Cloning and Characterization of Human Agmatinase

Basic local alignment search tool

Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669 · see citing works

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

Arginine metabolism: nitric oxide and beyond

WU, G., & MORRIS, S. M. (1998) · Biochemical Journal · doi:10.1042/bj3360001 · Cited by 2,811 · see citing works

ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling

Peitsch, M. C. (1996) · Biochemical Society Transactions · doi:10.1042/bst0240274 · Cited by 943 · see citing works

Polyamines: Mysterious Modulators of Cellular Functions

Igarashi, K., & Kashiwagi, K. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2601 · Cited by 888 · see citing works

[4] Plasmid transformation of Escherichia coli and other bacteria

Hanahan, D., Jessee, J. A., & Bloom, F. R. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)04006-a · Cited by 621 · see citing works

Comparative properties of arginases

Jenkinson, C. P., Grody, W. W., & Cederbaum, S. D. (1996) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/0305-0491(95)02138-8 · Cited by 610 · see citing works

Agmatine, the bacterial amine, is widely distributed in mammalian tissues

Raasch, W., Regunathan, S., Li, G., & Reis, D. J. (1995) · Life Sciences · doi:10.1016/0024-3205(95)00226-v · Cited by 250 · see citing works

Agmatine reverses pain induced by inflammation, neuropathy, and spinal cord injury

Fairbanks, C. A., Schreiber, K. L., Brewer, K. L., Yu, C.-G., Stone, L. S., Kitto, K. F., Nguyen, H. O., Grocholski, B. M., Shoeman, D. W., Kehl, L. J., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.19.10584 · Cited by 232 · see citing works

Arginase activity in human breast cancer cell lines: N(omega)-hydroxy-L-arginine selectively inhibits cell proliferation and induces apoptosis in MDA-MB-468 cells.

Singh, R., Pervin, S., Karimi, A., Cederbaum, S. D., & Chaudhuri, G. (2000) · PubMed · Cited by 185 · see citing works

Agmatine, a bioactive metabolite of arginine. Production, degradation, and functional effects in the kidney of the rat.

Lortie, M. J., Novotny, W. F., Peterson, Ö. W., Vallon, V., Malvey, K., Mendonca, M., Satriano, J. A., Insel, P. A., Thomson, S. C., & Blantz, R. C. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118430 · Cited by 168 · see citing works

Protection by imidazol(ine) drugs and agmatine of glutamate‐induced neurotoxicity in cultured cerebellar granule cells through blockade of NMDA receptor

Olmos, G., DeGregorio‐Rocasolano, N., Regalado, M. P., Gasull, T., Boronat, M. A., Trullás, R., Villarroel, Á., Lerma, J., & Garcı́a-Sevilla, J. A. (1999) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0702679 · Cited by 166 · see citing works

Endogenous and exogenous polyamines in support of tumor growth.

Seiler, N., SARHAN, S., Grauffel, C., Jones, R., Knödgen, B., & Moulinoux, J.-P. (1990) · PubMed · Cited by 160 · see citing works

Agmatine Suppresses Proliferation by Frameshift Induction of Antizyme and Attenuation of Cellular Polyamine Levels

Satriano, J. A., Matsufuji, S., Murakami, Y., Lortie, M. J., Schwartz, D., Kelly, C., Hayashi, S., & Blantz, R. C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15313 · Cited by 137 · see citing works

Agmatinase Activity in Rat Brain: A Metabolic Pathway for the Degradation of Agmatine

Sastre, M., Regunathan, S., Galea, E., & Reis, D. J. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67041761.x · Cited by 133 · see citing works

INHIBITORY EFFECT OF AGMATINE ON NALOXONE-PRECIPITATED ABSTINENCE SYNDROME IN MORPHINE DEPENDENT RATS

Aricioǧlu-Kartal, F., & Uzbay, T. I. (1997) · Life Sciences · doi:10.1016/s0024-3205(97)00801-1 · Cited by 122 · see citing works

Agmatine Enhances the NADPH Oxidase Activity of Neuronal NO Synthase and Leads to Oxidative Inactivation of the Enzyme

Demady, D. R., Jianmongkol, S., Vuletich, J. L., Bender, A. T., & Osawa, Y. (2001) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)12352-8 · Cited by 107 · see citing works

Polyamine-Mediated Regulation of Mouse Ornithine Decarboxylase Is Posttranslational

Wetters, T. V. D., Macrae, M., Brabant, M., Sittler, A., & Coffino, P. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.12.5484 · Cited by 93 · see citing works

Imidazoline receptors and agmatine in blood vessels: a novel system inhibiting vascular smooth muscle proliferation.

