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Volumn 427, Issue 21, 2015, Pages 3389-3406

Remaining Mysteries of Molecular Biology: The Role of Polyamines in the Cell

Author keywords

Cancer; Hypusine; Neurodegenerative diseases; Proliferation; Stress response

Indexed keywords

ADENOSYLMETHIONINE DECARBOXYLASE; ANTIZYME; CADAVERINE; ORNITHINE DECARBOXYLASE; PUTRESCINE; SPERMIDINE; SPERMINE; POLYAMINE;

EID: 84944278561     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2015.06.020     Document Type: Review
Times cited : (501)

References (244)
  • 1
    • 76549155767 scopus 로고
    • Spermidine, spermine, and related amines
    • H. Tabor, and C.W. Tabor Spermidine, spermine, and related amines Pharmacol. Rev. 16 1964 245 300
    • (1964) Pharmacol. Rev. , vol.16 , pp. 245-300
    • Tabor, H.1    Tabor, C.W.2
  • 2
    • 79952199559 scopus 로고    scopus 로고
    • The early history of polyamine research
    • U. Bachrach The early history of polyamine research Plant Physiol. Biochem. 48 2010 490 495
    • (2010) Plant Physiol. Biochem. , vol.48 , pp. 490-495
    • Bachrach, U.1
  • 3
    • 0004139057 scopus 로고    scopus 로고
    • Oxford University Press Oxford, United Kingdom
    • S.S. Cohen A guide to polyamines 1997 Oxford University Press Oxford, United Kingdom
    • (1997) A Guide to Polyamines
    • Cohen, S.S.1
  • 4
    • 40549096043 scopus 로고    scopus 로고
    • A multifaceted role for polyamines in bacterial pathogens
    • P. Shah, and E. Swiatlo A multifaceted role for polyamines in bacterial pathogens Mol. Microbiol. 68 2008 4 16
    • (2008) Mol. Microbiol. , vol.68 , pp. 4-16
    • Shah, P.1    Swiatlo, E.2
  • 6
    • 34548150619 scopus 로고    scopus 로고
    • Physiological polyamines: Simple primordial stress molecules
    • H.J. Rhee, E.-J. Kim, and J.K. Lee Physiological polyamines: simple primordial stress molecules J. Cell. Mol. Med. 11 2007 685 703
    • (2007) J. Cell. Mol. Med. , vol.11 , pp. 685-703
    • Rhee, H.J.1    Kim, E.-J.2    Lee, J.K.3
  • 7
    • 47249122499 scopus 로고    scopus 로고
    • Polyamines: Essential factors for growth and survival
    • T. Kusano, T. Berberich, C. Tateda, and Y. Takahashi Polyamines: essential factors for growth and survival Planta 228 2008 367 381
    • (2008) Planta , vol.228 , pp. 367-381
    • Kusano, T.1    Berberich, T.2    Tateda, C.3    Takahashi, Y.4
  • 8
    • 0033049344 scopus 로고    scopus 로고
    • Trypanosoma cruzi epimastigotes lack ornithine decarboxylase but can express a foreign gene encoding this enzyme
    • C. Carrillo, S. Cejas, N.S. González, and I.D. Algranati Trypanosoma cruzi epimastigotes lack ornithine decarboxylase but can express a foreign gene encoding this enzyme FEBS Lett. 454 1999 192 196
    • (1999) FEBS Lett. , vol.454 , pp. 192-196
    • Carrillo, C.1    Cejas, S.2    González, N.S.3    Algranati, I.D.4
  • 9
    • 0034798209 scopus 로고    scopus 로고
    • Arabidopsis polyamine biosynthesis: Absence of ornithine decarboxylase and the mechanism of arginine decarboxylase activity
    • C. Hanfrey, S. Sommer, M.J. Mayer, D. Burtin, and A.J. Michael Arabidopsis polyamine biosynthesis: absence of ornithine decarboxylase and the mechanism of arginine decarboxylase activity Plant J. 27 2001 551 560
    • (2001) Plant J. , vol.27 , pp. 551-560
    • Hanfrey, C.1    Sommer, S.2    Mayer, M.J.3    Burtin, D.4    Michael, A.J.5
  • 10
    • 77950255730 scopus 로고    scopus 로고
    • A high-affinity putrescine-cadaverine transporter from Trypanosoma cruzi
    • M.P. Hasne, I. Coppens, R. Soysa, and B. Ullman A high-affinity putrescine-cadaverine transporter from Trypanosoma cruzi Mol. Microbiol. 76 2010 78 91
    • (2010) Mol. Microbiol. , vol.76 , pp. 78-91
    • Hasne, M.P.1    Coppens, I.2    Soysa, R.3    Ullman, B.4
  • 11
    • 0029898712 scopus 로고    scopus 로고
    • Regulation of a high-affinity diamine transport system in Trypanosoma cruzi epimastigotes
    • S.A. Le Quesne, and A.H. Fairlamb Regulation of a high-affinity diamine transport system in Trypanosoma cruzi epimastigotes Biochem. J. 316 1996 481 486
    • (1996) Biochem. J. , vol.316 , pp. 481-486
    • Le Quesne, S.A.1    Fairlamb, A.H.2
  • 12
    • 84885234353 scopus 로고    scopus 로고
    • Cadaverine: A lysine catabolite involved in plant growth and development
    • P.C. Tomar, N. Lakra, and S.N. Mishra Cadaverine: a lysine catabolite involved in plant growth and development Plant Signal Behav. 8 2013 1 15
    • (2013) Plant Signal Behav. , vol.8 , pp. 1-15
    • Tomar, P.C.1    Lakra, N.2    Mishra, S.N.3
  • 13
    • 0030808549 scopus 로고    scopus 로고
    • The Escherichia coli ldcC gene encodes another lysine decarboxylase, probably a constitutive enzyme
    • Y. Yamamoto, Y. Miwa, K. Miyoshi, J. Furuyama, and H. Ohmori The Escherichia coli ldcC gene encodes another lysine decarboxylase, probably a constitutive enzyme Genes Genet. Syst. 72 1997 167 172
    • (1997) Genes Genet. Syst. , vol.72 , pp. 167-172
    • Yamamoto, Y.1    Miwa, Y.2    Miyoshi, K.3    Furuyama, J.4    Ohmori, H.5
  • 14
    • 84874733888 scopus 로고    scopus 로고
    • Three-component lysine/ornithine decarboxylation system in Lactobacillus saerimneri 30a
    • A. Romano, H. Trip, J.S. Lolkema, and P.M. Lucas Three-component lysine/ornithine decarboxylation system in Lactobacillus saerimneri 30a J. Bacteriol. 195 2013 1249 1254
    • (2013) J. Bacteriol. , vol.195 , pp. 1249-1254
    • Romano, A.1    Trip, H.2    Lolkema, J.S.3    Lucas, P.M.4
  • 15
    • 42149149977 scopus 로고    scopus 로고
    • Lysine decarboxylase of Vibrio parahaemolyticus: Kinetics of transcription and role in acid resistance
    • Y. Tanaka, B. Kimura, H. Takahashi, T. Watanabe, H. Obata, A. Kai, and et al. Lysine decarboxylase of Vibrio parahaemolyticus: kinetics of transcription and role in acid resistance J. Appl. Microbiol. 104 2008 1283 1293
    • (2008) J. Appl. Microbiol. , vol.104 , pp. 1283-1293
    • Tanaka, Y.1    Kimura, B.2    Takahashi, H.3    Watanabe, T.4    Obata, H.5    Kai, A.6
  • 16
    • 0018766202 scopus 로고
    • Decarboxylation of ornithine and lysine in rat tissues
    • A.E. Pegg, and S. McGill Decarboxylation of ornithine and lysine in rat tissues Biochim. Biophys. Acta 568 1979 416 427
    • (1979) Biochim. Biophys. Acta , vol.568 , pp. 416-427
    • Pegg, A.E.1    McGill, S.2
  • 17
    • 0018096894 scopus 로고
    • Polyamine auxotrophs of Saccharomyces cerevisiae
    • P.A. Whitney, and D.R. Morris Polyamine auxotrophs of Saccharomyces cerevisiae J. Bacteriol. 134 1978 214 220
    • (1978) J. Bacteriol. , vol.134 , pp. 214-220
    • Whitney, P.A.1    Morris, D.R.2
  • 18
    • 0020433097 scopus 로고
    • Polyamine-deficient Neurospora crassa mutants and synthesis of cadaverine
    • T.J. Paulus, P. Kiyono, and R.H. Davis Polyamine-deficient Neurospora crassa mutants and synthesis of cadaverine J. Bacteriol. 152 1982 291 297
    • (1982) J. Bacteriol. , vol.152 , pp. 291-297
    • Paulus, T.J.1    Kiyono, P.2    Davis, R.H.3
  • 19
    • 0030561324 scopus 로고    scopus 로고
    • Formation of cadaverine derivatives in Saccharomyces cerevisiae
    • D. Walters, and T. Cowley Formation of cadaverine derivatives in Saccharomyces cerevisiae FEMS Microbiol. Lett. 145 1996 255 259
    • (1996) FEMS Microbiol. Lett. , vol.145 , pp. 255-259
    • Walters, D.1    Cowley, T.2
  • 20
    • 0021846289 scopus 로고
    • Formation of cadaverine as an effect of alpha-difluoromethylornithine on chick embryo fibroblasts transformed with rous sarcoma virus
    • U. Bachrach, and A. Shtorch Formation of cadaverine as an effect of alpha-difluoromethylornithine on chick embryo fibroblasts transformed with rous sarcoma virus Cancer Res. 45 1985 2159 2164
    • (1985) Cancer Res. , vol.45 , pp. 2159-2164
    • Bachrach, U.1    Shtorch, A.2
  • 21
    • 0022512208 scopus 로고
    • Formation of a compensatory polyamine by Escherichia coli polyamine-requiring mutants during growth in the absence of polyamines
    • K. Igarashi, K. Kashiwagi, H. Hamasaki, A. Miura, T. Kakegawa, S. Hirose, and et al. Formation of a compensatory polyamine by Escherichia coli polyamine-requiring mutants during growth in the absence of polyamines J. Bacteriol. 166 1986 128 134
    • (1986) J. Bacteriol. , vol.166 , pp. 128-134
    • Igarashi, K.1    Kashiwagi, K.2    Hamasaki, H.3    Miura, A.4    Kakegawa, T.5    Hirose, S.6
  • 22
    • 0023881236 scopus 로고
    • Polyamine metabolism and its importance in neoplastic growth and a target for chemotherapy
    • A.E. Pegg Polyamine metabolism and its importance in neoplastic growth and a target for chemotherapy Cancer Res. 48 1988 759 774
    • (1988) Cancer Res. , vol.48 , pp. 759-774
    • Pegg, A.E.1
  • 23
    • 0025184767 scopus 로고
    • Cell type-specific mechanisms of regulating expression of the ornithine decarboxylase gene after growth stimulation
    • M.S. Abrahamsen, and D.R. Morris Cell type-specific mechanisms of regulating expression of the ornithine decarboxylase gene after growth stimulation Mol. Cell. Biol. 10 1990 5525 5528
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5525-5528
    • Abrahamsen, M.S.1    Morris, D.R.2
  • 24
    • 0021265350 scopus 로고
    • Ornithine decarboxylase as a biologic marker in familial colonic polyposis
    • G.D. Luk, and S.B. Baylin Ornithine decarboxylase as a biologic marker in familial colonic polyposis N. Engl. J. Med. 311 1984 80 83
    • (1984) N. Engl. J. Med. , vol.311 , pp. 80-83
    • Luk, G.D.1    Baylin, S.B.2
  • 25
    • 0017078044 scopus 로고
    • Increased ornithine decarboxylase activity in murine sarcoma virus infected cells
    • A.F. Gazdar, H.B. Stull, L.J. Kilton, and U. Bachrach Increased ornithine decarboxylase activity in murine sarcoma virus infected cells Nature 262 1976 696 698
    • (1976) Nature , vol.262 , pp. 696-698
    • Gazdar, A.F.1    Stull, H.B.2    Kilton, L.J.3    Bachrach, U.4
  • 26
    • 0016840337 scopus 로고
    • Polyamine metabolism in normal and in virus-transformed chick embryo fibroblasts
    • S. Don, and U. Bachrach Polyamine metabolism in normal and in virus-transformed chick embryo fibroblasts Cancer Res. 35 1975 3618 3622
    • (1975) Cancer Res. , vol.35 , pp. 3618-3622
    • Don, S.1    Bachrach, U.2
  • 27
    • 0030476712 scopus 로고    scopus 로고
    • Ornithine decarboxylase activity is a marker of premalignancy in longstanding Helicobacter pylori infection
    • S.E. Patchett, P.H. Katelaris, Z.W. Zhang, E.M. Alstead, P. Domizio, and M.J. Farthing Ornithine decarboxylase activity is a marker of premalignancy in longstanding Helicobacter pylori infection Gut 39 1996 807 810
    • (1996) Gut , vol.39 , pp. 807-810
    • Patchett, S.E.1    Katelaris, P.H.2    Zhang, Z.W.3    Alstead, E.M.4    Domizio, P.5    Farthing, M.J.6
  • 28
    • 0032857184 scopus 로고    scopus 로고
    • Increased colonic ornithine decarboxylase activity in inflammatory bowel disease in children
    • R.B. Pillai, V. Tolia, R. Rabah, P.M. Simpson, R. Vijesurier, and C.H. Lin Increased colonic ornithine decarboxylase activity in inflammatory bowel disease in children Dig. Dis. Sci. 44 1999 1565 1570
    • (1999) Dig. Dis. Sci. , vol.44 , pp. 1565-1570
    • Pillai, R.B.1    Tolia, V.2    Rabah, R.3    Simpson, P.M.4    Vijesurier, R.5    Lin, C.H.6
  • 29
    • 33744951504 scopus 로고    scopus 로고
    • Regulation of ornithine decarboxylase
    • A.E. Pegg Regulation of ornithine decarboxylase J. Biol. Chem. 281 2006 14529 14532
    • (2006) J. Biol. Chem. , vol.281 , pp. 14529-14532
    • Pegg, A.E.1
  • 30
