolic regulator. Am J Physiol Endocrinol Metab 2008; 294: E995-1010.
    • (2008) Am J Physiol Endocrinol Metab , vol.294 , pp. 995-1010
    • Pegg, A.E.1
  • 41
    • 50849141905 scopus 로고    scopus 로고
    • The crystal structure of spermidine/spermine N1-acetyltransferase in complex with spermine provides insights into substrate binding and catalysis
    • Montemayor EJ, Hoffman DW. The crystal structure of spermidine/spermine N1-acetyltransferase in complex with spermine provides insights into substrate binding and catalysis. Biochemistry 2008; 47: 9145-53.
    • (2008) Biochemistry , vol.47 , pp. 9145-9153
    • Montemayor, E.J.1    Hoffman, D.W.2
  • 42
    • 34250874505 scopus 로고    scopus 로고
    • Mechanistic and structural analysis of human spermidine/spermine N1-acetyltransferase
    • Hegde SS, Chandler J, Vetting MW, Yu M, Blanchard JS. Mechanistic and structural analysis of human spermidine/spermine N1-acetyltransferase. Biochemistry 2007; 46: 7187-95.
    • (2007) Biochemistry , vol.46 , pp. 7187-7195
    • Hegde, S.S.1    Chandler, J.2    Vetting, M.W.3    Yu, M.4    Blanchard, J.S.5
  • 43
    • 0021750983 scopus 로고
    • Studies of the induction of spermidinespermine N1-acetyltransferase using a specific antiserum
    • Persson L, Pegg AE. Studies of the induction of spermidinespermine N1-acetyltransferase using a specific antiserum. J Biol Chem 1984; 259: 12364-7.
    • (1984) J Biol Chem , vol.259 , pp. 12364-12367
    • Persson, L.1    Pegg, A.E.2
  • 44
    • 0028891384 scopus 로고
    • Post-transcriptional regulation of the content of spermidine/spemine N1-acetyltransferase by N1N12-bis(ethyl)spermine
    • Parry L, Balana Fouge R, Pegg AE. Post-transcriptional regulation of the content of spermidine/spemine N1-acetyltransferase by N1N12-bis(ethyl)spermine. Biochem J 1995; 305: 451-8.
    • (1995) Biochem J , vol.305 , pp. 451-458
    • Parry, L.1    Balana Fouge, R.2    Pegg, A.E.3
  • 45
    • 0037442525 scopus 로고    scopus 로고
    • Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion
    • Vujcic S, Liang P, Diegelman P, Kramer DL, Porter CW. Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion. Biochem J 2003; 370: 19-28.
    • (2003) Biochem J , vol.370 , pp. 19-28
    • Vujcic, S.1    Liang, P.2    Diegelman, P.3    Kramer, D.L.4    Porter, C.W.5
  • 46
    • 0017623867 scopus 로고
    • Oxidation of spermidine and spermine in rat liver: Purification and properties of polyamine oxidase
    • Hölttä E. Oxidation of spermidine and spermine in rat liver: purification and properties of polyamine oxidase. Biochemistry 1977; 16: 91-100.
    • (1977) Biochemistry , vol.16 , pp. 91-100
    • Hölttä, E.1
  • 47
    • 0035878846 scopus 로고    scopus 로고
    • Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure
    • Wang Y, Devereux W, Woster PM, et al. Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure. Cancer Res 2001; 61: 5370-3.
    • (2001) Cancer Res , vol.61 , pp. 5370-5373
    • Wang, Y.1    Devereux, W.2    Woster, P.M.3
  • 48
    • 75349100932 scopus 로고    scopus 로고
    • Mechanistic studies of human spermine oxidase: Kinetic mechanism and pH effects
    • Adachi MS, Juarez PR, Fitzpatrick PF. Mechanistic studies of human spermine oxidase: kinetic mechanism and pH effects. Biochemistry 2010; 49: 386-92.
    • (2010) Biochemistry , vol.49 , pp. 386-392
    • Adachi, M.S.1    Juarez, P.R.2    Fitzpatrick, P.F.3
  • 49
    • 79954436519 scopus 로고    scopus 로고
    • Probing mammalian spermine oxidase enzyme-substrate complex through molecular modeling, site-directed mutagenesis and biochemical characterization
    • Tavladoraki P, Cervelli M, Antonangeli F, et al. Probing mammalian spermine oxidase enzyme-substrate complex through molecular modeling, site-directed mutagenesis and biochemical characterization. Amino Acids 2011; 40: 1115-26.
    • (2011) Amino Acids , vol.40 , pp. 1115-1126
    • Tavladoraki, P.1    Cervelli, M.2    Antonangeli, F.3
  • 50
    • 80053079336 scopus 로고    scopus 로고
    • Polyamine catabolism contributes to enterotoxigenic Bacteroides fragilisinduced colon tumorigenesis
    • Goodwin AC, Destefano Shields CE, Wu S, et al. Polyamine catabolism contributes to enterotoxigenic Bacteroides fragilisinduced colon tumorigenesis. Proc Natl Acad Sci U S A 2011; 108: 15354-9.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 15354-15359
    • Goodwin, A.C.1    Destefano Shields, C.E.2    Wu, S.3
  • 51
    • 3042653176 scopus 로고    scopus 로고
    • Catabolism of polyamines
    • Seiler N. Catabolism of polyamines. Amino Acids 2004; 26: 217-33.
    • (2004) Amino Acids , vol.26 , pp. 217-233
    • Seiler, N.1
  • 52
    • 0019771417 scopus 로고
    • Interconversion, catabolism and elimination of the polyamines
    • Seiler N, Bolkenius FN, Rennert OM. Interconversion, catabolism and elimination of the polyamines. Med Biol 1981; 59: 334-46.
    • (1981) Med Biol , vol.59 , pp. 334-346
    • Seiler, N.1    Bolkenius, F.N.2    Rennert, O.M.3
  • 53
    • 0020079659 scopus 로고
    • Polyamine degradation in foetal and adult bovine serum
    • Gahl WA, Pitot HC. Polyamine degradation in foetal and adult bovine serum. Biochem J 1982; 202: 603-11.
    • (1982) Biochem J , vol.202 , pp. 603-611
    • Gahl, W.A.1    Pitot, H.C.2
  • 54
    • 0021920139 scopus 로고
    • The influence of catabolic reactions on polyamine excretion
    • Seiler N, Bolkenius FN, Knodgen B. The influence of catabolic reactions on polyamine excretion. Biochem J 1985; 225: 219-26.
    • (1985) Biochem J , vol.225 , pp. 219-226
    • Seiler, N.1    Bolkenius, F.N.2    Knodgen, B.3
  • 55
    • 0043037215 scopus 로고    scopus 로고
    • Cations as hydrogen bond donors: A view of electrostatic interactions in DNA
    • Subirana JA, Soler-Lopez M. Cations as hydrogen bond donors: a view of electrostatic interactions in DNA. Annu Rev Biophys Biomol Struct 2003; 32: 27-45.
    • (2003) Annu Rev Biophys Biomol Struct , vol.32 , pp. 27-45
    • Subirana, J.A.1    Soler-Lopez, M.2
  • 56
    • 0035393302 scopus 로고    scopus 로고
    • Amino acid-base interactions: A three-dimensional analysis of protein-DNA interactions at an atomic level
    • Luscombe NM, Laskowski RA, Thornton JM. Amino acid-base interactions: a three-dimensional analysis of protein-DNA interactions at an atomic level. Nucleic Acids Res 2001; 29: 2860-74.
    • (2001) Nucleic Acids Res , vol.29 , pp. 2860-2874
    • Luscombe, N.M.1    Laskowski, R.A.2    Thornton, J.M.3
  • 57
    • 0021014567 scopus 로고
    • Ion competition and micrococcal nuclease digestion studies of spermidine-condensed calf thymus DNA. Evidence for torus organization by circumferential DNA wrapping
    • Marx KA, Reynolds TC. Ion competition and micrococcal nuclease digestion studies of spermidine-condensed calf thymus DNA. Evidence for torus organization by circumferential DNA wrapping. Biochim Biophys Acta 1983; 741: 279-87.
    • (1983) Biochim Biophys Acta , vol.741 , pp. 279-287
    • Marx, K.A.1    Reynolds, T.C.2
  • 58
    • 0026100889 scopus 로고
    • Role of unsaturated derivatives of spermidine as substrates for spermine synthase and in supporting growth of SV-3T3 cells
    • Pegg AE, Nagarajan S, Naficy S, Ganem B. Role of unsaturated derivatives of spermidine as substrates for spermine synthase and in supporting growth of SV-3T3 cells. Biochem J 1991; 274: 167-71.
    • (1991) Biochem J , vol.274 , pp. 167-171
    • Pegg, A.E.1    Nagarajan, S.2    Naficy, S.3    Ganem, B.4
  • 59
    • 0025716865 scopus 로고
    • Spermine-like functions of N1, N12-bis(ethyl)spermine: Stimulation of protein synthesis and cell growth and inhibition of gastric ulceration
    • Igarashi K, Kashiwagi K, Fukuchi J-I, et al. Spermine-like functions of N1, N12-bis(ethyl)spermine: stimulation of protein synthesis and cell growth and inhibition of gastric ulceration. Biochem Biophys Res Commun 1990; 172: 715-20.
    • (1990) Biochem Biophys Res Commun , vol.172 , pp. 715-720
    • Igarashi, K.1    Kashiwagi, K.2    Fukuchi, J.-I.3
  • 60
    • 0024416719 scopus 로고
    • Correlation between the effects of polyamine analogues on DNA conformation and cell growth
    • Basu HS, Feuerstein BG, Denn DF, et al. Correlation between the effects of polyamine analogues on DNA conformation and cell growth. Cancer Res 1989; 49: 5591-7.
    • (1989) Cancer Res , vol.49 , pp. 5591-5597
    • Basu, H.S.1    Feuerstein, B.G.2    Denn, D.F.3
  • 61
    • 0345055328 scopus 로고    scopus 로고
    • DNA bending by small, mobile multivalent cations
    • Rouzina I, Bloomfield VA. DNA bending by small, mobile multivalent cations. Biophys J 1998; 74: 3152-64.
    • (1998) Biophys J , vol.74 , pp. 3152-3164
    • Rouzina, I.1    Bloomfield, V.A.2
  • 62
    • 80855163383 scopus 로고    scopus 로고
    • Investigations on the spermine provoked liquid crystalline phase behavior of high molecular weight DNA in the presence of alkali and alkaline earth metal ions
    • Sundaresan N, Thomas T, Thomas TJ, Pillai CKS. Investigations on the spermine provoked liquid crystalline phase behavior of high molecular weight DNA in the presence of alkali and alkaline earth metal ions. Polym Chem 2011; 2: 2835-41.
    • (2011) Polym Chem , vol.2 , pp. 2835-2841
    • Sundaresan, N.1    Thomas, T.2    Thomas, T.J.3    Pillai, C.K.S.4
  • 63
    • 0021715060 scopus 로고
    • The role of polyamine depletion and accumulation of decarboxylated S-adenosyl-methionine in the inhibition of growth of SV-3T3 cells treated with alpha-difluoromethylornithine
    • Pegg AE. The role of polyamine depletion and accumulation of decarboxylated S-adenosyl-methionine in the inhibition of growth of SV-3T3 cells treated with alpha-difluoromethylornithine. Biochem J 1984; 224: 29-38.
    • (1984) Biochem J , vol.224 , pp. 29-38
    • Pegg, A.E.1
  • 64
    • 79960181862 scopus 로고    scopus 로고
    • The use of novel C-methylated spermidine derivatives to investigate the regulation of polyamine metabolism
    • Hyvönen MT, Keinänen TA, Khomutov M, et al. The use of novel C-methylated spermidine derivatives to investigate the regulation of polyamine metabolism. J Med Chem 2011; 54: 4611-8.