Regunathan, S., Youngson, C., Raasch, W., Wang, H., & REIS, D. J. (1996) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)12405-1 · Cited by 92 · see citing works

Agmatine suppresses nitric oxide production in microglia

Abe, K., Abe, Y., & Saitō, H. (2000) · Brain Research · doi:10.1016/s0006-8993(00)02517-8 · Cited by 91 · see citing works

Agmatine: An Endogenous Ligand at Imidazoline Receptors Is a Novel Neurotransmittera

Reis, D. J., & Regunathan, S. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb09343.x · Cited by 88 · see citing works

Antizyme, a mediator of ubiquitin-independent proteasomal degradation

Coffino, P. (2001) · Biochimie · doi:10.1016/s0300-9084(01)01252-4 · Cited by 83 · see citing works

Agmatine (decarboxylated arginine) is synthesized and stored in astrocytes

Regunathan, S., Feinstein, D. L., Raasch, W., & Reis, D. J. (1995) · Neuroreport · doi:10.1097/00001756-199510020-00018 · Cited by 80 · see citing works

Altering the Binuclear Manganese Cluster of Arginase Diminishes Thermostability and Catalytic Function

Scolnick, L. R., Kanyo, Z. F., Cavalli, R. C., Ash, D. E., & Christianson, D. W. (1997) · Biochemistry · doi:10.1021/bi970800v · Cited by 80 · see citing works

Polyamines in Mammalian Tumors Part I

Scalabrino, G., & Ferioli, M. E. (1981) · Advances in cancer research · doi:10.1016/s0065-230x(08)60911-2 · Cited by 80 · see citing works

Regulation of intracellular polyamine biosynthesis and transport by NO and cytokines TNF-α and IFN-γ

Satriano, J. A., Ishizuka, S., Archer, D. C., Blantz, R. C., & Kelly, C. (1999) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1999.276.4.c892 · Cited by 79 · see citing works

Metabolism of agmatine in macrophages: modulation by lipopolysaccharide and inhibitory cytokines

Sastre, M., Galea, E., Feinstein, D. L., REIS, J. D., & Regunathan, S. (1998) · Biochemical Journal · doi:10.1042/bj3301405 · Cited by 74 · see citing works

Partial cloning and characterization of an arginine decarboxylase in the kidney

Morrissey, J. J., McCracken, R., Ishidoya, S., & Klahr, S. (1995) · Kidney International · doi:10.1038/ki.1995.204 · Cited by 71 · see citing works

Agmatine modulates polyamine content in hepatocytes by inducing spermidine/spermine acetyltransferase

Vargiu, C., Cabella, C., Belliardo, S., Cravanzola, C., GRILLO, M. A., & Colombatto, S. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00126.x · Cited by 62 · see citing works

Uptake of Agmatine into Rat Brain Synaptosomes: Possible Role of Cation Channels

Sastre, M., Regunathan, S., & Reis, D. J. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69062421.x · Cited by 61 · see citing works

Transport and metabolism of agmatine in rat hepatocyte cultures

Cabella, C., Gardini, G., Corpillo, D., Testore, G., BEDINO, S., Solinas, S. P., Cravanzola, C., Vargiu, C., GRILLO, M. A., & Colombatto, S. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.01955.x · Cited by 59 · 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

Agmatine Inhibits Cell Proliferation and Improves Renal Function in Anti—Thy-1 Glomerulonephritis

Ishizuka, S., Cunard, R. A., Poucell-Hatton, S., Wead, L. M., Lortie, M. J., Thomson, S. C., Gabbai, F. B., Satriano, J. A., & Blantz, R. C. (2000) · Journal of the American Society of Nephrology · doi:10.1681/asn.v11122256 · Cited by 40 · see citing works

Regulation of Ornithine Decarboxylase Activity and Polyamine Transport by Agmatine in Rat Pulmonary Artery Endothelial Cells

Babál, P., Ruchko, M. V., Campbell, C. C., Gilmour, S. P., Mitchell, J. L. A., Olson, J. W., & Gillespie, M. N. (2001) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)38743-9 · Cited by 35 · see citing works

Concomitant Changes in Polyamine Pools and DNA Methylation during Growth Inhibition of Human Colonic Cancer Cells

Duranton, B., Keith, G., Gossé, F., Bergmann, C., Schleiffer, R., & Raul, F. (1998) · Experimental Cell Research · doi:10.1006/excr.1998.4148 · Cited by 29 · see citing works

Role of a serine/threonine kinase, Mst1, in megakaryocyte differentiation

Sun, S., & Ravid, K. (2000) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(20000101)76:1 · Cited by 13 · 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

Arginine Metabolism: Boundaries of Our Knowledge

Morris, S. M. (2007) · Journal of Nutrition · doi:10.1093/jn/137.6.1602s · Cited by 640 · see citing works

Arginine: beyond protein

Morris, S. M. (2006) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/83.2.508s · Cited by 424 · see citing works

Enzymes of Arginine Metabolism

Morris, S. M. (2004) · Journal of Nutrition · doi:10.1093/jn/134.10.2743s · Cited by 357 · see citing works