    • 0027691216 scopus 로고
    • C-Myc induces the expression and activity of ornithine decarboxylase
    • A.J. Wagner, C. Meyers, L.A. Laimins, and N. Hay c-Myc induces the expression and activity of ornithine decarboxylase Cell Growth Differ. 4 1993 879 883
    • (1993) Cell Growth Differ. , vol.4 , pp. 879-883
    • Wagner, A.J.1    Meyers, C.2    Laimins, L.A.3    Hay, N.4
  • 31
    • 0035168068 scopus 로고    scopus 로고
    • Core promoter involvement in the induction of rat ornithine decarboxylase by phorbol esters
    • B. Zhao, and A.P. Butler Core promoter involvement in the induction of rat ornithine decarboxylase by phorbol esters Mol. Carcinog. 32 2001 92 99
    • (2001) Mol. Carcinog. , vol.32 , pp. 92-99
    • Zhao, B.1    Butler, A.P.2
  • 32
    • 3142714386 scopus 로고    scopus 로고
    • Estrogen-dependent regulation of ornithine decarboxylase in breast cancer cells through activation of nongenomic cAMP-dependent pathways
    • C. Qin, I. Samudio, S. Ngwenya, and S. Safe Estrogen-dependent regulation of ornithine decarboxylase in breast cancer cells through activation of nongenomic cAMP-dependent pathways Mol. Carcinog. 40 2004 160 170
    • (2004) Mol. Carcinog. , vol.40 , pp. 160-170
    • Qin, C.1    Samudio, I.2    Ngwenya, S.3    Safe, S.4
  • 33
    • 0032967255 scopus 로고    scopus 로고
    • Translational regulation of ornithine decarboxylase and other enzymes of the polyamine pathway
    • L.M. Shantz, and A.E. Pegg Translational regulation of ornithine decarboxylase and other enzymes of the polyamine pathway Int. J. Biochem. Cell Biol. 31 1999 107 122
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 107-122
    • Shantz, L.M.1    Pegg, A.E.2
  • 34
    • 0030011284 scopus 로고    scopus 로고
    • Regulation of ornithine decarboxylase in a transformed cell line that overexpresses translation initiation factor eIF-4E
    • L.M. Shantz, R.H. Hu, and A.E. Pegg Regulation of ornithine decarboxylase in a transformed cell line that overexpresses translation initiation factor eIF-4E Cancer Res. 56 1996 3265 3269
    • (1996) Cancer Res. , vol.56 , pp. 3265-3269
    • Shantz, L.M.1    Hu, R.H.2    Pegg, A.E.3
  • 35
    • 0035047614 scopus 로고    scopus 로고
    • The regulation of ornithine decarboxylase gene expression by sucrose and small upstream open reading frame in tomato (Lycopersicon esculentum Mill)
    • S.H. Kwak, and S.H. Lee The regulation of ornithine decarboxylase gene expression by sucrose and small upstream open reading frame in tomato (Lycopersicon esculentum Mill) Plant Cell Physiol. 42 2001 314 323
    • (2001) Plant Cell Physiol. , vol.42 , pp. 314-323
    • Kwak, S.H.1    Lee, S.H.2
  • 36
    • 48249118705 scopus 로고    scopus 로고
    • UORFs with unusual translational start codons autoregulate expression of eukaryotic ornithine decarboxylase homologs
    • I.P. Ivanov, G. Loughran, and J.F. Atkins uORFs with unusual translational start codons autoregulate expression of eukaryotic ornithine decarboxylase homologs Proc. Natl. Acad. Sci. U. S. A. 105 2008 10079 10084
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 10079-10084
    • Ivanov, I.P.1    Loughran, G.2    Atkins, J.F.3
  • 37
    • 0033634723 scopus 로고    scopus 로고
    • A cell cycle-dependent internal ribosome entry site
    • S. Pyronnet, L. Pradayrol, and N. Sonenberg A cell cycle-dependent internal ribosome entry site Mol. Cell 5 2000 607 616
    • (2000) Mol. Cell , vol.5 , pp. 607-616
    • Pyronnet, S.1    Pradayrol, L.2    Sonenberg, N.3
  • 38
    • 0014512849 scopus 로고
    • Amine synthesis in regenerating rat liver: Extremely rapid turnover of ornithine decarboxylase
    • D.H. Russell, and S.H. Snyder Amine synthesis in regenerating rat liver: extremely rapid turnover of ornithine decarboxylase Mol. Pharmacol. 5 1969 253 262
    • (1969) Mol. Pharmacol. , vol.5 , pp. 253-262
    • Russell, D.H.1    Snyder, S.H.2
  • 39
    • 0025232520 scopus 로고
    • Intestinal ornithine decarboxylase: Half-life and regulation by putrescine
    • K. Iwami, J.Y. Wang, R. Jain, S. McCormack, and L.R. Johnson Intestinal ornithine decarboxylase: half-life and regulation by putrescine Am. J. Physiol. 258 1990 G308 G315
    • (1990) Am. J. Physiol. , vol.258 , pp. G308-G315
    • Iwami, K.1    Wang, J.Y.2    Jain, R.3    McCormack, S.4    Johnson, L.R.5
  • 40
    • 0026714435 scopus 로고
    • Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination
    • Y. Murakami, S. Matsufuji, T. Kameji, S. Hayashi, K. Igarashi, T. Tamura, and et al. Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination Nature 360 1992 597 599
    • (1992) Nature , vol.360 , pp. 597-599
    • Murakami, Y.1    Matsufuji, S.2    Kameji, T.3    Hayashi, S.4    Igarashi, K.5    Tamura, T.6
  • 41
    • 84890174353 scopus 로고
    • Ubiquitin-independent proteasomal degradation
    • J. Erales, and P. Coffino Ubiquitin-independent proteasomal degradation Biochim. Biophys. Acta 2014 1843 216 221
    • (1843) Biochim. Biophys. Acta , vol.2014 , pp. 216-221
    • Erales, J.1    Coffino, P.2
  • 42
    • 0015612171 scopus 로고
    • Control of ornithine decarboxylase activity in stimulated human lymphocytes by putrescine and spermidine
    • J.E. Kay, and V.J. Lindsay Control of ornithine decarboxylase activity in stimulated human lymphocytes by putrescine and spermidine Biochem. J. 132 1973 791 796
    • (1973) Biochem. J. , vol.132 , pp. 791-796
    • Kay, J.E.1    Lindsay, V.J.2
  • 43
    • 0345955882 scopus 로고
    • Induction of a protein inhibitor to ornithine decarboxylase by the end products of its reaction
    • J.S. Heller, W.F. Fong, and E.S. Canellakis Induction of a protein inhibitor to ornithine decarboxylase by the end products of its reaction Proc. Natl. Acad. Sci. U. S. A. 73 1976 1858 1862
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 1858-1862
    • Heller, J.S.1    Fong, W.F.2    Canellakis, E.S.3
  • 44
    • 0026577742 scopus 로고
    • Cloning and characterization of a rat gene encoding ornithine decarboxylase antizyme
    • Y. Miyazaki, S. Matsufuji, and S. Hayashi Cloning and characterization of a rat gene encoding ornithine decarboxylase antizyme Gene 113 1992 191 197
    • (1992) Gene , vol.113 , pp. 191-197
    • Miyazaki, Y.1    Matsufuji, S.2    Hayashi, S.3
  • 45
    • 0027512650 scopus 로고
    • Degradation of ornithine decarboxylase: Exposure of the C-terminal target by a polyamine-inducible inhibitory protein
    • X. Li, and P. Coffino Degradation of ornithine decarboxylase: exposure of the C-terminal target by a polyamine-inducible inhibitory protein Mol. Cell. Biol. 13 1993 2377 2383
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2377-2383
    • Li, X.1    Coffino, P.2
  • 47
    • 0345701307 scopus 로고    scopus 로고
    • Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrate
    • M. Zhang, C.M. Pickart, and P. Coffino Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrate EMBO J. 22 2003 1488 1496
    • (2003) EMBO J. , vol.22 , pp. 1488-1496
    • Zhang, M.1    Pickart, C.M.2    Coffino, P.3
  • 48
    • 79952452227 scopus 로고    scopus 로고
    • The N-terminal unstructured domain of yeast ODC functions as a transplantable and replaceable ubiquitin-independent degron
    • D. Gödderz, E. Schäfer, R. Palanimurugan, and R.J. Dohmen The N-terminal unstructured domain of yeast ODC functions as a transplantable and replaceable ubiquitin-independent degron J. Mol. Biol. 407 2011 354 367
    • (2011) J. Mol. Biol. , vol.407 , pp. 354-367
    • Gödderz, D.1    Schäfer, E.2    Palanimurugan, R.3    Dohmen, R.J.4
  • 49
    • 35348851301 scopus 로고    scopus 로고
    • Antizyme1 mediates AURKAIP1-dependent degradation of Aurora-A
    • S.K. Lim, and G. Gopalan Antizyme1 mediates AURKAIP1-dependent degradation of Aurora-A Oncogene 26 2007 6593 6603
    • (2007) Oncogene , vol.26 , pp. 6593-6603
    • Lim, S.K.1    Gopalan, G.2
  • 50
    • 0024153603 scopus 로고
    • Regulation of polyamine biosynthesis in Escherichia coli by the acidic antizyme and the ribosomal proteins S20 and L34
    • C.A. Panagiotidis, S.C. Huang, S.A. Tsirka, D.A. Kyriakidis, and E.S. Canellakis Regulation of polyamine biosynthesis in Escherichia coli by the acidic antizyme and the ribosomal proteins S20 and L34 Adv. Exp. Med. Biol. 250 1988 13 24
    • (1988) Adv. Exp. Med. Biol. , vol.250 , pp. 13-24
    • Panagiotidis, C.A.1    Huang, S.C.2    Tsirka, S.A.3    Kyriakidis, D.A.4    Canellakis, E.S.5
  • 51
    • 34247876224 scopus 로고    scopus 로고
    • Ribosomal frameshifting in decoding antizyme mRNAs from yeast and protists to humans: Close to 300 cases reveal remarkable diversity despite underlying conservation
    • I.P. Ivanov, and J.F. Atkins Ribosomal frameshifting in decoding antizyme mRNAs from yeast and protists to humans: close to 300 cases reveal remarkable diversity despite underlying conservation Nucleic Acids Res. 35 2007 1842 1858
    • (2007) Nucleic Acids Res. , vol.35 , pp. 1842-1858
    • Ivanov, I.P.1    Atkins, J.F.2
  • 52
    • 12144284818 scopus 로고    scopus 로고
    • The role of bacterial antizyme: From an inhibitory protein to A-to-C transcriptional regulator
    • E.E. Lioliou, and D.A. Kyriakidis The role of bacterial antizyme: from an inhibitory protein to A-to-C transcriptional regulator Microb. Cell Factories 3 2004 8
    • (2004) Microb. Cell Factories , vol.3 , pp. 8
    • Lioliou, E.E.1    Kyriakidis, D.A.2
  • 53
    • 11244337377 scopus 로고    scopus 로고
    • Polyamines regulate their synthesis by inducing expression and blocking degradation of ODC antizyme
    • R. Palanimurugan, H. Scheel, K. Hofmann, and R.J. Dohmen Polyamines regulate their synthesis by inducing expression and blocking degradation of ODC antizyme EMBO J. 23 2004 4857 4867
    • (2004) EMBO J. , vol.23 , pp. 4857-4867
    • Palanimurugan, R.1    Scheel, H.2    Hofmann, K.3    Dohmen, R.J.4
  • 54
    • 0034177792 scopus 로고    scopus 로고
    • Properties of a polyamine transporter regulated by antizyme
    • K. Sakata, K. Kashiwagi, and K. Igarashi Properties of a polyamine transporter regulated by antizyme Biochem. J. 347 2000 297 303
    • (2000) Biochem. J. , vol.347 , pp. 297-303
    • Sakata, K.1    Kashiwagi, K.2    Igarashi, K.3
  • 55
    • 30144434501 scopus 로고    scopus 로고
    • Polyamine transport by mammalian cells and mitochondria: Role of antizyme and glycosaminoglycans
    • K. Hoshino, E. Momiyama, K. Yoshida, K. Nishimura, S. Sakai, T. Toida, and et al. Polyamine transport by mammalian cells and mitochondria: role of antizyme and glycosaminoglycans J. Biol. Chem. 280 2005 42801 42808
    • (2005) J. Biol. Chem. , vol.280 , pp. 42801-42808
    • Hoshino, K.1    Momiyama, E.2    Yoshida, K.3    Nishimura, K.4    Sakai, S.5    Toida, T.6
  • 56
    • 80053133170 scopus 로고    scopus 로고
    • Polyamine sensing by nascent ornithine decarboxylase antizyme stimulates decoding of its mRNA
    • L. Kurian, R. Palanimurugan, D. Gödderz, and R.J. Dohmen Polyamine sensing by nascent ornithine decarboxylase antizyme stimulates decoding of its mRNA Nature 477 2011 490 494
    • (2011) Nature , vol.477 , pp. 490-494
    • Kurian, L.1    Palanimurugan, R.2    Gödderz, D.3    Dohmen, R.J.4
  • 57
    • 0020483536 scopus 로고
    • A macromolecular inhibitor of the antizyme to ornithine decarboxylase
    • K. Fujita, Y. Murakami, and S. Hayashi A macromolecular inhibitor of the antizyme to ornithine decarboxylase Biochem. J. 204 1982 647 652
    • (1982) Biochem. J. , vol.204 , pp. 647-652
    • Fujita, K.1    Murakami, Y.2    Hayashi, S.3
  • 58
