Biosynthesis of polyamines and polyamine-containing molecules

POLYAMINES

Tabor, C. W., & Tabor, H. (1984) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.53.070184.003533 · Cited by 3,064 · see citing works

Catalytic irreversible inhibition of mammalian ornithine decarboxylase (E.C.4.1.1.17) by substrate and product analogs

Metcalf, B. W., Bey, P., Danzin, C., Jung, M. J., Casara, P., & Vevert, J. (1978) · Journal of the American Chemical Society · doi:10.1021/ja00476a050 · Cited by 1,005 · see citing works

Pyridoxal Phosphate Enzymes: Mechanistic, Structural, and Evolutionary Considerations

Eliot, A. C., & Kirsch, J. F. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074021 · Cited by 955 · see citing works

Polyamines in microorganisms

Tabor, C. W., & Tabor, H. (1985) · Microbiological Reviews · doi:10.1128/mr.49.1.81-99.1985 · Cited by 907 · see citing works

Species-specific polyamines from diatoms control silica morphology

Kröger, N., Deutzmann, R., Bergsdorf, C., & Sumper, M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.260496497 · Cited by 685 · see citing works

eIF5A Promotes Translation of Polyproline Motifs

Gutierrez, E., Shin, B., Woolstenhulme, C. J., Kim, J.-R., Saini, P., Buskirk, A. R., & Dever, T. E. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.04.021 · Cited by 525 · see citing works

An archaeal origin of eukaryotes supports only two primary domains of life

Williams, T. A., Foster, P. G., Cox, C. J., & Embley, T. M. (2013) · Nature · doi:10.1038/nature12779 · Cited by 519 · see citing works

Structure of a unique binuclear manganese cluster in arginase

Kanyo, Z. F., Scolnick, L. R., Ash, D. E., & Christianson, D. W. (1996) · Nature · doi:10.1038/383554a0 · Cited by 441 · see citing works

Anti-proliferative properties of DL-α-difluoromethyl ornithine in cultured cells. A consequence of the irreversible inhibition of ornithine decarboxylase

Mamont, P. S., Duchesne, M.-C., Grove, J., & Bey, P. (1978) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(78)91630-3 · Cited by 399 · see citing works

Structure, evolution and action of vitamin B6-dependent enzymes

Jansonius, J. N. (1998) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(98)80096-1 · Cited by 395 · see citing works

Polyamine catabolism and disease

Casero, R. A., & Pegg, A. E. (2009) · Biochemical Journal · doi:10.1042/bj20090598 · Cited by 380 · see citing works

Evolutionary relationships among pyridoxal‐5′‐phosphate‐dependent enzymes

ALEXANDER, F. W., Sandmeier, E., Mehta, P. K., & Christen, P. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb18577.x · Cited by 373 · see citing works

The Post-Translational Synthesis of a Polyamine-Derived Amino Acid, Hypusine, in the Eukaryotic Translation Initiation Factor 5A (eIF5A)

Park, M. H. (2006) · The Journal of Biochemistry · doi:10.1093/jb/mvj034 · Cited by 353 · 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

Regulation of cellular polyamines by antizyme

Coffino, P. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056508 · Cited by 350 · see citing works

A protective role for the polyamine spermine against drought stress in Arabidopsis

Yamaguchi, K., Takahashi, Y., Berberich, T., Imai, A., Takahashi, T., Michael, A. J., & Kusano, T. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.11.041 · Cited by 320 · see citing works

Gene Expression in Tobacco Low-Nicotine Mutants

Hibi, N., Higashiguchi, S., Hashimoto, T., & Yamada, Y. (1994) · The Plant Cell · doi:10.1105/tpc.6.5.723 · Cited by 316 · see citing works

Identification of hypusine, an unusual amino acid, in a protein from human lymphocytes and of spermidine as its biosynthetic precursor.

Park, M. H., Cooper, H. L., & Folk, J. E. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.5.2869 · Cited by 309 · 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

The Biosynthesis of Spermidine and Spermine from Putrescine and Methionine

Tabor, H., Rosenthal, S. M., & Tabor, C. W. (1958) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64676-9 · Cited by 296 · see citing works

ACAULIS5, an Arabidopsis gene required for stem elongation, encodes a spermine synthase

Hanzawa, Y., Takahashi, T., Michael, A. J., Burtin, D., Long, D., Piñeiro, M., Coupland, G., & Komeda, Y. (2000) · The EMBO Journal · doi:10.1093/emboj/19.16.4248 · Cited by 280 · see citing works

Concentrations of putrescine and polyamines and their enzymic synthesis during androgen-induced prostatic growth

Pegg, A. E., Lockwood, D. H., & Williams-Ashman, H. G. (1970) · Biochemical Journal · doi:10.1042/bj1170017 · Cited by 276 · see citing works

The Ornithine Decarboxylase Gene Is Essential for Cell Survival during Early Murine Development

Pendeville, H., Carpino, N., Marine, J., Takahashi, Y., Müller, M., MARTIAL, J. A., & Cleveland, J. L. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.19.6549-6558.2001 · Cited by 262 · see citing works

The function of spermine

Pegg, A. E. (2014) · IUBMB Life · doi:10.1002/iub.1237 · Cited by 251 · see citing works

Multiple evolutionary origin of pyridoxal‐5′‐phosphate‐dependent amino acid decarboxylases

Sandmeier, E., HALE, T. I., & Christen, P. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb18816.x · Cited by 239 · see citing works

Spermidine Synthase Genes Are Essential for Survival of Arabidopsis

Imai, A., Matsuyama, T., Hanzawa, Y., Akiyama, T., Tamaoki, M., Saji, H., Shirano, Y., Kato, T., Hayashi, H., Shibata, D., et al. (2004) · PLANT PHYSIOLOGY · doi:10.1104/pp.104.041699 · Cited by 239 · see citing works

Nucleotide sequence of the Escherichia coli cad operon: a system for neutralization of low extracellular pH

Meng, S., & Bennett, G. N. (1992) · Journal of Bacteriology · doi:10.1128/jb.174.8.2659-2669.1992 · Cited by 236 · 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

Petrobactin, a Photoreactive Siderophore Produced by the Oil-Degrading Marine Bacterium Marinobacter hydrocarbonoclasticus

Barbeau, K. A., Zhang, G., Live, D. H., & Butler, A. (2001) · Journal of the American Chemical Society · doi:10.1021/ja0119088 · Cited by 226 · see citing works

Putative spermine synthases from Thalassiosira pseudonana and Arabidopsis thaliana synthesize thermospermine rather than spermine

Knott, J. M., Römer, P., & Sumper, M. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.05.074 · Cited by 213 · see citing works

Expanding Small-Molecule Functional Metagenomics through Parallel Screening of Broad-Host-Range Cosmid Environmental DNA Libraries in Diverse Proteobacteria

Craig, J. W., Chang, F., Kim, J. H., Obiajulu, S. C., & Brady, S. F. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.02169-09 · Cited by 202 · see citing works

A BAHD acyltransferase is expressed in the tapetum of Arabidopsis anthers and is involved in the synthesis of hydroxycinnamoyl spermidines

Grienenberger, E., Besseau, S., Geoffroy, P., Debayle, D., Heintz, D., Lapierre, C., Pollet, B., Heitz, T., & Legrand, M. (2008) · The Plant Journal · doi:10.1111/j.1365-313x.2008.03773.x · Cited by 201 · see citing works

Polyamines Are Essential for the Formation of Plague Biofilm

Patel, C. N., Wortham, B. W., Lines, J. L., Fetherston, J. D., Perry, R. D., & Oliveira, M. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.7.2355-2363.2006 · Cited by 198 · see citing works

Characterization of Biosynthetic Enzymes for Ectoine as a Compatible Solute in a Moderately Halophilic Eubacterium, Halomonas elongata

Ono, H., Sawada, K., Khunajakr, N., Tao, T., Yamamoto, M., Hiramoto, M., Shinmyō, A., Takano, M., & Murooka, Y. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.1.91-99.1999 · Cited by 196 · see citing works

NspS, a Predicted Polyamine Sensor, Mediates Activation of Vibrio cholerae Biofilm Formation by Norspermidine

Karatan, E., Duncan, T. R., & Watnick, P. I. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.21.7434-7443.2005 · Cited by 187 · 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

An Alternative Polyamine Biosynthetic Pathway Is Widespread in Bacteria and Essential for Biofilm Formation in Vibrio cholerae

Lee, J., Sperandio, V., Frantz, D. E., Longgood, J. C., Camilli, A., Phillips, M. A., & Michael, A. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900110200 · Cited by 186 · see citing works

Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase

Ober, D., & Hartmann, T. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.26.14777 · Cited by 186 · see citing works

Spermine synthase

Pegg, A. E., & Michael, A. J. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0165-5 · Cited by 180 · see citing works

The hypusine-containing translation factor eIF5A

Dever, T. E., Gutierrez, E., & Shin, B. (2014) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2014.939608 · Cited by 178 · see citing works

Linkage between the bacterial acid stress and stringent responses: the structure of the inducible lysine decarboxylase

Kanjee, U., Gutsche, I., Alexopoulos, E., Zhao, B., Bakkouri, M. E., Thibault, G., Liu, K., Ramachandran, S., Snider, J. D., PAI, E. F., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.5 · Cited by 177 · see citing works

Evolutionary Diversification in Polyamine Biosynthesis

Minguet, E. G., Vera‐Sirera, F., Marina, A., Carbonell, J., & Blázquez, M. A. (2008) · Molecular Biology and Evolution · doi:10.1093/molbev/msn161 · Cited by 169 · see citing works

Accumulation of hydroxycinnamic acid amides induced by pathogen infection and identification of agmatine coumaroyltransferase in Arabidopsis thaliana

Muroi, A., Ishihara, A., Tanaka, C., Ishizuka, A., Takabayashi, J., Miyoshi, H., & Nishi­oka, T. (2009) · Planta · doi:10.1007/s00425-009-0960-0 · Cited by 169 · see citing works

PoxA, YjeK, and Elongation Factor P Coordinately Modulate Virulence and Drug Resistance in Salmonella enterica

