Arginine Metabolism Revisited

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

Protein Arginine Methylation in Mammals: Who, What, and Why

Bedford, M. T., & Clarke, S. G. (2009) · Molecular Cell · doi:10.1016/j.molcel.2008.12.013 · Cited by 1,810 · see citing works

An amino-acid taste receptor

Nelson, G., Chandrashekar, J. V., Hoon, M. A., Feng, L., Zhao, G., Ryba, N. J. P., & Zuker, C. S. (2002) · Nature · doi:10.1038/nature726 · Cited by 1,523 · see citing works

Arginine metabolism and nutrition in growth, health and disease

Wu, G., Bazer, F. W., Davis, T. A., Kim, S. W., Li, P., Marc Rhoads, J., Carey Satterfield, M., Smith, S. B., Spencer, T. E., & Yin, Y. (2009) · Amino Acids · doi:10.1007/s00726-008-0210-y · Cited by 1,362 · see citing works

Nutrient-sensing mechanisms and pathways

Efeyan, A., Comb, W. C., & Sabatini, D. M. (2015) · Nature · doi:10.1038/nature14190 · Cited by 1,110 · see citing works

PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease

Vossenaar, E. R., Zendman, A. J. W., VENROOIJ, W. J. V., & Pruijn, G. J. M. (2003) · BioEssays · doi:10.1002/bies.10357 · Cited by 986 · see citing works

The CASTOR Proteins Are Arginine Sensors for the mTORC1 Pathway

Chantranupong, L., Scaria, S. M., Saxton, R. A., Gygi, M. P., Shen, K., Wyant, G. A., Wang, T., Harper, J. W., Gygi, S. P., & Sabatini, D. M. (2016) · Cell · doi:10.1016/j.cell.2016.02.035 · Cited by 843 · see citing works

The amino acid transporter SLC38A9 is a key component of a lysosomal membrane complex that signals arginine sufficiency to mTORC1

Wang, S., Tsun, Z., Wolfson, R. L., Shen, K., Wyant, G., Plovanich, M. E., Yuan, E. D., Jones, T. D., Chantranupong, L., Comb, W. C., et al. (2015) · Science · doi:10.1126/science.1257132 · Cited by 772 · see citing works

CATs and HATs: the SLC7 family of amino acid transporters

Verrey, F., Closs, E. I., Wagner, C. A., Palacı́n, M., Endou, H., & Kanai, Y. (2004) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-003-1086-z · Cited by 709 · see citing works

Arginase: an emerging key player in the mammalian immune system

Munder, M. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00291.x · Cited by 701 · see citing works

SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1

Rebsamen, M., Pochini, L., Stasyk, T., de Araújo, M. E. G., Galluccio, M., Kandasamy, R. K., Snijder, B., Fauster, A., Rudashevskaya, E. L., Bruckner, M., et al. (2015) · Nature · doi:10.1038/nature14107 · Cited by 673 · 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

Signaling Pathways and Molecular Mechanisms through which Branched-Chain Amino Acids Mediate Translational Control of Protein Synthesis

Kimball, S. R., & Jefferson, L. S. (2006) · Journal of Nutrition · doi:10.1093/jn/136.1.227s · Cited by 637 · see citing works

Recent advances in arginine metabolism: roles and regulation of the arginases

Morris Jr, S. M. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00278.x · Cited by 485 · see citing works

Biological significance of endogenous methylarginines that inhibit nitric oxide synthases

Leiper, J. (1999) · Cardiovascular Research · doi:10.1016/s0008-6363(99)00162-5 · Cited by 458 · 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

Purification and properties of a new enzyme, N, N-dimethylarginine dimethylaminohydrolase, from rat kidney

Ogawa, T., Kimoto, M., & Sasaoka, K. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81786-0 · Cited by 364 · see citing works

Translational control of inducible nitric oxide synthase expression by arginine can explain the arginine paradox

Lee, J.-H., Ryu, H., Ferrante, R. J., Morris, S. M., & Ratan, R. R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0735876100 · Cited by 358 · see citing works

Plasma Membrane Transporters for Arginine

Closs, E. I., Simon, A., Vékony, N., & Rotmann, A. (2004) · Journal of Nutrition · doi:10.1093/jn/134.10.2752s · Cited by 297 · see citing works

The role of asymmetric and symmetric dimethylarginines in renal disease

Schwedhelm, E., & Böger, R. H. (2011) · Nature Reviews Nephrology · doi:10.1038/nrneph.2011.31 · Cited by 262 · see citing works

Structure and Function of Cationic Amino Acid Transporters (CATs)

Closs, E. I., Boissel, J., Habermeier, A., & Rotmann, A. (2006) · The Journal of Membrane Biology · doi:10.1007/s00232-006-0875-7 · Cited by 249 · see citing works

Evidence for the Pathophysiological Role of Endogenous Methylarginines in Regulation of Endothelial NO Production and Vascular Function

Cardounel, A. J., Cui, H., Samouilov, A., Johnson, W., Kearns, P. N., Tsai, A.-L., Berka, V., & Zweier, J. L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603606200 · Cited by 246 · see citing works

