Remaining mysteries of molecular biology: the role of polyamines in the cell

Induction of autophagy by spermidine promotes longevity

Eisenberg, T., Knauer, H., Schauer, A., Büttner, S., Ruckenstuhl, C., Carmona-Gutierrez, D., Ring, J., Schroeder, S., Magnes, C., Antonacci, L., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1975 · Cited by 1,680 · see citing works

Polyamine metabolism and its importance in neoplastic growth and a target for chemotherapy.

Pegg, A. E. (1988) · PubMed · Cited by 1,522 · see citing works

Polyamines and cancer: old molecules, new understanding

Gerner, E. W., & Meyskens, F. L. (2004) · Nature reviews. Cancer · doi:10.1038/nrc1454 · Cited by 1,163 · see citing works

Polyamines: essential factors for growth and survival

Kusano, T., Berberich, T., Tateda, C., & Takahashi, Y. (2008) · Planta · doi:10.1007/s00425-008-0772-7 · Cited by 896 · see citing works

Modulation of cellular function by polyamines

Igarashi, K., & Kashiwagi, K. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.07.009 · Cited by 852 · see citing works

Polyamines and abiotic stress: recent advances

Groppa, M. D., & Benavides, M. P. (2007) · Amino Acids · doi:10.1007/s00726-007-0501-8 · Cited by 788 · see citing works

Mammalian polyamine metabolism and function

Pegg, A. E. (2009) · IUBMB Life · doi:10.1002/iub.230 · Cited by 786 · see citing works

Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination

Murakami, Y., Matsufuji, S., Kameji, T., Hayashi, S., Igarashi, K., Tamura, T., Tanaka, K., & Ichihara, A. (1992) · Nature · doi:10.1038/360597a0 · Cited by 783 · see citing works

The ornithine decarboxylase gene is a transcriptional target of c-Myc.

Bello-Fernández, C., Packham, G., & Cleveland, J. L. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.16.7804 · Cited by 783 · see citing works

Amine synthesis in rapidly growing tissues: ornithine decarboxylase activity in regenerating rat liver, chick embryo, and various tumors.

Russell, D., & Snyder, S. H. (1968) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.60.4.1420 · Cited by 747 · see citing works

Large-scale analysis of gene function in Caenorhabditis elegans by high-throughput RNAi

Maeda, I., Kohara, Y., Yamamoto, M., et al. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00052-5 · Cited by 698 · see citing works

The natural polyamine spermine functions directly as a free radical scavenger

Ha, H. C., Sirisoma, N. S., Kuppusamy, P., Zweier, J. L., Woster, P. M., & Casero, R. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.19.11140 · Cited by 676 · see citing works

SPERMIDINE, SPERMINE, AND RELATED AMINES

Tabor, H., & Tabor, C. W. (1964) · Pharmacological Reviews · doi:10.1016/s0031-6997(25)07047-4 · Cited by 552 · see citing works

Improved method for chick whole-embryo culture using a filter paper carrier

Chapman, S. C., Collignon, J., Schoenwolf, G. C., & Lumsden, A. (2001) · Developmental Dynamics · doi:10.1002/1097-0177(20010301)220:3 · Cited by 482 · see citing works

Regulation of Ornithine Decarboxylase

Pegg, A. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.r500031200 · Cited by 477 · see citing works

A multifaceted role for polyamines in bacterial pathogens

Shah, P., & Swiatlo, E. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06126.x · Cited by 423 · see citing works

Polyamine-dependent gene expression

Childs, A. C., Mehta, D. J., & Gerner, E. W. (2003) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-003-2332-4 · Cited by 416 · see citing works

Amine Synthesis in Regenerating Rat Liver: Extremely Rapid Turnover of Ornithine Decarboxylase

Russell, D. H., & Snyder, S. H. (1969) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)14666-x · Cited by 385 · see citing works

Regulators of oxidative stress response genes in Escherichia coli and their functional conservation in bacteria

Chiang, S. M., & Schellhorn, H. E. (2012) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2012.02.007 · Cited by 381 · see citing works

Restoring polyamines protects from age-induced memory impairment in an autophagy-dependent manner

Gupta, V., Scheunemann, L., Eisenberg, T., Mertel, S., Bhukel, A., Koemans, T. S., Kramer, J. M., Liu, K. S. Y., Schroeder, S., Stunnenberg, H. G., et al. (2013) · Nature Neuroscience · doi:10.1038/nn.3512 · Cited by 370 · see citing works

Induction of a protein inhibitor to ornithine decarboxylase by the end products of its reaction.

Heller, J. S., Fong, W. F., & Canellakis, E. S. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.6.1858 · Cited by 369 · see citing works

Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae.

Schnier, J. B., Schwelberger, H. G., Smit‐McBride, Z., et al. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.6.3105 · Cited by 357 · see citing works

Functional significance of eIF5A and its hypusine modification in eukaryotes

Park, M. H., Nishimura, K., Zanelli, C. F., et al. (2009) · Amino Acids · doi:10.1007/s00726-009-0408-7 · Cited by 352 · see citing works

Spermidine/spermine- N 1 -acetyltransferase: a key metabolic regulator

Pegg, A. E. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90217.2008 · Cited by 351 · see citing works

The ubiquitin-proteasome system in neurodegenerative diseases: precipitating factor, yet part of the solution

Dantuma, N. P., & Bott, L. C. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00070 · Cited by 336 · see citing works

A Cell Cycle–Dependent Internal Ribosome Entry Site

Pyronnet, S., Pradayrol, L., & Sonenberg, N. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80240-3 · Cited by 329 · see citing works

Polyamines as physiological substrates for transglutaminases.

Folk, J. E., Park, M. H., Chung, S. I., et al. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85760-5 · Cited by 314 · see citing works

Spermine and spermidine mediate protection against oxidative damage caused by hydrogen peroxide

Rider, J. E., Hacker, A., Mackintosh, C. A., Pegg, A. E., Woster, P. M., & Casero, R. A. (2007) · Amino Acids · doi:10.1007/s00726-007-0513-4 · Cited by 308 · see citing works

Toxicity of Polyamines and Their Metabolic Products

Pegg, A. E. (2013) · Chemical Research in Toxicology · doi:10.1021/tx400316s · Cited by 306 · see citing works

Polyamines and cancer: implications for chemotherapy and chemoprevention

Nowotarski, S. L., Woster, P. M., & Casero, R. A. (2013) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2013.3 · Cited by 306 · see citing works

Arabidopsis polyamine biosynthesis: absence of ornithine decarboxylase and the mechanism of arginine decarboxylase activity

Hanfrey, C. C., Sommer, S., Mayer, M. J., Burtin, D., & Michael, A. J. (2001) · The Plant Journal · doi:10.1046/j.1365-313x.2001.01100.x · Cited by 297 · see citing works

Effect of initiation factor eIF-5A depletion on protein synthesis and proliferation of Saccharomyces cerevisiae.