Navarre, W. W., Zou, S. B., Roy, H., Xie, J. L., Savchenko, A. V., Singer, A. U., Edvokimova, E., Prost, L. R., Kumar, R. D., Ibba, M., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.06.021 · Cited by 167 · see citing works

A Novel Polyamine Acyltransferase Responsible for the Accumulation of Spermidine Conjugates in Arabidopsis Seed

Luo, J., Fuell, C., PARR, A. J., Hill, L. M., Bailey, P. C. E., Elliott, K. A., Fairhurst, S. A., Martin, C. R., & Michael, A. J. (2009) · The Plant Cell · doi:10.1105/tpc.108.063511 · Cited by 165 · 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

Polyamines As A Chemotaxonomic Marker in Bacterial Systematics

Hamana, K., & Matsuzaki, S. (1992) · Critical Reviews in Microbiology · doi:10.3109/10408419209113518 · Cited by 156 · see citing works

Arginine catabolic mobile element encoded speG abrogates the unique hypersensitivity of Staphylococcus aureus to exogenous polyamines

Joshi, G. S., Spontak, J. S., Klapper, D. G., & Richardson, A. R. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07809.x · 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

Crystal structure of human ornithine decarboxylase at 2.1 å resolution: structural insights to antizyme binding

Almrud, J. J., Oliveira, M., Kern, A. D., Grishin, N. V., Phillips, M. A., & Hackert, M. L. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3331 · Cited by 152 · see citing works

Evidence that putrescine acts as an extracellular signal required for swarming in Proteus mirabilis

Sturgill, G. M., & Rather, P. N. (2004) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03835.x · Cited by 151 · 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

A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor P

Yanagisawa, T., Sumida, T., Ishii, R., Takemoto, C., & Yokoyama, S. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1889 · Cited by 150 · see citing works

Aminopropyltransferases: Function, Structure and Genetics

Ikeguchi, Y., Bewley, M. C., & Pegg, A. E. (2006) · The Journal of Biochemistry · doi:10.1093/jb/mvj019 · Cited by 148 · see citing works

X-ray Structure of Ornithine Decarboxylase from Trypanosoma brucei: The Native Structure and the Structure in Complex with α-Difluoromethylornithine,

Grishin, N. V., Osterman, A. L., Brooks, H. B., Phillips, M. A., & Goldsmith, E. J. (1999) · Biochemistry · doi:10.1021/bi9915115 · Cited by 145 · see citing works

Lysine Decarboxylase Catalyzes the First Step of Quinolizidine Alkaloid Biosynthesis and Coevolved with Alkaloid Production in Leguminosae

Bunsupa, S., Kae, K., Ikeura, E., Oikawa, A., Toyooka, K., Saito, K., & Yamazaki, M. (2012) · The Plant Cell · doi:10.1105/tpc.112.095885 · Cited by 145 · see citing works

Spermine is not essential for survival of Arabidopsis

Imai, A., Akiyama, T., Kato, T., Sato, S., Tabata, S., Yamamoto, K. T., & Takahashi, T. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)01395-4 · Cited by 144 · see citing works

Agmatine-conjugated cytidine in a tRNA anticodon is essential for AUA decoding in archaea

Ikeuchi, Y., 木村聡, Numata, T., Nakamura, D., Yokogawa, T., Ogata, T., Wada, T., Suzuki, T., & Suzuki, T. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.323 · Cited by 141 · see citing works

Arabidopsis ADC genes involved in polyamine biosynthesis are essential for seed development

Urano, K., Hobo, T., & Shinozaki, K. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.01.048 · Cited by 140 · see citing works

The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor

Korolev, S., Ikeguchi, Y., Skarina, T., Beasley, S., Arrowsmith, C. H., Edwards, A. M., Joachimiak, A., Pegg, A. E., & Savchenko, A. V. (2001) · Nature Structural Biology · doi:10.1038/nsb737 · Cited by 138 · see citing works

Evolution and Multiplicity of Arginine Decarboxylases in Polyamine Biosynthesis and Essential Role in Bacillus subtilis Biofilm Formation

Burrell, M. R., Hanfrey, C. C., Murray, E. J., Stanley‐Wall, N. R., & Michael, A. J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.163154 · Cited by 135 · see citing works

Disruption of Putrescine Biosynthesis in Shewanella oneidensis Enhances Biofilm Cohesiveness and Performance in Cr(VI) Immobilization

Ding, Y., Peng, N., Du, Y., Ji, L., & Cao, B. (2013) · Applied and Environmental Microbiology · doi:10.1128/aem.03461-13 · Cited by 135 · see citing works

Alternative Spermidine Biosynthetic Route Is Critical for Growth of Campylobacter jejuni and Is the Dominant Polyamine Pathway in Human Gut Microbiota

Hanfrey, C. C., Pearson, B. M., Hazeldine, S. T., Lee, J., Gaskin, D. J. H., Woster, P. M., Phillips, M. A., & Michael, A. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.307835 · Cited by 132 · see citing works

Excretion of putrescine by the putrescine-ornithine antiporter encoded by the potE gene of Escherichia coli.

Kashiwagi, K., Miyamoto, S., Suzuki, F., Kobayashi, H., & Igarashi, K. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.10.4529 · Cited by 130 · see citing works

Agmatidine, a modified cytidine in the anticodon of archaeal tRNA Ile , base pairs with adenosine but not with guanosine

Mandal, D., Köhrer, C., Su, D., Russell, S. P., Krivos, K. L., Castleberry, C. M., Blum, P., Limbach, P. A., Söll, D. G., & RajBhandary, U. L. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914869107 · Cited by 130 · see citing works

Essential role of S‐adenosylmethionine decarboxylase in mouse embryonic development

Nishimura, K., Nakatsu, F., Kashiwagi, K., Ohno, H., Saito, T., & Igarashi, K. (2002) · Genes to Cells · doi:10.1046/j.1356-9597.2001.00494.x · 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

Reconstitution and Characterization of the Vibrio cholerae Vibriobactin Synthetase from VibB, VibE, VibF, and VibH

Keating, T. A., Marshall, C. G., & Walsh, C. T. (2000) · Biochemistry · doi:10.1021/bi0016523 · Cited by 126 · see citing works

A Single Enzyme Catalyses Formation of Trypanothione from Glutathione and Spermidine in Trypanosoma cruzi

Oza, S. L., Tétaud, E., Ariyanayagam, M. R., Warnon, S. S., & Fairlamb, A. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204403200 · Cited by 124 · see citing works

A New Class of N-Hydroxycinnamoyltransferases

Burhenne, K., Kristensen, B. K., & Rasmussen, S. K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213041200 · 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

Crystallographic Structure of a PLP-Dependent Ornithine Decarboxylase fromLactobacillus30a to 3.0 Å Resolution

Momany, C., Ernst, S. R., Ghosh, R., Chang, N., & Hackert, M. L. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0526 · Cited by 123 · see citing works

Abrogation of Upstream Open Reading Frame-mediated Translational Control of a Plant S-Adenosylmethionine Decarboxylase Results in Polyamine Disruption and Growth Perturbations

Hanfrey, C. C., Franceschetti, M., Mayer, M. J., Illingworth, C., & Michael, A. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206161200 · Cited by 121 · 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

Crystal Structure of Human Spermine Synthase

Wu, H., Min, J., Zeng, H., McCloskey, D. E., Ikeguchi, Y., Loppnau, P., Michael, A. J., Pegg, A. E., & Plotnikov, A. N. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710323200 · Cited by 118 · see citing works

Vibriobactin Biosynthesis in Vibrio cholerae: VibH Is an Amide Synthase Homologous to Nonribosomal Peptide Synthetase Condensation Domains

Keating, T. A., Marshall, C. G., & Walsh, C. T. (2000) · Biochemistry · doi:10.1021/bi001651a · Cited by 116 · see citing works

Identification of the putrescine biosynthetic genes in Pseudomonas aeruginosa and characterization of agmatine deiminase and N-carbamoylputrescine amidohydrolase of the arginine decarboxylase pathway

Nakada, Y., & Itoh, Y. (2003) · Microbiology · doi:10.1099/mic.0.26009-0 · Cited by 115 · see citing works

Characterization of monocot and dicot plant S-adenosyl-l-methionine decarboxylase gene families including identification in the mRNA of a highly conserved pair of upstream overlapping open reading frames

Franceschetti, M., Hanfrey, C. C., Scaramagli, S., Torrigiani, P., Bagni, N., Burtin, D., & Michael, A. J. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530403 · Cited by 113 · see citing works

Structure and Mechanism of Spermidine Synthases

Wu, H., Min, J., Ikeguchi, Y., Zeng, H., Dong, A., Loppnau, P., Pegg, A. E., & Plotnikov, A. N. (2007) · Biochemistry · doi:10.1021/bi602498k · Cited by 110 · see citing works

The Upstream Open Reading Frame of the mRNA Encoding S-Adenosylmethionine Decarboxylase Is a Polyamine-responsive Translational Control Element

Ruan, H., Shantz, L. M., Pegg, A. E., & Morris, D. R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.47.29576 · Cited by 104 · 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

Plant C-N Hydrolases and the Identification of a Plant N-Carbamoylputrescine Amidohydrolase Involved in Polyamine Biosynthesis

Piotrowski, M., Janowitz, T., & Kneifel, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m205699200 · Cited by 102 · see citing works

Identification and characterization of plant agmatine iminohydrolase, the last missing link in polyamine biosynthesis of plants

Janowitz, T., Kneifel, H., & Piotrowski, M. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00515-5 · Cited by 102 · 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

Degradation of Ornithine Decarboxylase by the 26S Proteasome

Murakami, Y., Matsufuji, S., Hayashi, S., Tanahashi, N., & Tanaka, K. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1706 · Cited by 96 · see citing works

Antizyme and antizyme inhibitor, a regulatory tango

Kahana, C. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0033-3 · Cited by 96 · see citing works

Surface-associated motility, a common trait of clinical isolates of Acinetobacter baumannii, depends on 1,3-diaminopropane

Skiebe, E., de Berardinis, V., Morczinek, P., Kerrinnes, T., Faber, F., Lepka, D., Hammer, B., Zimmermann, O., Ziesing, S., Wichelhaus, T. A., et al. (2012) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2012.03.003 · Cited by 94 · see citing works

In the Human Malaria Parasite Plasmodium falciparum,Polyamines Are Synthesized by a Bifunctional Ornithine Decarboxylase,S-Adenosylmethionine Decarboxylase

Müller, S., Da’dara, A. A., Lüersen, K., Wrenger, C., Gupta, R. D., Madhubala, R., & Walter, R. D. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.11.8097 · Cited by 91 · see citing works

Glutathionylspermidine Metabolism in Escherichia coli.