    • 0037347195 scopus 로고    scopus 로고
    • Mitochondrial localization of antizyme is determined by context-dependent alternative utilization of two AUG initiation codons
    • S. Gandre, Z. Bercovich, and C. Kahana Mitochondrial localization of antizyme is determined by context-dependent alternative utilization of two AUG initiation codons Mitochondrion 2 2003 245 256
    • (2003) Mitochondrion , vol.2 , pp. 245-256
    • Gandre, S.1    Bercovich, Z.2    Kahana, C.3
  • 59
    • 0242666128 scopus 로고    scopus 로고
    • Identification of nuclear export signals in antizyme-1
    • N. Murai, Y. Murakami, and S. Matsufuji Identification of nuclear export signals in antizyme-1 J. Biol. Chem. 278 2003 44791 44798
    • (2003) J. Biol. Chem. , vol.278 , pp. 44791-44798
    • Murai, N.1    Murakami, Y.2    Matsufuji, S.3
  • 60
    • 0035108971 scopus 로고    scopus 로고
    • Nuclear translocation of antizyme and expression of ornithine decarboxylase and antizyme are developmentally regulated
    • A. Gritli-Linde, J. Nilsson, M. Bohlooly-Y, O. Heby, and A. Linde Nuclear translocation of antizyme and expression of ornithine decarboxylase and antizyme are developmentally regulated Dev. Dyn. 220 2001 259 275
    • (2001) Dev. Dyn. , vol.220 , pp. 259-275
    • Gritli-Linde, A.1    Nilsson, J.2    Bohlooly-Y, M.3    Heby, O.4    Linde, A.5
  • 61
    • 77449159833 scopus 로고    scopus 로고
    • S-Adenosylmethionine decarboxylase
    • A.E. Pegg S-Adenosylmethionine decarboxylase Essays Biochem. 46 2009 25 45
    • (2009) Essays Biochem. , vol.46 , pp. 25-45
    • Pegg, A.E.1
  • 62
    • 77953042159 scopus 로고    scopus 로고
    • Structural biology of S-adenosylmethionine decarboxylase
    • S. Bale, and S.E. Ealick Structural biology of S-adenosylmethionine decarboxylase Amino Acids 38 2010 451 460
    • (2010) Amino Acids , vol.38 , pp. 451-460
    • Bale, S.1    Ealick, S.E.2
  • 63
    • 0035859868 scopus 로고    scopus 로고
    • The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase
    • W.D. Tolbert, J.L. Ekstrom, I.I. Mathews, J.A. Secrist, P. Kapoor, A.E. Pegg, and et al. The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase Biochemistry 40 2001 9484 9494
    • (2001) Biochemistry , vol.40 , pp. 9484-9494
    • Tolbert, W.D.1    Ekstrom, J.L.2    Mathews, I.I.3    Secrist, J.A.4    Kapoor, P.5    Pegg, A.E.6
  • 64
    • 57649134245 scopus 로고    scopus 로고
    • Structural basis for putrescine activation of human S-adenosylmethionine decarboxylase
    • S. Bale, M.M. Lopez, G.I. Makhatadze, Q. Fang, A.E. Pegg, and S.E. Ealick Structural basis for putrescine activation of human S-adenosylmethionine decarboxylase Biochemistry 47 2008 13404 13417
    • (2008) Biochemistry , vol.47 , pp. 13404-13417
    • Bale, S.1    Lopez, M.M.2    Makhatadze, G.I.3    Fang, Q.4    Pegg, A.E.5    Ealick, S.E.6
  • 65
    • 0035859781 scopus 로고    scopus 로고
    • Structure of a human S-adenosylmethionine decarboxylase self-processing ester intermediate and mechanism of putrescine stimulation of processing as revealed by the H243A mutant
    • J.L. Ekstrom, W.D. Tolbert, H. Xiong, A.E. Pegg, and S.E. Ealick Structure of a human S-adenosylmethionine decarboxylase self-processing ester intermediate and mechanism of putrescine stimulation of processing as revealed by the H243A mutant Biochemistry 40 2001 9495 9504
    • (2001) Biochemistry , vol.40 , pp. 9495-9504
    • Ekstrom, J.L.1    Tolbert, W.D.2    Xiong, H.3    Pegg, A.E.4    Ealick, S.E.5
  • 67
    • 70350780368 scopus 로고    scopus 로고
    • Mammalian polyamine metabolism and function
    • A.E. Pegg Mammalian polyamine metabolism and function IUBMB Life 61 2009 880 894
    • (2009) IUBMB Life , vol.61 , pp. 880-894
    • Pegg, A.E.1
  • 68
    • 16344369002 scopus 로고    scopus 로고
    • HSG cells differentiated by culture on extracellular matrix involves induction of S-adenosylmethione decarboxylase and ornithine decarboxylase
    • K. Lam, L. Zhang, M. Bewick, and R.M. Lafrenie HSG cells differentiated by culture on extracellular matrix involves induction of S-adenosylmethione decarboxylase and ornithine decarboxylase J. Cell. Physiol. 203 2005 353 361
    • (2005) J. Cell. Physiol. , vol.203 , pp. 353-361
    • Lam, K.1    Zhang, L.2    Bewick, M.3    Lafrenie, R.M.4
  • 69
    • 0027510121 scopus 로고
    • Cell-specific translational regulation of S-adenosylmethionine decarboxylase mRNA. Dependence on translation and coding capacity of the cis-acting upstream open reading frame
    • J.R. Hill, and D.R. Morris Cell-specific translational regulation of S-adenosylmethionine decarboxylase mRNA. Dependence on translation and coding capacity of the cis-acting upstream open reading frame J. Biol. Chem. 268 1993 726 731
    • (1993) J. Biol. Chem. , vol.268 , pp. 726-731
    • Hill, J.R.1    Morris, D.R.2
  • 70
    • 0037155130 scopus 로고    scopus 로고
    • Regulated translation termination at the upstream open reading frame in S-adenosylmethionine decarboxylase mRNA
    • A. Raney, G.L. Law, G.J. Mize, and D.R. Morris Regulated translation termination at the upstream open reading frame in S-adenosylmethionine decarboxylase mRNA J. Biol. Chem. 277 2002 5988 5994
    • (2002) J. Biol. Chem. , vol.277 , pp. 5988-5994
    • Raney, A.1    Law, G.L.2    Mize, G.J.3    Morris, D.R.4
  • 71
    • 0035851192 scopus 로고    scopus 로고
    • Polyamine regulation of ribosome pausing at the upstream open reading frame of S-adenosylmethionine decarboxylase
    • G.L. Law, A. Raney, C. Heusner, and D.R. Morris Polyamine regulation of ribosome pausing at the upstream open reading frame of S-adenosylmethionine decarboxylase J. Biol. Chem. 276 2001 38036 38043
    • (2001) J. Biol. Chem. , vol.276 , pp. 38036-38043
    • Law, G.L.1    Raney, A.2    Heusner, C.3    Morris, D.R.4
  • 72
    • 28244500966 scopus 로고    scopus 로고
    • A dual upstream open reading frame-based autoregulatory circuit controlling polyamine-responsive translation
    • C. Hanfrey, K.A. Elliott, M. Franceschetti, M.J. Mayer, C. Illingworth, and A.J. Michael A dual upstream open reading frame-based autoregulatory circuit controlling polyamine-responsive translation J. Biol. Chem. 280 2005 39229 39237
    • (2005) J. Biol. Chem. , vol.280 , pp. 39229-39237
    • Hanfrey, C.1    Elliott, K.A.2    Franceschetti, M.3    Mayer, M.J.4    Illingworth, C.5    Michael, A.J.6
  • 73
    • 0141682707 scopus 로고    scopus 로고
    • Extremely rapid turnover of S-adenosylmethionine decarboxylase in Crithidia fasciculata
    • S. Nasizadeh, and L. Persson Extremely rapid turnover of S-adenosylmethionine decarboxylase in Crithidia fasciculata FEBS Lett. 553 2003 131 134
    • (2003) FEBS Lett. , vol.553 , pp. 131-134
    • Nasizadeh, S.1    Persson, L.2
  • 74
    • 1842582077 scopus 로고    scopus 로고
    • S-Adenosylmethionine decarboxylase degradation by the 26S proteasome is accelerated by substrate-mediated transamination
    • A. Yerlikaya, and B.A. Stanley S-Adenosylmethionine decarboxylase degradation by the 26S proteasome is accelerated by substrate-mediated transamination J. Biol. Chem. 279 2004 12469 12478
    • (2004) J. Biol. Chem. , vol.279 , pp. 12469-12478
    • Yerlikaya, A.1    Stanley, B.A.2
  • 75
    • 0038419788 scopus 로고    scopus 로고
    • Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase
    • T. Wu, V. Yankovskaya, and W.S. McIntire Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase J. Biol. Chem. 278 2003 20514 20525
    • (2003) J. Biol. Chem. , vol.278 , pp. 20514-20525
    • Wu, T.1    Yankovskaya, V.2    McIntire, W.S.3
  • 76
    • 0037115754 scopus 로고    scopus 로고
    • Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics
    • T. Murray-Stewart, Y. Wang, W. Devereux, and R.A. Casero Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics Biochem. J. 368 2002 673 677
    • (2002) Biochem. J. , vol.368 , pp. 673-677
    • Murray-Stewart, T.1    Wang, Y.2    Devereux, W.3    Casero, R.A.4
  • 78
    • 33747113587 scopus 로고    scopus 로고
    • Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion
    • P. Tavladoraki, M.N. Rossi, G. Saccuti, M.A. Perez-Amador, F. Polticelli, R. Angelini, and et al. Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion Plant Physiol. 141 2006 1519 1532
    • (2006) Plant Physiol. , vol.141 , pp. 1519-1532
    • Tavladoraki, P.1    Rossi, M.N.2    Saccuti, G.3    Perez-Amador, M.A.4    Polticelli, F.5    Angelini, R.6
  • 79
    • 0034819549 scopus 로고    scopus 로고
    • A barley polyamine oxidase isoform with distinct structural features and subcellular localization
    • M. Cervelli, A. Cona, R. Angelini, F. Polticelli, R. Federico, and P. Mariottini A barley polyamine oxidase isoform with distinct structural features and subcellular localization Eur. J. Biochem. 268 2001 3816 3830
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3816-3830
    • Cervelli, M.1    Cona, A.2    Angelini, R.3    Polticelli, F.4    Federico, R.5    Mariottini, P.6
  • 80
    • 0038136943 scopus 로고    scopus 로고
    • Heterologous expression and characterization of mouse spermine oxidase
    • M. Cervelli, F. Polticelli, R. Federico, and P. Mariottini Heterologous expression and characterization of mouse spermine oxidase J. Biol. Chem. 278 2003 5271 5276
    • (2003) J. Biol. Chem. , vol.278 , pp. 5271-5276
    • Cervelli, M.1    Polticelli, F.2    Federico, R.3    Mariottini, P.4
  • 83
    • 21844481660 scopus 로고
    • Diamine oxidase from millet catalyzes the oxidation of 1,3 diaminopropane
    • H.M.A. Awal, and E. Hirasawa Diamine oxidase from millet catalyzes the oxidation of 1,3 diaminopropane J. Plant Res. 108 1995 395 397
    • (1995) J. Plant Res. , vol.108 , pp. 395-397
    • Awal, H.M.A.1    Hirasawa, E.2
  • 86
    • 47549106852 scopus 로고    scopus 로고
    • Spermidine/spermine-N(1)-acetyltransferase: A key metabolic regulator
    • A.E. Pegg Spermidine/spermine-N(1)-acetyltransferase: a key metabolic regulator Am. J. Physiol. Endocrinol. Metab. 294 2008 E995 E1010
    • (2008) Am. J. Physiol. Endocrinol. Metab. , vol.294 , pp. E995-E1010
    • Pegg, A.E.1
  • 87
    • 0028070407 scopus 로고
    • Properties and structure of spermidine acetyltransferase in Escherichia coli
    • J.I. Fukuchi, K. Kashiwagi, K. Takio, and K. Igarashi Properties and structure of spermidine acetyltransferase in Escherichia coli J. Biol. Chem. 269 1994 22581 22585
    • (1994) J. Biol. Chem. , vol.269 , pp. 22581-22585
    • Fukuchi, J.I.1    Kashiwagi, K.2    Takio, K.3    Igarashi, K.4
  • 88
    • 20444451644 scopus 로고    scopus 로고
    • A yeast polyamine acetyltransferase
    • B. Liu, A. Sutton, and R. Sternglanz A yeast polyamine acetyltransferase J. Biol. Chem. 280 2005 16659 16664
    • (2005) J. Biol. Chem. , vol.280 , pp. 16659-16664
    • Liu, B.1    Sutton, A.2    Sternglanz, R.3
  • 90
    • 0023620631 scopus 로고
    • Functions of polyamine acetylation
    • N. Seiler Functions of polyamine acetylation Can. J. Physiol. Pharmacol. 65 1987 2024 2035
    • (1987) Can. J. Physiol. Pharmacol. , vol.65 , pp. 2024-2035
    • Seiler, N.1
  • 91
    • 0032545459 scopus 로고    scopus 로고
    • 1-acetyltransferase gene transcription
    • 1-acetyltransferase gene transcription J. Biol. Chem. 273 1998 34623 34630
    • (1998) J. Biol. Chem. , vol.273 , pp. 34623-34630
    • Wang, Y.1
  • 92
    • 0033618279 scopus 로고    scopus 로고
    • Cloning and characterization of human polyamine-modulated factor-1, a transcriptional cofactor that regulates the transcription of the spermidine/spermine N(1)-acetyltransferase gene