Kang, H. A., & Hershey, J. W. B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41723-6 · Cited by 294 · see citing works

Increased Polyamine Concentrations in the Urine of Human Cancer Patients

Russell, D. H. (1971) · Nature New Biology · doi:10.1038/newbio233144a0 · Cited by 287 · see citing works

Polyamine transport in bacteria and yeast

Igarashi, K., & Kashiwagi, K. (1999) · Biochemical Journal · doi:10.1042/bj3440633 · Cited by 262 · see citing works

Functions of polyamine acetylation

Seiler, N. (1987) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y87-317 · Cited by 256 · see citing works

Ornithine Decarboxylase as a Biologic Marker in Familial Colonic Polyposis

Luk, G. D., & Baylin, S. B. (1984) · New England Journal of Medicine · doi:10.1056/nejm198407123110202 · Cited by 254 · see citing works

Physiological polyamines: simple primordial stress molecules

Rhee, H. J., Kim, E., & Lee, J. K. (2007) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2007.00077.x · Cited by 249 · see citing works

Ubiquitin-independent proteasomal degradation

Erales, J., & Coffino, P. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.05.008 · Cited by 243 · see citing works

The polyamine spermine protects against high salt stress in Arabidopsis thaliana

Yamaguchi, K., Takahashi, Y., Berberich, T., Imai, A., Miyazaki, A., Takahashi, T., Michael, A., & Kusano, T. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.10.078 · Cited by 234 · see citing works

Hypusine: its post-translational formation in eukaryotic initiation factor 5A and its potential role in cellular regulation.

Park, M. H., Wolff, E. C., & Folk, J. E. (1993) · PubMed · Cited by 225 · see citing works

Transformation of NIH/3T3 cells by ornithine decarboxylase overexpression.

Moshier, J. A., Dosescu, J., Skunca, M., et al. (1993) · PubMed · Cited by 220 · see citing works

Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin‐independent substrate

Zhang, M., Pickart, C. M., & Coffino, P. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg158 · Cited by 219 · see citing works

Identification of the hypusine-containing protein hy+ as translation initiation factor eIF-4D.

Cooper, H. L., Park, M. H., Folk, J. E., Safer, B., & Braverman, R. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.7.1854 · Cited by 213 · see citing works

Targeting ornithine decarboxylase in Myc-induced lymphomagenesis prevents tumor formation

Nilsson, J. A., Keller, U. B., Baudino, T. A., Yang, C., Norton, S., Old, J. B., Nilsson, L. M., Neale, G. A. M., Kramer, D. L., Porter, C. W., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.03.036 · Cited by 210 · see citing works

Transglutaminase and Polyamination of Tubulin: Posttranslational Modification for Stabilizing Axonal Microtubules

Song, Y., Kirkpatrick, L., Schilling, A. B., Helseth, D. L., Chabot, N., Keillor, J. W., Johnson, G. V. W., & Brady, S. T. (2013) · Neuron · doi:10.1016/j.neuron.2013.01.036 · Cited by 209 · see citing works

Spermine oxidase mediates the gastric cancer risk associated with Helicobacter pylori CagA

Chaturvedi, R., Asim, M., Romero–Gallo, J., Barry, D. P., Hoge, S., de Sablet, T., Delgado, A. G., Wroblewski, L. E., Piazuelo, M. B., Yan, F., et al. (2011) · Gastroenterology · doi:10.1053/j.gastro.2011.07.045 · Cited by 208 · see citing works

Identification of elements involved in transcriptional regulation of the Escherichia coli cad operon by external pH

Watson, N., Dunyak, D. S., Rosey, E. L., Slonczewski, J. L., & Olson, E. R. (1992) · Journal of Bacteriology · doi:10.1128/jb.174.2.530-540.1992 · Cited by 206 · see citing works

Polyamines as markers of response and disease activity in cancer chemotherapy.

Durie, B. G. M., Salmon, S. E., & Russell, D. H. (1977) · PubMed · Cited by 204 · see citing works

Pronounced reduction in adenoma recurrence associated with aspirin use and a polymorphism in the ornithine decarboxylase gene

Martı́nez, M. E., O’Brien, T. G., Fultz, K. E., Babbar, N., Yerushalmi, H. F., Qu, N., Guo, Y., Boorman, D. W., Einspahr, J. G., Alberts, D. S., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1332465100 · Cited by 196 · see citing works

Selective translation initiation by ribosome jumping in adenovirus-infected and heat-shocked cells.Preprint

Yueh, A., & Schneider, R. J. (1996) · Genes & Development · doi:10.1101/gad.10.12.1557 · Cited by 193 · see citing works

Spermidine: A novel autophagy inducer and longevity elixir

Madeo, F., Eisenberg, T., Büttner, S., Ruckenstuhl, C., & Kroemer, G. (2010) · Autophagy · doi:10.4161/auto.6.1.10600 · Cited by 186 · see citing works

Excretion and uptake of cadaverine by CadB and its physiological functions in Escherichia coli

Soksawatmaekhin, W., Kuraishi, A., Sakata, K., Kashiwagi, K., & Igarashi, K. (2004) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03913.x · Cited by 186 · see citing works

Characteristics of cellular polyamine transport in prokaryotes and eukaryotes

Igarashi, K., & Kashiwagi, K. (2010) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2010.01.017 · Cited by 183 · see citing works

Formation of a compensatory polyamine by Escherichia coli polyamine-requiring mutants during growth in the absence of polyamines

Igarashi, K., Kashiwagi, K., Hamasaki, H., et al. (1986) · Journal of Bacteriology · doi:10.1128/jb.166.1.128-134.1986 · Cited by 179 · see citing works

Polyamine depletion arrests cell cycle and induces inhibitors p21 Waf1/Cip1 , p27 Kip1 , and p53 in IEC-6 cells

Ray, R. M., Zimmerman, B. J., McCormack, S. A., Patel, T. B., & Johnson, L. R. (1999) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1999.276.3.c684 · Cited by 179 · see citing works

X-linked spermine synthase gene (SMS) defect: the first polyamine deficiency syndrome

Cason, A. L., Ikeguchi, Y., Skinner, C. D., Wood, T. C., Holden, K. R., Lubs, H. A., Martı́nez, F., Simensen, R. J., Stevenson, R. E., Pegg, A. E., et al. (2003) · European Journal of Human Genetics · doi:10.1038/sj.ejhg.5201072 · Cited by 176 · see citing works

Developmental expression and biochemical analysis of the Arabidopsis atao1 gene encoding an H 2 O 2 ‐generating diamine oxidase

Møller, S. G., & McPherson, M. J. (1998) · The Plant Journal · doi:10.1046/j.1365-313x.1998.00080.x · Cited by 174 · see citing works

Regulation of Arabidopsis thaliana (L.) Heynh Arginine Decarboxylase by Potassium Deficiency Stress

Watson, M. B., & Malmberg, R. L. (1996) · PLANT PHYSIOLOGY · doi:10.1104/pp.111.4.1077 · Cited by 168 · see citing works

Hydroxyl radical scavenging and singlet oxygen quenching properties of polyamines

Das, K. C., & Misra, H. P. (2004) · Molecular and Cellular Biochemistry · doi:10.1023/b:mcbi.0000038227.91813.79 · Cited by 167 · see citing works

Degradation of ornithine decarboxylase: exposure of the C-terminal target by a polyamine-inducible inhibitory protein.