Bollinger, J. M., Jr., Kwon, D. S., Huisman, G. W., Kolter, R., & Walsh, C. T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.23.14031 · Cited by 89 · see citing works

Putrescine production via the ornithine decarboxylation pathway improves the acid stress survival of Lactobacillus brevis and is part of a horizontally transferred acid resistance locus

Romano, A., Ladero, V., Álvarez, M. A., & Lucas, P. (2014) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2014.01.009 · Cited by 88 · see citing works

Allosteric regulation of an essential trypanosome polyamine biosynthetic enzyme by a catalytically dead homolog

Willert, E. K., Fitzpatrick, R., & Phillips, M. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701111104 · Cited by 88 · 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

Spermine Synthesis Is Required for Normal Viability, Growth, and Fertility in the Mouse

Wang, X., Ikeguchi, Y., McCloskey, D. E., Nelson, P., & Pegg, A. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410471200 · Cited by 87 · see citing works

Genetic analysis of spermidine synthase from Leishmania donovani

Roberts, S. (2001) · Molecular and Biochemical Parasitology · doi:10.1016/s0166-6851(01)00293-6 · Cited by 84 · see citing works

Crystal structure of the NAD complex of human deoxyhypusine synthase: an enzyme with a ball-and-chain mechanism for blocking the active site

Liao, D., Wolff, E. C., Park, M. H., & Davies, D. R. (1998) · Structure · doi:10.1016/s0969-2126(98)00004-5 · Cited by 82 · see citing works

Polyamines Are Not Required for Aerobic Growth of Escherichia coli : Preparation of a Strain with Deletions in All of the Genes for Polyamine Biosynthesis

Chattopadhyay, M. K., Tabor, C. W., & Tabor, H. (2009) · Journal of Bacteriology · doi:10.1128/jb.00381-09 · Cited by 82 · see citing works

Expression of the cloned genes encoding the putrescine biosynthetic enzymes and methionine adenosyltransferase of Escherichia coli (speA, speB, speC and metK)

Boyle, S. M., Markham, G. D., Hafner, E. W., WRIGHT, J. M., Tabor, H., & Tabor, C. W. (1984) · Gene · doi:10.1016/0378-1119(84)90113-6 · Cited by 81 · see citing works

The Inhibitory Upstream Open Reading Frame from Mammalian S-Adenosylmethionine Decarboxylase mRNA Has a Strict Sequence Specificity in Critical Positions

Mize, G. J., Ruan, H., Low, J. J., & Morris, D. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.49.32500 · Cited by 80 · see citing works

Polyamine Oxidase 7 is a Terminal Catabolism-Type Enzyme in Oryza sativa and is Specifically Expressed in Anthers

Liu, T., Kim, D. W., Niitsu, M., Maeda, S., Watanabe, M., Kamio, Y., Berberich, T., & Kusano, T. (2014) · Plant and Cell Physiology · doi:10.1093/pcp/pcu047 · Cited by 80 · see citing works

Arginine Biosynthesis in Escherichia coli

Caldara, M., Dupont, G., Leroy, F., Goldbeter, A., Vuyst, L. D., & Cunin, R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705884200 · Cited by 78 · see citing works

The ornithine decarboxylase gene odc is required for alcaligin siderophore biosynthesis in Bordetella spp.: putrescine is a precursor of alcaligin

Brickman, T. J., & Armstrong, S. K. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.1.54-60.1996 · Cited by 78 · see citing works

S-Adenosylmethionine Decarboxylase fromLeishmania donovani

Roberts, S. C., Scott, J. R., Gasteier, J. E., Jiang, Y., Brooks, B., Jardim, A., Carter, N. S., Heby, O., & Ullman, B. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110118200 · Cited by 78 · see citing works

N1-Aminopropylagmatine, a New Polyamine Produced as a Key Intermediate in Polyamine Biosynthesis of an Extreme Thermophile, Thermus thermophilus

Ohnuma, M., Terui, Y., Tamakoshi, M., Mitome, H., Niitsu, M., Samejima, K., Kawashima, E., & Oshima, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413332200 · Cited by 76 · see citing works

Characterization of polyamine synthesis pathway in Bacillus subtilis 168

Sekowska, A., Bertin, P., & Danchin, A. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00979.x · Cited by 76 · see citing works

Palmitoylputrescine, an Antibiotic Isolated from the Heterologous Expression of DNA Extracted from Bromeliad Tank Water

Brady, S. F., & Clardy, J. (2004) · Journal of Natural Products · doi:10.1021/np0499766 · Cited by 75 · see citing works

Spermine is not essential for growth of Saccharomyces cerevisiae: identification of the SPE4 gene (spermine synthase) and characterization of a spe4 deletion mutant

Hamasaki‐Katagiri, N., Katagiri, Y., Tabor, C. W., & Tabor, H. (1998) · Gene · doi:10.1016/s0378-1119(98)00027-4 · Cited by 75 · see citing works

The diverse bacterial origins of the Arabidopsis polyamine biosynthetic pathway

Illingworth, C., Mayer, M. J., Elliott, K. A., Hanfrey, C. C., Walton, N. J., & Michael, A. J. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00756-7 · Cited by 73 · see citing works

Identification and analysis of a gene encoding L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase involved in the 1,3-diaminopropane production pathway in Acinetobacter baumannii

Ikai, H., & Yamamoto, S. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.16.5118-5125.1997 · Cited by 73 · see citing works

Functional Characterization of an Aminotransferase Required for Pyoverdine Siderophore Biosynthesis in Pseudomonas aeruginosa PAO1

Vandenende, C., Vlasschaert, M., & Seah, S. Y. K. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.17.5596-5602.2004 · Cited by 72 · see citing works

On the evolution of arginases and related enzymes

Ouzounis, C. A., & Kyrpides, N. C. (1994) · Journal of Molecular Evolution · doi:10.1007/bf00178255 · Cited by 71 · see citing works

Spermidine biosynthesis in Saccharomyces cerevisiae: Polyaminerequirement of a null mutant of the SPE3 gene (spermidine synthase)

Hamasaki‐Katagiri, N., Tabor, C. W., & Tabor, H. (1997) · Gene · doi:10.1016/s0378-1119(96)00660-9 · Cited by 71 · see citing works

Norspermidine Is Not a Self-Produced Trigger for Biofilm Disassembly

Hobley, L., Kim, S. H., Maezato, Y., Wyllie, S., Fairlamb, A. H., Stanley‐Wall, N. R., & Michael, A. J. (2014) · Cell · doi:10.1016/j.cell.2014.01.012 · Cited by 70 · see citing works

Cell Cycle Arrest in Archaea by the Hypusination Inhibitor N 1 -Guanyl-1,7-Diaminoheptane

Jansson, B. P. M., Malandrin, L., & Johansson, H. E. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.4.1158-1161.2000 · Cited by 69 · see citing works

Characterization of monocot and dicot plant S-adenosyl-l-methionine decarboxylase gene families including identification in the mRNA of a highly conserved pair of upstream overlapping open reading frames

Franceschetti, M., Hanfrey, C. C., Scaramagli, S., et al. (2001) · Biochemical Journal · doi:10.1042/bj3530403 · Cited by 68 · see citing works

Regulated Expression of an Essential Allosteric Activator of Polyamine Biosynthesis in African Trypanosomes

Willert, E. K., & Phillips, M. A. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000183 · Cited by 66 · see citing works

Dual Biosynthesis Pathway for Longer-Chain Polyamines in the Hyperthermophilic Archaeon Thermococcus kodakarensis

Morimoto, N., Fukuda, W., Nakajima, N., Masuda, T., Terui, Y., Kanai, T., Oshima, T., Imanaka, T., & Fujiwara, S. (2010) · Journal of Bacteriology · doi:10.1128/jb.00279-10 · Cited by 63 · see citing works

The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 Å resolution reveals a novel fold

Ekstrom, J. L., Mathews, I. I., Stanley, B. A., Pegg, A. E., & Ealick, S. E. (1999) · Structure · doi:10.1016/s0969-2126(99)80074-4 · Cited by 62 · see citing works

Putrescine Biosynthesis in Escherichia coli

Morris, D. R., & Koffron, K. L. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63510-0 · Cited by 61 · see citing works

Evolution and Multifarious Horizontal Transfer of an Alternative Biosynthetic Pathway for the Alternative Polyamine sym-Homospermidine

Shaw, F. L., Elliott, K. A., Kinch, L. N., Fuell, C., Phillips, M. A., & Michael, A. J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.107219 · Cited by 61 · see citing works

Purification and properties of agmatine ureohydrolyase, a putrescine biosynthetic enzyme in Escherichia coli

Satishchandran, C., & Boyle, S. M. (1986) · Journal of Bacteriology · doi:10.1128/jb.165.3.843-848.1986 · Cited by 60 · see citing works

Formation of a Distinctive Complex between the Inducible Bacterial Lysine Decarboxylase and a Novel AAA+ ATPase

Snider, J. D., Gutsche, I., Lin, M., Baby, S., Cox, B., Butland, G. P., Greenblatt, J., Emili, A., & Houry, W. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m511172200 · Cited by 60 · see citing works

Evolution of a novel lysine decarboxylase in siderophore biosynthesis

Burrell, M. R., Hanfrey, C. C., Kinch, L. N., Elliott, K. A., & Michael, A. J. (2012) · Molecular Microbiology · doi:10.1111/j.1365-2958.2012.08208.x · Cited by 59 · see citing works

Antizyme inhibitor: mysterious modulator of cell proliferation

Loizides‐Mangold, U. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5583-4 · Cited by 59 · see citing works