    • Y. Wang, W. Devereux, T.M. Stewart, and R.A. Casero Cloning and characterization of human polyamine-modulated factor-1, a transcriptional cofactor that regulates the transcription of the spermidine/spermine N(1)-acetyltransferase gene J. Biol. Chem. 274 1999 22095 22101
    • (1999) J. Biol. Chem. , vol.274 , pp. 22095-22101
    • Wang, Y.1    Devereux, W.2    Stewart, T.M.3    Casero, R.A.4
  • 95
    • 17444385938 scopus 로고    scopus 로고
    • Induction of a SSAT isoform in response to hypoxia or iron deficiency and its protective effects on cell death
    • K. Kim, J.-H. Ryu, J.-W. Park, M.-S. Kim, and Y.-S. Chun Induction of a SSAT isoform in response to hypoxia or iron deficiency and its protective effects on cell death Biochem. Biophys. Res. Commun. 331 2005 78 85
    • (2005) Biochem. Biophys. Res. Commun. , vol.331 , pp. 78-85
    • Kim, K.1    Ryu, J.-H.2    Park, J.-W.3    Kim, M.-S.4    Chun, Y.-S.5
  • 98
    • 77449136427 scopus 로고    scopus 로고
    • A profusion of upstream open reading frame mechanisms in polyamine-responsive translational regulation
    • I.P. Ivanov, J.F. Atkins, and A.J. Michael A profusion of upstream open reading frame mechanisms in polyamine-responsive translational regulation Nucleic Acids Res. 38 2010 353 359
    • (2010) Nucleic Acids Res. , vol.38 , pp. 353-359
    • Ivanov, I.P.1    Atkins, J.F.2    Michael, A.J.3
  • 100
    • 0035882159 scopus 로고    scopus 로고
    • 1-acetyltransferase and prevent its targeting to the proteasome for degradation
    • 1-acetyltransferase and prevent its targeting to the proteasome for degradation Biochem. J. 358 2001 137 145
    • (2001) Biochem. J. , vol.358 , pp. 137-145
    • Coleman, C.S.1    Pegg, A.E.2
  • 101
    • 0027250513 scopus 로고
    • Functions of PotA and PotD proteins in spermidine-preferential uptake system in Escherichia coli
    • K. Kashiwagi, S. Miyamoto, E. Nukui, H. Kobayashi, and K. Igarashi Functions of PotA and PotD proteins in spermidine-preferential uptake system in Escherichia coli J. Biol. Chem. 268 1993 19358 19363
    • (1993) J. Biol. Chem. , vol.268 , pp. 19358-19363
    • Kashiwagi, K.1    Miyamoto, S.2    Nukui, E.3    Kobayashi, H.4    Igarashi, K.5
  • 102
    • 0035002972 scopus 로고    scopus 로고
    • Polyamine uptake systems in Escherichia coli
    • K. Igarashi, K. Ito, and K. Kashiwagi Polyamine uptake systems in Escherichia coli Res. Microbiol. 152 2001 271 278
    • (2001) Res. Microbiol. , vol.152 , pp. 271-278
    • Igarashi, K.1    Ito, K.2    Kashiwagi, K.3
  • 103
    • 78649869949 scopus 로고    scopus 로고
    • Characteristics of cellular polyamine transport in prokaryotes and eukaryotes
    • K. Igarashi, and K. Kashiwagi Characteristics of cellular polyamine transport in prokaryotes and eukaryotes Plant Physiol. Biochem. 48 2010 506 512
    • (2010) Plant Physiol. Biochem. , vol.48 , pp. 506-512
    • Igarashi, K.1    Kashiwagi, K.2
  • 104
    • 0030889906 scopus 로고    scopus 로고
    • Excretion and uptake of putrescine by the PotE protein in Escherichia coli
    • K. Kashiwagi, S. Shibuya, H. Tomitori, A. Kuraishi, and K. Igarashi Excretion and uptake of putrescine by the PotE protein in Escherichia coli J. Biol. Chem. 272 1997 6318 6323
    • (1997) J. Biol. Chem. , vol.272 , pp. 6318-6323
    • Kashiwagi, K.1    Shibuya, S.2    Tomitori, H.3    Kuraishi, A.4    Igarashi, K.5
  • 105
    • 1542721578 scopus 로고    scopus 로고
    • Excretion and uptake of cadaverine by CadB and its physiological functions in Escherichia coli
    • W. Soksawatmaekhin, A. Kuraishi, K. Sakata, K. Kashiwagi, and K. Igarashi Excretion and uptake of cadaverine by CadB and its physiological functions in Escherichia coli Mol. Microbiol. 51 2004 1401 1412
    • (2004) Mol. Microbiol. , vol.51 , pp. 1401-1412
    • Soksawatmaekhin, W.1    Kuraishi, A.2    Sakata, K.3    Kashiwagi, K.4    Igarashi, K.5
  • 106
    • 38649122069 scopus 로고    scopus 로고
    • Identification of a spermidine excretion protein complex (MdtJI) in Escherichia coli
    • K. Higashi, H. Ishigure, R. Demizu, T. Uemura, K. Nishino, A. Yamaguchi, and et al. Identification of a spermidine excretion protein complex (MdtJI) in Escherichia coli J. Bacteriol. 190 2008 872 878
    • (2008) J. Bacteriol. , vol.190 , pp. 872-878
    • Higashi, K.1    Ishigure, H.2    Demizu, R.3    Uemura, T.4    Nishino, K.5    Yamaguchi, A.6
  • 107
    • 13844266300 scopus 로고    scopus 로고
    • Uptake of putrescine and spermidine by Gap1p on the plasma membrane in Saccharomyces cerevisiae
    • T. Uemura, K. Kashiwagi, and K. Igarashi Uptake of putrescine and spermidine by Gap1p on the plasma membrane in Saccharomyces cerevisiae Biochem. Biophys. Res. Commun. 328 2005 1028 1033
    • (2005) Biochem. Biophys. Res. Commun. , vol.328 , pp. 1028-1033
    • Uemura, T.1    Kashiwagi, K.2    Igarashi, K.3
  • 108
    • 34147156603 scopus 로고    scopus 로고
    • Polyamine uptake by DUR3 and SAM3 in Saccharomyces cerevisiae
    • T. Uemura, K. Kashiwagi, and K. Igarashi Polyamine uptake by DUR3 and SAM3 in Saccharomyces cerevisiae J. Biol. Chem. 282 2007 7733 7741
    • (2007) J. Biol. Chem. , vol.282 , pp. 7733-7741
    • Uemura, T.1    Kashiwagi, K.2    Igarashi, K.3
  • 109
    • 21244494094 scopus 로고    scopus 로고
    • AGP2 encodes the major permease for high affinity polyamine import in Saccharomyces cerevisiae
    • M. Aouida, A. Leduc, R. Poulin, and D. Ramotar AGP2 encodes the major permease for high affinity polyamine import in Saccharomyces cerevisiae J. Biol. Chem. 280 2005 24267 24276
    • (2005) J. Biol. Chem. , vol.280 , pp. 24267-24276
    • Aouida, M.1    Leduc, A.2    Poulin, R.3    Ramotar, D.4
  • 110
    • 84878629644 scopus 로고    scopus 로고
    • Agp2, a member of the yeast amino acid permease family, positively regulates polyamine transport at the transcriptional level
    • M. Aouida, M. Rubio-Texeira, J.M. Thevelein, R. Poulin, and D. Ramotar Agp2, a member of the yeast amino acid permease family, positively regulates polyamine transport at the transcriptional level PLoS One 8 6 2013 Jun 3 e65717
    • (2013) PLoS One , vol.8 , Issue.6 , pp. e65717
    • Aouida, M.1    Rubio-Texeira, M.2    Thevelein, J.M.3    Poulin, R.4    Ramotar, D.5
  • 111
    • 1342281677 scopus 로고    scopus 로고
    • Uptake of GABA and putrescine by UGA4 on the vacuolar membrane in Saccharomyces cerevisiae
    • T. Uemura, Y. Tomonari, K. Kashiwagi, and K. Igarashi Uptake of GABA and putrescine by UGA4 on the vacuolar membrane in Saccharomyces cerevisiae Biochem. Biophys. Res. Commun. 315 2004 1082 1087
    • (2004) Biochem. Biophys. Res. Commun. , vol.315 , pp. 1082-1087
    • Uemura, T.1    Tomonari, Y.2    Kashiwagi, K.3    Igarashi, K.4
  • 112
    • 0033572636 scopus 로고    scopus 로고
    • Polyamine transport in bacteria and yeast
    • K. Igarashi, and K. Kashiwagi Polyamine transport in bacteria and yeast Biochem J 344 Pt 3 1999 633 642
    • (1999) Biochem J , vol.344 , pp. 633-642
    • Igarashi, K.1    Kashiwagi, K.2
  • 113
    • 79956217992 scopus 로고    scopus 로고
    • Identification and assays of polyamine transport systems in Escherichia coli and Saccharomyces cerevisiae
    • K. Kashiwagi, and K. Igarashi Identification and assays of polyamine transport systems in Escherichia coli and Saccharomyces cerevisiae Methods Mol. Biol 720 2011 295 308
    • (2011) Methods Mol. Biol , vol.720 , pp. 295-308
    • Kashiwagi, K.1    Igarashi, K.2
  • 114
    • 16844385961 scopus 로고    scopus 로고
    • Excretion of putrescine and spermidine by the protein encoded by YKL174c (TPO5) in Saccharomyces cerevisiae
    • K. Tachihara, T. Uemura, K. Kashiwagi, and K. Igarashi Excretion of putrescine and spermidine by the protein encoded by YKL174c (TPO5) in Saccharomyces cerevisiae J. Biol. Chem. 280 2005 12637 12642
    • (2005) J. Biol. Chem. , vol.280 , pp. 12637-12642
    • Tachihara, K.1    Uemura, T.2    Kashiwagi, K.3    Igarashi, K.4
  • 117
    • 79953680750 scopus 로고    scopus 로고
    • Yeast response and tolerance to polyamine toxicity involving the drug: H+ antiporter Qdr3 and the transcription factors Yap1 and Gcn4
    • M.C. Teixeira, T.R. Cabrito, Z.M. Hanif, R.C. Vargas, S. Tenreiro, and I. Sá-Correia Yeast response and tolerance to polyamine toxicity involving the drug: H+ antiporter Qdr3 and the transcription factors Yap1 and Gcn4 Microbiology 157 2011 945 956
    • (2011) Microbiology , vol.157 , pp. 945-956
    • Teixeira, M.C.1    Cabrito, T.R.2    Hanif, Z.M.3    Vargas, R.C.4    Tenreiro, S.5    Sá-Correia, I.6
  • 118
    • 0037630437 scopus 로고    scopus 로고
    • Localization and function of the yeast multidrug transporter Tpo1p
    • M. Albertsen, I. Bellahn, R. Krämer, and S. Waffenschmidt Localization and function of the yeast multidrug transporter Tpo1p J. Biol. Chem. 278 2003 12820 12825
    • (2003) J. Biol. Chem. , vol.278 , pp. 12820-12825
    • Albertsen, M.1    Bellahn, I.2    Krämer, R.3    Waffenschmidt, S.4
  • 119
    • 79952277996 scopus 로고    scopus 로고
    • Targeting trypanothione metabolism in trypanosomatid human parasites
    • V. Olin-Sandoval, R. Moreno-Sánchez, and E. Saavedra Targeting trypanothione metabolism in trypanosomatid human parasites Curr. Drug Targets 11 12 2010 Dec 1614 1630
    • (2010) Curr. Drug Targets , vol.11 , Issue.12 , pp. 1614-1630
    • Olin-Sandoval, V.1    Moreno-Sánchez, R.2    Saavedra, E.3
  • 120
    • 17644403556 scopus 로고    scopus 로고
    • Identification and characterization of a polyamine permease from the protozoan parasite Leishmania major
    • M.P. Hasne, and B. Ullman Identification and characterization of a polyamine permease from the protozoan parasite Leishmania major J. Biol. Chem. 280 2005 15188 15194
    • (2005) J. Biol. Chem. , vol.280 , pp. 15188-15194
    • Hasne, M.P.1    Ullman, B.2
  • 121
    • 84861677889 scopus 로고    scopus 로고
    • Recent advances in the molecular biology of metazoan polyamine transport
    • R. Poulin, R.A. Casero, and D. Soulet Recent advances in the molecular biology of metazoan polyamine transport Amino Acids 42 2012 711 723
    • (2012) Amino Acids , vol.42 , pp. 711-723
    • Poulin, R.1    Casero, R.A.2    Soulet, D.3
  • 122
    • 84900859915 scopus 로고    scopus 로고
    • Identification of polyamine transporters in plants:paraquat transport provides crucial clues
    • M.S.K. Fujita Identification of polyamine transporters in plants:paraquat transport provides crucial clues Plant Cell Physiol. 55 2014 855 861
    • (2014) Plant Cell Physiol. , vol.55 , pp. 855-861
    • Fujita, M.S.K.1
  • 125
    • 0029147992 scopus 로고
    • Polyamine-mediated conformational perturbations in DNA alter the binding of estrogen receptor to poly(dG-m5dC).poly(dG-m5dC) and a plasmid containing the estrogen response element
    • T. Thomas, M.A. Gallo, C.M. Klinge, and T.J. Thomas Polyamine-mediated conformational perturbations in DNA alter the binding of estrogen receptor to poly(dG-m5dC).poly(dG-m5dC) and a plasmid containing the estrogen response element J. Steroid Biochem. Mol. Biol. 54 1995 89 99
    • (1995) J. Steroid Biochem. Mol. Biol. , vol.54 , pp. 89-99
    • Thomas, T.1    Gallo, M.A.2    Klinge, C.M.3    Thomas, T.J.4
  • 126
    • 67249127378 scopus 로고    scopus 로고
    • Elevated polyamines induce c- MYC overexpression by perturbing quadruplex-WC duplex equilibrium
    • N. Kumar, R. Basundra, and S. Maiti Elevated polyamines induce c- MYC overexpression by perturbing quadruplex-WC duplex equilibrium Nucleic Acids Res. 37 2009 3321 3331