Li, X., & Coffino, P. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.4.2377 · Cited by 166 · see citing works

Polyamine Modulon in Escherichia coli: Genes Involved in the Stimulation of Cell Growth by Polyamines

Igarashi, K., & Kashiwagi, K. (2006) · The Journal of Biochemistry · doi:10.1093/jb/mvj020 · Cited by 162 · see citing works

alpha-Difluoromethylornithine, an irreversible inhibitor of ornithine decarboxylase, inhibits tumor promoter-induced polyamine accumulation and carcinogenesis in mouse skin.

Weeks, C. E., Herrmann, A. L., Nelson, F., et al. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.19.6028 · Cited by 162 · see citing works

Heterologous Expression and Biochemical Characterization of a Polyamine Oxidase from Arabidopsis Involved in Polyamine Back Conversion

Tavladoraki, P., Rossi, M. N., Saccuti, G., et al. (2006) · PLANT PHYSIOLOGY · doi:10.1104/pp.106.080911 · Cited by 162 · see citing works

A Unifying Model for the Role of Polyamines in Bacterial Cell Growth, the Polyamine Modulon

Yoshida, M., Kashiwagi, K., Shigemasa, A., Taniguchi, S., Yamamoto, K., Makinoshima, H., Ishihama, A., & Igarashi, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404393200 · Cited by 161 · see citing works

Functional diversity inside the Arabidopsis polyamine oxidase gene family

Fincato, P., Moschou, P. N., Spedaletti, V., Tavazza, R., Angelini, R., Federico, R., Roubelakis–Angelakis, K. A., & Tavladoraki, P. (2010) · Journal of Experimental Botany · doi:10.1093/jxb/erq341 · Cited by 161 · see citing works

Polyamine pathway contributes to the pathogenesis of Parkinson disease

Lewandowski, N. M., Ju, S., Verbitsky, M., Ross, B., Geddie, M. L., Rockenstein, E. M., Adame, A., Muhammad, A., Vonsattel, J. P., Ringe, D., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011751107 · Cited by 156 · see citing works

c-Myc induces the expression and activity of ornithine decarboxylase.

Wagner, A. J., Meyers, C., Laimins, L. A., & Hay, N. (1993) · PubMed · Cited by 154 · see citing works

A Dual Upstream Open Reading Frame-based Autoregulatory Circuit Controlling Polyamine-responsive Translation

Hanfrey, C. C., Elliott, K. A., Franceschetti, M., Mayer, M. J., Illingworth, C., & Michael, A. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509340200 · Cited by 152 · see citing works

Deoxyhypusine Synthase Activity Is Essential for Cell Viability in the Yeast Saccharomyces cerevisiae

Park, M. H., Joe, Y. A., & Kang, K. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.3.1677 · Cited by 151 · see citing works

Metabolic profiling of Alzheimer's disease brains

Inoue, K., Tsutsui, H., Akatsu, H., Hashizume, Y., Matsukawa, N., Yamamoto, T., & Toyo’oka, T. (2013) · Scientific Reports · doi:10.1038/srep02364 · Cited by 150 · see citing works

The polyamine spermine protects Arabidopsis from heat stress-induced damage by increasing expression of heat shock-related genes

Sagor, G. H. M., Berberich, T., Takahashi, Y., et al. (2012) · Transgenic Research · doi:10.1007/s11248-012-9666-3 · Cited by 149 · see citing works

Polyamine Regulation of Ribosome Pausing at the Upstream Open Reading Frame of S-Adenosylmethionine Decarboxylase

Law, G. L., Raney, A., Heusner, C. L., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105944200 · Cited by 146 · see citing works

Posttranslational synthesis of hypusine: evolutionary progression and specificity of the hypusine modification

Wolff, E. C., Kang, K. R., Ys, K., et al. (2007) · Amino Acids · doi:10.1007/s00726-007-0525-0 · Cited by 144 · see citing works

Increased frequency of spontaneous skin tumors in transgenic mice which overexpress ornithine decarboxylase.

Megosh, L. C., Gilmour, S. K., Rosson, D., et al. (1995) · PubMed · Cited by 142 · see citing works

Polyamines Improve K+/Na+ Homeostasis in Barley Seedlings by Regulating Root Ion Channel Activities

Zhao, F., Song, C., He, J., & Zhu, H. (2007) · PLANT PHYSIOLOGY · doi:10.1104/pp.107.105882 · Cited by 142 · see citing works

Oncogenic Role of eIF-5A2 in the Development of Ovarian Cancer

Guan, X., Fung, J. M.-W., Ma, N., et al. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-3747 · Cited by 141 · see citing works

Efficacy and toxicity of eflornithine for treatment of Trypanosoma brucei gambiense sleeping sickness

Milord, F., Milord, F., Pépin, J., et al. (1992) · The Lancet · doi:10.1016/0140-6736(92)92180-n · Cited by 138 · see citing works

Distribution and properties of human intestinal diamine oxidase and its relevance for the histamine catabolism

Biegański, T., Kusche, J., Lorenz, W. E., et al. (1983) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(83)90092-2 · Cited by 137 · see citing works

Polyamines regulate their synthesis by inducing expression and blocking degradation of ODC antizyme

Palanimurugan, R., Scheel, H., Hofmann, K., & Dohmen, R. J. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600473 · Cited by 137 · see citing works

A macromolecular inhibitor of the antizyme to ornithine decarboxylase

Fujita, K., Murakami, Y., & Hayashi, S. (1982) · Biochemical Journal · doi:10.1042/bj2040647 · Cited by 136 · see citing works

Control of ornithine decarboxylase activity in stimulated human lymphocytes by putrescine and spermidine

Kay, J. E., & Lindsay, V. J. (1973) · Biochemical Journal · doi:10.1042/bj1320791 · Cited by 134 · see citing works

Multiple polyamine transport systems on the vacuolar membrane in yeast

Tomitori, H., Kashiwagi, K., Asakawa, T., Kakinuma, Y., Michael, A. J., & Igarashi, K. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530681 · Cited by 133 · see citing works

The Role of Polyamines in Supporting Growth of Mammalian Cells Is Mediated through Their Requirement for Translation Initiation and Elongation

Landau, G., Bercovich, Z., Park, M. H., & Kahana, C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.106419 · Cited by 130 · see citing works

S-Adenosylmethionine decarboxylase

Pegg, A. E. (2009) · Essays in Biochemistry · doi:10.1042/bse0460003 · Cited by 129 · see citing works

Are drought-resistance promoting bacteria cross-compatible with different plant models?