    • (2011) J Med Chem , vol.54 , pp. 4611-4618
    • Hyvönen, M.T.1    Keinänen, T.A.2    Khomutov, M.3
  • 65
    • 77955358041 scopus 로고    scopus 로고
    • Synthesis and biological characterization of novel charge-deficient spermine analogues
    • Weisell J, Hyvönen MT, Häkkinen MR, et al. Synthesis and biological characterization of novel charge-deficient spermine analogues. J Med Chem 2010; 53: 5738-48.
    • (2010) J Med Chem , vol.53 , pp. 5738-5748
    • Weisell, J.1    Hyvönen, M.T.2    Häkkinen, M.R.3
  • 67
    • 77956311711 scopus 로고    scopus 로고
    • eIF5A promotes translation elongation, polysome disassembly and stress granule assembly
    • Li CH, Ohn T, Ivanov P, Tisdale S, Anderson P. eIF5A promotes translation elongation, polysome disassembly and stress granule assembly. PLoS One 2010; 5: e9942.
    • (2010) PLoS One , vol.5
    • Li, C.H.1    Ohn, T.2    Ivanov, P.3    Tisdale, S.4    Anderson, P.5
  • 68
    • 77955669607 scopus 로고    scopus 로고
    • Polyamines accelerate codon recognition by transfer RNAs on the ribosome
    • Hetrick B, Khade PK, Lee K, et al. Polyamines accelerate codon recognition by transfer RNAs on the ribosome. Biochemistry 2010; 49: 7179-89.
    • (2010) Biochemistry , vol.49 , pp. 7179-7189
    • Hetrick, B.1    Khade, P.K.2    Lee, K.3
  • 69
    • 0024588671 scopus 로고
    • Structure-function correlations of polyamine analog-induced increases in spermidine/spermine acetyltransferase activity
    • Libby PR, Bergeron RJ, Porter CW. Structure-function correlations of polyamine analog-induced increases in spermidine/spermine acetyltransferase activity. Biochem Pharmacol 1989; 38: 1435-42.
    • (1989) Biochem Pharmacol , vol.38 , pp. 1435-1442
    • Libby, P.R.1    Bergeron, R.J.2    Porter, C.W.3
  • 70
    • 0036714176 scopus 로고    scopus 로고
    • Antizyme induction by polyamine analogues as a factor of cell growth inhibition
    • Mitchell JL, Leyser A, Holtorff MS, et al. Antizyme induction by polyamine analogues as a factor of cell growth inhibition. Biochem J 2002; 366: 663-71.
    • (2002) Biochem J , vol.366 , pp. 663-671
    • Mitchell, J.L.1    Leyser, A.2    Holtorff, M.S.3
  • 71
    • 0025833516 scopus 로고
    • Correlations between polyamine analogue-induced increases in spermidine/spermine N1-acetyltransferase activity, polyamine pool depletion, and growth inhibition in human melanoma cell lines
    • Porter CW, Ganis B, Libby PR, Bergeron RJ. Correlations between polyamine analogue-induced increases in spermidine/spermine N1-acetyltransferase activity, polyamine pool depletion, and growth inhibition in human melanoma cell lines. Cancer Res 1991; 51: 3715-20.
    • (1991) Cancer Res , vol.51 , pp. 3715-3720
    • Porter, C.W.1    Ganis, B.2    Libby, P.R.3    Bergeron, R.J.4
  • 72
    • 0028062056 scopus 로고
    • Antiproliferative properties of polyamine analogues: A structure-activity study
    • Bergeron RJ, McManis JS, Liu CZ, et al. Antiproliferative properties of polyamine analogues: a structure-activity study. J Med Chem 1994; 37: 3464-76.
    • (1994) J Med Chem , vol.37 , pp. 3464-3476
    • Bergeron, R.J.1    McManis, J.S.2    Liu, C.Z.3
  • 73
    • 34547684794 scopus 로고    scopus 로고
    • Anthraquinone polyamines: Novel channel blockers of N-methyl-D-aspartate receptors
    • Kashiwagi K, Williams K, Igarashi K. Anthraquinone polyamines: novel channel blockers of N-methyl-D-aspartate receptors. Amino Acids 2007; 33: 299-304.
    • (2007) Amino Acids , vol.33 , pp. 299-304
    • Kashiwagi, K.1    Williams, K.2    Igarashi, K.3
  • 74
    • 0031662088 scopus 로고    scopus 로고
    • Block of the Kir2. 1 channel pore by alkylamine analogues of endogenous polyamines
    • Pearson WL, Nichols CG. Block of the Kir2. 1 channel pore by alkylamine analogues of endogenous polyamines. J Gen Physiol 1998; 112: 351-63.
    • (1998) J Gen Physiol , vol.112 , pp. 351-363
    • Pearson, W.L.1    Nichols, C.G.2
  • 75
    • 0030853492 scopus 로고    scopus 로고
    • Interactions of polyamines with ion channels
    • Williams K. Interactions of polyamines with ion channels. Biochem J 1997; 325: 289-97.
    • (1997) Biochem J , vol.325 , pp. 289-297
    • Williams, K.1
  • 76
    • 0030474273 scopus 로고    scopus 로고
    • Polyamine analogue regulation of NMDA MK-801 binding: A structure-activity study
    • Bergeron RJ, Weimar WR, Wu Q, Feng Y, McManis JS. Polyamine analogue regulation of NMDA MK-801 binding: a structure-activity study. J Med Chem 1996; 39: 5257-66.
    • (1996) J Med Chem , vol.39 , pp. 5257-5266
    • Bergeron, R.J.1    Weimar, W.R.2    Wu, Q.3    Feng, Y.4    McManis, J.S.5
  • 77
    • 36849048654 scopus 로고    scopus 로고
    • Role of hypusinated eukaryotic translation initiation factor 5A in polyamine depletion-induced cytostasis
    • Hyvönen MT, Keinänen TA, Cerrada-Gimenez M, et al. Role of hypusinated eukaryotic translation initiation factor 5A in polyamine depletion-induced cytostasis. J Biol Chem 2007; 282: 34700-6.
    • (2007) J Biol Chem , vol.282 , pp. 34700-34706
    • Hyvönen, M.T.1    Keinänen, T.A.2    Cerrada-Gimenez, M.3
  • 78
    • 0035179156 scopus 로고    scopus 로고
    • Cell culture analysis of the regulatory frameshift event required for the expression of mammalian antizymes
    • Howard MT, Shirts BH, Zhou J, et al. Cell culture analysis of the regulatory frameshift event required for the expression of mammalian antizymes. Genes Cells 2001; 6: 931-41.
    • (2001) Genes Cells , vol.6 , pp. 931-941
    • Howard, M.T.1    Shirts, B.H.2    Zhou, J.3
  • 79
    • 0035851192 scopus 로고    scopus 로고
    • Polyamine regulation of ribosome pausing at the upstream open reading frame of Sadenosylmethionine decarboxylase
    • Law GL, Raney A, Heusner C, Morris DR. Polyamine regulation of ribosome pausing at the upstream open reading frame of Sadenosylmethionine decarboxylase. J Biol Chem 2001; 276: 38036-43.
    • (2001) J Biol Chem , vol.276 , pp. 38036-38043
    • Law, G.L.1    Raney, A.2    Heusner, C.3    Morris, D.R.4
  • 80
    • 2442575980 scopus 로고    scopus 로고
    • Polyamines as clinical laboratory tools
    • Gugliucci A. Polyamines as clinical laboratory tools. Clin Chim Acta 2004; 344: 23-35.
    • (2004) Clin Chim Acta , vol.344 , pp. 23-35
    • Gugliucci, A.1
  • 81
    • 42949166398 scopus 로고    scopus 로고
    • Polyamine acetylation modulates polyamine metabolic flux, a prelude to broader metabolic consequences
    • Kramer DL, Diegelman P, Jell J, et al. Polyamine acetylation modulates polyamine metabolic flux, a prelude to broader metabolic consequences. J Biol Chem 2008; 283: 4241-51.
    • (2008) J Biol Chem , vol.283 , pp. 4241-4251
    • Kramer, D.L.1    Diegelman, P.2    Jell, J.3
  • 82
    • 34347347166 scopus 로고    scopus 로고
    • Enhanced polyamine catabolism alters homeostatic control of white adipose tissue, and energy, and glucose metabolism
    • Pirinen E, Kuulasmaa T, Pietilä M, et al. Enhanced polyamine catabolism alters homeostatic control of white adipose tissue, and energy, and glucose metabolism. Mol Cell Biol 2007; 27: 4953-67.
    • (2007) Mol Cell Biol , vol.27 , pp. 4953-4967
    • Pirinen, E.1    Kuulasmaa, T.2    Pietilä, M.3
  • 83
    • 34247113677 scopus 로고    scopus 로고
    • Mechanisms of polyamine catabolism-induced acute pancreatitis
    • Hyvönen MT, Merentie M, Uimari A, et al. Mechanisms of polyamine catabolism-induced acute pancreatitis. Biochem Soc Trans 2007: 35: 326-30.
    • (2007) Biochem Soc Trans , vol.35 , pp. 326-330
    • Hyvönen, M.T.1    Merentie, M.2    Uimari, A.3
  • 84
    • 34247122250 scopus 로고    scopus 로고
    • Inflammation and polyamine catabolism: The good, the bad and the ugly
    • Babbar N, Murray-Stewart T, Casero RA, Jr. Inflammation and polyamine catabolism: the good, the bad and the ugly. Biochem Soc Trans 2007; 35: 300-4.
    • (2007) Biochem Soc Trans , vol.35 , pp. 300-304
    • Babbar, N.1    Murray-Stewart, T.2    Casero Jr., R.A.3
  • 85
    • 85046980953 scopus 로고    scopus 로고
    • Spermine oxidase, a polyamine catabolic enzyme that links Helicobacter pylori CagA and gastric cancer risk
    • Chaturvedi R, de Sablet T, Peek R, Wilson K. Spermine oxidase, a polyamine catabolic enzyme that links Helicobacter pylori CagA and gastric cancer risk. Gut Microbes 2012; 3: 48-56.
    • (2012) Gut Microbes , vol.3 , pp. 48-56
    • Chaturvedi, R.1    de Sablet, T.2    Peek, R.3    Wilson, K.4
  • 86
    • 17444421537 scopus 로고    scopus 로고
    • The aldehyde acrolein induces apoptosis via activation of the mitochondrial pathway
    • Tanel A, Averill-Bates DA. The aldehyde acrolein induces apoptosis via activation of the mitochondrial pathway. Biochim Biophys Acta 2005; 1743: 255-67.
    • (2005) Biochim Biophys Acta , vol.1743 , pp. 255-267
    • Tanel, A.1    Averill-Bates, D.A.2
  • 87
    • 36849084656 scopus 로고    scopus 로고
    • Metabolic regulatory properties of S-adenosylmethionine and S-adenosylhomocysteine
    • Finkelstein JD. Metabolic regulatory properties of S-adenosylmethionine and S-adenosylhomocysteine. Clin Chem Lab Med 2007; 45: 1694-9.
    • (2007) Clin Chem Lab Med , vol.45 , pp. 1694-1699
    • Finkelstein, J.D.1
  • 88
    • 77955497115 scopus 로고    scopus 로고
    • A central role for polyamines in microtubule assembly in cells
    • Savarin P, Barbet A, Delga S, et al. A central role for polyamines in microtubule assembly in cells. Biochem J 2010; 430: 151-9.