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3321-3331
    • Kumar, N.1    Basundra, R.2    Maiti, S.3
  • 129
    • 8544226985 scopus 로고    scopus 로고
    • A unifying model for the role of polyamines in bacterial cell growth, the polyamine modulon
    • M. Yoshida, K. Kashiwagi, A. Shigemasa, S. Taniguchi, K. Yamamoto, H. Makinoshima, and et al. A unifying model for the role of polyamines in bacterial cell growth, the polyamine modulon J. Biol. Chem. 279 2004 46008 46013
    • (2004) J. Biol. Chem. , vol.279 , pp. 46008-46013
    • Yoshida, M.1    Kashiwagi, K.2    Shigemasa, A.3    Taniguchi, S.4    Yamamoto, K.5    Makinoshima, H.6
  • 130
    • 70349290575 scopus 로고    scopus 로고
    • Identification of proteins whose synthesis is preferentially enhanced by polyamines at the level of translation in mammalian cells
    • K. Nishimura, H. Okudaira, E. Ochiai, K. Higashi, M. Kaneko, I. Ishii, and et al. Identification of proteins whose synthesis is preferentially enhanced by polyamines at the level of translation in mammalian cells Int. J. Biochem. Cell Biol. 41 2009 2251 2261
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 2251-2261
    • Nishimura, K.1    Okudaira, H.2    Ochiai, E.3    Higashi, K.4    Kaneko, M.5    Ishii, I.6
  • 131
    • 32944472627 scopus 로고    scopus 로고
    • Polyamine modulon in Escherichia coli: Genes involved in the stimulation of cell growth by polyamines
    • K. Igarashi, and K. Kashiwagi Polyamine modulon in Escherichia coli: genes involved in the stimulation of cell growth by polyamines J. Biochem. 139 2006 11 16
    • (2006) J. Biochem. , vol.139 , pp. 11-16
    • Igarashi, K.1    Kashiwagi, K.2
  • 132
    • 33947096829 scopus 로고    scopus 로고
    • Enhancement of the synthesis of RpoN, Cra, and H-NS by polyamines at the level of translation in Escherichia coli cultured with glucose and glutamate
    • Y. Terui, K. Higashi, S. Taniguchi, A. Shigemasa, K. Nishimura, K. Yamamoto, and et al. Enhancement of the synthesis of RpoN, Cra, and H-NS by polyamines at the level of translation in Escherichia coli cultured with glucose and glutamate J. Bacteriol. 189 2007 2359 2368
    • (2007) J. Bacteriol. , vol.189 , pp. 2359-2368
    • Terui, Y.1    Higashi, K.2    Taniguchi, S.3    Shigemasa, A.4    Nishimura, K.5    Yamamoto, K.6
  • 133
    • 0033529644 scopus 로고    scopus 로고
    • Polyamine stimulation of the synthesis of oligopeptide-binding protein (OppA). Involvement of a structural change of the Shine-Dalgarno sequence and the initiation codon aug in OppA mRNA
    • M. Yoshida, D. Meksuriyen, K. Kashiwagi, G. Kawai, and K. Igarashi Polyamine stimulation of the synthesis of oligopeptide-binding protein (OppA). Involvement of a structural change of the Shine-Dalgarno sequence and the initiation codon aug in OppA mRNA J. Biol. Chem. 274 1999 22723 22728
    • (1999) J. Biol. Chem. , vol.274 , pp. 22723-22728
    • Yoshida, M.1    Meksuriyen, D.2    Kashiwagi, K.3    Kawai, G.4    Igarashi, K.5
  • 134
    • 0035844218 scopus 로고    scopus 로고
    • Polyamine enhancement of the synthesis of adenylate cyclase at the translational level and the consequential stimulation of the synthesis of the RNA polymerase σ28 subunit
    • M. Yoshida, K. Kashiwagi, G. Kawai, A. Ishihama, and K. Igarashi Polyamine enhancement of the synthesis of adenylate cyclase at the translational level and the consequential stimulation of the synthesis of the RNA polymerase σ28 subunit J. Biol. Chem. 276 2001 16289 16295
    • (2001) J. Biol. Chem. , vol.276 , pp. 16289-16295
    • Yoshida, M.1    Kashiwagi, K.2    Kawai, G.3    Ishihama, A.4    Igarashi, K.5
  • 135
  • 136
    • 0029785142 scopus 로고    scopus 로고
    • Selective translation initiation by ribosome jumping in adenovirus- infected and heat-shocked cells
    • A. Yueh, and R.J. Schneider Selective translation initiation by ribosome jumping in adenovirus- infected and heat-shocked cells Genes Dev. 10 1996 1557 1567
    • (1996) Genes Dev. , vol.10 , pp. 1557-1567
    • Yueh, A.1    Schneider, R.J.2
  • 137
    • 0037020166 scopus 로고    scopus 로고
    • Polyamines enhance synthesis of the RNA polymerase σ38 subunit by suppression of an amber termination codon in the open reading frame
    • M. Yoshida, K. Kashiwagi, G. Kawai, A. Ishihama, and K. Igarashi Polyamines enhance synthesis of the RNA polymerase σ38 subunit by suppression of an amber termination codon in the open reading frame J. Biol. Chem. 277 2002 37139 37146
    • (2002) J. Biol. Chem. , vol.277 , pp. 37139-37146
    • Yoshida, M.1    Kashiwagi, K.2    Kawai, G.3    Ishihama, A.4    Igarashi, K.5
  • 138
    • 77951219633 scopus 로고    scopus 로고
    • The role of polyamines in supporting growth of mammalian cells is mediated through their requirement for translation initiation and elongation
    • G. Landau, Z. Bercovich, M.H. Park, and C. Kahana The role of polyamines in supporting growth of mammalian cells is mediated through their requirement for translation initiation and elongation J. Biol. Chem. 285 2010 12474 12481
    • (2010) J. Biol. Chem. , vol.285 , pp. 12474-12481
    • Landau, G.1    Bercovich, Z.2    Park, M.H.3    Kahana, C.4
  • 139
    • 84913102207 scopus 로고
    • Spermine and related polyamines as growth stimulants for Lactobacillus casei
    • H. Kihara, and E.E. Snell Spermine and related polyamines as growth stimulants for Lactobacillus casei Proc. Natl. Acad. Sci. U. S. A. 43 1957 867 871
    • (1957) Proc. Natl. Acad. Sci. U. S. A. , vol.43 , pp. 867-871
    • Kihara, H.1    Snell, E.E.2
  • 140
    • 0017265206 scopus 로고
    • Cyclic change in polyamine concentrations in sea urchin eggs related with cleavage cycle
    • S. Kusunoki, and I. Yasumasu Cyclic change in polyamine concentrations in sea urchin eggs related with cleavage cycle Biochem. Biophys. Res. Commun. 68 1976 881 885
    • (1976) Biochem. Biophys. Res. Commun. , vol.68 , pp. 881-885
    • Kusunoki, S.1    Yasumasu, I.2
  • 141
    • 0018067850 scopus 로고
    • Inhibitory effect of α-hydrazinoornithine on egg cleavage in sea urchin eggs
    • S. Kusunoki, and I. Yasumasu Inhibitory effect of α-hydrazinoornithine on egg cleavage in sea urchin eggs Dev. Biol. 67 1978 336 345
    • (1978) Dev. Biol. , vol.67 , pp. 336-345
    • Kusunoki, S.1    Yasumasu, I.2
  • 142
    • 0016757779 scopus 로고
    • Isolation, characterization, and mapping of Escherichia coli mutants blocked in the synthesis of ornithine decarboxylase
    • S. Cunningham-Rundles, and W.K. Maas Isolation, characterization, and mapping of Escherichia coli mutants blocked in the synthesis of ornithine decarboxylase J. Bacteriol. 124 1975 791 799
    • (1975) J. Bacteriol. , vol.124 , pp. 791-799
    • Cunningham-Rundles, S.1    Maas, W.K.2
  • 143
    • 0027415389 scopus 로고
    • Deletion mutations in the speED operon: Spermidine is not essential for the growth of Escherichia coli
    • Q.-W. Xie, C.W. Tabor, and H. Tabor Deletion mutations in the speED operon: spermidine is not essential for the growth of Escherichia coli Gene 126 1993 115 117
    • (1993) Gene , vol.126 , pp. 115-117
    • Xie, Q.-W.1    Tabor, C.W.2    Tabor, H.3
  • 144
    • 0032895918 scopus 로고    scopus 로고
    • Polyamine depletion arrests cell cycle and induces inhibitors p21(Waf1/Cip1), p27(Kip1), and p53 in IEC-6 cells
    • R.M. Ray, B.J. Zimmerman, S.A. McCormack, T.B. Patel, and L.R. Johnson Polyamine depletion arrests cell cycle and induces inhibitors p21(Waf1/Cip1), p27(Kip1), and p53 in IEC-6 cells Am. J. Physiol. 276 1999 C684 C691
    • (1999) Am. J. Physiol. , vol.276 , pp. C684-C691
    • Ray, R.M.1    Zimmerman, B.J.2    McCormack, S.A.3    Patel, T.B.4    Johnson, L.R.5
  • 145
    • 59449110483 scopus 로고    scopus 로고
    • Polyamine synthesis inhibition induces S phase cell cycle arrest in vascular smooth muscle cells
    • M. Odenlund, B. Holmqvist, B. Baldetorp, P. Hellstrand, and B.-O. Nilsson Polyamine synthesis inhibition induces S phase cell cycle arrest in vascular smooth muscle cells Amino Acids 36 2009 273 282
    • (2009) Amino Acids , vol.36 , pp. 273-282
    • Odenlund, M.1    Holmqvist, B.2    Baldetorp, B.3    Hellstrand, P.4    Nilsson, B.-O.5
  • 146
    • 0036678118 scopus 로고    scopus 로고
    • Absolute requirement of spermidine for growth and cell cycle progression of fission yeast (Schizosaccharomyces pombe)
    • M.K. Chattopadhyay, C.W. Tabor, and H. Tabor Absolute requirement of spermidine for growth and cell cycle progression of fission yeast (Schizosaccharomyces pombe) Proc. Natl. Acad. Sci. U. S. A. 99 2002 10330 10334
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 10330-10334
    • Chattopadhyay, M.K.1    Tabor, C.W.2    Tabor, H.3
  • 147
    • 0026053025 scopus 로고
    • Spermidine or spermine is essential for the aerobic growth of Saccharomyces cerevisiae
    • D. Balasundaram, C.W. Tabor, and H. Tabor Spermidine or spermine is essential for the aerobic growth of Saccharomyces cerevisiae Proc. Natl. Acad. Sci. U. S. A. 88 1991 5872 5876
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 5872-5876
    • Balasundaram, D.1    Tabor, C.W.2    Tabor, H.3
  • 148
    • 0025218986 scopus 로고
    • The genetics of polyamine synthesis in Neurospora crassa
    • J. Pitkin, and R.H. Davis The genetics of polyamine synthesis in Neurospora crassa Arch. Biochem. Biophys. 278 1990 386 391
    • (1990) Arch. Biochem. Biophys. , vol.278 , pp. 386-391
    • Pitkin, J.1    Davis, R.H.2
  • 149
    • 0016489245 scopus 로고
    • Cell cycle specific fluctuations in adenosine 3′:5′-cyclic monophosphate and polyamines of Chinese hamster cells
    • D.H. Russell, and P.J. Stambrook Cell cycle specific fluctuations in adenosine 3′:5′-cyclic monophosphate and polyamines of Chinese hamster cells Proc. Natl. Acad. Sci. U. S. A. 72 1975 1482 1486
    • (1975) Proc. Natl. Acad. Sci. U. S. A. , vol.72 , pp. 1482-1486
    • Russell, D.H.1    Stambrook, P.J.2
  • 150
  • 151
    • 0019429488 scopus 로고
    • The relationship between levels and rates of synthesis of polyamines during mammalian cell cycle
    • P.S. Sunkara, S. Ramakrishna, K. Nishioka, and P.N. Rao The relationship between levels and rates of synthesis of polyamines during mammalian cell cycle Life Sci. 28 1981 1497 1506
    • (1981) Life Sci. , vol.28 , pp. 1497-1506
    • Sunkara, P.S.1    Ramakrishna, S.2    Nishioka, K.3    Rao, P.N.4
  • 152
    • 0015526404 scopus 로고
    • Ornithine decarboxylase activity in synchronously growing Don C cells
    • S.J. Friedman, R.A. Bellantone, and E.S. Canellakis Ornithine decarboxylase activity in synchronously growing Don C cells Biochim. Biophys. Acta 261 1972 188 193
    • (1972) Biochim. Biophys. Acta , vol.261 , pp. 188-193
    • Friedman, S.J.1    Bellantone, R.A.2    Canellakis, E.S.3
  • 153
    • 0028985470 scopus 로고
    • Ornithine decarboxylase and S-adenosylmethionine decarboxylase expression during the cell cycle of Chinese hamster ovary cells
    • J.O. Fredlund, M.C. Johansson, E. Dahlberg, and S.M. Oredsson Ornithine decarboxylase and S-adenosylmethionine decarboxylase expression during the cell cycle of Chinese hamster ovary cells Exp. Cell Res. 216 1995 86 92
    • (1995) Exp. Cell Res. , vol.216 , pp. 86-92
    • Fredlund, J.O.1    Johansson, M.C.2    Dahlberg, E.3    Oredsson, S.M.4
  • 155
    • 0020660762 scopus 로고
    • An inhibitor of polyamine synthesis arrests cells at an earlier stage of G1 than does calcium deprivation
    • B.F. Cheetham An inhibitor of polyamine synthesis arrests cells at an earlier stage of G1 than does calcium deprivation Mol. Cell. Biol. 3 1983 480 483