Marasco, R., Rolli, E., Vigani, G., Borin, S., Sorlini, C., Ouzari, H., Zocchi, G., & Daffonchio, D. G. (2013) · Plant Signaling & Behavior · doi:10.4161/psb.26741 · Cited by 129 · see citing works

The early history of polyamine research

Bachrach, U. (2010) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2010.02.003 · Cited by 129 · see citing works

Serum Metabolomics of Slow vs. Rapid Motor Progression Parkinson’s Disease: a Pilot Study

Roede, J. R., Uppal, K., Park, Y. H., Lee, K., Tran, V., Walker, D. I., Strobel, F. H., Rhodes, S. L., Ritz, B. R., & Jones, D. P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077629 · Cited by 128 · see citing works

Ribosomal frameshifting in decoding antizyme mRNAs from yeast and protists to humans: close to 300 cases reveal remarkable diversity despite underlying conservation

Ivanov, I. P., & Atkins, J. F. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm035 · Cited by 127 · see citing works

Translational regulation of ornithine decarboxylase and other enzymes of the polyamine pathway

Shantz, L. M., & Pegg, A. E. (1999) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(98)00135-6 · Cited by 126 · see citing works

Hypusine modification for growth is the major function of spermidine in Saccharomyces cerevisiae polyamine auxotrophs grown in limiting spermidine

Chattopadhyay, M. K., Park, M. H., & Tabor, H. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0710970105 · Cited by 124 · see citing works

Essential role of eIF5A-1 and deoxyhypusine synthase in mouse embryonic development

Nishimura, K., Lee, S. B., Park, J. H., & Park, M. H. (2011) · Amino Acids · doi:10.1007/s00726-011-0986-z · Cited by 123 · see citing works

Cell-specific translational regulation of S-adenosylmethionine decarboxylase mRNA. Dependence on translation and coding capacity of the cis-acting upstream open reading frame.

Hill, J. R., & Morris, D. R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54212-5 · Cited by 121 · see citing works

Human ornithine decarboxylase-overproducing NIH3T3 cells induce rapidly growing, highly vascularized tumors in nude mice.

Auvinen, M. I., Laine, A., Paasinen-Sohns, A., Kangas, A., Kangas, L., Saksela, O., Andersson, L. C., & Hölttä, E. (1997) · PubMed · Cited by 121 · see citing works

Cloning, Sequencing, and Heterologous Expression of the Murine Peroxisomal Flavoprotein, N1-Acetylated Polyamine Oxidase

Wu, T., Yankovskaya, V. L., & McIntire, W. S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302149200 · Cited by 120 · see citing works

Deoxyhypusine synthase gene is essential for cell viability in the yeast Saccharomyces cerevisiae

Sasaki, K., Abid, R., & Miyazaki, M. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00310-9 · Cited by 119 · see citing works

Stress and polyamine metabolism in fungi

Valdés‐Santiago, L., & Ruíz-Herrera, J. (2014) · Frontiers in Chemistry · doi:10.3389/fchem.2013.00042 · Cited by 119 · see citing works

Complex Inhibition of OmpF and OmpC Bacterial Porins by Polyamines

Iyer, R., & Delcour, A. H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.30.18595 · Cited by 119 · see citing works

Polyamine uptake systems in Escherichia coli

Igarashi, K., Ito, K., & Kashiwagi, K. (2001) · Research in Microbiology · doi:10.1016/s0923-2508(01)01198-6 · Cited by 118 · see citing works

Polyamines decrease Escherichia coli outer membrane permeability

Vega, A. L. D., & Delcour, A. H. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.13.3715-3721.1996 · Cited by 116 · see citing works

Posttranslational formation of hypusine in a single major protein occurs generally in growing cells and is associated with activation of lymphocyte growth

Cooper, H. L., Park, M. H., & Folk, J. E. (1982) · Cell · doi:10.1016/0092-8674(82)90441-x · Cited by 115 · see citing works

Spermidine or spermine is essential for the aerobic growth of Saccharomyces cerevisiae.

Balasundaram, D., Tabor, C. W., & Tabor, H. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.13.5872 · Cited by 115 · see citing works

Interactions between Polyamines and Abiotic Stress Pathway Responses Unraveled by Transcriptome Analysis of Polyamine Overproducers

Marco, F., Alcázar, R., Tiburcio, A. F., et al. (2011) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2011.0084 · Cited by 114 · see citing works

Recent advances in the molecular biology of metazoan polyamine transport

Poulin, R., Casero, R. A., & Soulet, D. (2011) · Amino Acids · doi:10.1007/s00726-011-0987-y · Cited by 113 · see citing works

Decarboxylation of ornithine and lysine in rat tissues

Pegg, A. E., & McGill, S. M. (1979) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(79)90310-3 · Cited by 113 · see citing works

Inhibition of Intestinal Carcinogenesis in Rats: Effect of Difluoromethylornithine With Piroxicam or Fish Oil 2

Nigro, N. D., Bull, A. W., & Boyd, M. E. (1986) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/77.6.1309 · Cited by 111 · see citing works

Effect of salt and osmotic stress on changes in polyamine content and arginine decarboxylase activity in Lupinus luteus seedlings

Legocka, J., & Kluk, A. (2005) · Journal of Plant Physiology · doi:10.1016/j.jplph.2004.08.009 · Cited by 111 · see citing works

Transcription of ahpC, katG, and katE genes in Escherichia coli is regulated by polyamines: polyamine-deficient mutant sensitive to H2O2-induced oxidative damage

Jung, I. L., & Kim, I. G. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00064-0 · Cited by 109 · see citing works

Identification of a Spermidine Excretion Protein Complex (MdtJI) in Escherichia coli

Higashi, K., Ishigure, H., Demizu, R., Uemura, T., Nishino, K., Yamaguchi, A., Kashiwagi, K., & Igarashi, K. (2007) · Journal of Bacteriology · doi:10.1128/jb.01505-07 · Cited by 108 · see citing works