    • (2010) Biochem J , vol.430 , pp. 151-159
    • Savarin, P.1    Barbet, A.2    Delga, S.3
  • 89
    • 84865812201 scopus 로고    scopus 로고
    • How cells know the size of their organelles
    • Chan YH, Marshall WF. How cells know the size of their organelles. Science 2012; 337: 1186-9.
    • (2012) Science , vol.337 , pp. 1186-1189
    • Chan, Y.H.1    Marshall, W.F.2
  • 90
    • 0030856485 scopus 로고    scopus 로고
    • Polyamine-dependent alterations in the structure of microfilaments, Golgi apparatus, endoplasmic reticulum, and proteoglycan synthesis in BHK cells
    • Parkkinen JJ, Lammi MJ, Ågren U, et al. Polyamine-dependent alterations in the structure of microfilaments, Golgi apparatus, endoplasmic reticulum, and proteoglycan synthesis in BHK cells. J Cell Biochem 1997; 66: 165-74.
    • (1997) J Cell Biochem , vol.66 , pp. 165-174
    • Parkkinen, J.J.1    Lammi, M.J.2    Ågren, U.3
  • 91
    • 77955847340 scopus 로고    scopus 로고
    • Ornithine decarboxylase and extracellular polyamines regulate microvascular sprouting and actin cytoskeleton dynamics in endothelial cells
    • Kucharzewska P, Welch JE, Svensson KJ, Belting M. Ornithine decarboxylase and extracellular polyamines regulate microvascular sprouting and actin cytoskeleton dynamics in endothelial cells. Exp Cell Res 2010; 316: 2683-91.
    • (2010) Exp Cell Res , vol.316 , pp. 2683-2691
    • Kucharzewska, P.1    Welch, J.E.2    Svensson, K.J.3    Belting, M.4
  • 92
    • 0016687709 scopus 로고
    • Physiology of the natural polyamines putrescine, spermidine and spermine
    • Raina A, Jänne J. Physiology of the natural polyamines putrescine, spermidine and spermine. Med Biol 1975; 53: 121-47.
    • (1975) Med Biol , vol.53 , pp. 121-147
    • Raina, A.1    Jänne, J.2
  • 93
    • 0018349870 scopus 로고
    • Suppression of the formation of polyamines and macromolecules by DL-alpha-difluoromethylornithine and methylglyoxal bis(guanylhydrazone) in phytohaemagglutinin-activated human lymphocytes
    • Hölttä E, Jänne J, Hovi T. Suppression of the formation of polyamines and macromolecules by DL-alpha-difluoromethylornithine and methylglyoxal bis(guanylhydrazone) in phytohaemagglutinin-activated human lymphocytes. Biochem J 1979; 178: 109-17.
    • (1979) Biochem J , vol.178 , pp. 109-117
    • Hölttä, E.1    Jänne, J.2    Hovi, T.3
  • 94
    • 77953233134 scopus 로고    scopus 로고
    • Ornithine decarboxylase antizyme inhibitor 2 regulates intracellular vesicle trafficking
    • Kanerva K, Makitie LT, Back N, Andersson LC. Ornithine decarboxylase antizyme inhibitor 2 regulates intracellular vesicle trafficking. Exp Cell Res 2010; 316: 1896-906.
    • (2010) Exp Cell Res , vol.316 , pp. 1896-1906
    • Kanerva, K.1    Makitie, L.T.2    Back, N.3    Andersson, L.C.4
  • 95
    • 77953039922 scopus 로고    scopus 로고
    • Functional significance of eIF5A and its hypusine modification in eukaryotes
    • Park MH, Nishimura K, Zanelli CF, Valentini SR. Functional significance of eIF5A and its hypusine modification in eukaryotes. Amino Acids 2010; 38: 491-500.
    • (2010) Amino Acids , vol.38 , pp. 491-500
    • Park, M.H.1    Nishimura, K.2    Zanelli, C.F.3    Valentini, S.R.4
  • 96
    • 10944251575 scopus 로고    scopus 로고
    • Identification of mRNA that binds to eukaryotic initiation factor 5A by affinity co-purification and differential display
    • Xu A, Jao DL, Chen KY. Identification of mRNA that binds to eukaryotic initiation factor 5A by affinity co-purification and differential display. Biochem J 2004; 384: 585-90.
    • (2004) Biochem J , vol.384 , pp. 585-590
    • Xu, A.1    Jao, D.L.2    Chen, K.Y.3
  • 97
    • 0028145708 scopus 로고
    • Effect of initiation factor eIF-5A depletion on protein synthesis and proliferation of Saccharomyces cerevisiae
    • Kang HA, Hershey JW. Effect of initiation factor eIF-5A depletion on protein synthesis and proliferation of Saccharomyces cerevisiae. J Biol Chem 1994; 269: 3934-40.
    • (1994) J Biol Chem , vol.269 , pp. 3934-3940
    • Kang, H.A.1    Hershey, J.W.2
  • 98
    • 77953186469 scopus 로고    scopus 로고
    • The unique hypusine modification of eIF5A promotes islet beta cell inflammation and dysfunction in mice
    • Maier B, Ogihara T, Trace AP, et al. The unique hypusine modification of eIF5A promotes islet beta cell inflammation and dysfunction in mice. J Clin Invest 2010; 120: 2156-70.
    • (2010) J Clin Invest , vol.120 , pp. 2156-2170
    • Maier, B.1    Ogihara, T.2    Trace, A.P.3
  • 99
    • 78650053328 scopus 로고    scopus 로고
    • Inhibition of deoxyhypusine synthase enhances islet {beta} cell function and survival in the setting of endoplasmic reticulum stress and type 2 diabetes
    • Robbins RD, Tersey SA, Ogihara T, et al. Inhibition of deoxyhypusine synthase enhances islet {beta} cell function and survival in the setting of endoplasmic reticulum stress and type 2 diabetes. J Biol Chem 2010; 285: 39943-52.
    • (2010) J Biol Chem , vol.285 , pp. 39943-39952
    • Robbins, R.D.1    Tersey, S.A.2    Ogihara, T.3
  • 100
    • 79959769631 scopus 로고    scopus 로고
    • Hypusine: A new target for therapeutic intervention in diabetic inflammation
    • Maier B, Tersey SA, Mirmira RG. Hypusine: a new target for therapeutic intervention in diabetic inflammation. Discov Med 2010; 10: 18-23.
    • (2010) Discov Med , vol.10 , pp. 18-23
    • Maier, B.1    Tersey, S.A.2    Mirmira, R.G.3
  • 101
    • 70449529855 scopus 로고    scopus 로고
    • Induction of autophagy by spermidine promotes longevity
    • Eisenberg T, Knauer H, Schauer A, et al. Induction of autophagy by spermidine promotes longevity. Nat Cell Biol 2009; 11: 1305-14.
    • (2009) Nat Cell Biol , vol.11 , pp. 1305-1314
    • Eisenberg, T.1    Knauer, H.2    Schauer, A.3
  • 102
    • 80655130325 scopus 로고    scopus 로고
    • Thapsigargin distinguishes membrane fusion in the late stages of endocytosis and autophagy
    • Ganley IG, Wong PM, Jiang X. Thapsigargin distinguishes membrane fusion in the late stages of endocytosis and autophagy. Autophagy 2011; 7: 1397-9.
    • (2011) Autophagy , vol.7 , pp. 1397-1399
    • Ganley, I.G.1    Wong, P.M.2    Jiang, X.3
  • 103
    • 79959346132 scopus 로고    scopus 로고
    • Distinct autophagosomal-lysosomal fusion mechanism revealed by thapsigargin-induced autophagy arrest
    • Ganley IG, Wong PM, Gammoh N, Jiang X. Distinct autophagosomal-lysosomal fusion mechanism revealed by thapsigargin-induced autophagy arrest. Mol Cell 2011; 42: 731-43.
    • (2011) Mol Cell , vol.42 , pp. 731-743
    • Ganley, I.G.1    Wong, P.M.2    Gammoh, N.3    Jiang, X.4
  • 104
    • 79951889242 scopus 로고    scopus 로고
    • Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome
    • Morselli E, Marino G, Bennetzen MV, et al. Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome. J Cell Biol 2011; 192: 615-29.
    • (2011) J Cell Biol , vol.192 , pp. 615-629
    • Morselli, E.1    Marino, G.2    Bennetzen, M.V.3
  • 105
    • 79957879876 scopus 로고    scopus 로고
    • Longevity-relevant regulation of autophagy at the level of the acetylproteome
    • Marino G, Morselli E, Bennetzen MV, et al. Longevity-relevant regulation of autophagy at the level of the acetylproteome. Autophagy 2011; 7: 647-9.
    • (2011) Autophagy , vol.7 , pp. 647-649
    • Marino, G.1    Morselli, E.2    Bennetzen, M.V.3
  • 106
    • 78649869949 scopus 로고    scopus 로고
    • Characteristics of cellular polyamine transport in prokaryotes and eukaryotes
    • Igarashi K, Kashiwagi K. Characteristics of cellular polyamine transport in prokaryotes and eukaryotes. Plant Physiol Biochem 2010; 48: 506-12.
    • (2010) Plant Physiol Biochem , vol.48 , pp. 506-512
    • Igarashi, K.1    Kashiwagi, K.2
  • 107
    • 84861677889 scopus 로고    scopus 로고
    • Recent advances in the molecular biology of metazoan polyamine transport
    • Poulin R, Casero RA, Soulet D. Recent advances in the molecular biology of metazoan polyamine transport. Amino Acids 2012; 42: 711-23.
    • (2012) Amino Acids , vol.42 , pp. 711-723
    • Poulin, R.1    Casero, R.A.2    Soulet, D.3
  • 108
    • 30144434501 scopus 로고    scopus 로고
    • Polyamine transport by mammalian cells and mitochondria: Role of antizyme and glycosaminoglycans
    • Hoshino K, Momiyama E, Yoshida K, et al. Polyamine transport by mammalian cells and mitochondria: role of antizyme and glycosaminoglycans. J Biol Chem 2005; 280: 42801-8.
    • (2005) J Biol Chem , vol.280 , pp. 42801-42808
    • Hoshino, K.1    Momiyama, E.2    Yoshida, K.3
  • 109
    • 0037347195 scopus 로고    scopus 로고
    • Mitochondrial localization of antizyme is determined by context-dependent alternative utilization of two AUG initiation codons
    • Gandre S, Bercovich Z, Kahana C. Mitochondrial localization of antizyme is determined by context-dependent alternative utilization of two AUG initiation codons. Mitochondrion 2003; 2: 245-56.
    • (2003) Mitochondrion , vol.2 , pp. 245-256
    • Gandre, S.1    Bercovich, Z.2    Kahana, C.3
  • 110
    • 84861666361 scopus 로고    scopus 로고
    • Effect of peroxides on spermine transport in rat brain and liver mitochondria
    • Battaglia V, Tibaldi E, Grancara S, et al. Effect of peroxides on spermine transport in rat brain and liver mitochondria. Amino Acids 2012; 42: 741-9.
    • (2012) Amino Acids , vol.42 , pp. 741-749
    • Battaglia, V.1    Tibaldi, E.2    Grancara, S.3
  • 111
    • 1542330759 scopus 로고    scopus 로고
    • Effects of polyamines on mitochondrial Ca(2+) transport
    • Salvi M, Toninello A. Effects of polyamines on mitochondrial Ca(2+) transport. Biochim Biophys Acta 2004; 1661: 113-24.
    • (2004) Biochim Biophys Acta , vol.1661 , pp. 113-124
    • Salvi, M.1    Toninello, A.2
  • 113
    • 84861661599 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress induced by Ca2+ and monoamines: Different behaviour of liver and brain mitochondria in undergoing permeability transition
    • Grancara S, Battaglia V, Martinis P, et al. Mitochondrial oxidative stress induced by Ca2+ and monoamines: different behaviour of liver and brain mitochondria in undergoing permeability transition. Amino Acids 2012; 42: 751-9.