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 480-483
    • Cheetham, B.F.1
  • 156
    • 0033559550 scopus 로고    scopus 로고
    • Polyamine analogue induction of the p53-p21WAF1/CIP1-Rb pathway and G1 arrest in human melanoma cells
    • D.L. Kramer, S. Vujcic, P. Diegelman, J. Alderfer, J.T. Miller, J.D. Black, and et al. Polyamine analogue induction of the p53-p21WAF1/CIP1-Rb pathway and G1 arrest in human melanoma cells Cancer Res. 59 1999 1278 1286
    • (1999) Cancer Res. , vol.59 , pp. 1278-1286
    • Kramer, D.L.1    Vujcic, S.2    Diegelman, P.3    Alderfer, J.4    Miller, J.T.5    Black, J.D.6
  • 157
    • 0018187647 scopus 로고
    • Interference with S and G2 phase progression by polyamine synthesis inhibitors
    • O. Heby, G. Andersson, and J.W. Gray Interference with S and G2 phase progression by polyamine synthesis inhibitors Exp. Cell Res. 111 1978 461 464
    • (1978) Exp. Cell Res. , vol.111 , pp. 461-464
    • Heby, O.1    Andersson, G.2    Gray, J.W.3
  • 158
    • 0021432506 scopus 로고
    • Polyamine starvation prolongs the S and G2 phases of polyamine-dependent (arginase-deficient) CHO cells
    • S. Anehus, P. Pohjanpelto, B. Baldetorp, E. Långström, and O. Heby Polyamine starvation prolongs the S and G2 phases of polyamine-dependent (arginase-deficient) CHO cells Mol. Cell. Biol. 4 1984 915 922
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 915-922
    • Anehus, S.1    Pohjanpelto, P.2    Baldetorp, B.3    Långström, E.4    Heby, O.5
  • 159
    • 0035865678 scopus 로고    scopus 로고
    • Manipulation of the expression of regulatory genes of polyamine metabolism results in specific alterations of the cell-cycle progression
    • F. Scorcioni, A. Corti, P. Davalli, S. Astancolle, and S. Bettuzzi Manipulation of the expression of regulatory genes of polyamine metabolism results in specific alterations of the cell-cycle progression Biochem. J. 354 2001 217 223
    • (2001) Biochem. J. , vol.354 , pp. 217-223
    • Scorcioni, F.1    Corti, A.2    Davalli, P.3    Astancolle, S.4    Bettuzzi, S.5
  • 161
    • 0025810272 scopus 로고
    • Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae
    • J. Schnier, H.G. Schwelberger, Z. Smit-McBride, H.A. Kang, and J.W. Hershey Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae Mol. Cell. Biol. 11 1991 3105 3114
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3105-3114
    • Schnier, J.1    Schwelberger, H.G.2    Smit-McBride, Z.3    Kang, H.A.4    Hershey, J.W.5
  • 162
    • 0020580011 scopus 로고
    • Identification of the hypusine-containing protein Hy + as translation initiation factor eIF-4D
    • H.L. Cooper, M.H. Park, J.E. Folk, B. Safer, and R. Braverman Identification of the hypusine-containing protein Hy + as translation initiation factor eIF-4D Proc. Natl. Acad. Sci. U. S. A. 80 1983 1854 1857
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 1854-1857
    • Cooper, H.L.1    Park, M.H.2    Folk, J.E.3    Safer, B.4    Braverman, R.5
  • 163
    • 0020162215 scopus 로고
    • Posttranslational formation of hypusine in a single major protein occurs generally in growing cells and is associated with activation of lymphocyte growth
    • H.L. Cooper, M.H. Park, and J.E. Folk Posttranslational formation of hypusine in a single major protein occurs generally in growing cells and is associated with activation of lymphocyte growth Cell 29 1982 791 797
    • (1982) Cell , vol.29 , pp. 791-797
    • Cooper, H.L.1    Park, M.H.2    Folk, J.E.3
  • 164
    • 77953039922 scopus 로고    scopus 로고
    • Functional significance of eIF5A and its hypusine modification in eukaryotes
    • M.H. Park, K. Nishimura, C.F. Zanelli, and S.R. Valentini Functional significance of eIF5A and its hypusine modification in eukaryotes Amino Acids 38 2010 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
  • 165
    • 0027197906 scopus 로고
    • Hypusine: Its post-translational formation in eukaryotic initiation factor 5A and its potential role in cellular regulation
    • M.H. Park, E.C. Wolff, and J.E. Folk Hypusine: its post-translational formation in eukaryotic initiation factor 5A and its potential role in cellular regulation Biofactors 4 1993 95 104
    • (1993) Biofactors , vol.4 , pp. 95-104
    • Park, M.H.1    Wolff, E.C.2    Folk, J.E.3
  • 166
    • 0029873356 scopus 로고    scopus 로고
    • The polyamine-derived amino acid hypusine: Its post-translational formation in eIF-5A and its role in cell proliferation
    • M.H. Park, Y.A. Joe, K.R. Kang, Y.B. Lee, and E.C. Wolff The polyamine-derived amino acid hypusine: its post-translational formation in eIF-5A and its role in cell proliferation Amino Acids 10 1996 109 121
    • (1996) Amino Acids , vol.10 , pp. 109-121
    • Park, M.H.1    Joe, Y.A.2    Kang, K.R.3    Lee, Y.B.4    Wolff, E.C.5
  • 167
    • 34547676811 scopus 로고    scopus 로고
    • Posttranslational synthesis of hypusine: Evolutionary progression and specificity of the hypusine modification
    • E.C. Wolff, K.R. Kang, Y.S. Kim, and M.H. Park Posttranslational synthesis of hypusine: evolutionary progression and specificity of the hypusine modification Amino Acids 33 2007 341 350
    • (2007) Amino Acids , vol.33 , pp. 341-350
    • Wolff, E.C.1    Kang, K.R.2    Kim, Y.S.3    Park, M.H.4
  • 168
    • 0030000577 scopus 로고    scopus 로고
    • Deoxyhypusine synthase gene is essential for cell viability in the yeast Saccharomyces cerevisiae
    • K. Sasaki, M.R. Abid, and M. Miyazaki Deoxyhypusine synthase gene is essential for cell viability in the yeast Saccharomyces cerevisiae FEBS Lett. 384 1996 151 154
    • (1996) FEBS Lett. , vol.384 , pp. 151-154
    • Sasaki, K.1    Abid, M.R.2    Miyazaki, M.3
  • 169
    • 0006806047 scopus 로고    scopus 로고
    • Deoxyhypusine synthase activity is essential for cell viability in the yeast Saccharomyces cerevisiae
    • M.H. Park, Y.A. Joe, and K.R. Kang Deoxyhypusine synthase activity is essential for cell viability in the yeast Saccharomyces cerevisiae J. Biol. Chem. 273 1998 1677 1683
    • (1998) J. Biol. Chem. , vol.273 , pp. 1677-1683
    • Park, M.H.1    Joe, Y.A.2    Kang, K.R.3
  • 170
    • 0028145708 scopus 로고
    • Effect of initiation factor eIF-5A depletion on protein synthesis and proliferation of Saccharomyces cerevisiae
    • H.A. Kang, and J.W. Hershey Effect of initiation factor eIF-5A depletion on protein synthesis and proliferation of Saccharomyces cerevisiae J. Biol. Chem. 269 1994 3934 3940
    • (1994) J. Biol. Chem. , vol.269 , pp. 3934-3940
    • Kang, H.A.1    Hershey, J.W.2
  • 171
    • 44349133214 scopus 로고    scopus 로고
    • Hypusine modification for growth is the major function of spermidine in Saccharomyces cerevisiae polyamine auxotrophs grown in limiting spermidine
    • M.K. Chattopadhyay, M.H. Park, and H. Tabor Hypusine modification for growth is the major function of spermidine in Saccharomyces cerevisiae polyamine auxotrophs grown in limiting spermidine Proc. Natl. Acad. Sci. U. S. A. 105 2008 6554 6559
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 6554-6559
    • Chattopadhyay, M.K.1    Park, M.H.2    Tabor, H.3
  • 172
    • 0345133303 scopus 로고    scopus 로고
    • Spermidine but not spermine is essential for hypusine biosynthesis and growth in Saccharomyces cerevisiae: Spermine is converted to spermidine in vivo by the FMS1-amine oxidase
    • M.K. Chattopadhyay, C.W. Tabor, and H. Tabor Spermidine but not spermine is essential for hypusine biosynthesis and growth in Saccharomyces cerevisiae: spermine is converted to spermidine in vivo by the FMS1-amine oxidase Proc. Natl. Acad. Sci. U. S. A. 100 2003 13869 13874
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 13869-13874
    • Chattopadhyay, M.K.1    Tabor, C.W.2    Tabor, H.3
  • 173
    • 67649607136 scopus 로고    scopus 로고
    • The Drosophila deoxyhypusine hydroxylase homologue nero and its target eIF5A are required for cell growth and the regulation of autophagy
    • P.H. Patel, M. Costa-Mattioli, K.L. Schulze, and H.J. Bellen The Drosophila deoxyhypusine hydroxylase homologue nero and its target eIF5A are required for cell growth and the regulation of autophagy J. Cell Biol. 185 2009 1181 1194
    • (2009) J. Cell Biol. , vol.185 , pp. 1181-1194
    • Patel, P.H.1    Costa-Mattioli, M.2    Schulze, K.L.3    Bellen, H.J.4
  • 174
    • 0035128859 scopus 로고    scopus 로고
    • Large-scale analysis of gene function in Caenorhabditis elegans by high-throughput RNAi
    • I. Maeda, Y. Kohara, M. Yamamoto, and A. Sugimoto Large-scale analysis of gene function in Caenorhabditis elegans by high-throughput RNAi Curr. Biol. 11 2001 171 176
    • (2001) Curr. Biol. , vol.11 , pp. 171-176
    • Maeda, I.1    Kohara, Y.2    Yamamoto, M.3    Sugimoto, A.4
  • 175
    • 84905816669 scopus 로고    scopus 로고
    • A novel mouse model for inhibition of DOHH-mediated hypusine modification reveals a crucial function in embryonic development, proliferation and oncogenic transformation
    • H. Sievert, N. Pällmann, K.K. Miller, I. Hermans-Borgmeyer, S. Venz, A. Sendoel, and et al. A novel mouse model for inhibition of DOHH-mediated hypusine modification reveals a crucial function in embryonic development, proliferation and oncogenic transformation Dis. Model. Mech. 7 2014 963 976
    • (2014) Dis. Model. Mech. , vol.7 , pp. 963-976
    • Sievert, H.1    Pällmann, N.2    Miller, K.K.3    Hermans-Borgmeyer, I.4    Venz, S.5    Sendoel, A.6
  • 176
    • 84861197887 scopus 로고    scopus 로고
    • Essential role of eIF5A-1 and deoxyhypusine synthase in mouse embryonic development
    • K. Nishimura, S.B. Lee, J.H. Park, and M.H. Park Essential role of eIF5A-1 and deoxyhypusine synthase in mouse embryonic development Amino Acids 42 2012 703 710
    • (2012) Amino Acids , vol.42 , pp. 703-710
    • Nishimura, K.1    Lee, S.B.2    Park, J.H.3    Park, M.H.4
  • 177
  • 178
    • 0032007505 scopus 로고    scopus 로고
    • Osmotic stress induces variation in cellular levels of ornithine decarboxylase-antizyme
    • J.L. Mitchell, G.G. Judd, A. Leyser, and C. Choe Osmotic stress induces variation in cellular levels of ornithine decarboxylase-antizyme Biochem. J. 329 1998 453 459
    • (1998) Biochem. J. , vol.329 , pp. 453-459
    • Mitchell, J.L.1    Judd, G.G.2    Leyser, A.3    Choe, C.4
  • 179
    • 0030221359 scopus 로고    scopus 로고
    • Regulation of Arabidopsis thaliana (L.) Heynh Arginine decarboxylase by potassium deficiency stress
    • M.B. Watson, and R.L. Malmberg Regulation of Arabidopsis thaliana (L.) Heynh Arginine decarboxylase by potassium deficiency stress Plant Physiol. 111 1996 1077 1083
    • (1996) Plant Physiol. , vol.111 , pp. 1077-1083
    • Watson, M.B.1    Malmberg, R.L.2
  • 180
    • 19544393714 scopus 로고    scopus 로고
    • Effect of salt and osmotic stress on changes in polyamine content and arginine decarboxylase activity in Lupinus luteus seedlings
    • J. Legocka, and A. Kluk Effect of salt and osmotic stress on changes in polyamine content and arginine decarboxylase activity in Lupinus luteus seedlings J. Plant Physiol. 162 2005 662 668
    • (2005) J. Plant Physiol. , vol.162 , pp. 662-668
    • Legocka, J.1    Kluk, A.2
  • 181
    • 0030499122 scopus 로고    scopus 로고
    • Regulation of arginine decarboxylase by spermine in osmotically stressed oat leaves
    • A. Borrell, R.T. Besford, T. Altabella, C. Masgrau, and A.F. Tiburcio Regulation of arginine decarboxylase by spermine in osmotically stressed oat leaves Physiol. Plant. 98 1996 105 110