Crystal Structure of the Acid-Induced Arginine Decarboxylase from Escherichia coli : Reversible Decamer Assembly Controls Enzyme Activity

Andréll, J., Hicks, M. G., Palmer, T., Carpenter, E. P., Iwata, S., & Maher, M. J. (2009) · Biochemistry · doi:10.1021/bi900075d · Cited by 58 · 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

Phylogenetic Diversity and the Structural Basis of Substrate Specificity in the β/α-Barrel Fold Basic Amino Acid Decarboxylases

Lee, J., Michael, A. J., Martynowski, D., Goldsmith, E. J., & Phillips, M. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704066200 · Cited by 56 · see citing works

Gene Cloning and Molecular Characterization of Lysine Decarboxylase from Selenomonas ruminantium Delineate Its Evolutionary Relationship to Ornithine Decarboxylases from Eukaryotes

Takatsuka, Y., Yamaguchi, Y., Ono, M., & Kamio, Y. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.23.6732-6741.2000 · Cited by 56 · see citing works

Methanococcus jannaschii Uses a Pyruvoyl-dependent Arginine Decarboxylase in Polyamine Biosynthesis

Graham, D. E., Xu, H., & White, R. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203467200 · Cited by 54 · see citing works

Enzymes of agmatine degradation and the control of their synthesis in Streptococcus faecalis

Simon, J. P., & Stalon, V. (1982) · Journal of Bacteriology · doi:10.1128/jb.152.2.676-681.1982 · Cited by 53 · see citing works

Validation of spermidine synthase as a drug target in African trypanosomes

Taylor, M. C., Kaur, H., Blessington, B., Kelly, J. M., & Wilkinson, S. R. (2007) · Biochemical Journal · doi:10.1042/bj20071185 · Cited by 53 · see citing works

Decarboxylated S-adenosylmethionine in mammalian cells.

Hibasami, H., Hoffman, J. L., & Pegg, A. E. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43623-x · Cited by 52 · see citing works

Detection of Norspermidine and Norspermine in Medicago sativa L. (Alfalfa)

Rodríguez‐Garay, B., Phillips, G. C., & Kuehn, G. D. (1989) · PLANT PHYSIOLOGY · doi:10.1104/pp.89.2.525 · Cited by 52 · see citing works

Putrescine Aminopropyltransferase Is Responsible for Biosynthesis of Spermidine, Spermine, and Multiple Uncommon Polyamines in Osmotic Stress-Tolerant Alfalfa

Bagga, S., Rochford, J., Klaene, Z., Kuehn, G. D., & Phillips, G. C. (1997) · PLANT PHYSIOLOGY · doi:10.1104/pp.114.2.445 · Cited by 50 · see citing works

Biosynthetic arginine decarboxylase in Escherichia coli is synthesized as a precursor and located in the cell envelope

Buch, J.-M., & Boyle, S. M. (1985) · Journal of Bacteriology · doi:10.1128/jb.163.2.522-527.1985 · Cited by 49 · see citing works

Analysis and sequence of the speB gene encoding agmatine ureohydrolase, a putrescine biosynthetic enzyme in Escherichia coli

Szumanski, M. B., & Boyle, S. M. (1990) · Journal of Bacteriology · doi:10.1128/jb.172.2.538-547.1990 · Cited by 49 · see citing works

Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily

Ahn, H. J., Kim, K. H., Lee, J., Ha, J.-Y., Lee, H. H., Kim, D., Yoon, H., Kwon, A., & Suh, S. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409246200 · Cited by 49 · see citing works

Allosteric Activation of Trypanosomatid Deoxyhypusine Synthase by a Catalytically Dead Paralog

Nguyen, S., Jones, D. C., Wyllie, S., Fairlamb, A. H., & Phillips, M. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.461137 · Cited by 49 · see citing works

Identification of a Novel Aminopropyltransferase Involved in the Synthesis of Branched-Chain Polyamines in Hyperthermophiles

Okada, K., Hidese, R., Fukuda, W., Niitsu, M., Takao, K., Horai, Y., Umezawa, N., Higuchi, T., Oshima, T., Yoshikawa, Y., et al. (2014) · Journal of Bacteriology · doi:10.1128/jb.01515-14 · Cited by 48 · see citing works

RNA Interference-Mediated Silencing of Ornithine Decarboxylase and Spermidine Synthase Genes in Trypanosoma brucei Provides Insight into Regulation of Polyamine Biosynthesis

Xiao, Y., McCloskey, D. E., & Phillips, M. A. (2009) · Eukaryotic Cell · doi:10.1128/ec.00047-09 · Cited by 48 · see citing works

Cloning and Characterization of the Two Enzymes Responsible for Trypanothione Biosynthesis in Crithidia fasciculata

Tétaud, E., Manai, F., Barrett, M. P., Nadeau, K. C., Walsh, C. T., & Fairlamb, A. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.31.19383 · Cited by 47 · see citing works

Origin of the Putrescine-Producing Ability of the Coagulase-Negative BacteriumStaphylococcus epidermidis2015B

Coton, E., Mulder, N. L., Coton, M., Pochet, S., Trip, H., & Lolkema, J. S. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.00441-10 · Cited by 47 · see citing works

Manganese Is Essential for Catalytic Activity ofEscherichia coliAgmatinase

Carvajal, N., López, V., Salas, M., Uribe, E. A., Herrera, P., & Cerpa, J. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0709 · Cited by 46 · see citing works

Identification of essential active-site residues in ornithine decarboxylase of Nicotiana glutinosa decarboxylating both l-ornithine and l-lysine

Yong-Sun, L. E. E., & Young-Dong, C. H. O. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3600657 · Cited by 45 · see citing works

The Essential Role of Spermidine in Growth of Agrobacterium tumefaciens Is Determined by the 1,3-Diaminopropane Moiety

Kim, S. H., Wang, Y., Хомутов, М. А., Khomutov, A. R., Fuqua, C., & Michael, A. J. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00893 · Cited by 45 · see citing works

A New Pathway for the Biosynthesis of Spermidine

TAIT, G. H. (1976) · Biochemical Society Transactions · doi:10.1042/bst0040610 · Cited by 44 · see citing works

Purification, Molecular Cloning and Expression in Escherichia coli of Homospermidine Synthase from Rhodopseudomonas viridis

Tholl, D., Ober, D., Martin, W. F., Kellermann, J., & Hartmann, T. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0373h.x · Cited by 40 · see citing works

The Formation of Homospermidine by an Enzyme from Rhodopseudomonas viridis

TAIT, G. H. (1979) · Biochemical Society Transactions · doi:10.1042/bst0070199 · Cited by 40 · see citing works

Pyruvoyl-Dependent Arginine Decarboxylase from Methanococcus jannaschii

Tolbert, W. D., Graham, D. E., White, R. H., & Ealick, S. E. (2003) · Structure · doi:10.1016/s0969-2126(03)00026-1 · Cited by 39 · see citing works

Protein S-Thiolation by Glutathionylspermidine (Gsp)

Chiang, B., Chen, T.-C., Pai, C., Chou, C., Chen, H.-H., Ko, T., Hsu, W.-H., Chang, C.-Y., Wu, W.-F., Wang, A. H. ‐., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.133363 · Cited by 39 · see citing works

Chlorella Virus PBCV-1 Encodes a Functional Homospermidine Synthase

Kaiser, A. E., Vollmert, M., Tholl, D., Graves, M. V., Gurnon, J. R., Xing, W., Lisec, A. D., Nickerson, K. W., & Etten, J. L. V. (1999) · Virology · doi:10.1006/viro.1999.9972 · Cited by 38 · see citing works

S‐adenosylmethionine decarboxylase of Bacillus subtilis is closely related to archaebacterial counterparts

Sekowska, A., Coppée, J., Caër, J. L., Martin‐Verstraete, I., & Danchin, A. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01930.x · Cited by 38 · see citing works

Evolution of the key alkaloid enzyme putrescine N-methyltransferase from spermidine synthase

Junker, A., Fischer, J., Sichhart, Y., Brandt, W., & Dräger, B. (2013) · Frontiers in Plant Science · doi:10.3389/fpls.2013.00260 · Cited by 37 · see citing works

Evolution of Enzymatic Activities in the Enolase Superfamily: Stereochemically Distinct Mechanisms in Two Families of cis,cis-Muconate Lactonizing Enzymes

Sakai, A., Fedorov, A. A., Fedorov, E. V., Schnoes, A. M., Glasner, M. E., Brown, S. D., Rutter, M. E., Bain, K. T., Chang, S., Gheyi, T., et al. (2009) · Biochemistry · doi:10.1021/bi802277h · Cited by 37 · see citing works

Petrobactin biosynthesis: AsbB catalyzes condensation of spermidine with N8-citryl-spermidine and its N1-(3,4-dihydroxybenzoyl) derivative

Oves‐Costales, D., Kadi, N., Fogg, M. J., Song, L., Wilson, K. S., & Challis, G. L. (2008) · Chemical Communications · doi:10.1039/b809353a · Cited by 37 · see citing works

Spermidine Biosynthesis and Transport Modulate Pneumococcal Autolysis

Potter, A. J., & Paton, J. C. (2014) · Journal of Bacteriology · doi:10.1128/jb.01981-14 · Cited by 37 · see citing works

Molecular Cloning of a cDNA Encoding Human Spermine Synthase

Korhonen, V., Halmekytö, M., Kauppinen, L., Myöhänen, S., Wahlfors, J., Keinänen, T. A., Hyvönen, T., Alhonen, L. I., Eloranta, T. O., & Jänne, J. (1995) · DNA and Cell Biology · doi:10.1089/dna.1995.14.841 · Cited by 35 · see citing works

Crenarchaeal Arginine Decarboxylase Evolved from an S-Adenosylmethionine Decarboxylase Enzyme

Giles, T. N., & Graham, D. E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802674200 · Cited by 35 · see citing works

A new model for disruption of the ornithine decarboxylase gene, SPE1, in Saccharomyces cerevisiae exhibits growth arrest and genetic instability at the MAT locus