Agmatine: clinical applications after 100 years in translation

Piletz, J. E., Arıcıoğlu, F., Cheng, J., Fairbanks, C. A., Gilad, V. H., Haenisch, B., Halaris, A. E., Hong, S., Lee, J. E., Li, J., et al. (2013) · Drug Discovery Today · doi:10.1016/j.drudis.2013.05.017 · Cited by 248 · see citing works

Paracrinicity: The Story of 30 Years of Cellular Pituitary Crosstalk

Denef, C. (2007) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.2007.01616.x · Cited by 244 · see citing works

Agmatine

Halaris, A. E., & Piletz, J. E. (2007) · CNS Drugs · doi:10.2165/00023210-200721110-00002 · Cited by 237 · see citing works

Arginases I and II: do their functions overlap?

Cederbaum, S. D., Yu, H., Grody, W. W., Kern, R. M., Yoo, P. K., & Iyer, R. K. (2004) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2003.10.012 · Cited by 236 · see citing works

Arginase Plays a Pivotal Role in Polyamine Precursor Metabolism in Leishmania

Roberts, S. C., Tancer, M. J., Polinsky, M. R., Gibson, K. M., Heby, O., & Ullman, B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402042200 · Cited by 177 · see citing works

Functionally important role for arginase 1 in the airway hyperresponsiveness of asthma

North, M. L., Khanna, N., Marsden, P. A., Grasemann, H., & Scott, J. A. (2009) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00025.2009 · Cited by 140 · see citing works

Arginine and immunity: a unique perspective

Nieves, C., & Langkamp‐Henken, B. (2002) · Biomedicine & Pharmacotherapy · doi:10.1016/s0753-3322(02)00291-3 · Cited by 120 · see citing works

Agmatine: multifunctional arginine metabolite and magic bullet in clinical neuroscience?

Laube, G., & Bernstein, H. (2017) · Biochemical Journal · doi:10.1042/bcj20170007 · Cited by 110 · see citing works

Expression of human arginine decarboxylase, the biosynthetic enzyme for agmatine

Zhu, M. (2003) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2003.11.006 · Cited by 108 · see citing works

Recent advances in arginine metabolism

Morris, S. M. (2003) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/00075197-200401000-00009 · Cited by 107 · see citing works

Putrescine biosynthesis in mammalian tissues

Coleman, C. S., Guirong, H. U., & Pegg, A. E. (2004) · Biochemical Journal · doi:10.1042/bj20040035 · Cited by 106 · see citing works

Agmatine (decarboxylated l-arginine): Physiological role and therapeutic potential

Molderings, G. J., & Haenisch, B. (2011) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2011.12.005 · Cited by 101 · see citing works

Single-cell spatial multi-omics and deep learning dissect enhancer-driven gene regulatory networks in liver zonation

Bravo González-Blas, C., Matetovici, I., Hillen, H., Taskiran, I. I., Vandepoel, R., Christiaens, V., Sansores-García, L., Verboven, E., Hulselmans, G., Poovathingal, S., et al. (2024) · Nature Cell Biology · doi:10.1038/s41556-023-01316-4 · Cited by 85 · see citing works

Encapsulated in silica: genome, proteome and physiology of the thermophilic bacterium Anoxybacillus flavithermus WK1

Saw, J. H. W., Mountain, B. W., Feng, L., Omelchenko, M. V., Hou, S., Saito, J. A., Stott, M. B., Li, D., Zhao, G., Wu, J., et al. (2008) · Genome biology · doi:10.1186/gb-2008-9-11-r161 · Cited by 80 · see citing works

Effect of Agmatine Against Cell Death Induced by NMDA and Glutamate in Neurons and PC12 Cells

Zhu, M., Piletz, J. E., Halaris, A. E., & Regunathan, S. (2003) · Cellular and Molecular Neurobiology · doi:10.1023/a:1025069407173 · Cited by 75 · see citing works

Polyamines: therapeutic perspectives in oxidative stress and inflammatory diseases

Hussain, T., Tan, B., Ren, W., Rahu, N., Dad, R., Kalhoro, D. H., & Yin, Y. (2017) · Amino Acids · doi:10.1007/s00726-017-2447-9 · Cited by 61 · see citing works

Mouse Ornithine Decarboxylase-like Gene Encodes an Antizyme Inhibitor Devoid of Ornithine and Arginine Decarboxylating Activity

Lopez-Contreras, A. J., López‐García, C., Jiménez‐Cervantes, C., Cremades, A., & Peñafiel, R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602840200 · Cited by 60 · see citing works

Metabolism and function in animal tissues of agmatine, a biogenic amine formed from arginine

GRILLO, M. A., & Colombatto, S. (2003) · Amino Acids · doi:10.1007/s00726-003-0030-z · Cited by 56 · see citing works