    • (1996) Physiol. Plant. , vol.98 , pp. 105-110
    • Borrell, A.1    Besford, R.T.2    Altabella, T.3    Masgrau, C.4    Tiburcio, A.F.5
  • 182
    • 0028101319 scopus 로고
    • Arginine decarboxylase of oats is activated by enzymatic cleavage into two polypeptides
    • R.L. Malmberg, and M.L. Cellino Arginine decarboxylase of oats is activated by enzymatic cleavage into two polypeptides J. Biol. Chem. 269 1994 2703 2706
    • (1994) J. Biol. Chem. , vol.269 , pp. 2703-2706
    • Malmberg, R.L.1    Cellino, M.L.2
  • 184
    • 4344564153 scopus 로고    scopus 로고
    • Hydroxyl radical scavenging and singlet oxygen quenching properties of polyamines
    • K.C. Das, and H.P. Misra Hydroxyl radical scavenging and singlet oxygen quenching properties of polyamines Mol. Cell. Biochem. 262 2004 127 133
    • (2004) Mol. Cell. Biochem. , vol.262 , pp. 127-133
    • Das, K.C.1    Misra, H.P.2
  • 185
    • 17444381592 scopus 로고    scopus 로고
    • Kinetic evaluation of polyamines as radical scavengers
    • S. Fujisawa, and Y. Kadoma Kinetic evaluation of polyamines as radical scavengers Anticancer Res. 25 2005 965 969
    • (2005) Anticancer Res. , vol.25 , pp. 965-969
    • Fujisawa, S.1    Kadoma, Y.2
  • 186
    • 33749251817 scopus 로고    scopus 로고
    • Free radical scavenging action of the natural polyamine spermine in rat liver mitochondria
    • I.G. Sava, V. Battaglia, C.A. Rossi, M. Salvi, and A. Toninello Free radical scavenging action of the natural polyamine spermine in rat liver mitochondria Free Radic. Biol. Med. 41 2006 1272 1281
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 1272-1281
    • Sava, I.G.1    Battaglia, V.2    Rossi, C.A.3    Salvi, M.4    Toninello, A.5
  • 187
    • 34547702823 scopus 로고    scopus 로고
    • Spermine and spermidine mediate protection against oxidative damage caused by hydrogen peroxide
    • J.E. Rider, A. Hacker, C.A. Mackintosh, A.E. Pegg, P.M. Woster, and R.A. Casero Spermine and spermidine mediate protection against oxidative damage caused by hydrogen peroxide Amino Acids 33 2007 231 240
    • (2007) Amino Acids , vol.33 , pp. 231-240
    • Rider, J.E.1    Hacker, A.2    Mackintosh, C.A.3    Pegg, A.E.4    Woster, P.M.5    Casero, R.A.6
  • 188
    • 33845475232 scopus 로고    scopus 로고
    • The polyamine spermine protects against high salt stress in Arabidopsis thaliana
    • K. Yamaguchi, Y. Takahashi, T. Berberich, A. Imai, A. Miyazaki, T. Takahashi, and et al. The polyamine spermine protects against high salt stress in Arabidopsis thaliana FEBS Lett. 580 2006 6783 6788
    • (2006) FEBS Lett. , vol.580 , pp. 6783-6788
    • Yamaguchi, K.1    Takahashi, Y.2    Berberich, T.3    Imai, A.4    Miyazaki, A.5    Takahashi, T.6
  • 189
    • 0030839791 scopus 로고    scopus 로고
    • Complex inhibition of OmpF and OmpC bacterial porins by polyamines
    • R. Iyer, and A.H. Delcour Complex inhibition of OmpF and OmpC bacterial porins by polyamines J. Biol. Chem. 272 1997 18595 18601
    • (1997) J. Biol. Chem. , vol.272 , pp. 18595-18601
    • Iyer, R.1    Delcour, A.H.2
  • 190
    • 8944248272 scopus 로고    scopus 로고
    • Polyamines decrease Escherichia coli outer membrane permeability
    • A.L. Dela Vega, and A.H. Delcour Polyamines decrease Escherichia coli outer membrane permeability J. Bacteriol. 178 1996 3715 3721
    • (1996) J. Bacteriol. , vol.178 , pp. 3715-3721
    • Dela Vega, A.L.1    Delcour, A.H.2
  • 191
    • 84889078549 scopus 로고    scopus 로고
    • Tpo1-mediated spermine and spermidine export controls cell cycle delay and times antioxidant protein expression during the oxidative stress response
    • A. Krüger, J. Vowinckel, M. Mülleder, P. Grote, F. Capuano, K. Bluemlein, and et al. Tpo1-mediated spermine and spermidine export controls cell cycle delay and times antioxidant protein expression during the oxidative stress response EMBO Rep. 14 2013 1113 1119
    • (2013) EMBO Rep. , vol.14 , pp. 1113-1119
    • Krüger, A.1    Vowinckel, J.2    Mülleder, M.3    Grote, P.4    Capuano, F.5    Bluemlein, K.6
  • 192
    • 0242335090 scopus 로고    scopus 로고
    • Polyamines as modulators of gene expression under oxidative stress in Escherichia coli
    • A.G. Tkachenko, and L.Y. Nesterova Polyamines as modulators of gene expression under oxidative stress in Escherichia coli Biochem 68 2003 850 856
    • (2003) Biochem , vol.68 , pp. 850-856
    • Tkachenko, A.G.1    Nesterova, L.Y.2
  • 194
    • 84877774231 scopus 로고    scopus 로고
    • The polyamine spermine protects Arabidopsis from heat stress-induced damage by increasing expression of heat shock-related genes
    • G.H.M. Sagor, T. Berberich, Y. Takahashi, M. Niitsu, and T. Kusano The polyamine spermine protects Arabidopsis from heat stress-induced damage by increasing expression of heat shock-related genes Transgenic Res. 22 2013 595 605
    • (2013) Transgenic Res. , vol.22 , pp. 595-605
    • Sagor, G.H.M.1    Berberich, T.2    Takahashi, Y.3    Niitsu, M.4    Kusano, T.5
  • 195
    • 84863437568 scopus 로고    scopus 로고
    • Spermidine affects the transcriptome responses to high temperature stress in ripening tomato fruit
    • L. Cheng, R. Sun, F. Wang, Z. Peng, F. Kong, J. Wu, and et al. Spermidine affects the transcriptome responses to high temperature stress in ripening tomato fruit J. Zhejiang Univ. Sci. B 13 2012 283 297
    • (2012) J. Zhejiang Univ. Sci. B , vol.13 , pp. 283-297
    • Cheng, L.1    Sun, R.2    Wang, F.3    Peng, Z.4    Kong, F.5    Wu, J.6
  • 196
    • 82355169406 scopus 로고    scopus 로고
    • Interactions between polyamines and abiotic stress pathway responses unraveled by transcriptome analysis of polyamine overproducers
    • F. Marco, R. Alcázar, A.F. Tiburcio, and P. Carrasco Interactions between polyamines and abiotic stress pathway responses unraveled by transcriptome analysis of polyamine overproducers OMICS 15 2011 775 781
    • (2011) OMICS , vol.15 , pp. 775-781
    • Marco, F.1    Alcázar, R.2    Tiburcio, A.F.3    Carrasco, P.4
  • 197
    • 84864600170 scopus 로고    scopus 로고
    • Regulators of oxidative stress response genes in Escherichia coli and their functional conservation in bacteria
    • S.M. Chiang, and H.E. Schellhorn Regulators of oxidative stress response genes in Escherichia coli and their functional conservation in bacteria Arch. Biochem. Biophys. 525 2012 161 169
    • (2012) Arch. Biochem. Biophys. , vol.525 , pp. 161-169
    • Chiang, S.M.1    Schellhorn, H.E.2
  • 198
    • 38149120434 scopus 로고    scopus 로고
    • Polyamines and abiotic stress: Recent advances
    • M.D.B.M. Groppa Polyamines and abiotic stress: recent advances Amino Acids 34 2008 35 45
    • (2008) Amino Acids , vol.34 , pp. 35-45
    • Groppa, M.D.B.M.1
  • 199
    • 0033763135 scopus 로고    scopus 로고
    • Polyamine transport and role of potE in response to osmotic stress in Escherichia coli
    • D. Schiller, D. Kruse, H. Kneifel, R. Kramer, and A. Burkovski Polyamine transport and role of potE in response to osmotic stress in Escherichia coli J. Bacteriol. 182 2000 6247 6249
    • (2000) J. Bacteriol. , vol.182 , pp. 6247-6249
    • Schiller, D.1    Kruse, D.2    Kneifel, H.3    Kramer, R.4    Burkovski, A.5
  • 201
    • 36249019325 scopus 로고    scopus 로고
    • + homeostasis in barley seedlings by regulating root ion channel activities
    • + homeostasis in barley seedlings by regulating root ion channel activities Plant Physiol. 145 2007 1061 1072
    • (2007) Plant Physiol. , vol.145 , pp. 1061-1072
    • Zhao, F.1    Song, C.-P.2    He, J.3    Zhu, H.4
  • 202
  • 203
    • 0026542813 scopus 로고
    • Identification of elements involved in transcriptional regulation of the Escherichia coli cad operon by external pH
    • N. Watson, D.S. Dunyak, E.L. Rosey, J.L. Slonczewski, and E.R. Olson Identification of elements involved in transcriptional regulation of the Escherichia coli cad operon by external pH J. Bacteriol. 174 1992 530 540
    • (1992) J. Bacteriol. , vol.174 , pp. 530-540
    • Watson, N.1    Dunyak, D.S.2    Rosey, E.L.3    Slonczewski, J.L.4    Olson, E.R.5
  • 204
  • 205
    • 0014323475 scopus 로고
    • Amine synthesis in rapidly growing tissues: Ornithine decarboxylase activity in regenerating rat liver, chick embryo, and various tumors
    • D. Russell, and S.H. Snyder Amine synthesis in rapidly growing tissues: ornithine decarboxylase activity in regenerating rat liver, chick embryo, and various tumors Proc. Natl. Acad. Sci. U. S. A. 60 1968 1420 1427
    • (1968) Proc. Natl. Acad. Sci. U. S. A. , vol.60 , pp. 1420-1427
    • Russell, D.1    Snyder, S.H.2
  • 206
    • 0017324934 scopus 로고
    • Polyamines as markers of response and disease activity in cancer chemotherapy
    • B.G. Durie, S.E. Salmon, and D.H. Russell Polyamines as markers of response and disease activity in cancer chemotherapy Cancer Res. 37 1977 214 221
    • (1977) Cancer Res. , vol.37 , pp. 214-221
    • Durie, B.G.1    Salmon, S.E.2    Russell, D.H.3
  • 207
    • 0015244583 scopus 로고
    • Increased polyamine concentrations in the urine of human cancer patients
    • D.H. RUSSELL Increased polyamine concentrations in the urine of human cancer patients Nature 233 1971 144 145
    • (1971) Nature , vol.233 , pp. 144-145
    • Russell, D.H.1
  • 208
    • 77649208537 scopus 로고    scopus 로고
    • Targeting ornithine decarboxylase for the prevention of nonmelanoma skin cancer in humans
    • C.A. Elmets, and M. Athar Targeting ornithine decarboxylase for the prevention of nonmelanoma skin cancer in humans Cancer Prev. Res. (Phila.) 3 2010 8 11
    • (2010) Cancer Prev. Res. (Phila.) , vol.3 , pp. 8-11
    • Elmets, C.A.1    Athar, M.2
  • 210
    • 0027263467 scopus 로고
    • Transformation of NIH/3T3 cells by ornithine decarboxylase overexpression
    • J.A. Moshier, J. Dosescu, M. Skunca, and G.D. Luk Transformation of NIH/3T3 cells by ornithine decarboxylase overexpression Cancer Res. 53 1993 2618 2622
    • (1993) Cancer Res. , vol.53 , pp. 2618-2622
    • Moshier, J.A.1    Dosescu, J.2    Skunca, M.3    Luk, G.D.4
  • 211
    • 0028790834 scopus 로고
    • Ornithine decarboxylase- and ras-induced cell transformations: Reversal by protein tyrosine kinase inhibitors and role of pp130CAS
    • M. Auvinen, A. Paasinen-Sohns, H. Hirai, L.C. Andersson, and E. Hölttä Ornithine decarboxylase- and ras-induced cell transformations: reversal by protein tyrosine kinase inhibitors and role of pp130CAS Mol. Cell. Biol. 15 1995 6513 6525
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6513-6525
    • Auvinen, M.1    Paasinen-Sohns, A.2    Hirai, H.3    Andersson, L.C.4    Hölttä, E.5
  • 212
    • 0030834335 scopus 로고    scopus 로고
    • Human ornithine decarboxylase-overproducing NIH3T3 cells induce rapidly growing, highly vascularized tumors in nude mice
    • M. Auvinen, A. Laine, A. Paasinen-Sohns, A. Kangas, L. Kangas, O. Saksela, and et al. Human ornithine decarboxylase-overproducing NIH3T3 cells induce rapidly growing, highly vascularized tumors in nude mice Cancer Res. 57 1997 3016 3025
    • (1997) Cancer Res. , vol.57 , pp. 3016-3025
    • Auvinen, M.1    Laine, A.2    Paasinen-Sohns, A.3    Kangas, A.4    Kangas, L.5    Saksela, O.6
  • 213
    • 0037934362 scopus 로고    scopus 로고
    • Pronounced reduction in adenoma recurrence associated with aspirin use and a polymorphism in the ornithine decarboxylase gene
    • M.E. Martinez, T.G. O'Brien, K.E. Fultz, N. Babbar, H. Yerushalmi, N. Qu, and et al. Pronounced reduction in adenoma recurrence associated with aspirin use and a polymorphism in the ornithine decarboxylase gene Proc. Natl. Acad. Sci. U. S. A. 100 2003 7859 7864