Schwartz, B., Hittelman, A. B., Daneshvar, L., Basu, H. S., Marton, L. J., & Feuerstein, B. G. (1995) · Biochemical Journal · doi:10.1042/bj3120083 · Cited by 34 · see citing works

Distinct Difference in the Polyamine Compositions of Bryophyta and Pteridophyta1

Hamana, K., & Matsuzaki, S. (1985) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a135216 · Cited by 34 · see citing works

Evolutionary Links as Revealed by the Structure of Thermotoga maritima S-Adenosylmethionine Decarboxylase

Toms, A. V., Kinsland, C. L., McCloskey, D. E., Pegg, A. E., & Ealick, S. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403369200 · Cited by 34 · see citing works

Molecular machines encoded by bacterially-derived multi-domain gene fusions that potentially synthesize,N-methylate and transfer long chain polyamines in diatoms

Michael, A. J. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.07.038 · Cited by 34 · see citing works

Deoxyhypusine Modification of Eukaryotic Translation Initiation Factor 5A (eIF5A) Is Essential for Trypanosoma brucei Growth and for Expression of Polyprolyl-containing Proteins

Nguyen, S., Leija, C., Kinch, L. N., Regmi, S., Li, Q., Grishin, N. V., & Phillips, M. A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.656785 · Cited by 33 · see citing works

A New Polyamine 4-Aminobutylcadaverine

Fujihara, S., Abe, H., & Yoneyama, T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.17.9932 · Cited by 32 · see citing works

Evolution of Substrate Specificity within a Diverse Family of β/α-Barrel-fold Basic Amino Acid Decarboxylases

Deng, X., Lee, J., Michael, A. J., Tomchick, D. R., Goldsmith, E. J., & Phillips, M. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.121137 · Cited by 32 · see citing works

Horizontal gene transfer and archaeal origin of deoxyhypusine synthase homologous genes in bacteria

Brochier‐Armanet, C., López‐García, P., & Moreira, D. (2004) · Gene · doi:10.1016/j.gene.2004.01.018 · Cited by 32 · see citing works

Crystal Structures and Enzymatic Properties of a Triamine/Agmatine Aminopropyltransferase from Thermus thermophilus

Ohnuma, M., Ganbe, T., Terui, Y., Niitsu, M., Sato, T., Tanaka, N., Tamakoshi, M., Samejima, K., Kumasaka, T., & Oshima, T. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.03.025 · Cited by 29 · see citing works

Distribution of norspermidine as a cellular polyamine within micro green algae including non-photosynthetic achlorophyllous Polytoma, Polytomella, Prototheca and Helicosporidium

Hamana, K., Aizaki, T., Arai, E., Saito, A., 内方, 薫., & Ohnishi, H. (2004) · The Journal of General and Applied Microbiology · doi:10.2323/jgam.50.289 · Cited by 28 · see citing works

Biosynthesis of long‐chain polyamines by crenarchaeal polyamine synthases from Hyperthermus butylicus and Pyrobaculum aerophilum

Knott, J. M. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.10.014 · Cited by 27 · see citing works

Identification of essential active-site residues in ornithine decarboxylase of Nicotiana glutinosa decarboxylating both l-ornithine and l-lysine

Yong-Sun, L. E. E., & Young-Dong, C. H. O. (2001) · Biochemical Journal · doi:10.1042/bj3600657 · Cited by 27 · see citing works

Comprehensive Structural Characterization of the Bacterial Homospermidine Synthase–an Essential Enzyme of the Polyamine Metabolism

Krossa, S., Faust, A., Ober, D., & Scheidig, A. J. (2016) · Scientific Reports · doi:10.1038/srep19501 · Cited by 26 · see citing works

The polyamine oxidase from lycophyteSelaginella lepidophylla (SelPAO5), unlike that of angiosperms, back‐converts thermospermine to norspermidine

Sagor, G. H. M., Inoue, M., Kim, D. W., Kojima, S., Niitsu, M., Berberich, T., & Kusano, T. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.08.045 · Cited by 25 · see citing works

Evidence for the presence of a novel biosynthetic pathway for norspermidine in Vibrio

Yamamoto, S., Hamanaka, K., Suemoto, Y., Ono, B., & Shinoda, S. (1986) · Canadian Journal of Microbiology · doi:10.1139/m86-021 · Cited by 25 · see citing works

X-ray Structure of Paramecium bursaria Chlorella Virus Arginine Decarboxylase: Insight into the Structural Basis for Substrate Specificity

Shah, R., Akella, R., Goldsmith, E. J., & Phillips, M. A. (2007) · Biochemistry · doi:10.1021/bi6023447 · Cited by 25 · see citing works

S -Adenosylmethionine Decarboxylase from the Archaeon Methanococcus jannaschii : Identification of a Novel Family of Pyruvoyl Enzymes

Kim, A. D., Graham, D. E., Seeholzer, S. H., & Markham, G. D. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.23.6667-6672.2000 · Cited by 25 · see citing works

Characterization of an Acid-Dependent Arginine Decarboxylase Enzyme from Chlamydophila pneumoniae

Giles, T. N., & Graham, D. E. (2007) · Journal of Bacteriology · doi:10.1128/jb.00772-07 · Cited by 24 · see citing works

Purification and some properties of carboxynorspermidine synthase participating in a novel biosynthetic pathway for norspermidine in Vibrio alginolyticus

Nakao, H., Shinoda, S., & Yamamoto, S. (1991) · Journal of General Microbiology · doi:10.1099/00221287-137-7-1737 · Cited by 24 · see citing works

Mechanistic Studies of Agmatine Deiminase from Multiple Bacterial Species

Jones, J. E., Dreyton, C. J., Flick, H., Causey, C. P., & Thompson, P. R. (2010) · Biochemistry · doi:10.1021/bi101405y · Cited by 22 · see citing works

Independent evolutionary origins of functional polyamine biosynthetic enzyme fusions catalysingde novodiamine to triamine formation

Green, R., Hanfrey, C. C., Elliott, K. A., McCloskey, D. E., Wang, X., Kanugula, S., Pegg, A. E., & Michael, A. J. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07757.x · Cited by 22 · see citing works

Evidence for the occurrence of polyamine oxidase in the dicotyledonous plant Medicago sativa L. (alfalfa)

Bagga, S., Dharma, A., Phillips, G., & Kuehn, G. D. (1991) · Plant Cell Reports · doi:10.1007/bf00232509 · Cited by 21 · see citing works

Enantioselective desymmetrisation of citric acid catalysed by the substrate-tolerant petrobactin biosynthetic enzyme AsbA

Oves‐Costales, D., Song, L., & Challis, G. L. (2009) · Chemical Communications · doi:10.1039/b823147h · Cited by 20 · see citing works

A Comprehensive Analysis of the Importance of Translation Initiation Factors for Haloferax volcanii Applying Deletion and Conditional Depletion Mutants

Gäbel, K., Schmitt, J., Schulz, S., Näther, D. J., & Soppa, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077188 · Cited by 20 · see citing works

Occurrence of aminopropylcadaverine and its aminopropyl derivatives aminopentylnorspermidine andN,N′ -bis(3-aminopropyl)cadaverine inHalococcus acetoinfaciens

Hamana, K., Niitsu, M., Samejima, K., & Matsuzaki, S. (1988) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1988.tb02915.x · Cited by 20 · see citing works

Cloning and expression of a cDNA encoding homospermidine synthase from Senecio vulgaris (Asteraceae) in Escherichia coli

Kaiser, A. E. (1999) · The Plant Journal · doi:10.1046/j.1365-313x.1999.00509.x · Cited by 20 · see citing works

Cloning and expression in Escherichia coli of the gene encoding a novel L-2,4-diaminobutyrate decarboxylase of Acinetobacter baumannii

Ikai, H., & Yamamoto, S. (1994) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1994.tb07288.x · Cited by 19 · see citing works

Structures of bacterial biosynthetic arginine decarboxylases

Forouhar, F., Lew, S., Seetharaman, J., Xiao, R., Acton, T., Montelione, G. T., & Tong, L. (2010) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309110040649 · Cited by 18 · see citing works

Different polyamine pathways from bacteria have replaced eukaryotic spermidine biosynthesis in ciliates T etrahymena thermophila and P aramecium tetaurelia

Li, B., Kim, S. H., Zhang, Y., Hanfrey, C. C., Elliott, K. A., Ealick, S. E., & Michael, A. J. (2015) · Molecular Microbiology · doi:10.1111/mmi.13066 · Cited by 17 · see citing works

Outer and Inner Membrane Proteins Compose an Arginine-Agmatine Exchange System inChlamydophila pneumoniae

Smith, C. B., & Graham, D. E. (2008) · Journal of Bacteriology · doi:10.1128/jb.00652-08 · Cited by 15 · see citing works

A New Subfamily of Agmatinases Present in Methanogenic Archaea Is Fe(II) Dependent

Miller, D., Xu, H., & White, R. H. (2012) · Biochemistry · doi:10.1021/bi300039f · Cited by 15 · see citing works

Cloning and nucleotide sequence of the carboxynorspermidine decarboxylase gene from Vibrio alginolyticus

Yamamoto, S., Sugahara, T., Tougou, K., & Shinoda, S. (1994) · Microbiology · doi:10.1099/13500872-140-11-3117 · Cited by 10 · see citing works

Primary structure of the speC gene encoding biosynthetic ornithine decarboxylase in Escherichia coli

Boyle, S. M., Barroso, L. A., Moore, R. C., WRIGHT, J. M., & Patel, T. (1994) · Gene · doi:10.1016/0378-1119(94)90648-3 · Cited by 10 · see citing works

Binding-competent states for L-arginine in E. coli arginine repressor apoprotein

Pandey, S. K., Řeha, D., Zayats, V., Melicherčík, M., Carey, J., & Ettrich, R. H. (2014) · Journal of Molecular Modeling · doi:10.1007/s00894-014-2330-5 · Cited by 7 · see citing works

Occurrence of aminopropylcadaverine and its aminopropyl derivatives aminopentylnorspermidine and N, N′ -bis(3-aminopropyl)cadaverine in Halococcus acetoinfaciens

Hamana, K. (1988) · FEMS Microbiology Letters · doi:10.1016/0378-1097(88)90214-5 · Cited by 6 · 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

Regulation of Intestinal Barrier Function by Microbial Metabolites

Ghosh, S., Whitley, C. S., Haribabu, B., & Jala, V. R. (2021) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2021.02.007 · Cited by 835 · see citing works

Modifications in Organic Acid Profiles During Fruit Development and Ripening: Correlation or Causation?