Human agmatinase is diminished in the clear cell type of renal cell carcinoma

Dallmann, K., Junker, H., Balabanov, S., Zimmermann, U., Giebel, J., & Walther, R. (2003) · International Journal of Cancer · doi:10.1002/ijc.11459 · Cited by 55 · 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

Agmatinase promotes the lung adenocarcinoma tumorigenesis by activating the NO-MAPKs-PI3K/Akt pathway

Zhu, H.-E., Yin, J., Chen, D.-X., he, S. T., & Chen, H. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-2082-3 · Cited by 45 · see citing works

Effects of agmatine accumulation in human colon carcinoma cells on polyamine metabolism, DNA synthesis and the cell cycle

Mayeur, C., Veuillet, G., Michaud, M., Raul, F., Blottière, H. M., & Blachier, F. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.12.004 · Cited by 45 · see citing works

Regulatory mechanisms underlying agmatine homeostasis in humans

Haenisch, B., von Kügelgen, I., Bönisch, H., Göthert, M., Sauerbruch, T., Schepke, M., Marklein, G., Höfling, K., Schröder, D., & Molderings, G. J. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.90374.2008 · Cited by 44 · see citing works

On the Binding of Monoamine Oxidase Inhibitors to Some Sites Distinct from the MAO Active Site, and Effects Thereby Elicited

Holt, A. (2003) · NeuroToxicology · doi:10.1016/s0161-813x(03)00104-9 · Cited by 43 · see citing works

Agmatine reduces only peripheral-related behavioral signs, not the central signs, of morphine withdrawal in nNOS deficient transgenic mice

Arıcıoğlu, F., Paul, I. A., & Regunathan, S. (2003) · Neuroscience Letters · doi:10.1016/j.neulet.2003.10.010 · Cited by 43 · see citing works

Neuropharmacokinetic and Dynamic Studies of Agmatine (Decarboxylated Arginine)

Nguyen, H. O., Goracke‐Postle, C. J., KAMINSKI, L. L., Overland, A. C., MORGAN, A. D., & Fairbanks, C. A. (2003) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1304.009 · Cited by 43 · see citing works

Localization and differential expression of arginase II in the kidney of male and female mice

Levillain, O., Balvay, S., & Peyrol, S. (2004) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-004-1336-8 · Cited by 39 · see citing works

iTRAQ-based proteomic analysis on the mitochondrial responses in gill tissues of juvenile olive flounder Paralichthys olivaceus exposed to cadmium

Lu, Z. Z., Wang, S., Ji, C., Li, F., Cong, M., Shan, X., & Wu, H. (2019) · Environmental Pollution · doi:10.1016/j.envpol.2019.113591 · Cited by 38 · see citing works

Effect of Agmatine on Acute and Mononeuropathic Pain

Arıcıoğlu, F., KORCEGEZ, E., Bozkurt, A., & Özyalçın, S. (2003) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1304.010 · Cited by 38 · see citing works

Kinetic and structural analysis of human ALDH9A1

Končitíková, R., Vigouroux, A., Kopečná, M., Šebela, M., Moréra, S., & Kopečný, D. (2019) · Bioscience Reports · doi:10.1042/bsr20190558 · Cited by 37 · see citing works

Neuroprotection by agmatine: Possible involvement of the gut microbiome?

Saha, P., Panda, S., Holkar, A., Vashishth, R., Rana, S. S., Arumugam, M., Ashraf, G. M., Haque, S., & Ahmad, F. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102056 · Cited by 35 · see citing works

The virulence factor urease and its unexplored role in the metabolism of Cryptococcus neoformans

Toplis, B., Bosch, C., Schwartz, I. S., Kenyon, C. R., Boekhout, T., Perfect, J. R., & Botha, A. (2020) · FEMS Yeast Research · doi:10.1093/femsyr/foaa031 · Cited by 35 · see citing works

Three Related Enzymes in Candida albicans Achieve Arginine- and Agmatine-Dependent Metabolism That Is Essential for Growth and Fungal Virulence

Schaefer, K., Wagener, J., Ames, R. M., Christou, S., MacCallum, D. M., Bates, S., & Gow, N. A. R. (2020) · mBio · doi:10.1128/mbio.01845-20 · Cited by 31 · see citing works

Supraspinally-administered agmatine attenuates the development of oral fentanyl self-administration

Wade, C. L., Schuster, D. J., Domingo, K. M., Kitto, K. F., & Fairbanks, C. A. (2008) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2008.04.007 · Cited by 30 · see citing works

Metabolic strategies for the degradation of the neuromodulator agmatine in mammals

Benítez, J., García, D., Romero, N., González, A., Martínez‐Oyanedel, J., Figueroa, M., Salas, M., López, V., García, M. D. L. Á., Dodd, P. R., et al. (2017) · Metabolism · doi:10.1016/j.metabol.2017.11.005 · Cited by 30 · see citing works