    • (2012) Amino Acids , vol.42 , pp. 751-759
    • Grancara, S.1    Battaglia, V.2    Martinis, P.3
  • 114
    • 0000594806 scopus 로고    scopus 로고
    • The natural polyamine spermine functions directly as a free radical scavenger
    • Ha HC, Sirisoma NS, Kuppusamy P, et al. The natural polyamine spermine functions directly as a free radical scavenger. Proc Natl Acad Sci USA 1998; 95: 11140-45.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 11140-11145
    • Ha, H.C.1    Sirisoma, N.S.2    Kuppusamy, P.3
  • 115
    • 34548150619 scopus 로고    scopus 로고
    • Physiological polyamines: Simple primordial stress molecules
    • Rhee HJ, Kim EJ, Lee JK. Physiological polyamines: simple primordial stress molecules. J Cell Mol Med 2007; 11: 685-703.
    • (2007) J Cell Mol Med , vol.11 , pp. 685-703
    • Rhee, H.J.1    Kim, E.J.2    Lee, J.K.3
  • 116
    • 0014981738 scopus 로고
    • Inhibition of nucleic acid and protein synthesis in Escherichia coli by oxidized polyamines and acrolein
    • Kimes BW, Morris DR. Inhibition of nucleic acid and protein synthesis in Escherichia coli by oxidized polyamines and acrolein. Biochim Biophys Acta 1971; 228: 235-44.
    • (1971) Biochim Biophys Acta , vol.228 , pp. 235-244
    • Kimes, B.W.1    Morris, D.R.2
  • 117
    • 34547662510 scopus 로고    scopus 로고
    • Antiviral activity of oxidized polyamines
    • Bachrach U. Antiviral activity of oxidized polyamines. Amino Acids 2007; 33: 267-72.
    • (2007) Amino Acids , vol.33 , pp. 267-272
    • Bachrach, U.1
  • 118
    • 0022493556 scopus 로고
    • Detection of tetrafluoroputrescine in RBCs by fluorine-19 nuclear magnetic resonance spectroscopy
    • Digenis GA, Hawi AA, Yip H, Layton WJ. Detection of tetrafluoroputrescine in RBCs by fluorine-19 nuclear magnetic resonance spectroscopy. Life Sci 1986; 38: 2307-9.
    • (1986) Life Sci , vol.38 , pp. 2307-2309
    • Digenis, G.A.1    Hawi, A.A.2    Yip, H.3    Layton, W.J.4
  • 119
    • 0022527974 scopus 로고
    • 2-[18F]fluoroputrescine: Preparation, biodistribution, and mechanism of defluorination
    • Hwang DR, Jerabek PA, Kadmon D, et al. 2-[18F]fluoroputrescine: preparation, biodistribution, and mechanism of defluorination. Int J Rad Appl Instrum A 1986; 37: 607-12.
    • (1986) Int J Rad Appl Instrum A , vol.37 , pp. 607-612
    • Hwang, D.R.1    Jerabek, P.A.2    Kadmon, D.3
  • 120
    • 34548176036 scopus 로고    scopus 로고
    • Alpha-methylated polyamines as potential drugs and experimental tools in enzymology
    • Keinänen TA, Järvinen A, Uimari A, et al. Alpha-methylated polyamines as potential drugs and experimental tools in enzymology. Mini Rev Med Chem 2007; 7: 813-20.
    • (2007) Mini Rev Med Chem , vol.7 , pp. 813-820
    • Keinänen, T.A.1    Järvinen, A.2    Uimari, A.3
  • 121
    • 0024215527 scopus 로고
    • Chain-fluorinated polyamines as tumor markers-IV. Comparison of 2-fluoroputrescine and 2, 2-difluoro-putrescine as substrates of spermidine synthase in vitro and in vivo
    • Dezeure F, Sarhan S, Seiler N. Chain-fluorinated polyamines as tumor markers-IV. Comparison of 2-fluoroputrescine and 2, 2-difluoro-putrescine as substrates of spermidine synthase in vitro and in vivo. Int J Biochem 1988; 20: 1299-312.
    • (1988) Int J Biochem , vol.20 , pp. 1299-1312
    • Dezeure, F.1    Sarhan, S.2    Seiler, N.3
  • 122
    • 11144346697 scopus 로고    scopus 로고
    • Determination of protonation constants of some fluorinated polyamines by means of 13C NMR data processed by the new computer program HypNMR2000. Protonation sequence in polyamines
    • Frassineti C, Alderighi L, Gans P, et al. Determination of protonation constants of some fluorinated polyamines by means of 13C NMR data processed by the new computer program HypNMR2000. Protonation sequence in polyamines. Anal Bioanal Chem 2003; 376: 1041-52.
    • (2003) Anal Bioanal Chem , vol.376 , pp. 1041-1052
    • Frassineti, C.1    Alderighi, L.2    Gans, P.3
  • 123
    • 0023747638 scopus 로고
    • Fluorinated analogues of spermidine as substrates of spermine synthase
    • Baillon JG, Mamont PS, Wagner J, Gerhart F, Lux P. Fluorinated analogues of spermidine as substrates of spermine synthase. Eur J Biochem 1988; 176: 237-42.
    • (1988) Eur J Biochem , vol.176 , pp. 237-242
    • Baillon, J.G.1    Mamont, P.S.2    Wagner, J.3    Gerhart, F.4    Lux, P.5
  • 124
    • 0023220612 scopus 로고
    • Chain-fluorinated polyamines as tumor markers-I. In vivo transformation of 2, 2-difluoroputrescine into 6, 6-difluorospermidine and 6, 6-difluorospermine
    • Sarhan S, Knodgen B, Gerhart F, Seiler N. Chain-fluorinated polyamines as tumor markers-I. In vivo transformation of 2, 2-difluoroputrescine into 6, 6-difluorospermidine and 6, 6-difluorospermine. Int J Biochem 1987; 19: 843-52.
    • (1987) Int J Biochem , vol.19 , pp. 843-852
    • Sarhan, S.1    Knodgen, B.2    Gerhart, F.3    Seiler, N.4
  • 125
    • 0028828901 scopus 로고
    • Use of 4-fluoro-Lornithine to monitor metabolic flux through the polyamine biosynthetic pathway
    • Kramer D, Stanek J, Diegelman P, et al. Use of 4-fluoro-Lornithine to monitor metabolic flux through the polyamine biosynthetic pathway. Biochem Pharmacol 1995; 50: 1433-43.
    • (1995) Biochem Pharmacol , vol.50 , pp. 1433-1443
    • Kramer, D.1    Stanek, J.2    Diegelman, P.3
  • 126
    • 0024325586 scopus 로고
    • Activation of rat liver Sadenosylmethionine decarboxylase by putrescine and 2-substituted 1, 4,-butanediamines
    • Dezeure F, Gerhart F, Seiler N. Activation of rat liver Sadenosylmethionine decarboxylase by putrescine and 2-substituted 1, 4,-butanediamines. Int J Biochem 1989; 21: 889-99.
    • (1989) Int J Biochem , vol.21 , pp. 889-899
    • Dezeure, F.1    Gerhart, F.2    Seiler, N.3
  • 127
    • 84861668845 scopus 로고    scopus 로고
    • Polyamine flux analysis by determination of heavy isotope incorporation from (13)C, (15)N-enriched amino acids into polyamines by LC-MS/MS
    • Cerrada-Gimenez M, Häkkinen MR, Vepsäläinen J, et al. Polyamine flux analysis by determination of heavy isotope incorporation from (13)C, (15)N-enriched amino acids into polyamines by LC-MS/MS. Amino Acids 2012; 42: 451-60.
    • (2012) Amino Acids , vol.42 , pp. 451-460
    • Cerrada-Gimenez, M.1    Häkkinen, M.R.2    Vepsäläinen, J.3
  • 128
    • 0023868486 scopus 로고
    • Chain-fluorinated polyamines as tumor markers. II. Metabolic aspects in normal tissues
    • Seiler N, Sarhan S, Knödgen B, Gerhart F. Chain-fluorinated polyamines as tumor markers. II. Metabolic aspects in normal tissues. J Cancer Res Clin Oncol 1988; 114: 71-80.
    • (1988) J Cancer Res Clin Oncol , vol.114 , pp. 71-80
    • Seiler, N.1    Sarhan, S.2    Knödgen, B.3    Gerhart, F.4
  • 129
    • 0025077338 scopus 로고
    • Aminooxy analogues of spermidine as inhibitors of spermine synthase and substrates of hepatic polyamine acetylating activity
    • Eloranta TO, Khomutov AR, Khomutov RM, Hyvönen T. Aminooxy analogues of spermidine as inhibitors of spermine synthase and substrates of hepatic polyamine acetylating activity. J Biochem 1990; 108: 593-8.
    • (1990) J Biochem , vol.108 , pp. 593-598
    • Eloranta, T.O.1    Khomutov, A.R.2    Khomutov, R.M.3    Hyvönen, T.4
  • 130
    • 0027518126 scopus 로고
    • Features of the spermidinebinding site of deoxyhypusine synthase as derived from inhibition studies
    • Jakus J, Wolff EC, Park MH, Folk JE. Features of the spermidinebinding site of deoxyhypusine synthase as derived from inhibition studies. J Biol Chem 1993; 268: 13151-59.
    • (1993) J Biol Chem , vol.268 , pp. 13151-13159
    • Jakus, J.1    Wolff, E.C.2    Park, M.H.3    Folk, J.E.4
  • 131
    • 0041355635 scopus 로고    scopus 로고
    • Reversal of the deoxyhypusine synthesis reaction. Generation of spermidine or homospermidine from deoxyhypusine by deoxyhypusine synthase
    • Park JH, Wolff EC, Folk JE, Park MH. Reversal of the deoxyhypusine synthesis reaction. Generation of spermidine or homospermidine from deoxyhypusine by deoxyhypusine synthase. J Biol Chem 2003; 278: 32683-91.
    • (2003) J Biol Chem , vol.278 , pp. 32683-32691
    • Park, J.H.1    Wolff, E.C.2    Folk, J.E.3    Park, M.H.4
  • 133
    • 0025281643 scopus 로고
    • Effects of variation in the structure of spermine on the association with DNA and the induction of DNA conformational changes
    • Basu HS, Schwietert HCA, Feuerstein BG, Marton LJ. Effects of variation in the structure of spermine on the association with DNA and the induction of DNA conformational changes. Biochem J 1990; 269: 329-34.
    • (1990) Biochem J , vol.269 , pp. 329-334
    • Basu, H.S.1    Schwietert, H.C.A.2    Feuerstein, B.G.3    Marton, L.J.4
  • 135
    • 0000015939 scopus 로고
    • A Thermodynamic Study of Some Complexes of Metal Ions with Polyamines
    • Bertsch CR, Fernelius WC, Block BP. A Thermodynamic Study of Some Complexes of Metal Ions with Polyamines. J Phys Chem 1958; 62: 444-50.
    • (1958) J Phys Chem , vol.62 , pp. 444-450
    • Bertsch, C.R.1    Fernelius, W.C.2    Block, B.P.3
  • 136
    • 77953046262 scopus 로고    scopus 로고
    • Novel isosteric charge-deficient spermine analogue-1, 12-diamino-3, 6, 9-triazadodecane: Synthesis, pK(a) measurement and biological activity
    • Weisell J, Hyvönen MT, Vepsäläinen J, et al. Novel isosteric charge-deficient spermine analogue-1, 12-diamino-3, 6, 9-triazadodecane: synthesis, pK(a) measurement and biological activity. Amino Acids 2010; 38: 501-7.