Polyamines alter sequence-specific DNA-protein interactions

Panagiotidis, C. Α., Artandi, S. E., Calame, K. L., et al. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.10.1800 · Cited by 106 · see citing works

Identification and Characterization of a Polyamine Permease from the Protozoan Parasite Leishmania major

Hasne, M.-P., & Ullman, B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411331200 · Cited by 106 · see citing works

Cadaverine Inhibition of Porin Plays a Role in Cell Survival at Acidic pH

Samartzidou, H., Mehrazin, M., Xu, Z., Benedik, M. J., & Delcour, A. H. (2002) · Journal of Bacteriology · doi:10.1128/jb.185.1.13-19.2003 · Cited by 105 · see citing works

Polyamine sensing by nascent ornithine decarboxylase antizyme stimulates decoding of its mRNA

Kurian, L., Palanimurugan, R., Gödderz, D., & Dohmen, R. J. (2011) · Nature · doi:10.1038/nature10393 · Cited by 104 · see citing works

Excretion and Uptake of Putrescine by the PotE Protein in Escherichia coli

Kashiwagi, K., Shibuya, S., Tomitori, H., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.10.6318 · Cited by 104 · see citing works

Polyamine analogue induction of the p53-p21WAF1/CIP1-Rb pathway and G1 arrest in human melanoma cells.

Kramer, D. L., Vujcic, S., Diegelman, P., Alderfer, J. L., Miller, J. T., Black, J. D., Bergeron, R. J., & Porter, C. W. (1999) · PubMed · Cited by 103 · see citing works

Polyamine Uptake by DUR3 and SAM3 in Saccharomyces cerevisiae

Uemura, T., Kashiwagi, K., & Igarashi, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611105200 · Cited by 103 · see citing works

Cellular Polyamines Promote Amyloid-Beta (Aβ) Peptide Fibrillation and Modulate the Aggregation Pathways

Luo, J., Yu, C., Yu, H., Borštnar, R., Kamerlin, S. C. L., Gräslund, A., Abrahams, J. P., & Wärmländer, S. K. T. S. (2013) · ACS Chemical Neuroscience · doi:10.1021/cn300170x · Cited by 103 · see citing works

uORFs with unusual translational start codons autoregulate expression of eukaryotic ornithine decarboxylase homologs

Ivanov, I. P., Loughran, G., & Atkins, J. F. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801590105 · Cited by 103 · see citing works

Heterologous Expression and Characterization of Mouse Spermine Oxidase

Cervelli, M., Polticelli, F., Federico, R., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m207888200 · Cited by 99 · see citing works

Regulated Translation Termination at the Upstream Open Reading Frame in S-Adenosylmethionine Decarboxylase mRNA

Raney, A., Law, G. L., Mize, G. J., & Morris, D. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108375200 · Cited by 98 · see citing works

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

Chattopadhyay, M. K., Tabor, C. W., & Tabor, H. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1835918100 · Cited by 98 · see citing works

Changes in L-ornithine decarboxylase activity during the cell cycle

Heby, O., Gray, J. W., Lindl, P. A., et al. (1976) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(76)90254-0 · Cited by 97 · see citing works

Spermine reverses lipopolysaccharide-induced memory deficit in mice

Frühauf, P. K. S., Ineu, R. P., Tomazi, L., Duarte, T., Mello, C. F., & Rubin, M. A. (2015) · Journal of Neuroinflammation · doi:10.1186/s12974-014-0220-5 · Cited by 96 · see citing works

Free radical scavenging action of the natural polyamine spermine in rat liver mitochondria

Sava, I. G., Battaglia, V., Rossi, C. A., Salvi, M., & Toninello, A. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.07.008 · Cited by 94 · see citing works

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

Wood, P. L., Khan, M. A., & Moskal, J. R. (2007) · Brain Research · doi:10.1016/j.brainres.2006.10.004 · Cited by 92 · see citing works

Cloning and Characterization of Human Polyamine-modulated Factor-1, a Transcriptional Cofactor That Regulates the Transcription of the Spermidine/SpermineN 1-Acetyltransferase Gene

Wang, Y., Devereux, W. L., Stewart, T. M., & Casero, R. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.31.22095 · Cited by 91 · see citing works

Isolation, characterization, and mapping of Escherichia coli mutants blocked in the synthesis of ornithine decarboxylase

Cunningham-Rundles, S., & Maas, W. K. (1975) · Journal of Bacteriology · doi:10.1128/jb.124.2.791-799.1975 · Cited by 90 · see citing works

Multiple polyamine transport systems on the vacuolar membrane in yeast

Tomitori, H., Kashiwagi, K., Asakawa, T., et al. (2001) · Biochemical Journal · doi:10.1042/bj3530681 · Cited by 88 · see citing works

Polyamine auxotrophs of Saccharomyces cerevisiae

Whitney, P. A., & Morris, D. R. (1978) · Journal of Bacteriology · doi:10.1128/jb.134.1.214-220.1978 · Cited by 87 · see citing works

A profusion of upstream open reading frame mechanisms in polyamine-responsive translational regulation

Ivanov, I. P., Atkins, J. F., & Michael, A. J. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp1037 · Cited by 87 · see citing works

AGP2 Encodes the Major Permease for High Affinity Polyamine Import in Saccharomyces cerevisiae

Aouida, M., Leduc, A., Poulin, R., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503071200 · Cited by 87 · see citing works

The Identification of a Cis-element and a Trans-acting Factor Involved in the Response to Polyamines and Polyamine Analogues in the Regulation of the Human Spermidine/Spermine N 1-Acetyltransferase Gene Transcription

Wang, Y., Xiao, L., Thiagalingam, A., Nelkin, B. D., & Casero, R. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.51.34623 · Cited by 86 · see citing works

Identification of Polyamine Transporters in Plants: Paraquat Transport Provides Crucial Clues

Fujita, M., & Shinozaki, K. (2014) · Plant and Cell Physiology · doi:10.1093/pcp/pcu032 · Cited by 84 · see citing works

Properties of a polyamine transporter regulated by antizyme

Sakata, K., Kashiwagi, K., & Igarashi, K. (2000) · Biochemical Journal · doi:10.1042/bj3470297 · Cited by 83 · see citing works

Functions of potA and potD proteins in spermidine-preferential uptake system in Escherichia coli.