Batista‐Silva, W., Nascimento, V. L., Medeiros, D. B., Nunes‐Nesi, A., Ribeiro, D. M., Zsögön, A., & Araújo, W. L. (2018) · Frontiers in Plant Science · doi:10.3389/fpls.2018.01689 · Cited by 364 · 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

Alterations of gut microbiome in autoimmune hepatitis

Wei, Y., Li, Y., Li, Y., Sun, C., Miao, Q., Wang, Q., Xiao, X., Lian, M., Li, B., Chen, Y., et al. (2019) · Gut · doi:10.1136/gutjnl-2018-317836 · Cited by 306 · see citing works

The scaffold-forming steps of plant alkaloid biosynthesis

Lichman, B. R. (2020) · Natural Product Reports · doi:10.1039/d0np00031k · Cited by 247 · 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

Retapamulin-Assisted Ribosome Profiling Reveals the Alternative Bacterial Proteome

Meydan, S., Marks, J., Klepacki, D., Sharma, V., Baranov, P. V., Firth, A. E., Margus, T., Kefi, A., Vázquez-Laslop, N., & Mankin, A. S. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.02.017 · Cited by 184 · see citing works

Polyamine function in archaea and bacteria

Michael, A. J. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.tm118.005670 · Cited by 190 · see citing works

Plant growth promoting rhizobacteria isolated from halophytes and drought-tolerant plants: genomic characterisation and exploration of phyto-beneficial traits

Λεοντίδου, Κ., Genitsaris, S., Papadopoulou, A., Kamou, N. N., Bosmali, I., Matsi, T., Madesis, P. B., Vokou, D., Karamanoli, K., & Mellidou, Ι. (2020) · Scientific Reports · doi:10.1038/s41598-020-71652-0 · Cited by 176 · see citing works

Metabolomics of tomato xylem sap during bacterial wilt reveals Ralstonia solanacearum produces abundant putrescine, a metabolite that accelerates wilt disease

Lowe‐Power, T. M., Hendrich, C. G., von Roepenack‐Lahaye, E., Li, B., Wu, D., Mitra, R. M., Dalsing, B. L., Ricca, P., Naidoo, J., Cook, D. E., et al. (2017) · Environmental Microbiology · doi:10.1111/1462-2920.14020 · Cited by 162 · see citing works

Effects of Fish n-3 PUFAs on Intestinal Microbiota and Immune System

Parolini, C. (2019) · Marine Drugs · doi:10.3390/md17060374 · Cited by 155 · see citing works

Pollen development at high temperature and role of carbon and nitrogen metabolites

Santiago, J. P., & Sharkey, T. D. (2019) · Plant Cell & Environment · doi:10.1111/pce.13576 · Cited by 135 · see citing works

Arginase 2 Suppresses Renal Carcinoma Progression via Biosynthetic Cofactor Pyridoxal Phosphate Depletion and Increased Polyamine Toxicity

Ochocki, J. D., Khare, S., Hess, M., Ackerman, D., Qiu, B., Daisak, J. I., Worth, A. J., Lin, N., Lee, P., Xie, H. J., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.04.009 · Cited by 127 · see citing works

Microbial Metabolites, Postbiotics, and Intestinal Epithelial Function

Mayorgas, A., Dotti, I., & Salas, A. (2020) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.202000188 · Cited by 118 · see citing works

The role of polyamine metabolism in cellular function and physiology

Schibalski, R. S., Shulha, A. S., Tsao, B. P., Palygin, O., & Ilatovskaya, D. V. (2024) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00074.2024 · Cited by 107 · see citing works

Diverse Functions of Polyamines in Virus Infection

Firpo, M. R., & Mounce, B. C. (2020) · Biomolecules · doi:10.3390/biom10040628 · Cited by 78 · 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

Small Is Mighty—Chemical Communication Systems inPseudomonas aeruginosa

Ahator, S. D., & Zhang, L. (2019) · Annual Review of Microbiology · doi:10.1146/annurev-micro-020518-120044 · Cited by 73 · see citing works

Comprehensive analysis of polyamine transport and biosynthesis in the dominant human gut bacteria: Potential presence of novel polyamine metabolism and transport genes

Sugiyama, Y., Nara, M., Sakanaka, M., Gotoh, A., Kitakata, A., Okuda, S., & Kurihara, S. (2017) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.10.015 · Cited by 65 · see citing works

Nutritional Modulation of Immune and Central Nervous System Homeostasis: The Role of Diet in Development of Neuroinflammation and Neurological Disease

Estrada, J. A., & Contreras, I. (2019) · Nutrients · doi:10.3390/nu11051076 · Cited by 65 · see citing works

Engineering yeast metabolism for the discovery and production of polyamines and polyamine analogues

Qin, J., Krivoruchko, A., Ji, B., Chen, Y., Kristensen, M., Özdemir, E., Keasling, J. D., Jensen, M. K., & Nielsen, J. (2021) · Nature Catalysis · doi:10.1038/s41929-021-00631-z · Cited by 63 · see citing works

The Spermine Synthase OsSPMS1 Regulates Seed Germination, Grain Size, and Yield

Tao, Y., Wang, J., Miao, J., Chen, J., Wu, S., Zhu, J., Zhang, D., Gu, H., Cui, H., Shi, S. Y., et al. (2018) · PLANT PHYSIOLOGY · doi:10.1104/pp.18.00877 · Cited by 58 · see citing works

The Biology of Glial Cells and Their Complex Roles in Alzheimer’s Disease: New Opportunities in Therapy

Nirzhor, S., Khan, R., & Neelotpol, S. (2018) · Biomolecules · doi:10.3390/biom8030093 · Cited by 54 · see citing works

Citrus Polyamines: Structure, Biosynthesis, and Physiological Functions

Killiny, N., & Nehela, Y. (2020) · Plants · doi:10.3390/plants9040426 · Cited by 54 · see citing works

Polyamines in protozoan pathogens

Phillips, M. A. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.tm118.003342 · Cited by 54 · see citing works

Diversity, properties and functions of bacterial arginases

Hernández, V. M., Ide, A. A., & Dunn, M. F. (2021) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuab034 · Cited by 55 · see citing works

Spermidine promotes Bacillus subtilis biofilm formation by activating expression of the matrix regulator slrR

Hobley, L., Li, B., Wood, J. L., Kim, S. H., Naidoo, J., Ferreira, A. S., Хомутов, М. А., Khomutov, A. R., Stanley‐Wall, N. R., & Michael, A. J. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.789644 · Cited by 53 · see citing works

The Biosynthesis and Functions of Polyamines in the Interaction of Plant Growth-Promoting Rhizobacteria with Plants

Dunn, M. F., & Becerra-Rivera, V. A. (2023) · Plants · doi:10.3390/plants12142671 · Cited by 49 · see citing works

Evolution of biosynthetic diversity

Michael, A. J. (2017) · Biochemical Journal · doi:10.1042/bcj20160823 · Cited by 49 · see citing works

Research progress on the microbial metabolism and transport of polyamines and their roles in animal gut homeostasis

Zhang, C., Zhen, Y., Weng, Y., Lin, J., Xu, X., Ma, J., Zhong, Y., & Wang, M. (2025) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-025-01193-x · Cited by 48 · see citing works

TGase regulates salt stress tolerance through enhancing bound polyamines-mediated antioxidant enzymes activity in tomato

Zhong, M., Song, R., Wang, Y., Shu, S., Sun, J., & Guo, S. (2020) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2020.104191 · Cited by 48 · see citing works

Polyamine Metabolism and Oxidative Protein Folding in the ER as ROS-Producing Systems Neglected in Virology

Smirnova, O. A., Bartosch, B., Zakirova, N. F., Kochetkov, S. N., & Ivanov, A. V. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19041219 · Cited by 43 · see citing works

Production of Norspermidine Contributes to Aminoglycoside Resistance in pmrAB Mutants of Pseudomonas aeruginosa

Bolard, A., Schniederjans, M., Häußler, S., Triponney, P., Valot, B., Plésiat, P., & Jeannot, K. (2019) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01044-19 · Cited by 43 · see citing works

Polyamine Deacetylase Structure and Catalysis: Prokaryotic Acetylpolyamine Amidohydrolase and Eukaryotic HDAC10

Shinsky, S. A., & Christianson, D. W. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00079 · Cited by 41 · see citing works

Production and Excretion of Polyamines To Tolerate High Ammonia, a Case Study on Soil Ammonia-Oxidizing Archaeon “ Candidatus Nitrosocosmicus agrestis”

Liu, L., Liu, M., Jiang, Y., Lin, W., & Luo, J. (2021) · mSystems · doi:10.1128/msystems.01003-20 · Cited by 42 · see citing works

Pyridoxal-5′-phosphate-dependent alkyl transfer in nucleoside antibiotic biosynthesis

Cui, Z., Overbay, J., Wang, X., Liu, X. F., Zhang, Y., Bhardwaj, M., Lemke, A., Wiegmann, D., Niro, G., Thorson, J. S., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0548-3 · Cited by 41 · see citing works

Reprioritization of biofilm metabolism is associated with nutrient adaptation and long-term survival of Haemophilus influenzae

Harrison, A., Hardison, R. L., Wallace, R. M., Fitch, J., Heimlich, D. R., Bryan, M. O., Dubois, L. G., John‐Williams, L. S., Sebra, R., White, P., et al. (2019) · npj Biofilms and Microbiomes · doi:10.1038/s41522-019-0105-6 · Cited by 40 · see citing works

Integration of metabolomics and existing omics data reveals new insights into phytoplasma-induced metabolic reprogramming in host plants