    • (2010) Amino Acids , vol.38 , pp. 501-507
    • Weisell, J.1    Hyvönen, M.T.2    Vepsäläinen, J.3
  • 137
    • 84875540773 scopus 로고    scopus 로고
    • Tautomeric populations of the charged species of 1, 12-diamino-3, 6, 9-triazadodecane (SpmTrien) studied with computer simulations and cluster expansions. J Phys Org
    • Weisell J, Vepsäläinen J, Peräkylä M. Tautomeric populations of the charged species of 1, 12-diamino-3, 6, 9-triazadodecane (SpmTrien) studied with computer simulations and cluster expansions. J Phys Org. Chem 2013; 26: 360-6.
    • (2013) Chem , vol.26 , pp. 360-366
    • Weisell, J.1    Vepsäläinen, J.2    Peräkylä, M.3
  • 139
    • 0028856017 scopus 로고
    • Structural requirements of analogues of polyamines for migration and growth of IEC-6 cells
    • McCormack SA, Zimmerman BJ, Israel M, Blanner P, Johnson LR. Structural requirements of analogues of polyamines for migration and growth of IEC-6 cells. Mol Pharmacol 1995; 48: 724-9.
    • (1995) Mol Pharmacol , vol.48 , pp. 724-729
    • McCormack, S.A.1    Zimmerman, B.J.2    Israel, M.3    Blanner, P.4    Johnson, L.R.5
  • 140
    • 0014693218 scopus 로고
    • Management of penicillamine nephropathy in Wilson's disease: A new chelating agent
    • Walshe JM. Management of penicillamine nephropathy in Wilson's disease: a new chelating agent. Lancet 1969; 2: 1401-2.
    • (1969) Lancet , vol.2 , pp. 1401-1402
    • Walshe, J.M.1
  • 141
    • 79960497233 scopus 로고    scopus 로고
    • Therapeutic potential of copper chelation with triethylenetetramine in managing diabetes mellitus and Alzheimer's disease
    • Cooper GJ. Therapeutic potential of copper chelation with triethylenetetramine in managing diabetes mellitus and Alzheimer's disease. Drugs 2011; 71: 1281-320.
    • (2011) Drugs , vol.71 , pp. 1281-1320
    • Cooper, G.J.1
  • 142
    • 61449239980 scopus 로고    scopus 로고
    • A copper(II)-selective chelator ameliorates left-ventricular hypertrophy in type 2 diabetic patients: A randomised placebo-controlled study
    • Cooper GJ, Young AA, Gamble GD, et al. A copper(II)-selective chelator ameliorates left-ventricular hypertrophy in type 2 diabetic patients: a randomised placebo-controlled study. Diabetologia 2009; 52: 715-22.
    • (2009) Diabetologia , vol.52 , pp. 715-722
    • Cooper, G.J.1    Young, A.A.2    Gamble, G.D.3
  • 143
    • 0242285611 scopus 로고    scopus 로고
    • Triethylene tetraamine: A novel telomerase inhibitor
    • Yin F, Liu J, Peng X. Triethylene tetraamine: a novel telomerase inhibitor. Bioorg Med Chem Lett 2003; 13: 3923-6.
    • (2003) Bioorg Med Chem Lett , vol.13 , pp. 3923-3926
    • Yin, F.1    Liu, J.2    Peng, X.3
  • 144
    • 77953743734 scopus 로고    scopus 로고
    • Pharmacokinetics, pharmacodynamics, and metabolism of triethylenetetramine in healthy human participants: An open-label trial
    • Lu J, Poppitt SD, Othman AA, et al. Pharmacokinetics, pharmacodynamics, and metabolism of triethylenetetramine in healthy human participants: an open-label trial. J Clin Pharmacol 2010; 50: 647-58.
    • (2010) J Clin Pharmacol , vol.50 , pp. 647-658
    • Lu, J.1    Poppitt, S.D.2    Othman, A.A.3
  • 145
    • 84871562864 scopus 로고    scopus 로고
    • Metabolism of triethylenetetramine and 1, 12-diamino-3, 6, 9-triazadodecane by the spermidine/spermine-N1-acetyltransferase and thialysine acetyltransferase
    • Hyvönen MT, Weisell J, Khomutov A, et al. Metabolism of triethylenetetramine and 1, 12-diamino-3, 6, 9-triazadodecane by the spermidine/spermine-N1-acetyltransferase and thialysine acetyltransferase. Drug Metab Dispos 2013; 41: 30-2.
    • (2013) Drug Metab Dispos , vol.41 , pp. 30-32
    • Hyvönen, M.T.1    Weisell, J.2    Khomutov, A.3
  • 146
    • 2942622157 scopus 로고    scopus 로고
    • Linear polyamine copper chelator tetraethylenepentamine augments long-term ex vivo expansion of cord blood-derived CD34+ cells and increases their engraftment potential in NOD/SCID mice
    • Peled T, Landau E, Mandel J, et al. Linear polyamine copper chelator tetraethylenepentamine augments long-term ex vivo expansion of cord blood-derived CD34+ cells and increases their engraftment potential in NOD/SCID mice. Exp Hematol 2004; 32: 547-55.
    • (2004) Exp Hematol , vol.32 , pp. 547-555
    • Peled, T.1    Landau, E.2    Mandel, J.3
  • 147
    • 43849087808 scopus 로고    scopus 로고
    • Transplantation of ex vivo expanded cord blood cells using the copper chelator tetraethylenepentamine: A phase I/II clinical trial
    • de Lima M, McMannis J, Gee A, et al. Transplantation of ex vivo expanded cord blood cells using the copper chelator tetraethylenepentamine: a phase I/II clinical trial. Bone Marrow Transplant 2008; 41: 771-8.
    • (2008) Bone Marrow Transplant , vol.41 , pp. 771-778
    • de Lima, M.1    McMannis, J.2    Gee, A.3
  • 149
    • 77953841809 scopus 로고    scopus 로고
    • Copper in diseases and treatments, and copper-based anticancer strategies
    • Tisato F, Marzano C, Porchia M, Pellei M, Santini C. Copper in diseases and treatments, and copper-based anticancer strategies. Med Res Rev 2010; 30: 708-49.
    • (2010) Med Res Rev , vol.30 , pp. 708-749
    • Tisato, F.1    Marzano, C.2    Porchia, M.3    Pellei, M.4    Santini, C.5
  • 151
    • 33846403733 scopus 로고    scopus 로고
    • Triethylenetetramine and metabolites: Levels in relation to copper and zinc excretion in urine of healthy volunteers and type 2 diabetic patients
    • Lu J, Chan YK, Gamble GD, et al. Triethylenetetramine and metabolites: levels in relation to copper and zinc excretion in urine of healthy volunteers and type 2 diabetic patients. Drug Metab Dispos 2007; 35: 221-7.
    • (2007) Drug Metab Dispos , vol.35 , pp. 221-227
    • Lu, J.1    Chan, Y.K.2    Gamble, G.D.3
  • 152
    • 0030791354 scopus 로고    scopus 로고
    • Metabolism of administered triethylene tetramine dihydrochloride in humans
    • Kodama H, Murata Y, Iitsuka T, Abe T. Metabolism of administered triethylene tetramine dihydrochloride in humans. Life Sci 1997; 61: 899-907.
    • (1997) Life Sci , vol.61 , pp. 899-907
    • Kodama, H.1    Murata, Y.2    Iitsuka, T.3    Abe, T.4
  • 153
    • 0004713598 scopus 로고
    • Catalytic irreversible inhibition of mammalian ornithine decarboxylase (E.C. 4. 1. 1. 17) by substrate and product analogues. J Am. Chem
    • Metcalf BW, Bey P, Danzin C, et al. Catalytic irreversible inhibition of mammalian ornithine decarboxylase (E. C. 4. 1. 1. 17) by substrate and product analogues. J Am. Chem. Soc 1978; 100: 2551-53.
    • (1978) Soc , vol.100 , pp. 2551-2553
    • Metcalf, B.W.1    Bey, P.2    Danzin, C.3
  • 154
    • 0141633535 scopus 로고    scopus 로고
    • Thirty years of polyamine-related approaches to cancer therapy. Retrospect and prospect. Part 1. Selective enzyme inhibitors
    • Seiler N. Thirty years of polyamine-related approaches to cancer therapy. Retrospect and prospect. Part 1. Selective enzyme inhibitors. Curr Drug Targets 2003; 4: 537-64.
    • (2003) Curr Drug Targets , vol.4 , pp. 537-564
    • Seiler, N.1
  • 155
    • 34247136255 scopus 로고    scopus 로고
    • Revival of 2-(difluoromethyl)ornithine (DFMO), an inhibitor of polyamine biosynthesis, as a cancer chemopreventive agent
    • Raul F. Revival of 2-(difluoromethyl)ornithine (DFMO), an inhibitor of polyamine biosynthesis, as a cancer chemopreventive agent. Biochem Soc Trans 2007; 35: 353-5.
    • (2007) Biochem Soc Trans , vol.35 , pp. 353-355
    • Raul, F.1
  • 156
    • 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. Targeting the polyamine biosynthetic enzymes: a promising approach to therapy of African sleeping sickness, Chagas' disease, and leishmaniasis. Amino Acids 2007; 33: 359-66.
    • (2007) Amino Acids , vol.33 , pp. 359-366
    • Heby, O.1    Persson, L.2    Rentala, M.3
  • 157
    • 33745644733 scopus 로고    scopus 로고
    • Human African trypanosomiasis-neurological aspects
    • Kennedy PG. Human African trypanosomiasis-neurological aspects. J Neurol 2006; 253: 411-6.
    • (2006) J Neurol , vol.253 , pp. 411-416
    • Kennedy, P.G.1
  • 158
    • 33845955654 scopus 로고    scopus 로고
    • Randomized, double-blind clinical evaluation of the efficacy and safety of topical eflornithine HCl 13. 9% cream in the treatment of women with facial hair
    • Wolf JE, Jr., Shander D, Huber F, et al. Randomized, double-blind clinical evaluation of the efficacy and safety of topical eflornithine HCl 13. 9% cream in the treatment of women with facial hair. Int J Dermatol 2007; 46: 94-8.
    • (2007) Int J Dermatol , vol.46 , pp. 94-98
    • Wolf Jr., J.E.1    Shander, D.2    Huber, F.3
  • 159
    • 77954900977 scopus 로고    scopus 로고
    • Hirsutism: Diagnosis and management
    • Brodell LA, Mercurio MG. Hirsutism: Diagnosis and management. Gend Med 2010; 7: 79-87.
    • (2010) Gend Med , vol.7 , pp. 79-87
    • Brodell, L.A.1    Mercurio, M.G.2
  • 160
    • 79551533724 scopus 로고    scopus 로고
    • Targeting polyamines and inflammation for cancer prevention
    • Babbar N, Gerner EW. Targeting polyamines and inflammation for cancer prevention. Recent Results Cancer Res 2011; 188: 49-64.
    • (2011) Recent Results Cancer Res , vol.188 , pp. 49-64
    • Babbar, N.1    Gerner, E.W.2
  • 161
    • 34247167537 scopus 로고    scopus 로고
    • Impact of dietary amino acids and polyamines on intestinal carcinogenesis and chemoprevention in mouse models
    • Gerner EW. Impact of dietary amino acids and polyamines on intestinal carcinogenesis and chemoprevention in mouse models. Biochem Soc Trans 2007; 35: 322-5.
    • (2007) Biochem Soc Trans , vol.35 , pp. 322-325
    • Gerner, E.W.1
  • 162
    • 84875228105 scopus 로고    scopus 로고
    • Role of dietary polyamines in a phase III clinical trial of difluoromethylornithine (DFMO) and sulindac for prevention of sporadic colorectal adenomas
    • Raj KP, Zell JA, Rock CL, et al. Role of dietary polyamines in a phase III clinical trial of difluoromethylornithine (DFMO) and sulindac for prevention of sporadic colorectal adenomas. Br J Cancer 2013; 108: 512-8.