The first description of complete invertebrate arginine metabolism pathways implies dose-dependent pathogen regulation in Apostichopus japonicus

Yina, S., Cheng-hua, L., Weiwei, Z., Zhenhui, W., & Lv, Z. (2016) · Scientific Reports · doi:10.1038/srep23783 · Cited by 29 · see citing works

Mutational analysis of substrate recognition by human arginase type I − agmatinase activity of the N130D variant

Alarcón, R., Orellana, M. S., Neira, B., Uribe, E. A., García, J. R., & Carvajal, N. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05551.x · Cited by 28 · see citing works

An alternative, arginase‐independent pathway for arginine metabolism in K luyveromyces lactis involves guanidinobutyrase as a key enzyme

Romagnoli, G., Verhoeven, M. D., Mans, R., Rey, Y. F., Bel‐Rhlid, R., van den Broek, M. A., Seifar, R. M., ten Pierick, A., Thompson, M., Müller, V., et al. (2014) · Molecular Microbiology · doi:10.1111/mmi.12666 · Cited by 27 · see citing works

Insights into the interaction of human arginase II with substrate and manganese ions by site‐directed mutagenesis and kinetic studies

López, V., Alarcón, R., Orellana, M. S., Enrı́quez, P., Uribe, E. A., Martı́nez, J., & Carvajal, N. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04874.x · Cited by 23 · see citing works

Prenatal alcohol exposure alters phosphorylation and glycosylation of proteins in rat offspring liver

Fofana, B., Yao, X., Rampitsch, C., Cloutier, S., Wilkins, J. A., & Nyomba, B. L. G. (2009) · PROTEOMICS · doi:10.1002/pmic.200800969 · Cited by 22 · see citing works

Polyamine homeostasis in arginase knockout mice

Deignan, J. L., Livesay, J. C., Shantz, L. M., Pegg, A. E., O’Brien, W. E., Iyer, R. K., Cederbaum, S. D., & Grody, W. W. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00393.2006 · Cited by 22 · see citing works

The first archaeal agmatinase from anaerobic hyperthermophilic archaeon Pyrococcus horikoshii: cloning, expression, and characterization

Goda, S., Sakuraba, H., Kawarabayasi, Y., & Ohshima, T. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.12.010 · Cited by 20 · see citing works

Agmatine signaling: odds and threads.

Berkels, R., Taubert, D., Gründemann, D., & Schömig, E. (2006) · Cardiovascular Drug Reviews · doi:10.1111/j.1527-3466.2004.tb00128.x · Cited by 16 · see citing works

Cloning and functional expression of a rodent brain cDNA encoding a novel protein with agmatinase activity, but not belonging to the arginase family

Uribe, E. A., Salas, M., Enríquez, S., Orellana, M. S., & Carvajal, N. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.01.002 · Cited by 19 · see citing works

Operational tolerance after hematopoietic stem cell transplantation is characterized by distinct transcriptional, phenotypic, and metabolic signatures

Dubouchet, L., Todorov, H., Seurinck, R., Vallet, N., Gassen, S. V., Corneau, A., Blanc, C., Zouali, H., Boland, A., Deleuze, J., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abg3083 · Cited by 18 · see citing works

Insights into the reaction mechanism of Escherichia coli agmatinase by site‐directed mutagenesis and molecular modelling

Salas, M., Rodríguez, R., López, N., Uribe, E. A., López, V., & Carvajal, N. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03255.x · Cited by 18 · see citing works

Vertebrate Agmatinases: What Role Do They Play in Agmatine Catabolism?

Morris, S. M. (2003) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1304.003 · Cited by 18 · see citing works

Enzymes of urea synthesis are expressed at the ocular surface, and decreased urea in the tear fluid is associated with dry-eye syndrome

Jäger, K., Kielstein, H., Dunse, M., Naß, N., Paulsen, F. P., & Sel, S. (2013) · Graefe s Archive for Clinical and Experimental Ophthalmology · doi:10.1007/s00417-013-2391-7 · Cited by 16 · see citing works

Expression and localization of an agmatinase-like protein in the rat brain

Mella, C., Martínez, F., García, M. D. L. Á., Nualart, F., Castro‐Fernández, V., Bustos, P., Carvajal, N., & Uribe, E. A. (2010) · Histochemistry and Cell Biology · doi:10.1007/s00418-010-0720-z · Cited by 16 · see citing works

Crystal Structure of Escherichia coli Agmatinase: Catalytic Mechanism and Residues Relevant for Substrate Specificity

Maturana, P., Orellana, M. S., Herrera, S. M., Martı́nez, I., Figueroa, M., Martínez‐Oyanedel, J., Castro‐Fernández, V., & Uribe, E. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094769 · Cited by 15 · see citing works