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 7859-7864
    • Martinez, M.E.1    O'Brien, T.G.2    Fultz, K.E.3    Babbar, N.4    Yerushalmi, H.5    Qu, N.6
  • 214
    • 0029050287 scopus 로고
    • Increased frequency of spontaneous skin tumors in transgenic mice which overexpress ornithine decarboxylase
    • L. Megosh, S.K. Gilmour, D. Rosson, A.P. Soler, M. Blessing, J.A. Sawicki, and et al. Increased frequency of spontaneous skin tumors in transgenic mice which overexpress ornithine decarboxylase Cancer Res. 55 1995 4205 4209
    • (1995) Cancer Res. , vol.55 , pp. 4205-4209
    • Megosh, L.1    Gilmour, S.K.2    Rosson, D.3    Soler, A.P.4    Blessing, M.5    Sawicki, J.A.6
  • 215
    • 13944284497 scopus 로고    scopus 로고
    • Haploinsufficiency for ODC modifies mouse skin tumor susceptibility
    • Y. Guo, J.L. Cleveland, and T.G. O'Brien Haploinsufficiency for ODC modifies mouse skin tumor susceptibility Cancer Res. 65 2005 1146 1149
    • (2005) Cancer Res. , vol.65 , pp. 1146-1149
    • Guo, Y.1    Cleveland, J.L.2    O'Brien, T.G.3
  • 216
    • 21144448938 scopus 로고    scopus 로고
    • Targeting ornithine decarboxylase in Myc-induced lymphomagenesis prevents tumor formation
    • J.A. Nilsson, U.B. Keller, T.A. Baudino, C. Yang, S. Norton, J.A. Old, and et al. Targeting ornithine decarboxylase in Myc-induced lymphomagenesis prevents tumor formation Cancer Cell 7 2005 433 444
    • (2005) Cancer Cell , vol.7 , pp. 433-444
    • Nilsson, J.A.1    Keller, U.B.2    Baudino, T.A.3    Yang, C.4    Norton, S.5    Old, J.A.6
  • 217
    • 80054859726 scopus 로고    scopus 로고
    • Spermine oxidase mediates the gastric cancer risk associated with Helicobacter pylori CagA
    • R. Chaturvedi, M. Asim, J. Romero-Gallo, D.P. Barry, S. Hoge, T. de Sablet, and et al. Spermine oxidase mediates the gastric cancer risk associated with Helicobacter pylori CagA Gastroenterology 141 2011 1696 1708
    • (2011) Gastroenterology , vol.141 , pp. 1696-1708
    • Chaturvedi, R.1    Asim, M.2    Romero-Gallo, J.3    Barry, D.P.4    Hoge, S.5    De Sablet, T.6
  • 218
    • 77956271268 scopus 로고    scopus 로고
    • Increased expression and cellular localization of spermine oxidase in ulcerative colitis and relationship to disease activity
    • S.-K.S. Hong, R. Chaturvedi, M.B. Piazuelo, L.A. Coburn, C.S. Williams, A.G. Delgado, and et al. Increased expression and cellular localization of spermine oxidase in ulcerative colitis and relationship to disease activity Inflamm. Bowel Dis. 16 2010 1557 1566
    • (2010) Inflamm. Bowel Dis. , vol.16 , pp. 1557-1566
    • Hong, S.-K.S.1    Chaturvedi, R.2    Piazuelo, M.B.3    Coburn, L.A.4    Williams, C.S.5    Delgado, A.G.6
  • 219
    • 0035881620 scopus 로고    scopus 로고
    • Targeted antizyme expression in the skin of transgenic mice reduces tumor promoter induction of ornithine decarboxylase and decreases sensitivity to chemical carcinogenesis
    • D.J. Feith, L.M. Shantz, and A.E. Pegg Targeted antizyme expression in the skin of transgenic mice reduces tumor promoter induction of ornithine decarboxylase and decreases sensitivity to chemical carcinogenesis Cancer Res. 61 2001 6073 6081
    • (2001) Cancer Res. , vol.61 , pp. 6073-6081
    • Feith, D.J.1    Shantz, L.M.2    Pegg, A.E.3
  • 220
    • 0000382583 scopus 로고
    • Alpha-Difluoromethylornithine, an irreversible inhibitor of ornithine decarboxylase, inhibits tumor promoter-induced polyamine accumulation and carcinogenesis in mouse skin
    • C.E. Weeks, A.L. Herrmann, F.R. Nelson, and T.J. Slaga alpha-Difluoromethylornithine, an irreversible inhibitor of ornithine decarboxylase, inhibits tumor promoter-induced polyamine accumulation and carcinogenesis in mouse skin Proc. Natl. Acad. Sci. U. S. A. 79 1982 6028 6032
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 6028-6032
    • Weeks, C.E.1    Herrmann, A.L.2    Nelson, F.R.3    Slaga, T.J.4
  • 221
    • 0022910889 scopus 로고
    • Inhibition of intestinal carcinogenesis in rats: Effect of difluoromethylornithine with piroxicam or fish oil
    • N.D. Nigro, A.W. Bull, and M.E. Boyd Inhibition of intestinal carcinogenesis in rats: effect of difluoromethylornithine with piroxicam or fish oil J. Natl. Cancer Inst. 77 1986 1309 1313
    • (1986) J. Natl. Cancer Inst. , vol.77 , pp. 1309-1313
    • Nigro, N.D.1    Bull, A.W.2    Boyd, M.E.3
  • 222
    • 0026660462 scopus 로고
    • Efficacy and toxicity of eflornithine for treatment of Trypanosoma brucei gambiense sleeping sickness
    • F. Milord, J. Pépin, L. Loko, L. Ethier, and B. Mpia Efficacy and toxicity of eflornithine for treatment of Trypanosoma brucei gambiense sleeping sickness Lancet 340 1992 652 655
    • (1992) Lancet , vol.340 , pp. 652-655
    • Milord, F.1    Pépin, J.2    Loko, L.3    Ethier, L.4    Mpia, B.5
  • 223
    • 84880515627 scopus 로고    scopus 로고
    • Polyamines and cancer: Implications for chemotherapy and chemoprevention
    • S.L. Nowotarski, P.M. Woster, and R.A. Casero Polyamines and cancer: implications for chemotherapy and chemoprevention Expert Rev. Mol. Med. 15 2013 e3
    • (2013) Expert Rev. Mol. Med. , vol.15 , pp. e3
    • Nowotarski, S.L.1    Woster, P.M.2    Casero, R.A.3
  • 224
    • 4944242891 scopus 로고    scopus 로고
    • Polyamines and cancer: Old molecules, new understanding
    • E.W. Gerner, and F.L. Meyskens Polyamines and cancer: old molecules, new understanding Nat. Rev. Cancer 4 2004 781 792
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 781-792
    • Gerner, E.W.1    Meyskens, F.L.2
  • 226
    • 0035907144 scopus 로고    scopus 로고
    • Polyamines in the basal ganglia of human brain. Influence of aging and degenerative movement disorders
    • M. Vivó, N. de Vera, R. Cortés, G. Mengod, L. Camón, and E. Martínez Polyamines in the basal ganglia of human brain. Influence of aging and degenerative movement disorders Neurosci. Lett. 304 2001 107 111
    • (2001) Neurosci. Lett. , vol.304 , pp. 107-111
    • Vivó, M.1    De Vera, N.2    Cortés, R.3    Mengod, G.4    Camón, L.5    Martínez, E.6
  • 227
    • 84884878909 scopus 로고    scopus 로고
    • Restoring polyamines protects from age-induced memory impairment in an autophagy-dependent manner
    • V.K. Gupta, L. Scheunemann, T. Eisenberg, S. Mertel, A. Bhukel, T.S. Koemans, and et al. Restoring polyamines protects from age-induced memory impairment in an autophagy-dependent manner Nat. Neurosci. 16 2013 1453 1460
    • (2013) Nat. Neurosci. , vol.16 , pp. 1453-1460
    • Gupta, V.K.1    Scheunemann, L.2    Eisenberg, T.3    Mertel, S.4    Bhukel, A.5    Koemans, T.S.6
  • 229
    • 84886066926 scopus 로고    scopus 로고
    • Serum metabolomics of slow vs. Rapid motor progression Parkinson's disease: A pilot study
    • J.R. Roede, K. Uppal, Y. Park, K. Lee, V. Tran, D. Walker, and et al. Serum metabolomics of slow vs. rapid motor progression Parkinson's disease: a pilot study PLoS One 8 2013 e77629
    • (2013) PLoS One , vol.8 , pp. e77629
    • Roede, J.R.1    Uppal, K.2    Park, Y.3    Lee, K.4    Tran, V.5    Walker, D.6
  • 230
    • 0036434881 scopus 로고    scopus 로고
    • Increased red blood cell polyamines in ALS and Parkinson's disease
    • C. Gomes-Trolin, I. Nygren, S.-M. Aquilonius, and H. Askmark Increased red blood cell polyamines in ALS and Parkinson's disease Exp. Neurol. 177 2002 515 520
    • (2002) Exp. Neurol. , vol.177 , pp. 515-520
    • Gomes-Trolin, C.1    Nygren, I.2    Aquilonius, S.-M.3    Askmark, H.4
  • 233
    • 84875502892 scopus 로고    scopus 로고
    • Cellular polyamines promote amyloid-beta (Aβ) peptide fibrillation and modulate the aggregation pathways
    • J. Luo, C.-H. Yu, H. Yu, R. Borstnar, S.C.L. Kamerlin, A. Gräslund, and et al. Cellular polyamines promote amyloid-beta (Aβ) peptide fibrillation and modulate the aggregation pathways ACS Chem. Neurosci. 4 2013 454 462
    • (2013) ACS Chem. Neurosci. , vol.4 , pp. 454-462
    • Luo, J.1    Yu, C.-H.2    Yu, H.3    Borstnar, R.4    Kamerlin, S.C.L.5    Gräslund, A.6
  • 235
    • 84868151117 scopus 로고    scopus 로고
    • Histaminylation of glutamine residues is a novel posttranslational modification implicated in G-protein signaling
    • J. Vowinckel, S. Stahlberg, N. Paulmann, K. Bluemlein, M. Grohmann, M. Ralser, and et al. Histaminylation of glutamine residues is a novel posttranslational modification implicated in G-protein signaling FEBS Lett. 586 2012 3819 3824
    • (2012) FEBS Lett. , vol.586 , pp. 3819-3824
    • Vowinckel, J.1    Stahlberg, S.2    Paulmann, N.3    Bluemlein, K.4    Grohmann, M.5    Ralser, M.6
  • 237
    • 84876089948 scopus 로고    scopus 로고
    • Transglutaminase and polyamination of tubulin: Posttranslational modification for stabilizing axonal microtubules
    • Y. Song, L.L. Kirkpatrick, A.B. Schilling, D.L. Helseth, N. Chabot, J.W. Keillor, and et al. Transglutaminase and polyamination of tubulin: posttranslational modification for stabilizing axonal microtubules Neuron 78 2013 109 123
    • (2013) Neuron , vol.78 , pp. 109-123
    • Song, Y.1    Kirkpatrick, L.L.2    Schilling, A.B.3    Helseth, D.L.4    Chabot, N.5    Keillor, J.W.6
  • 238
    • 84871960505 scopus 로고    scopus 로고
    • γ-Glutamylamines and neurodegenerative diseases
    • T.M. Jeitner, K. Battaile, and A.J.L. Cooper γ-Glutamylamines and neurodegenerative diseases Amino Acids 44 2013 129 142
    • (2013) Amino Acids , vol.44 , pp. 129-142
    • Jeitner, T.M.1    Battaile, K.2    Cooper, A.J.L.3
  • 240
    • 79953286790 scopus 로고    scopus 로고
    • Possible role of the transglutaminases in the pathogenesis of Alzheimer's disease and other neurodegenerative diseases
    • A. Martin, G. De Vivo, and V. Gentile Possible role of the transglutaminases in the pathogenesis of Alzheimer's disease and other neurodegenerative diseases Int. J. Alzheimers Dis. 2011 2011 865432
    • (2011) Int. J. Alzheimers Dis. , vol.2011 , pp. 865432
    • Martin, A.1    De Vivo, G.2    Gentile, V.3
  • 242
    • 84890459089 scopus 로고    scopus 로고
    • Toxicity of polyamines and their metabolic products
    • A.E. Pegg Toxicity of polyamines and their metabolic products Chem. Res. Toxicol. 26 2013 1782 1800
    • (2013) Chem. Res. Toxicol. , vol.26 , pp. 1782-1800
    • Pegg, A.E.1
  • 243
    • 33947689120 scopus 로고    scopus 로고
    • The concept of "aldehyde load" in neurodegenerative mechanisms: Cytotoxicity of the polyamine degradation products hydrogen peroxide, acrolein, 3-aminopropanal, 3-acetamidopropanal and 4-aminobutanal in a retinal ganglion cell line
    • P.L. Wood, M.A. Khan, and J.R. Moskal The concept of "aldehyde load" in neurodegenerative mechanisms: cytotoxicity of the polyamine degradation products hydrogen peroxide, acrolein, 3-aminopropanal, 3-acetamidopropanal and 4-aminobutanal in a retinal ganglion cell line Brain Res. 1145 2007 150 156
    • (2007) Brain Res. , vol.1145 , pp. 150-156
    • Wood, P.L.1    Khan, M.A.2    Moskal, J.R.3
  • 244
    • 84905257556 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in neurodegenerative diseases: Precipitating factor, yet part of the solution
    • N.P. Dantuma, and L.C. Bott The ubiquitin-proteasome system in neurodegenerative diseases: precipitating factor, yet part of the solution Front. Mol. Neurosci. 7 2014 70
    • (2014) Front. Mol. Neurosci. , vol.7 , pp. 70
    • Dantuma, N.P.1    Bott, L.C.2


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