    • (2013) Br J Cancer , vol.108 , pp. 512-518
    • Raj, K.P.1    Zell, J.A.2    Rock, C.L.3
  • 163
    • 0024327868 scopus 로고
    • Microbial flora in the gastrointestinal tract abolishes cytostatic effects of alphadifluoromethylornithine in vivo
    • Hessels J, Kingma AW, Ferwerda H, et al. Microbial flora in the gastrointestinal tract abolishes cytostatic effects of alphadifluoromethylornithine in vivo. Int J Cancer 1989; 43: 1155-64.
    • (1989) Int J Cancer , vol.43 , pp. 1155-1164
    • Hessels, J.1    Kingma, A.W.2    Ferwerda, H.3
  • 164
    • 0028364261 scopus 로고
    • Polyamine deprivation: A new tool in cancer treatment
    • Quemener V, Blanchard Y, Chamaillard L, et al. Polyamine deprivation: a new tool in cancer treatment. Anticancer Res 1994; 14: 443-8.
    • (1994) Anticancer Res , vol.14 , pp. 443-448
    • Quemener, V.1    Blanchard, Y.2    Chamaillard, L.3
  • 165
    • 0015948335 scopus 로고
    • Ornithine decarboxylase: Inhibition by alphahydrazino-ornithine
    • Harik SI, Snyder SH. Ornithine decarboxylase: inhibition by alphahydrazino-ornithine. Biochim Biophys Acta 1973; 327: 501-9.
    • (1973) Biochim Biophys Acta , vol.327 , pp. 501-509
    • Harik, S.I.1    Snyder, S.H.2
  • 166
    • 0016795145 scopus 로고
    • Effect of DLalpha-hydrazino-delta-aminovaleric acid, an inhibitor of ornithine decarboxylase, on polyamine metabolism in isoproterenolstimulated mouse parotid glands
    • Inoue H, Kato Y, Takigawa M, Adachi K, Takeda Y. Effect of DLalpha-hydrazino-delta-aminovaleric acid, an inhibitor of ornithine decarboxylase, on polyamine metabolism in isoproterenolstimulated mouse parotid glands. J Biochem 1975; 77: 879-93.
    • (1975) J Biochem , vol.77 , pp. 879-893
    • Inoue, H.1    Kato, Y.2    Takigawa, M.3    Adachi, K.4    Takeda, Y.5
  • 168
    • 0022155244 scopus 로고
    • Aminooxypropylamine as an effective inhibitor of ornithine decarboxylase in vitro and in vivo
    • Khomutov RM, Denisova GF, Khomutov AR, et al. Aminooxypropylamine as an effective inhibitor of ornithine decarboxylase in vitro and in vivo. Bioorgan Khim 1985; 11: 1574-76.
    • (1985) Bioorgan Khim , vol.11 , pp. 1574-1576
    • Khomutov, R.M.1    Denisova, G.F.2    Khomutov, A.R.3
  • 169
    • 0024456630 scopus 로고
    • Effect of 1-amino-oxy-3-aminopropane on polyamine metabolism and growth of L1210 cells
    • Poulin R, Secrist III JA, Pegg AE. Effect of 1-amino-oxy-3-aminopropane on polyamine metabolism and growth of L1210 cells. Biochem J 1989; 263: 215-21.
    • (1989) Biochem J , vol.263 , pp. 215-221
    • Poulin, R.1    Secrist III, J.A.2    Pegg, A.E.3
  • 170
    • 0017408848 scopus 로고
    • Detection of multiple forms of rat liver ornithine decarboxylase
    • Obenrader MF, Prouty WF. Detection of multiple forms of rat liver ornithine decarboxylase. J Biol Chem 1977; 252: 2860-65.
    • (1977) J Biol Chem , vol.252 , pp. 2860-2865
    • Obenrader, M.F.1    Prouty, W.F.2
  • 171
    • 0022393340 scopus 로고
    • 1-Aminooxy-3-aminopropane, a new and potent inhibitor of polyamine biosynthesis that inhibits ornithine decarboxylase, adenosylmethionine decarboxylase and spermidine synthase
    • Khomutov RM, Hyvönen T, Karvonen E, et al. 1-Aminooxy-3-aminopropane, a new and potent inhibitor of polyamine biosynthesis that inhibits ornithine decarboxylase, adenosylmethionine decarboxylase and spermidine synthase. Biochem Biophys Res Commun 1985; 130: 596-602.
    • (1985) Biochem Biophys Res Commun , vol.130 , pp. 596-602
    • Khomutov, R.M.1    Hyvönen, T.2    Karvonen, E.3
  • 172
    • 33846575594 scopus 로고    scopus 로고
    • Antileishmanial effect of 3-aminooxy-1-aminopropane is due to polyamine depletion
    • Singh S, Mukherjee A, Khomutov AR, et al. Antileishmanial effect of 3-aminooxy-1-aminopropane is due to polyamine depletion. Antimicrob Agents Chemother 2007; 51: 528-34.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 528-534
    • Singh, S.1    Mukherjee, A.2    Khomutov, A.R.3
  • 173
    • 34447117522 scopus 로고    scopus 로고
    • A structural insight into the inhibition of human and Leishmania donovani ornithine decarboxylases by 1-amino-oxy-3-aminopropane
    • Dufe VT, Ingner D, Heby O, et al. A structural insight into the inhibition of human and Leishmania donovani ornithine decarboxylases by 1-amino-oxy-3-aminopropane. Biochem J 2007; 405: 261-8.
    • (2007) Biochem J , vol.405 , pp. 261-268
    • Dufe, V.T.1    Ingner, D.2    Heby, O.3
  • 174
    • 21444448419 scopus 로고    scopus 로고
    • 3-Aminooxy-1-aminopropane and derivatives have an antiproliferative effect on cultured Plasmodium falciparum by decreasing intracellular polyamine concentrations
    • Das Gupta R, Krause-Ihle T, Bergmann B, et al. 3-Aminooxy-1-aminopropane and derivatives have an antiproliferative effect on cultured Plasmodium falciparum by decreasing intracellular polyamine concentrations. Antimicrob Agents Chemother 2005; 49: 2857-64.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 2857-2864
    • Das Gupta, R.1    Krause-Ihle, T.2    Bergmann, B.3
  • 175
    • 0026740249 scopus 로고
    • 2-substituted 3-(aminooxy) propanamines as inhibitors of ornithine decarboxylase: Synthesis and biological activity
    • Stanek J, Frei J, Mett H, Schneider P, Regenass U. 2-substituted 3-(aminooxy) propanamines as inhibitors of ornithine decarboxylase: synthesis and biological activity. J Med Chem 1992; 35: 1339-44.
    • (1992) J Med Chem , vol.35 , pp. 1339-1344
    • Stanek, J.1    Frei, J.2    Mett, H.3    Schneider, P.4    Regenass, U.5
  • 176
    • 0037441470 scopus 로고    scopus 로고
    • Comparative properties of a three-dimensional model of Plasmodium falciparum ornithine decarboxylase
    • Birkholtz L, Joubert F, Neitz AW, Louw AI. Comparative properties of a three-dimensional model of Plasmodium falciparum ornithine decarboxylase. Proteins 2003; 50: 464-73.
    • (2003) Proteins , vol.50 , pp. 464-473
    • Birkholtz, L.1    Joubert, F.2    Neitz, A.W.3    Louw, A.I.4
  • 177
    • 58149099860 scopus 로고    scopus 로고
    • Rapid oxime and hydrazone ligations with aromatic aldehydes for biomolecular labeling
    • Dirksen A, Dawson PE. Rapid oxime and hydrazone ligations with aromatic aldehydes for biomolecular labeling. Bioconjug Chem 2008; 19: 2543-8.
    • (2008) Bioconjug Chem , vol.19 , pp. 2543-2548
    • Dirksen, A.1    Dawson, P.E.2
  • 178
    • 0000595419 scopus 로고
    • Semicarbazone formation from pyridoxal, pyridoxal phosphate, and their Schiff bases
    • Cordes EH, Jencks WP. Semicarbazone formation from pyridoxal, pyridoxal phosphate, and their Schiff bases. Biochemistry 1962; 1: 773-8.
    • (1962) Biochemistry , vol.1 , pp. 773-778
    • Cordes, E.H.1    Jencks, W.P.2
  • 179
    • 0001340008 scopus 로고
    • Nucleophilic catalysis of semicarbazone formation by anilines
    • Cordes EH, Jencks WP. Nucleophilic catalysis of semicarbazone formation by anilines. J Am Chem Soc 1962; 84: 826-31.
    • (1962) J Am Chem Soc , vol.84 , pp. 826-831
    • Cordes, E.H.1    Jencks, W.P.2
  • 180
    • 0001520379 scopus 로고
    • Irreversible inhibition of S-adenosylmethionine decarboxylase by hydroxylamine-containing analogues of decarboxylated Sadenosylmethionine
    • Artamonova EY, Khomutov AR, Zavalova LL, Khomutov RM. Irreversible inhibition of S-adenosylmethionine decarboxylase by hydroxylamine-containing analogues of decarboxylated Sadenosylmethionine. Bioorgan Khim 1986; 12: 206-12.
    • (1986) Bioorgan Khim , vol.12 , pp. 206-212
    • Artamonova, E.Y.1    Khomutov, A.R.2    Zavalova, L.L.3    Khomutov, R.M.4
  • 181
    • 0034534695 scopus 로고    scopus 로고
    • The ornithine decarboxylase domain of the bifunctional ornithine decarboxylase/Sadenosylmethionine decarboxylase of Plasmodium falciparum: Recombinant expression and catalytic properties of two different constructs
    • Krause T, Luersen K, Wrenger C, et al. The ornithine decarboxylase domain of the bifunctional ornithine decarboxylase/Sadenosylmethionine decarboxylase of Plasmodium falciparum: recombinant expression and catalytic properties of two different constructs. Biochem J 2000; 352: 287-92.
    • (2000) Biochem J , vol.352 , pp. 287-292
    • Krause, T.1    Luersen, K.2    Wrenger, C.3
  • 182
    • 0014228781 scopus 로고
    • On the inhibition of L-glutamic acid decarboxylase by derivatives of hydroxylamine and related compounds
    • Sashchenko LP, Severin ES, Khomutov RM. [On the inhibition of L-glutamic acid decarboxylase by derivatives of hydroxylamine and related compounds]. Biokhimiia 1968; 33: 142-7.
    • (1968) Biokhimiia , vol.33 , pp. 142-147
    • Sashchenko, L.P.1    Severin, E.S.2    Khomutov, R.M.3
  • 183
    • 0012070239 scopus 로고
    • Elevation of gamma-aminobutyric acid in brain: Selective inhibition of gamma-aminobutyric-alphaketoglutaric acid transaminase
    • Baxter CF, Roberts E. Elevation of gamma-aminobutyric acid in brain: selective inhibition of gamma-aminobutyric-alphaketoglutaric acid transaminase. J Biol Chem 1961; 236: 3287-94.
    • (1961) J Biol Chem , vol.236 , pp. 3287-3294
    • Baxter, C.F.1    Roberts, E.2
  • 184
    • 0024307713 scopus 로고
    • Complexes of aspartate aminotransferase with hydroxylamine derivatives: Spectral studies in solution and in the crystalline state
    • Delbaere LT, Kallen J, Markovic-Housley Z, et al. Complexes of aspartate aminotransferase with hydroxylamine derivatives: spectral studies in solution and in the crystalline state. Biochimie 1989; 71: 449-59.