Effective whole cell biotransformation of arginine to a four-carbon diamine putrescine using engineered Escherichia coli

Yang, S.-C., Ting, W., & Ng, I. (2022) · Biochemical Engineering Journal · doi:10.1016/j.bej.2022.108502 · Cited by 15 · see citing works

Kinetic studies and site-directed mutagenesis of Escherichia coli agmatinase. A role for Glu274 in binding and correct positioning of the substrate guanidinium group

Carvajal, N., Orellana, M. S., Salas, M., Enrı́quez, P., Alarcón, R., Uribe, E. A., & López, V. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.07.005 · Cited by 15 · see citing works

Studies on the interaction of Escherichia coli agmatinase with manganese ions: structural and kinetic studies of the H126N and H151N variants

Salas, M., López, V., Uribe, E. A., & Carvajal, N. (2004) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2004.02.022 · Cited by 15 · see citing works

Functional characterization of arginine metabolic pathway enzymes in the antibacterial immune response of penaeid shrimp

Huang, Z., Zhang, Y., Zheng, X., Liu, Z., Yao, D., Zhao, Y., Chen, X., & Aweya, J. J. (2021) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2021.104293 · Cited by 14 · see citing works

Structure of the E. coli agmatinase, SPEB

Chitrakar, I., Ahmed, S. F., Torelli, A. T., & French, J. B. (2021) · PLoS ONE · doi:10.1371/journal.pone.0248991 · Cited by 14 · see citing works

Dynamics of arginase gene evolution in metazoans

Cao, J. W., & Shi, F. (2012) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2012.682207 · Cited by 14 · see citing works

Spermidine metabolism in parasitic protozoa - a comparison to the situation in prokaryotes, viruses, plants and fungi

Kaiser, A. E., Gottwald, A. M., Wiersch, C. S., Maier, W. A., III, & Seitz, H. M. (2003) · Folia Parasitologica · doi:10.14411/fp.2003.002 · Cited by 13 · see citing works

Insight on the interaction of an agmatinase-like protein with Mn2+ activator ions

Quiñones, M., Cofré, J., Benítez, J., García, D., Romero, N., González, A., Carvajal, N., García, M. D. L. Á., López, V., Schenk, G., et al. (2015) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2015.01.008 · Cited by 11 · see citing works

The efficacy of inhibitors involved in spermidine metabolism in Plasmodium falciparum, Anopheles stephensi and Trypanosoma evansi

Moritz, E., Seidensticker, S., Gottwald, A. M., Maier, W. A., III, Hoerauf, A. M., Njuguna, J. T., & Kaiser, A. E. (2004) · Parasitology Research · doi:10.1007/s00436-004-1162-0 · Cited by 11 · see citing works

Further insight into the inhibitory action of a LIM/double zinc-finger motif of an agmatinase-like protein

Cofré, J., Montes, P., Vallejos‐Almirall, A., Benítez, J., García, D., Martínez‐Oyanedel, J., Carvajal, N., & Uribe, E. A. (2013) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2013.12.006 · Cited by 10 · see citing works

Mammalian agmatinases constitute unusual members in the family of Mn 2+ -dependent ureahydrolases

Romero, N., Benítez, J., García, D., González, A., Bennun, L., García, M. D. L. Á., López, V., Wilson, L. A., Schenk, G., Carvajal, N., et al. (2016) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2016.11.015 · Cited by 10 · see citing works

A matter of life and death - polyamine metabolism during zygotic embryogenesis of pine

Vuosku, J. (2011) · Cited by 10 · see citing works

Cloning of two LIMCH1 isoforms: characterization of their distribution in rat brain and their agmatinase activity

García, D., Órdenes, P., Benítez, J., González, A., García, M. D. L. Á., López, V., Carvajal, N., & Uribe, E. A. (2015) · Histochemistry and Cell Biology · doi:10.1007/s00418-015-1389-0 · Cited by 9 · see citing works

Involvement of the biogenic active amine agmatine in mitochondrial membrane permeabilization and release of pro-apoptotic factors

Martinis, P., Grancara, S., Kanamori, Y., García‐Argáez, A. N., Pacella, E., Via, L. D., Toninello, A., & Agostinelli, E. (2019) · Amino Acids · doi:10.1007/s00726-019-02791-6 · Cited by 9 · see citing works

Insights into the Mn2+ Binding Site in the Agmatinase-Like Protein (ALP): A Critical Enzyme for the Regulation of Agmatine Levels in Mammals

Reyes, M.-B., Martínez‐Oyanedel, J., Navarrete, C., Mardones, E., Martı́nez, I., Salas, M., López, V., García, M. D. L. Á., Tarifeño-Saldivia, E., Figueroa, M., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21114132 · Cited by 9 · see citing works