Kashiwagi, K., Miyamoto, S., Nukui, E., et al. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36522-6 · Cited by 81 · see citing works

Polyamine Metabolism in Fungi with Emphasis on Phytopathogenic Species

Valdés‐Santiago, L., Chávez, J. A. C., León-Ramírez, C. G., & Ruíz-Herrera, J. (2012) · Journal of Amino Acids · doi:10.1155/2012/837932 · Cited by 80 · see citing works

Ornithine Decarboxylase- and ras -Induced Cell Transformations: Reversal by Protein Tyrosine Kinase Inhibitors and Role of pp130 CAS

Auvinen, M. I., Paasinen-Sohns, A., Hirai, H., et al. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.12.6513 · Cited by 80 · see citing works

Localization and Function of the Yeast Multidrug Transporter Tpo1p

Albertsen, M., Bellahn, I., Krämer, R., & Waffenschmidt, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210715200 · Cited by 79 · see citing works

Ornithine Decarboxylase and S-Adenosylmethionine Decarboxylase Expression during the Cell Cycle of Chinese Hamster Ovary Cells

Fredlund, J. O., Johansson, M. C., Dahlberg, E., et al. (1995) · Experimental Cell Research · doi:10.1006/excr.1995.1011 · Cited by 79 · see citing works

The Drosophila deoxyhypusine hydroxylase homologue nero and its target eIF5A are required for cell growth and the regulation of autophagy

Patel, P. H., Costa‐Mattioli, M., Schulze, K. L., et al. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200904161 · Cited by 78 · see citing works

Properties and structure of spermidine acetyltransferase in Escherichia coli.

Fukuchi, J., Kashiwagi, K., Takio, K., et al. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31685-x · Cited by 76 · see citing works

Tpo1‐mediated spermine and spermidine export controls cell cycle delay and times antioxidant protein expression during the oxidative stress response

Krüger, A., Vowinckel, J., Mülleder, M., Grote, P., Capuano, F., Bluemlein, K., & Ralser, M. (2013) · EMBO Reports · doi:10.1038/embor.2013.165 · Cited by 75 · see citing works

Antizyme1 mediates AURKAIP1-dependent degradation of Aurora-A

Lim, S. K., & Gopalan, G. (2007) · Oncogene · doi:10.1038/sj.onc.1210482 · Cited by 74 · see citing works

Polyamine content of AKR leukemic cells in relation to the cell cycle.

Heby, O., Sarna, G. P., Marton, L. J., et al. (1973) · PubMed · Cited by 74 · see citing works

Targeted antizyme expression in the skin of transgenic mice reduces tumor promoter induction of ornithine decarboxylase and decreases sensitivity to chemical carcinogenesis.

Feith, D. J., Shantz, L. M., & Pegg, A. E. (2001) · PubMed · Cited by 73 · see citing works

Regulation of ornithine decarboxylase in a transformed cell line that overexpresses translation initiation factor eIF-4E.

Shantz, L. M., Hu, R.-H., & Pegg, A. E. (1996) · PubMed · Cited by 72 · see citing works

Cell cycle specific fluctuations in adenosine 3':5'-cyclic monophosphate and polyamines of Chinese hamster cells.

Russell, D. H., & Stambrook, P. J. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.4.1482 · Cited by 72 · see citing works

Yeast Fms1 is a FAD-utilizing polyamine oxidase

Landry, J. W., & Sternglanz, R. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00416-9 · Cited by 71 · see citing works

Putrescine, a fast-acting switch for tolerance against osmotic stress

Kotakis, C., Theodoropoulou, E., Tassis, K., et al. (2013) · Journal of Plant Physiology · doi:10.1016/j.jplph.2013.09.015 · Cited by 71 · see citing works

Increased Red Blood Cell Polyamines in ALS and Parkinson's Disease

Gomes–Trolin, C., Nygren, I., Sm, A., & Askmark, H. (2002) · Experimental Neurology · doi:10.1006/exnr.2002.7952 · Cited by 70 · see citing works

Cadaverine

Tomar, P. C., Lakra, N., & Mishra, S. (2013) · Plant Signaling & Behavior · doi:10.4161/psb.25850 · Cited by 70 · see citing works

Polyamines in the basal ganglia of human brain. Influence of aging and degenerative movement disorders

Vivó, M., de Vera, N., Cortés, R., et al. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(01)01776-1 · Cited by 69 · see citing works

Polyamine Stimulation of the Synthesis of Oligopeptide-binding Protein (OppA)

Yoshida, M., Meksuriyen, D., Kashiwagi, K., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.32.22723 · Cited by 69 · see citing works

Regulation of arginine decarboxylase by spermine in osmotically‐stressed oat leaves

BORRELL, A., Besford, R. T., Altabella, T., et al. (1996) · Physiologia Plantarum · doi:10.1111/j.1399-3054.1996.tb00680.x · Cited by 69 · see citing works

Polyamine-regulated unproductive splicing and translation of spermidine/spermine N1-acetyltransferase

Hyvönen, M. T., Uimari, A., Keinänen, T. A., Heikkinen, S., Pellinen, R., Wahlfors, T., Korhonen, A., Närvänen, A. T. O., Wahlfors, J., Alhonen, L. I., et al. (2006) · RNA · doi:10.1261/rna.39806 · Cited by 68 · see citing works

Cloning and characterization of a rat gene encoding ornithine decarboxylase antizyme

Miyazaki, Y., Matsufuji, S., & Hayashi, S. (1992) · Gene · doi:10.1016/0378-1119(92)90395-6 · Cited by 68 · see citing works

Trypanosoma cruzi epimastigotes lack ornithine decarboxylase but can express a foreign gene encoding this enzyme

Carrillo, C., Cejas, S., González, N. S., & Algranati, I. D. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00804-2 · Cited by 68 · see citing works

Characterization of the interaction between the transcription factors human polyamine modulated factor (PMF-1) and NF-E2-related factor 2 (Nrf-2) in the transcriptional regulation of the spermidine/spermine N1-acetyltransferase (SSAT) gene

Yanlin, W. A. N. G., Devereux, W. L., Stewart, T. M., & Casero, R. A. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3550045 · Cited by 67 · see citing works

A high‐affinity putrescine‐cadaverine transporter from Trypanosoma cruzi

Hasne, M.-P., Coppens, I., Soysa, R., & Ullman, B. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07081.x · Cited by 67 · see citing works

A barley polyamine oxidase isoform with distinct structural features and subcellular localization

Cervelli, M., Cona, A., Angelini, R., et al. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02296.x · Cited by 67 · see citing works

Interference with S and G2 phase progression by polyamine synthesis inhibitors

Heby, O., Andersson, G. K. A., & Gray, J. W. (1978) · Experimental Cell Research · doi:10.1016/0014-4827(78)90192-1 · Cited by 65 · see citing works

Kinetic evaluation of polyamines as radical scavengers.