    • (1989) Biochimie , vol.71 , pp. 449-459
    • Delbaere, L.T.1    Kallen, J.2    Markovic-Housley, Z.3
  • 185
    • 0038312087 scopus 로고    scopus 로고
    • Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: Implications for substrate binding
    • Capitani G, Eliot AC, Gut H, et al. Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding. Biochim Biophys Acta 2003; 1647: 55-60.
    • (2003) Biochim Biophys Acta , vol.1647 , pp. 55-60
    • Capitani, G.1    Eliot, A.C.2    Gut, H.3
  • 186
    • 0030229536 scopus 로고    scopus 로고
    • Cystathionase: Catalytic activity of products of expression of cDNA fragments. Specific inhibition of native enzyme and fusion-protein by substrate-like O-substituted hydroxylamine
    • Gabibov AG, Shuster AM, Khomutov AR, et al. Cystathionase: catalytic activity of products of expression of cDNA fragments. Specific inhibition of native enzyme and fusion-protein by substrate-like O-substituted hydroxylamine. Dokl Akad Nauk Russian 1996; 350: 405-7.
    • (1996) Dokl Akad Nauk Russian , vol.350 , pp. 405-407
    • Gabibov, A.G.1    Shuster, A.M.2    Khomutov, A.R.3
  • 187
    • 0023858351 scopus 로고
    • Effect of inhibitors of Sadenosylmethionine decarboxylase on polyamine content and growth of L1210 cells
    • Pegg AE, Jones DB, Secrist III JA. Effect of inhibitors of Sadenosylmethionine decarboxylase on polyamine content and growth of L1210 cells. Biochemistry 1988; 27: 1408-15.
    • (1988) Biochemistry , vol.27 , pp. 1408-1415
    • Pegg, A.E.1    Jones, D.B.2    Secrist III, J.A.3
  • 188
    • 64349094192 scopus 로고    scopus 로고
    • New insights into the design of inhibitors of human S-adenosylmethionine decarboxylase: Studies of adenine C8 substitution in structural analogues of Sadenosylmethionine
    • McCloskey DE, Bale S, Secrist JA, 3rd, et al. New insights into the design of inhibitors of human S-adenosylmethionine decarboxylase: studies of adenine C8 substitution in structural analogues of Sadenosylmethionine. J Med Chem 2009; 52: 1388-407.
    • (2009) J Med Chem , vol.52 , pp. 1388-1407
    • McCloskey, D.E.1    Bale, S.2    Secrist III, J.A.3
  • 189
    • 0029930370 scopus 로고    scopus 로고
    • Crystal structures and solution studies of oxime adducts of mitochondrial aspartate aminotransferase
    • Markovic-Housley Z, Schirmer T, Hohenester E, et al. Crystal structures and solution studies of oxime adducts of mitochondrial aspartate aminotransferase. Eur J Biochem 1996; 236: 1025-32.
    • (1996) Eur J Biochem , vol.236 , pp. 1025-1032
    • Markovic-Housley, Z.1    Schirmer, T.2    Hohenester, E.3
  • 190
    • 4644248835 scopus 로고    scopus 로고
    • Crystal structures of unbound and aminooxyacetate-bound Escherichia coli gammaaminobutyrate aminotransferase
    • Liu W, Peterson PE, Carter RJ, et al. Crystal structures of unbound and aminooxyacetate-bound Escherichia coli gammaaminobutyrate aminotransferase. Biochemistry 2004; 43: 10896-905.
    • (2004) Biochemistry , vol.43 , pp. 10896-108905
    • Liu, W.1    Peterson, P.E.2    Carter, R.J.3
  • 191
    • 79958290113 scopus 로고    scopus 로고
    • Three-dimensional structures of noncovalent complexes of Citrobacter freundii methionine gamma-lyase with substrates
    • Revtovich SV, Morozova EA, Khurs EN, et al. Three-dimensional structures of noncovalent complexes of Citrobacter freundii methionine gamma-lyase with substrates. Biochemistry (Mosc) 2011; 76: 564-70.
    • (2011) Biochemistry (Mosc) , vol.76 , pp. 564-570
    • Revtovich, S.V.1    Morozova, E.A.2    Khurs, E.N.3
  • 192
    • 20644442880 scopus 로고    scopus 로고
    • The spermidine synthase of the malaria parasite Plasmodium falciparum: Molecular and biochemical characterisation of the polyamine synthesis enzyme
    • Haider N, Eschbach ML, Dias Sde S, et al. The spermidine synthase of the malaria parasite Plasmodium falciparum: molecular and biochemical characterisation of the polyamine synthesis enzyme. Mol Biochem Parasitol 2005; 142: 224-36.
    • (2005) Mol Biochem Parasitol , vol.142 , pp. 224-236
    • Haider, N.1    Eschbach, M.L.2    de Dias, S.S.3
  • 194
    • 0028171439 scopus 로고
    • Derivatives of 1-aminooxy-3-aminopropane as polyamine antimetabolites: Stability and effects on BHK21/C13 cells
    • Keinänen TA, Hyvönen T, Pankaskie MC, Vepsäläinen JJ, Eloranta TO. Derivatives of 1-aminooxy-3-aminopropane as polyamine antimetabolites: Stability and effects on BHK21/C13 cells. J Biochem 1994; 116: 1056-62.
    • (1994) J Biochem , vol.116 , pp. 1056-1062
    • Keinänen, T.A.1    Hyvönen, T.2    Pankaskie, M.C.3    Vepsäläinen, J.J.4    Eloranta, T.O.5
  • 195
    • 0026504737 scopus 로고
    • Monitoring of the uptake and metabolism of aminooxy analogues of polyamines in cultured cells by highperformance liquid chromatography
    • Hyvönen T, Keinänen TA, Khomutov AR, Khomutov RM, Eloranta TO. Monitoring of the uptake and metabolism of aminooxy analogues of polyamines in cultured cells by highperformance liquid chromatography. J Chromatogr 1992; 574: 17-21.
    • (1992) J Chromatogr , vol.574 , pp. 17-21
    • Hyvönen, T.1    Keinänen, T.A.2    Khomutov, A.R.3    Khomutov, R.M.4    Eloranta, T.O.5
  • 196
    • 0037103575 scopus 로고    scopus 로고
    • Insufficiently charged isosteric analogue of spermine: Interaction with polyamine uptake, and effect on Caco-2 cell growth
    • Turchanowa L, Shvetsov AS, Demin AV, et al. Insufficiently charged isosteric analogue of spermine: interaction with polyamine uptake, and effect on Caco-2 cell growth. Biochem Pharmacol 2002; 64: 649-55.
    • (2002) Biochem Pharmacol , vol.64 , pp. 649-655
    • Turchanowa, L.1    Shvetsov, A.S.2    Demin, A.V.3
  • 198
    • 0024501257 scopus 로고
    • Feedback regulation of S-adenosylmethionine synthesis
    • Persson L, Khomutov AR, Khomutov RM. Feedback regulation of S-adenosylmethionine synthesis. Biochem J 1989; 257: 929-31.
    • (1989) Biochem J , vol.257 , pp. 929-931
    • Persson, L.1    Khomutov, A.R.2    Khomutov, R.M.3
  • 199
    • 0023675955 scopus 로고
    • 1-Aminooxy-3-aminopropane reversibly prevents the proliferation of cultured Baby Hamster Kidney cells by interfering with polyamine synthesis
    • Hyvönen T, Alakuijala L, Andersson L, et al. 1-Aminooxy-3-aminopropane reversibly prevents the proliferation of cultured Baby Hamster Kidney cells by interfering with polyamine synthesis. J Biol Chem 1988; 263: 11138-44.
    • (1988) J Biol Chem , vol.263 , pp. 11138-11144
    • Hyvönen, T.1    Alakuijala, L.2    Andersson, L.3
  • 200
    • 0027409324 scopus 로고
    • Pharmacological properties of the ornithine decarboxylase inhibitor 3-aminooxy-1-propanamine and several structural analogues
    • Mett H, Stanek J, Lopez-Ballester JA, et al. Pharmacological properties of the ornithine decarboxylase inhibitor 3-aminooxy-1-propanamine and several structural analogues. Cancer Chemother Pharmacol 1993; 32: 39-45.
    • (1993) Cancer Chemother Pharmacol , vol.32 , pp. 39-45
    • Mett, H.1    Stanek, J.2    Lopez-Ballester, J.A.3
  • 201
    • 0035863266 scopus 로고    scopus 로고
    • Hydroxylaminecontaining inhibitors of polyamine biosynthesis and impairment of colon cancer cell growth
    • Milovic V, Turchanowa L, Khomutov AR, et al. Hydroxylaminecontaining inhibitors of polyamine biosynthesis and impairment of colon cancer cell growth. Biochem Pharmacol 2001; 61: 199-206.
    • (2001) Biochem Pharmacol , vol.61 , pp. 199-206
    • Milovic, V.1    Turchanowa, L.2    Khomutov, A.R.3
  • 203
    • 0000287934 scopus 로고    scopus 로고
    • Imine exchange in O-aryl and O-alkyl oximes as a base reaction for aqueous "dynamic" combinatorial libraries. Akinetic and thermodynamic study
    • Polyakov VA, Nelen MI, Nazarpac-Kandlousy N, Ryabov AD, Eliseev AV. Imine exchange in O-aryl and O-alkyl oximes as a base reaction for aqueous "dynamic" combinatorial libraries. Akinetic and thermodynamic study. J Phys Org Chem 1999; 12: 357-63.
    • (1999) J Phys Org Chem , vol.12 , pp. 357-363
    • Polyakov, V.A.1    Nelen, M.I.2    Nazarpac-Kandlousy, N.3    Ryabov, A.D.4    Eliseev, A.V.5
  • 205
    • 80051673618 scopus 로고    scopus 로고
    • Polyamine homoeostasis as a drug target in pathogenic protozoa: Peculiarities and possibilities
    • Birkholtz LM, Williams M, Niemand J, et al. Polyamine homoeostasis as a drug target in pathogenic protozoa: peculiarities and possibilities. Biochem J 2011; 438: 229-44.
    • (2011) Biochem J , vol.438 , pp. 229-244
    • Birkholtz, L.M.1    Williams, M.2    Niemand, J.3
  • 206
    • 50949128107 scopus 로고    scopus 로고
    • Novel agmatine analogue, gamma-guanidinooxypropylamine (GAPA) efficiently inhibits proliferation of Leishmania donovani by depletion of intracellular polyamine levels
    • Singh S, Jhingran A, Sharma A, et al. Novel agmatine analogue, gamma-guanidinooxypropylamine (GAPA) efficiently inhibits proliferation of Leishmania donovani by depletion of intracellular polyamine levels. Biochem Biophys Res Commun 2008; 375: 168-72.
    • (2008) Biochem Biophys Res Commun , vol.375 , pp. 168-172
    • Singh, S.1    Jhingran, A.2    Sharma, A.3
  • 207
    • 77953062135 scopus 로고    scopus 로고
    • Novel convenient synthesis of biologically active esters of hydroxylamine
    • Khomutov MA, Mandal S, Weisell J, et al. Novel convenient synthesis of biologically active esters of hydroxylamine. Amino Acids 2010; 38: 509-17.
    • (2010) Amino Acids , vol.38 , pp. 509-517
    • Khomutov, M.A.1    Mandal, S.2    Weisell, J.3
  • 208
    • 0022136423 scopus 로고
    • Prevention of a plant disease by specific inhibition of fungal polyamine biosynthesis
    • Rajam MV, Weinstein LH, Galston AW. Prevention of a plant disease by specific inhibition of fungal polyamine biosynthesis. Proc Natl Acad Sci USA 1985; 82: 6874-78.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 6874-6878
    • Rajam, M.V.1    Weinstein, L.H.2    Galston, A.W.3
  • 210
    • 0000365211 scopus 로고
    • Synthesis of Putrescine and Spermidine Aminooxyanalogues
    • Khomutov AR, Khomutov RM. Synthesis of Putrescine and Spermidine Aminooxyanalogues. Bioorgan Khim 1989; 15: 698-703.