Guanidino acid hydrolysis by the human enzyme annotated as agmatinase

Sinn, M., Stanoppi, M., Hauth, F., Fleming, J. R., Funck, D., Mayans, O. M., & Hartig, J. S. (2022) · Scientific Reports · doi:10.1038/s41598-022-26655-4 · Cited by 8 · see citing works

Evidence for an inhibitory LIM domain in a rat brain agmatinase-like protein

Castro‐Fernández, V., Fuentealba, P., Henríquez, A., Vallejos‐Almirall, A., Benítez, J., Lobos, M., Díaz, B., Carvajal, N., & Uribe, E. A. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.05.003 · Cited by 8 · see citing works

Transcriptome Analysis of Redox Systems and Polyamine Metabolic Pathway in Hepatoma and Non-Tumor Hepatocyte-like Cells

Ivanova, O. N., Krasnov, G. S., Snezhkina, A. V., Kudryavtseva, A. V., Fedorov, V. S., Zakirova, N. F., Golikov, M. V., Kochetkov, S. N., Bartosch, B., Треворович, В.-Э. В., et al. (2023) · Biomolecules · doi:10.3390/biom13040714 · Cited by 7 · see citing works

Adeno-Associated Virus-Mediated Knockdown of Agmatinase Attenuates Inflammation and Tumorigenesis in a Mouse Model of Colitis-Associated Colorectal Cancer

Wang, D.-L., Su, Q., Qu, Q., Li, Z.-L., & Liu, Z. (2023) · Human Gene Therapy · doi:10.1089/hum.2022.191 · Cited by 6 · see citing works

Cloning and comparative analysis the proximal promoter activities of arginase and agmatinase genes in Apostichopus japonicus

Shao, Y., Li, C., Zhang, W., Xu, W., Duan, X., Li, Y., Qiu, Q., & Jin, C. (2016) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2016.08.001 · Cited by 6 · see citing works

Identification of agmatinase from Vibrio splendidus and its roles in modulating arginine metabolism of Apostichopus japonicus

Shao, Y., Zhang, S., Li, C., Zhang, W., Zhao, X., & Xiong, J. (2018) · Aquaculture · doi:10.1016/j.aquaculture.2018.03.055 · Cited by 6 · see citing works

Cellular and Physiological Effects of Arginine in Seniors

Albaugh, V. L., Stewart, M. K., & Barbul, A. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805376-8.00027-7 · Cited by 6 · see citing works

Enhancer grammar of liver cell types and hepatocyte zonation states

González-Blas, C. B., Matetovici, I., Hillen, H., Taskiran, I. I., Vandepoel, R., Christiaens, V., Sansores-García, L., Verboven, E., Hulselmans, G., Poovathingal, S., et al. (2022) · doi:10.1101/2022.12.08.519575 · Cited by 5 · see citing works

Adeno-associated virus-mediated gene transfer of arginine decarboxylase to the central nervous system prevents opioid analgesic tolerance

Churchill, C. C., Peterson, C. D., Kitto, K. F., Pflepsen, K. R., Belur, L. R., McIvor, R. S., Vulchanova, L., Wilcox, G. L., & Fairbanks, C. A. (2024) · Frontiers in Pain Research · doi:10.3389/fpain.2023.1269017 · Cited by 5 · see citing works

Agmatine: A potential Neurotherapeutic Agent

Binjhade, N., Supare, V., Ghaywat, S. D., Trivedi, S., Wadher, K., & Umekar, M. J. (2021) · Journal of Drug Delivery and Therapeutics · doi:10.22270/jddt.v11i4.4855 · Cited by 5 · see citing works

A unique aromatic cluster near the active site of H. pylori CPA is essential for catalytic function

Sarkar, D., Vijayan, R., Gourinath, S., & Sau, A. K. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.12.020 · Cited by 4 · see citing works

Expression, crystallization and preliminary X-ray crystallographic analysis of human agmatinase

Kim, K. H., Ahn, H. J., Kim, D., Lee, H. H., Ha, J.-Y., Kim, H.-K., Yoon, H., & Suh, S. W. (2005) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309105027193 · Cited by 4 · see citing works

Pleiotropic effects of ActVI-ORFA as an unusual regulatory factor identified in the biosynthetic pathway of actinorhodin in Streptomyces coelicolor

Li, C., Li, L., Huang, L., & Li, A. (2021) · Microbiological Research · doi:10.1016/j.micres.2021.126792 · Cited by 3 · see citing works

Exploring polyamine metabolism of the yeast-like fungus, Emergomyces africanus

Koroleva, E., Toplis, B., Taylor, M. J. C., van Deventer, C., Steffen, H. C., van den Heever, C., Govender, N. P., de Hoog, S., & Botha, A. (2024) · FEMS Yeast Research · doi:10.1093/femsyr/foae038 · Cited by 3 · see citing works

Re-examining the origin and functions of the urea cyclePreprint

Song, X., Teng, L., & Zhao, X. (2022) · Research Square · doi:10.21203/rs.3.rs-1532969/v1 · Cited by 3 · see citing works

Molecular Cloning of the Gene for Edeine B1 Amidinohydrolase in Addition to the Agmatinase Activity in Bacillus subtilis.