Fujisawa, S., & Kadoma, Y. (2005) · PubMed · Cited by 64 · see citing works

Effect of Spermidine on Misfolding and Interactions of Alpha-Synuclein

Krasnoslobodtsev, A. V., Peng, J., Asiago, J. M., Hindupur, J., Rochet, J., & Lyubchenko, Y. L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0038099 · Cited by 63 · see citing works

Regulation of a high-affinity diamine transport system in Trypanosoma cruzi epimastigotes

Quesne, S. A. L., & Fairlamb, A. H. (1996) · Biochemical Journal · doi:10.1042/bj3160481 · Cited by 63 · see citing works

A novel mouse model for inhibition of DOHH mediated hypusine modification reveals crucial function for embryonic development, proliferation and oncogenic transformation

Sievert, H., Pällmann, N., Miller, K. K., Hermans‐Borgmeyer, I., Venz, S., Sendoel, A., Preukschas, M., Schweizer, M., Boettcher, S., Janiesch, P. C., et al. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.014449 · Cited by 62 · see citing works

Structural biology of S-adenosylmethionine decarboxylase

Bale, S., & Ealick, S. E. (2009) · Amino Acids · doi:10.1007/s00726-009-0404-y · Cited by 62 · see citing works

Structure of a Human S-Adenosylmethionine Decarboxylase Self-Processing Ester Intermediate and Mechanism of Putrescine Stimulation of Processing As Revealed by the H243A Mutant,

Ekstrom, J. L., Tolbert, W. D., Xiong, H., et al. (2001) · Biochemistry · doi:10.1021/bi010736o · Cited by 62 · see citing works

Increased levels of γ‐glutamylamines in Huntington disease CSF

Jeitner, T. M., Matson, W. R., Folk, J. E., et al. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05350.x · Cited by 62 · see citing works

Arginine decarboxylase of oats is activated by enzymatic cleavage into two polypeptides.

Malmberg, R. L., & Cellino, M. L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42000-x · Cited by 60 · see citing works

Polyamine metabolism in normal and in virus-transformed chick embryo fibroblasts.

Don, S., & Bachrach, U. (1975) · PubMed · Cited by 60 · see citing works

Polyamine-deficient Neurospora crassa mutants and synthesis of cadaverine

Paulus, T. J., Kiyono, P., & Davis, R. H. (1982) · Journal of Bacteriology · doi:10.1128/jb.152.1.291-297.1982 · Cited by 59 · see citing works

Polyamines as Modulators of Gene Expression under Oxidative Stress in Escherichia coli

Ткаченко, А. Г., & Nesterova, L. Y. (2003) · Biochemistry (Moscow) · doi:10.1023/a:1025790729797 · Cited by 58 · see citing works

Elevated polyamines induce c-MYC overexpression by perturbing quadruplex–WC duplex equilibrium

Kumar, N., Basundra, R., & Maiti, S. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp196 · Cited by 58 · see citing works

Divergent polyamine metabolism in the Apicomplexa

Cook, T., Roos, D. S., Morada, M., et al. (2007) · Microbiology · doi:10.1099/mic.0.2006/001768-0 · Cited by 58 · see citing works

Absolute requirement of spermidine for growth and cell cycle progression of fission yeast ( Schizosaccharomyces pombe )

Chattopadhyay, M. K., Tabor, C. W., & Tabor, H. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.162362899 · Cited by 57 · see citing works

The Escherichia coli ldcC gene encodes another lysine decarboxylase, probably a constitutive enzyme.

Yamamoto, Y., Miwa, Y., Miyoshi, K., Furuyama, J.-I., & Ohmori, H. (1997) · Genes & Genetic Systems · doi:10.1266/ggs.72.167 · Cited by 56 · see citing works

Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics

Stewart, T. M., Wang, Y., Devereux, W. L., et al. (2002) · Biochemical Journal · doi:10.1042/bj20021587 · Cited by 56 · see citing works

Lysine decarboxylase of Vibrio parahaemolyticus: kinetics of transcription and role in acid resistance

Tanaka, Y., Kimura, B., Takahashi, H., et al. (2007) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2007.03652.x · Cited by 56 · see citing works

Excretion of Putrescine and Spermidine by the Protein Encoded by YKL174c (TPO5) in Saccharomyces cerevisiae

Tachihara, K., Uemura, T., Kashiwagi, K., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m410778200 · Cited by 55 · see citing works

Targeting Trypanothione Metabolism in Trypanosomatid Human Parasites

Olín‐Sandoval, V., Moreno‐Sánchez, R., & Saavedra, E. (2010) · Current Drug Targets · doi:10.2174/1389450111009011614 · Cited by 55 · see citing works

The Structural Basis for Substrate Specificity and Inhibition of Human S-Adenosylmethionine Decarboxylase,

Tolbert, W. D., Ekstrom, J. L., Mathews, I. I., Secrist, J. A. I., Kapoor, P., Pegg, A. E., & Ealick, S. E. (2001) · Biochemistry · doi:10.1021/bi010735w · Cited by 54 · see citing works

Polyamine Transport and Role of potE in Response to Osmotic Stress in Escherichia coli

Schiller, D., Kruse, D., Kneifel, H., Krämer, R., & Burkovski, A. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.21.6247-6249.2000 · Cited by 53 · see citing works

Ornithine decarboxylase activity in synchronously growing Don C cells

Friedman, S. J., Bellantone, R. A., & Canellakis, E. S. (1972) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(72)90329-7 · Cited by 53 · see citing works

Uptake of GABA and putrescine by UGA4 on the vacuolar membrane in Saccharomyces cerevisiae

Uemura, T., Tomonari, Y., Kashiwagi, K., et al. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.01.162 · Cited by 53 · see citing works

Polyamine Transport by Mammalian Cells and Mitochondria

Hoshino, K., Momiyama, E., Yoshida, K., Nishimura, K., SAKAI, S., Toida, T., Kashiwagi, K., & Igarashi, K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505445200 · Cited by 53 · see citing works

Polyamine starvation prolongs the S and G2 phases of polyamine-dependent (arginase-deficient) CHO cells.