    • (1989) Bioorgan Khim , vol.15 , pp. 698-703
    • Khomutov, A.R.1    Khomutov, R.M.2
  • 212
    • 0029133121 scopus 로고
    • Diamine and triamine analogs and derivatives as inhibitors of deoxyhypusine synthase: Synthesis and biological activity
    • Lee YB, Park MH, Folk JE. Diamine and triamine analogs and derivatives as inhibitors of deoxyhypusine synthase: synthesis and biological activity. J Med Chem 1995; 38: 3053-61.
    • (1995) J Med Chem , vol.38 , pp. 3053-3061
    • Lee, Y.B.1    Park, M.H.2    Folk, J.E.3
  • 213
    • 0028363091 scopus 로고
    • Synthesis of novel oxaisosteres of spermidine and spermine
    • Lin PKT, Maguire NM, Brown DM. Synthesis of novel oxaisosteres of spermidine and spermine. Tetrahedron Lett 1994; 35: 3605-8.
    • (1994) Tetrahedron Lett , vol.35 , pp. 3605-3608
    • Lin, P.K.T.1    Maguire, N.M.2    Brown, D.M.3
  • 214
  • 216
    • 36949030232 scopus 로고    scopus 로고
    • Novel CoApolyamine conjugates for effective inhibition of spermine/spermidine-N-1-acetyltransferase
    • Simonian A, Khomutov A, Hyvönen T, et al. Novel CoApolyamine conjugates for effective inhibition of spermine/spermidine-N-1-acetyltransferase. Nucleosides Nucleotides Nucleic Acids 2007; 26: 1245-48.
    • (2007) Nucleosides Nucleotides Nucleic Acids , vol.26 , pp. 1245-1248
    • Simonian, A.1    Khomutov, A.2    Hyvönen, T.3
  • 217
    • 0021772472 scopus 로고
    • Differential inhibition of histone and polyamine acetylases by multisubstrate analogues
    • Erwin BG, Persson L, Pegg AE. Differential inhibition of histone and polyamine acetylases by multisubstrate analogues. Biochemistry 1984; 23: 4250-5.
    • (1984) Biochemistry , vol.23 , pp. 4250-4255
    • Erwin, B.G.1    Persson, L.2    Pegg, A.E.3
  • 218
    • 30444441271 scopus 로고    scopus 로고
    • Alpha-Methyl polyamines: Efficient synthesis and tolerance studies in vivo and in vitro. First evidence for dormant stereospecificity of polyamine oxidase
    • Järvinen AJ, Cerrada-Gimenez M, Grigorenko NA, et al. Alpha-Methyl polyamines: Efficient synthesis and tolerance studies in vivo and in vitro. First evidence for dormant stereospecificity of polyamine oxidase. J Med Chem 2006; 49: 399-406.
    • (2006) J Med Chem , vol.49 , pp. 399-406
    • Järvinen, A.J.1    Cerrada-Gimenez, M.2    Grigorenko, N.A.3
  • 219
    • 0028888587 scopus 로고
    • Aminooxy analogues of spermidine evidence the divergent roles of the charged amino nitrogens in the cellular physiology of spermidine
    • Hyvönen T, Keinänen TA, Khomutov AR, Khomutov RM, Eloranta TO. Aminooxy analogues of spermidine evidence the divergent roles of the charged amino nitrogens in the cellular physiology of spermidine. Life Sci 1995; 56: 349-60.
    • (1995) Life Sci , vol.56 , pp. 349-360
    • Hyvönen, T.1    Keinänen, T.A.2    Khomutov, A.R.3    Khomutov, R.M.4    Eloranta, T.O.5
  • 220
    • 0036846756 scopus 로고    scopus 로고
    • Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin
    • Vujcic S, Diegelman P, Bacchi CJ, Kramer DL, Porter CW. Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin. Biochem J 2002; 367: 665-75.
    • (2002) Biochem J , vol.367 , pp. 665-675
    • Vujcic, S.1    Diegelman, P.2    Bacchi, C.J.3    Kramer, D.L.4    Porter, C.W.5
  • 221
    • 0037449190 scopus 로고    scopus 로고
    • Properties of purified recombinant human polyamine oxidase, PAOh1/SMO
    • Wang Y, Murray-Stewart T, Devereux W, et al. Properties of purified recombinant human polyamine oxidase, PAOh1/SMO. Biochem Biophys Res Commun 2003; 304: 605-11.
    • (2003) Biochem Biophys Res Commun , vol.304 , pp. 605-611
    • Wang, Y.1    Murray-Stewart, T.2    Devereux, W.3
  • 222
    • 0034284109 scopus 로고    scopus 로고
    • Structural basis of polyamine-DNA recognition: Spermidine and spermine interactions with genomic B-DNAs of different GC content probed by raman spectroscopy
    • Deng H, Bloomfield VA, Benevides JM, Jr GJ. Structural basis of polyamine-DNA recognition: spermidine and spermine interactions with genomic B-DNAs of different GC content probed by raman spectroscopy. Nucleic Acids Res 2000; 28: 3379-85.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3379-3385
    • Deng, H.1    Bloomfield, V.A.2    Benevides Jr., J.M.G.J.3
  • 223
    • 0029039988 scopus 로고
    • Polyamine induced Zconformation of native calf thymus DNA
    • Hasan R, Moinuddin KA, Ali R. Polyamine induced Zconformation of native calf thymus DNA. FEBS Lett 1995; 368: 27-30.
    • (1995) FEBS Lett , vol.368 , pp. 27-30
    • Hasan, R.1    Moinuddin, K.A.2    Ali, R.3
  • 224
    • 0024546799 scopus 로고
    • Base only binding of spermine in the deep groove of the A-DNA octamer d(GTGTACAC)
    • Jain S, Zon G, Sundaralingam M. Base only binding of spermine in the deep groove of the A-DNA octamer d(GTGTACAC). Biochemistry 1989; 28: 2360-4.
    • (1989) Biochemistry , vol.28 , pp. 2360-2364
    • Jain, S.1    Zon, G.2    Sundaralingam, M.3
  • 225
    • 0028265282 scopus 로고
    • The low-temperature crystal structure of the pure-spermine form of Z-DNA reveals binding of a spermine moleculse in the minor groove
    • Bancroft D, Williams LD, Rich A, Egli M. The low-temperature crystal structure of the pure-spermine form of Z-DNA reveals binding of a spermine moleculse in the minor groove. Biochemistry 1994; 33: 1073-86.
    • (1994) Biochemistry , vol.33 , pp. 1073-1086
    • Bancroft, D.1    Williams, L.D.2    Rich, A.3    Egli, M.4
  • 226
    • 0024451743 scopus 로고
    • Molecular dynamics of spermine-DNA interactions: Sequence specificity and DNA bending for a simple ligand
    • Feuerstein BG, Pattabiraman N, Marton LJ. Molecular dynamics of spermine-DNA interactions: sequence specificity and DNA bending for a simple ligand. Nucleic Acids Res 1989; 17: 6883-92.
    • (1989) Nucleic Acids Res , vol.17 , pp. 6883-6892
    • Feuerstein, B.G.1    Pattabiraman, N.2    Marton, L.J.3
  • 227
    • 0033596851 scopus 로고    scopus 로고
    • Ionic and structural specificity effects of natural and synthetic polyamines on the aggregation and resolubilization of single-, double-, and triplestranded DNA
    • Saminathan M, Antony T, Shirahata A, et al. Ionic and structural specificity effects of natural and synthetic polyamines on the aggregation and resolubilization of single-, double-, and triplestranded DNA. Biochemistry 1999; 38: 3821-30.
    • (1999) Biochemistry , vol.38 , pp. 3821-3830
    • Saminathan, M.1    Antony, T.2    Shirahata, A.3
  • 228
    • 0037107834 scopus 로고    scopus 로고
    • Effects of aminooxy analogues of biogenic polyamines on aggregation and stability of calf thymus DNA
    • Ramirez FJ, Thomas TJ, Antony T, Ruiz-Chica J, Thomas T. Effects of aminooxy analogues of biogenic polyamines on aggregation and stability of calf thymus DNA. Biopolymers 2002; 65: 148-57.
    • (2002) Biopolymers , vol.65 , pp. 148-157
    • Ramirez, F.J.1    Thomas, T.J.2    Antony, T.3    Ruiz-Chica, J.4    Thomas, T.5
  • 229
    • 84892984031 scopus 로고
    • Polyfunctional O-substited hydroxilamines: Modification of nucleic acids, analogs of the decarboxylated S-adenosylmethionine
    • Khomutov AR, Kritsky AM, Artamonova EY, Khomutov RM. Polyfunctional O-substited hydroxilamines: modification of nucleic acids, analogs of the decarboxylated S-adenosylmethionine. Nucleosides & Nucleotides 1987; 6: 53-56.
    • (1987) Nucleosides & Nucleotides , vol.6 , pp. 53-56
    • Khomutov, A.R.1    Kritsky, A.M.2    Artamonova, E.Y.3    Khomutov, R.M.4
  • 230
    • 0023474240 scopus 로고
    • Method for the introduction of reactive functional groups via cytidine and or 3'-terminal of the nucleic acids
    • Kritsky AM, Khomutov AR, Yakovlev DY, et al. Method for the introduction of reactive functional groups via cytidine and or 3'-terminal of the nucleic acids. Nuc Acid Res Symp Ser 1987; 89-92.
    • (1987) Nuc Acid Res Symp Ser , pp. 89-92
    • Kritsky, A.M.1    Khomutov, A.R.2    Yakovlev, D.Y.3
  • 231
    • 0000406026 scopus 로고    scopus 로고
    • Synthesis of a chemiluminescent acridinium hydroxylamine (AHA) for the direct detection of abasic sites in DNA
    • Adamczyk M, Mattingly PG, Moore JA, Pan Y. Synthesis of a chemiluminescent acridinium hydroxylamine (AHA) for the direct detection of abasic sites in DNA. Org Lett 1999; 1: 779-81.
    • (1999) Org Lett , vol.1 , pp. 779-781
    • Adamczyk, M.1    Mattingly, P.G.2    Moore, J.A.3    Pan, Y.4
  • 232
    • 0016887316 scopus 로고
    • The mechanism of the mutagenic action of hydroxylamines
    • eds, In: Cohn WE, ed, Academic Press: New York San Francisco London
    • Budowsky EI. The mechanism of the mutagenic action of hydroxylamines. In: Cohn WE, ed. eds., Progress in Nucleic Acids Research and Molecular Biology. Academic Press: New York San Francisco London 1976; pp. 125-88.
    • (1976) Progress in Nucleic Acids Research and Molecular Biology , pp. 125-188
    • Budowsky, E.I.1
  • 234
    • 0029295973 scopus 로고
    • Modification of DNA with 4-aminooxybutylamine as a method for obtaining highly-sensitive hybridization probes. Mapping of the gene for human chorionic somatomammotropin hormone
    • Adarichev VA, Vorob'eva NV, Grafodatskii AS, Dymshits GM, Sablina OV. Modification of DNA with 4-aminooxybutylamine as a method for obtaining highly-sensitive hybridization probes. Mapping of the gene for human chorionic somatomammotropin hormone. Mol Biol (Mosk) 1995; 29: 538-45.
    • (1995) Mol Biol (Mosk) , vol.29 , pp. 538-545
    • Adarichev, V.A.1    Vorob'eva, N.V.2    Grafodatskii, A.S.3    Dymshits, G.M.4    Sablina, O.V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.