Shimotohno, K., Hidaka, T., Morishita, T., & Endō, T. (2003) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.26.262 · Cited by 2 · see citing works

Chronic exposure to agmatine results in the selection of agmatine-resistant hepatoma cells

Bandino, A., Battaglia, V., Bravoco, V., Busletta, C., Compagnone, A., Cravanzola, C., Floriana, M., Agostinelli, E., Parola, M., & Colombatto, S. (2011) · Amino Acids · doi:10.1007/s00726-011-0993-0 · Cited by 2 · see citing works

Crystallization and preliminary X-ray crystallographic analysis of a putative agmatinase fromDeinococcus radiodurans

Lee, J. A., Ahn, H. J., Ha, J. Y., Shim, S. M., Kim, K. H., Kim, H. K., & Suh, S. W. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904018761 · Cited by 2 · see citing works

NITRIC OXIDE AND NITROGEN OXIDES

Meurs, H., Maarsingh, H., & Zaagsma, J. (2006) · Elsevier eBooks · doi:10.1016/b0-12-370879-6/00265-9 · Cited by 1 · see citing works

Development and use of tools to study metabolic consequences of altered polyamine catabolism

Cerrada‐Gimenez, M. (2010) · UEF eRepo (University of Eastern Finland) · Cited by 1 · see citing works

Endogenous modulation of addiction: chronic pain and the NMDA/NOS cascade.

Wade, C. L. (2010) · University of Minnesota Digital Conservancy (University of Minnesota)

POLYAMINE MODULATION IN ALCOHOLISM: EXAMINATION USING A NOVEL SCREENING PROCEDURE DESIGNED TO PREDICT ANTI-RELAPSE AND NEUROPROTECTIVE EFFICACY

Lewis, J. (2011) · UKnowledge (University of Kentucky)

Regulation of subventricular zone stem cell proliferation and differentiation by agmatine

김사현 (2006)

Nitric Oxide and Nitrogen Oxides

Maarsingh, H., Scott, J. A., & Grasemann, H. (2021) · Elsevier eBooks · doi:10.1016/b978-0-08-102723-3.00102-5

Recent advances in nanomedicine targeting amino acid metabolism for anti-tumor therapy

Pang, C., Song, X., Luo, Y., Li, H., Guo, W., Liu, W., Feng, H., Wu, Y., Chu, X., & Lei, Z. (2025) · Journal of Nanoparticle Research · doi:10.1007/s11051-025-06344-9

Structural and Functional Insights into the Regulation of Helicobacter pylori CPA Activity by an Evolutionarily Conserved Motif

Molla, A., Sarkar, D., Khan, A., Ramachandran, V., Kausar, T., Gourinath, S., & Sau, A. K. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00045

Study of immune tolerance mechanisms following allogeneic hematopoietic stem cell transplantation in humans

Dubouchet, L. (2021) · doi:10.70675/39122d14z0b4dz47e7zb291zde85329b2175

Agmatinase Facilitates Gastric Cancer Tumorigenesis Through PI3K/AKT-Mediated Enhancement of Proliferation, Invasion, and Stemness

Li, X. B., Jia, J. X., Guan, S., & Yang, C. C.-K. (2026) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-026-05798-4

Expression of human arginine decarboxylase, the biosynthetic enzyme for agmatine

Zhu, M. (2003) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2003.11.006 · Cited by 108 · see citing works

The Gene Cluster for Agmatine Catabolism ofEnterococcus faecalis: Study of Recombinant Putrescine Transcarbamylase and Agmatine Deiminase and a Snapshot of Agmatine Deiminase Catalyzing Its Reaction

Llacer, J. L., Polo, L. M., Tavárez, S., Alarcón, B., Hilario, R., & Rubio, V. (2007) · Journal of Bacteriology · doi:10.1128/jb.01216-06 · Cited by 65 · see citing works

Unveiling the reaction mechanism of arginine decarboxylase in Aspergillus oryzae: Insights from crystal structure analysis

Odagaki, Y., Murakami, Y., Takita, T., Mizutani, K., Mikami, B., Fujiwara, S., & Yasukawa, K. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.150728 · Cited by 2 · see citing works

Enzymatic Synthesis of Agmatine by Immobilized Escherichia coli Cells with Arginine Decarboxylase Activity

张维国 (2011) · Chemical Research in Chinese Universities

Cloning and functional expression of a rodent brain cDNA encoding a novel protein with agmatinase activity, but not belonging to the arginase family

Uribe, E. A., Salas, M., Enríquez, S., Orellana, M. S., & Carvajal, N. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.01.002 · Cited by 19 · see citing works