Tan, Y. Y., Li, Q., Zhao, Y., Wei, H., Wang, J., Baker, C. J., Liu, Q., & Wei, W. (2021) · PLoS ONE · doi:10.1371/journal.pone.0246203 · Cited by 39 · see citing works

Silicon-driven approaches to salinity stress tolerance: Mechanisms, uptake dynamics, and microbial transformations

Manimaran, G., Selvi, D. T., Subramanium, T., Anandham, R., Alagarsamy, S., James, P., Selvamani, S., Perumal, D., Veerappan, M., Arunan, Y. E., et al. (2025) · Plant Stress · doi:10.1016/j.stress.2025.100825 · Cited by 36 · see citing works

Insights into Tissue-specific Specialized Metabolism in Tieguanyin Tea Cultivar by Untargeted Metabolomics

Chen, S., Lin, J. H., Liu, H., Gong, Z., Wang, X., Li, M., Aharoni, A., Yang, Z., & Yu, X. (2018) · Molecules · doi:10.3390/molecules23071817 · Cited by 36 · see citing works

Exogenously Applied Polyamines Reduce Reactive Oxygen Species, Enhancing Cell Division and the Shoot Regeneration from Brassica oleracea L. var. capitata Protoplasts

Kiełkowska, A., & Adamus, A. (2021) · Agronomy · doi:10.3390/agronomy11040735 · Cited by 36 · see citing works

The role of the symbiotic microecosystem in cancer: gut microbiota, metabolome, and host immunome

Xue, X., Li, R., Chen, Z., Li, G., Liu, B., Guo, S., Yue, Q., Yang, S., Xie, L., Zhang, Y., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1235827 · Cited by 36 · see citing works

Introduction to the Thematic Minireview Series: Sixty plus years of polyamine research

Pegg, A. E. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.tm118.006291 · Cited by 35 · see citing works

Alterations of commensal microbiota are associated with pancreatic cancer

Chen, T., Li, X., Li, G., Liu, Y., Huang, X., Ma, W., Qian, C., Jie, G., Wang, S., Qin, Q., et al. (2023) · The International Journal of Biological Markers · doi:10.1177/03936155231166721 · Cited by 32 · see citing works

Uncovering de novo polyamine biosynthesis in the gut microbiome and its alteration in inflammatory bowel disease

Li, X., Xia, X. L., Wang, S., Wu, B., Zhou, Y., & Deng, P. (2025) · Gut Microbes · doi:10.1080/19490976.2025.2464225 · Cited by 34 · see citing works

An extendable all-in-one injection twin derivatization LC-MS/MS strategy for the absolute quantification of multiple chemical-group-based submetabolomes

Huang, Y., Jiao, Y., Gao, Y., Zhang, P., Huang, W., Liu, Y., Huang, Y., Tian, Y., Wan, J., Zhang, Z., et al. (2019) · Analytica Chimica Acta · doi:10.1016/j.aca.2019.02.001 · Cited by 34 · see citing works

Advanced pathway engineering for phototrophic putrescine production

Freudenberg, R. A., Wittemeier, L., Einhaus, A., Baier, T., & Kruse, O. (2022) · Plant Biotechnology Journal · doi:10.1111/pbi.13879 · Cited by 33 · see citing works

A bacterial spermidine biosynthetic pathway via carboxyaminopropylagmatine

Xi, H., Nie, X., Gao, F., Liang, X., Hu, L. H., Zhou, H., Cai, Y., & Yang, C. (2023) · Science Advances · doi:10.1126/sciadv.adj9075 · Cited by 31 · see citing works

Polyamines: Α bioenergetic smart switch for plant protection and development

Navakoudis, E., & Kotzabasis, K. (2022) · Journal of Plant Physiology · doi:10.1016/j.jplph.2022.153618 · Cited by 31 · see citing works

Rainbow trout (Oncorhynchus mykiss) urea cycle and polyamine synthesis gene families show dynamic expression responses to inflammation

Clark, T. C., Tinsley, J., Macqueen, D. J., & Martín, S. (2019) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2019.03.075 · Cited by 30 · see citing works

Polyamine-containing natural products: structure, bioactivity, and biosynthesis

Long, Q., Zhou, W., Zhou, H., Tang, Y., Wu, C., Liu, Q., & Bian, X. (2023) · Natural Product Reports · doi:10.1039/d2np00087c · Cited by 30 · see citing works

A Family of Viral Satellites Manipulates Invading Virus Gene Expression and Can Affect Cholera Toxin Mobilization

Barth, Z. K., Netter, Z., Angermeyer, A., Bhardwaj, P., & Seed, K. D. (2020) · mSystems · doi:10.1128/msystems.00358-20 · Cited by 29 · see citing works

Recent Advances in the Siderophore Biology of Shewanella

Liu, L., Wang, W., Wu, S., & Gao, H. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.823758 · Cited by 31 · see citing works

Identification and characterization of enzymes involved in the biosynthesis of pyrimidine nucleoside antibiotics

McErlean, M., Liu, X., Cui, Z., Gust, B., & Lanen, S. G. V. (2021) · Natural Product Reports · doi:10.1039/d0np00064g · Cited by 28 · see citing works

Polyamine biosynthesis and biological roles in rhizobia

Becerra-Rivera, V. A., & Dunn, M. F. (2019) · FEMS Microbiology Letters · doi:10.1093/femsle/fnz084 · Cited by 27 · see citing works

Predicting substrate exchange in marine diatom‐heterocystous cyanobacteria symbioses

Nieves‐Morión, M., Flores, E., & Foster, R. A. (2020) · Environmental Microbiology · doi:10.1111/1462-2920.15013 · Cited by 27 · see citing works

Discovery of ancestral L-ornithine and L-lysine decarboxylases reveals parallel, pseudoconvergent evolution of polyamine biosynthesis

Li, B., Liang, J., Hanfrey, C. C., Phillips, M. A., & Michael, A. J. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101219 · Cited by 27 · see citing works

Homospermidine biosynthesis in the cyanobacterium Anabaena requires a deoxyhypusine synthase homologue and is essential for normal diazotrophic growth

Burnat, M., Li, B., Kim, S. H., Michael, A. J., & Flores, E. (2018) · Molecular Microbiology · doi:10.1111/mmi.14006 · Cited by 26 · see citing works

Bacillus subtilis STU6 Ameliorates Iron Deficiency in Tomato by Enhancement of Polyamine-Mediated Iron Remobilization

Zhou, C., Zhu, L., Guo, J., Xiao, X., Ma, Z., & Wang, J. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b05851 · Cited by 25 · see citing works

Arginine, ornithine and citrulline supplementation in rainbow trout: Free amino acid dynamics and gene expression responses to bacterial infection

Clark, T. C., Tinsley, J., Sigholt, T., Macqueen, D. J., & Martín, S. (2020) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2020.01.026 · Cited by 25 · see citing works

Natural Autophagy Activators to Fight Age-Related Diseases

Rivera, V. M. M., Juárez, J. R. T., Murillo-Melo, N. M., Leyva‐García, N., Magaña, J. J., Cordero‐Martínez, J., & Jiménez-Gutiérrez, G. E. (2024) · Cells · doi:10.3390/cells13191611 · Cited by 24 · see citing works

The unknown soldier in citrus plants: polyamines-based defensive mechanisms against biotic and abiotic stresses and their relationship with other stress-associated metabolites

Nehela, Y., & Killiny, N. (2020) · Plant Signaling & Behavior · doi:10.1080/15592324.2020.1761080 · Cited by 24 · see citing works

Endogenous and food-derived polyamines: determination by electrochemical sensing

Baratella, D., Bonaiuto, E., Magro, M., Roger, J. D. A., Kanamori, Y., Lima, G. P. P., Agostinelli, E., & Vianello, F. (2018) · Amino Acids · doi:10.1007/s00726-018-2617-4 · Cited by 24 · see citing works

Roles of S-Adenosylmethionine and Its Derivatives in Salt Tolerance of Cotton

Li, Y., Wang, X., Zhao, F., Zhang, X., Li, W., Huang, J., Pei, X., Ren, X., Liu, Y., He, K., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119517 · Cited by 23 · see citing works

The untapped potential of spermidine alkaloids: Sources, structures, bioactivities and syntheses

Shi, Y., Zhang, J., Wang, Y., Ding, K., Yu, Y., Xia, C., Li, X.-X., He, J., Zhang, W., & Xu, J. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114600 · Cited by 22 · see citing works

Spermidine-Regulated Biosynthesis of Heat-Stable Antifungal Factor (HSAF) in Lysobacter enzymogenes OH11

Chen, Y., Yu, L., Liu, F., & Du, L. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02984 · Cited by 21 · see citing works

The effect of spermidine on autoimmunity and beta cell function in NOD mice

Karacay, C., Prietl, B., Harer, C., Ehall, B., Haudum, C. W., Bounab, K., Franz, J., Eisenberg, T., Madeo, F., Kolb, D., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-08168-2 · Cited by 21 · see citing works

Spermine modulation of Alzheimer’s Tau and Parkinson’s α-synuclein: implications for biomolecular condensation and neurodegeneration

Sun, X., Saha, D., Wang, X. B., Mörman, C., Sternke‐Hoffmann, R., Gerez, J., Herranz-Trillo, F., Riek, R., Zheng, W., & Luo, J. (2025) · Nature Communications · doi:10.1038/s41467-025-65426-3 · Cited by 20 · see citing works

Highly efficient biosynthesis of spermidine from L-homoserine and putrescine using an engineered Escherichia coli with NADPH self-sufficient system

Liang, X., Deng, H., Bai, Y., Fan, T., Zheng, X., & Cai, Y. (2022) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-022-12110-x · Cited by 20 · see citing works

Functional polyamine metabolic enzymes and pathways encoded by the virosphere

Li, B., Liang, J., Baniasadi, H. R., Phillips, M. A., & Michael, A. J. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2214165120 · Cited by 21 · see citing works

Promiscuous Enzymes Cause Biosynthesis of Diverse Siderophores in Shewanella oneidensis

Wang, S.-J., Liang, H., Liu, L., Jiang, X., Wu, S., & Gao, H. (2020) · Applied and Environmental Microbiology · doi:10.1128/aem.00030-20 · Cited by 20 · see citing works