Anehus, S., Pohjanpelto, P., Baldetorp, B., et al. (1984) · Molecular and Cellular Biology · doi:10.1128/mcb.4.5.915 · Cited by 53 · see citing works

Polyamine depletion arrests growth of IEC-6 and Caco-2 cells by different mechanisms

Ray, R. M., McCormack, S. A., & Johnson, L. R. (2001) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.2001.281.1.g37 · Cited by 52 · see citing works

Polyamine analogues inhibit the ubiquitination of spermidine/spermine N1-acetyltransferase and prevent its targeting to the proteasome for degradation

Coleman, C. S., & Pegg, A. E. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3580137 · Cited by 51 · see citing works

Post-transcriptional regulation of the content of spermidine/spermine N1-acetyltransferase by N1N12-bis(ethyl)spermine

Parry, L., Fouce, R. B., & Pegg, A. E. (1995) · Biochemical Journal · doi:10.1042/bj3050451 · Cited by 50 · see citing works

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

Thomas, T., Thomas, T., Gallo, M. A., et al. (1995) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/0960-0760(95)00126-k · Cited by 50 · see citing works

Three-Component Lysine/Ornithine Decarboxylation System in Lactobacillus saerimneri 30a

Romano, A., Trip, H., Lolkema, J. S., et al. (2013) · Journal of Bacteriology · doi:10.1128/jb.02070-12 · Cited by 50 · see citing works

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

Yoshida, M., Kashiwagi, K., Kawai, G., Ishihama, A., & Igarashi, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011059200 · Cited by 49 · see citing works

Increased ornithine decarboxylase activity in murine sarcoma virus infected cells

Gazdar, A. F., Stull, H. B., Kilton, L. J., et al. (1976) · Nature · doi:10.1038/262696a0 · Cited by 48 · see citing works

Uptake of putrescine and spermidine by Gap1p on the plasma membrane in Saccharomyces cerevisiae

Uemura, T., Kashiwagi, K., & Igarashi, K. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.01.064 · Cited by 48 · see citing works

The Regulation of Ornithine Decarboxylase Gene Expression by Sucrose and Small Upstream Open Reading Frame in Tomato (Lycopersicon esculentum Mill)

Kwak, S.-H., & Lee, S. H. (2001) · Plant and Cell Physiology · doi:10.1093/pcp/pce040 · Cited by 47 · see citing works

Increased expression and cellular localization of spermine oxidase in ulcerative colitis and relationship to disease activity

Hong, S. S., Chaturvedi, R., Piazuelo, B. M., Coburn, L. A., Williams, C. S., Delgado, A. G., Casero, R. A., Schwartz, D. A., & Wilson, K. T. (2010) · Inflammatory Bowel Diseases · doi:10.1002/ibd.21224 · Cited by 46 · see citing works

Inhibitory effect of α-hydrazinoornithine on egg cleavage in sea urchin eggs

Kusunoki, S., & Yasumasu, I. (1978) · Developmental Biology · doi:10.1016/0012-1606(78)90204-x · Cited by 46 · see citing works

Polyamines Enhance Synthesis of the RNA Polymerase ς38 Subunit by Suppression of an Amber Termination Codon in the Open Reading Frame

Yoshida, M., Kashiwagi, K., Kawai, G., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206668200 · Cited by 46 · see citing works

The N-Terminal Unstructured Domain of Yeast ODC Functions as a Transplantable and Replaceable Ubiquitin-Independent Degron

Gödderz, D., Schäfer, E., Palanimurugan, R., & Dohmen, R. J. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.01.051 · Cited by 46 · see citing works

Haploinsufficiency for Odc Modifies Mouse Skin Tumor Susceptibility

Guo, Y., Cleveland, J. L., & O’Brien, T. G. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-3244 · Cited by 46 · see citing works

Cell type-specific mechanisms of regulating expression of the ornithine decarboxylase gene after growth stimulation.

Abrahamsen, M. S., & Morris, D. R. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.10.5525 · Cited by 45 · see citing works

Gut microbiota, metabolites and host immunity

Rooks, M. G., & Garrett, W. S. (2016) · Nature reviews. Immunology · doi:10.1038/nri.2016.42 · Cited by 3,409 · see citing works

Sickle cell disease

Kato, G. J., Piel, F. B., Reid, C. D., Gaston, M. H., Ohene-Frempong, K., Krishnamurti, L., Smith, W. R., Panepinto, J. A., Weatherall, D. J., Costa, F. F., et al. (2018) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2018.10 · Cited by 1,501 · see citing works

Understanding the Holobiont: How Microbial Metabolites Affect Human Health and Shape the Immune System

Postler, T. S., & Ghosh, S. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.05.008 · Cited by 876 · see citing works

Immune regulation by microbiome metabolites

Kim, C. H. (2018) · Immunology · doi:10.1111/imm.12930 · Cited by 375 · see citing works

Polyamines and gut microbiota

Tofalo, R., Cocchi, S., & Suzzi, G. (2019) · Frontiers in Nutrition · doi:10.3389/fnut.2019.00016 · Cited by 306 · see citing works

Daily eating patterns and their impact on health and disease

Zarrinpar, A., Chaix, A., & Panda, S. (2016) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2015.11.007 · Cited by 263 · see citing works

Dietary and Gut Microbiota Polyamines in Obesity- and Age-Related Diseases

Ramos-Molina, B., Queipo-Ortuño, M. I., Lambertos, A., Tinahones, F. J., & Peñafiel, R. (2019) · Frontiers in Nutrition · doi:10.3389/fnut.2019.00024 · Cited by 226 · see citing works

ATP13A3 is a major component of the enigmatic mammalian polyamine transport system

Hamouda, N. N., Van den Haute, C., Vanhoutte, R., Sannerud, R., Azfar, M., Mayer, R., Cortés Calabuig, Á., Swinnen, J. V., Agostinis, P., Baekelandt, V., et al. (2021) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013908 · Cited by 85 · see citing works

Gut-microbiota derived bioactive metabolites and their functions in host physiology

Debnath, N., Kumar, R., Kumar, A., Mehta, P. K., & Yadav, A. K. (2021) · Biotechnology and Genetic Engineering Reviews · doi:10.1080/02648725.2021.1989847 · Cited by 77 · see citing works

Participation of polyamines in the flowering of the short-day plant Pharbitis nil

Zielińska, M., Kęsy, J., & Kopcewicz, J. (2006) · Plant Growth Regulation · doi:10.1007/s10725-006-9111-9 · Cited by 8 · see citing works

Inhibition of Na,K-ATPase from Chick Brain by Polyamines

Heinrich-Hirsch, B., Ahlers, J., & Peter, H. W. (1977) · Enzyme and Protein · doi:10.1159/000458795 · Cited by 29 · see citing works

Feedback regulation of polyamine synthesis in Ehrlich ascites tumor cells. Analysis using nonmetabolizable derivatives of putrescine and spermine

Holm, I., Persson, L., Heby, O., et al. (1988) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(88)80054-9 · Cited by 5 · see citing works

Putrescine, spermidine and spermine in higher plants

Smith, T. A. (1970) · Phytochemistry · doi:10.1016/s0031-9422(00)85263-2 · Cited by 81 · see citing works

A rapid gas chromatographic method for the determination of plasma polyamines and its application to the prediction of tumour response to chemotherapy

Bakowski, M. T., Toseland, P. A., Wicks, J. F. C., et al. (1981) · Clinica Chimica Acta · doi:10.1016/0009-8981(81)90356-9 · Cited by 23 · see citing works