Compound organic acid could improve the growth performance, immunity and antioxidant properties, and intestinal health by altering the microbiota profile of weaned piglets

Li, Z., Liu, S., Zhao, Y., Wang, J., & Ma, X. (2023) · Journal of Animal Science · doi:10.1093/jas/skad196 · Cited by 19 · see citing works

Overexpression of OsACL5 triggers environmentally‐dependent leaf rolling and reduces grain size in rice

Mai, H., Qin, T., Wei, H. J., Yu, Z., Pang, G., Liang, Z., Ni, J., Yang, H., Tang, H., Xiao, L., et al. (2023) · Plant Biotechnology Journal · doi:10.1111/pbi.14227 · Cited by 19 · see citing works

PaeA (YtfL) protects from cadaverine and putrescine stress in Salmonella Typhimurium and E. coli

Iwadate, Y., Ramezanifard, R., Golubeva, Y. A., Fenlon, L. A., & Slauch, J. M. (2021) · Molecular Microbiology · doi:10.1111/mmi.14686 · Cited by 18 · see citing works

The Role of Cadaverine Synthesis on Pneumococcal Capsule and Protein Expression

Nakamya, M. F., Ayoola, M. B., Park, S., Shack, L. A., Swiatlo, E., & Nanduri, B. (2018) · Medical Sciences · doi:10.3390/medsci6010008 · Cited by 18 · see citing works

Natural combinatorial genetics and prolific polyamine production enable siderophore diversification in Serratia plymuthica

Cleto, S., Haslinger, K., Prather, K. L. J., & Lu, T. K. (2021) · BMC Biology · doi:10.1186/s12915-021-00971-z · Cited by 16 · see citing works

The potential links between human gut microbiota and cardiovascular health and disease - is there a gut-cardiovascular axis?

Almeida, C., Nobre, J. G., Costa, D. A., & Barata, P. (2023) · Frontiers in Gastroenterology · doi:10.3389/fgstr.2023.1235126 · Cited by 18 · see citing works

Crystal structure of thermospermine synthase from Medicago truncatula and substrate discriminatory features of plant aminopropyltransferases

Sekula, B., & Dauter, Z. (2018) · Biochemical Journal · doi:10.1042/bcj20170900 · Cited by 16 · see citing works

A novel subfamily of bacterial AAT-fold basic amino acid decarboxylases and functional characterization of its first representative: Pseudomonas aeruginosa LdcA

Carriel, D., Garcia, P. S., Castelli, F. A., Lamourette, P., Fenaille, F., Brochier‐Armanet, C., Elsen, S., & Gutsche, I. (2018) · Genome Biology and Evolution · doi:10.1093/gbe/evy228 · Cited by 15 · see citing works

Structure, Function, and Evolution of the Pseudomonas aeruginosa Lysine Decarboxylase LdcA

Kandiah, E., Carriel, D., Garcia, P. S., Félix, J., Banzhaf, M., Kritikos, G., Bacia‐Verloop, M., Brochier‐Armanet, C., Elsen, S., & Gutsche, I. (2019) · Structure · doi:10.1016/j.str.2019.10.003 · Cited by 15 · see citing works

Potential Metabolite Markers for Pancreatic Cancer Identified by Metabolomic Analysis of Induced Cancer-Associated Fibroblasts

Miyazaki, Y., Mori, N., Akagi, Y., Oda, T., & Kida, Y. S. (2022) · Cancers · doi:10.3390/cancers14061375 · Cited by 15 · see citing works

Functional Analysis of BipA in E. coli Reveals the Natural Plasticity of 50S Subunit Assembly

Gibbs, M. R., Moon, K., Warner, B. R., Chen, M., Bundschuh, R. A., Foster, L. J., & Fredrick, K. L. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.07.013 · Cited by 16 · see citing works

Alternative pathways utilize or circumvent putrescine for biosynthesis of putrescine-containing rhizoferrin

Li, B., Deng, X., Kim, S. H., Buhrow, L. M., Tomchick, D. R., Phillips, M. A., & Michael, A. J. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.016738 · Cited by 15 · see citing works

The Neighboring Subunit Is Engaged to Stabilize the Substrate in the Active Site of Plant Arginases

Sekula, B. (2020) · Frontiers in Plant Science · doi:10.3389/fpls.2020.00987 · Cited by 14 · see citing works

Structural and functional analysis of the Francisella lysine decarboxylase as a key actor in oxidative stress resistance

Félix, J., Siebert, C., Ducassou, J. N., Nigou, J., Garcia, P. S., Fraudeau, A., Huard, K., Mas, C., Brochier‐Armanet, C., Couté, Y., et al. (2021) · Scientific Reports · doi:10.1038/s41598-020-79611-5 · Cited by 14 · see citing works

Polyamines: Key elements in the rhizobia-legume symbiosis?

Hidalgo‐Castellanos, J., Marín-Peña, A. J., Herrera‐Cervera, J. A., & López‐Gómez, M. (2021) · Phytochemistry Reviews · doi:10.1007/s11101-021-09751-7 · Cited by 14 · see citing works

New functions for old factors: the role of polyamines during the establishment of pregnancy

Fenelon, J. C., & Murphy, B. D. (2018) · Reproduction Fertility and Development · doi:10.1071/rd18235 · Cited by 14 · see citing works

Overexpression of wheat spermidine synthase gene enhances wheat resistance to Fusarium head blight

Ren, J., Li, C., Xiu, Q., Xu, M., & Liu, H. (2024) · Phytopathology Research · doi:10.1186/s42483-024-00243-y · Cited by 13 · see citing works

The host metabolism following bacterial biofilm: what is the mechanism of action?

Mirzaei, R., Abdi, M., & Gholami, H. (2020) · Reviews in Medical Microbiology · doi:10.1097/mrm.0000000000000216 · Cited by 13 · see citing works

Polyamines and microbiota in bicuspid and tricuspid aortic valve aortopathy

Forte, A., Balistreri, C. R., FEO, M. D., Corte, A. D., Hellstrand, P., Persson, L., & Nilsson, B. (2019) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2019.02.014 · Cited by 13 · see citing works

Structural Study of Agmatine Iminohydrolase From Medicago truncatula, the Second Enzyme of the Agmatine Route of Putrescine Biosynthesis in Plants

Sekula, B., & Dauter, Z. (2019) · Frontiers in Plant Science · doi:10.3389/fpls.2019.00320 · Cited by 12 · see citing works

Genomic insight into strategy, interaction and evolution of nitrifiers in metabolizing key labile-dissolved organic nitrogen in different environmental niches

Liu, Q., Chen, Y., & Xu, X. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1273211 · Cited by 11 · see citing works

Salmonella Typhimurium exploits host polyamines for assembly of the type 3 secretion machinery

Miki, T., Uemura, T., Kinoshita, M., Ami, Y., Ito, M., Okada, N., Furuchi, T., Kurihara, S., Haneda, T., Minamino, T., et al. (2024) · PLoS Biology · doi:10.1371/journal.pbio.3002731 · Cited by 11 · see citing works

Dissection of Besnoitia besnoiti intermediate host life cycle stages: From morphology to gene expression

Ramakrishnan, C., Krishnan, A., Francisco, S., Schmid, M. W., Russo, G., Leitão, A., Hemphill, A. F., Soldati‐Favre, D., & Hehl, A. B. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010955 · Cited by 11 · see citing works

Metabolic alterations of the gut–liver axis induced by cholic acid contribute to hepatic steatosis in rats

Liu, H., Yokoyama, F., & Ishizuka, S. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2023.159319 · Cited by 11 · see citing works

The Sinorhizobium meliloti NspS-MbaA system affects biofilm formation, exopolysaccharide production and motility in response to specific polyamines

Chávez-Jacobo, V. M., Becerra-Rivera, V. A., Guerrero, G., & Dunn, M. F. (2023) · Microbiology · doi:10.1099/mic.0.001293 · Cited by 10 · see citing works

An ancient cis‐element targeted by Ralstonia solanacearum TALE‐like effectors facilitates the development of a promoter trap that could confer broad‐spectrum wilt resistance

Gallas, N., Li, X., von Roepenack‐Lahaye, E., Schandry, N., Jiang, Y., Wu, D., & Lahaye, T. (2023) · Plant Biotechnology Journal · doi:10.1111/pbi.14208 · Cited by 10 · see citing works

Identification of a novel substrate-derived spermine oxidase inhibitor

Dunston, T. T., Хомутов, М. А., Gabelli, S. B., Stewart, T. M., Foley, J. R., Kochetkov, S. N., Khomutov, A. R., & Casero, R. A. (2020) · Acta Naturae · doi:10.32607/actanaturae.10992 · Cited by 10 · see citing works

Characterization of a novel β-alanine biosynthetic pathway consisting of promiscuous metabolic enzymes

Perchat, N., Dubois, C., Mor-Gautier, R., Duquesne, S., Lechaplais, C., Roche, D., Fouteau, S., Darii, E., & Perret, A. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102067 · Cited by 10 · see citing works

Polyamines in Eukaryotes, Bacteria, and Archaea

Michael, A. J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r116.734780 · Cited by 309 · see citing works

Biosynthesis of Polyamines in Eukaryotes, Archaea, and Bacteria

Michael, A. J. (2014) · Springer eBooks · doi:10.1007/978-4-431-55212-3_1 · Cited by 20 · see citing works

Exploring Polyamine Biosynthetic Diversity Through Comparative and Functional Genomics

Michael, A. J. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-034-8_2 · Cited by 5 · see citing works

Evolutionary Diversification in Polyamine Biosynthesis

Minguet, E. G., Vera‐Sirera, F., Marina, A., Carbonell, J., & Blázquez, M. A. (2008) · Molecular Biology and Evolution · doi:10.1093/molbev/msn161 · Cited by 169 · see citing works

Discovery of ancestral L-ornithine and L-lysine decarboxylases reveals parallel, pseudoconvergent evolution of polyamine biosynthesis

Li, B., Liang, J., Hanfrey, C. C., Phillips, M. A., & Michael, A. J. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101219 · Cited by 27 · see citing works