Arginine de novo and nitric oxide production in disease states

Luiking, Y. C., Have, G. A. M. T., Wolfe, R. R., & Deutz, N. E. P. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00284.2012 · Cited by 243 · see citing works

Requirement of argininosuccinate lyase for systemic nitric oxide production

Erez, A., Nagamani, S. C. S., Shchelochkov, O. A., Premkumar, M. H., Campeau, P. M., Chen, Y., Garg, H. K., Li, L., Mian, A., Bertin, T. K., et al. (2011) · Nature Medicine · doi:10.1038/nm.2544 · Cited by 233 · see citing works

Amino acid sensing in dietary-restriction-mediated longevity: roles of signal-transducing kinases GCN2 and TOR

Gallinetti, J., Harputlugil, E., & Mitchell, J. R. (2012) · Biochemical Journal · doi:10.1042/bj20121098 · Cited by 231 · see citing works

Aldehyde dehydrogenase 1a1 mediates a GABA synthesis pathway in midbrain dopaminergic neurons

Kim, J.-I., Ganesan, S., Luo, S. X., Wu, Y.-W., Park, E., Huang, E. J., Chen, L., & Ding, J. B. (2015) · Science · doi:10.1126/science.aac4690 · Cited by 217 · see citing works

REGULATION OF CATIONIC AMINO ACID TRANSPORT: The Story of the CAT-1 Transporter

Hatzoglou, M., Fernandez, J., Yaman, İ., & Closs, E. I. (2004) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.23.011702.073120 · Cited by 207 · see citing works

Deorphanization of GPRC6A: A Promiscuous l-α-Amino Acid Receptor with Preference for Basic Amino Acids

Wellendorph, P., Hansen, K. B., Balsgaard, A., Greenwood, J. R., Egebjerg, J., & Bräuner‐Osborne, H. (2004) · Molecular Pharmacology · doi:10.1124/mol.104.007559 · Cited by 207 · see citing works

Substrate Specificity of NO Synthases: Detailed Comparison of l -Arginine, Homo- l -arginine, Their Nω-Hydroxy Derivatives, and Nω-Hydroxynor- l -arginine

Moali, C., Boucher, J., Sari, M., Stuehr, D. J., & Mansuy, D. (1998) · Biochemistry · doi:10.1021/bi980742t · Cited by 203 · see citing works

Putrescine catabolism in mammalian brain

Seiler, N., & Al‐Therib, M. J. (1974) · Biochemical Journal · doi:10.1042/bj1440029 · Cited by 201 · see citing works

The G Protein-Coupled Taste Receptor T1R1/T1R3 Regulates mTORC1 and Autophagy

Wauson, E., Zaganjor, E., Lee, A.-Y., Guerra, M. L., Ghosh, A. B., Bookout, A. L., Chambers, C. P., Jivan, A., McGlynn, K., Hutchison, M. R., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.08.001 · Cited by 197 · see citing works

Regulation of Internal Ribosomal Entry Site-mediated Translation by Phosphorylation of the Translation Initiation Factor eIF2α

Fernandez, J., Yaman, İ., Sarnow, P., Snider, M. D., & Hatzoglou, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201052200 · Cited by 196 · see citing works

Protein arginine methylation of non-histone proteins and its role in diseases

Han, W., Mundade, R., Lange, K., & Lu, T. (2013) · Cell Cycle · doi:10.4161/cc.27353 · Cited by 190 · see citing works

Homoarginine, Cardiovascular Risk, and Mortality

März, W., Meinitzer, A., Drechsler, C., Pilz, S., Krane, V., Kleber, M. E., Fischer, J. E., Winkelmann, B. R., Böhm, B. O., Ritz, E., et al. (2010) · Circulation · doi:10.1161/circulationaha.109.908988 · Cited by 186 · see citing works

Sustained Generation of Nitric Oxide and Control of Mycobacterial Infection Requires Argininosuccinate Synthase 1

Qualls, J. E., Subramanian, C., Rafi, W., Smith, A. M., Balouzian, L., DeFreitas, A. A., Shirey, K. A., Reutterer, B., Kernbauer, E., Stockinger, S., et al. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.07.012 · Cited by 184 · see citing works

Role of Dimethylarginine Dimethylaminohydrolases in the Regulation of Endothelial Nitric Oxide Production

Pope, A. J., Karuppiah, K. M., Kearns, P. N., Xia, Y., & Cardounel, A. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.037036 · Cited by 184 · see citing works

Role of arginine metabolism in immunity and immunopathology

Peranzoni, E., Marigo, I., Dolcetti, L., Ugel, S., Sonda, N., Taschin, E., Mantelli, B., Bronte, V., & Zanovello, P. (2007) · Immunobiology · doi:10.1016/j.imbio.2007.09.008 · Cited by 178 · see citing works

Argininosuccinate synthase: at the center of arginine metabolism.

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Citrulline: From metabolism to therapeutic use

Bahri, S., Zerrouk, N., Aussel, C., Moinard, C., Crenn, P. P., Curis, E., Chaumeil, J., Cynober, L., & Sfar, S. (2012) · Nutrition · doi:10.1016/j.nut.2012.07.002 · Cited by 175 · see citing works

Rat Liver Arginase: Kinetic Mechanism, Alternate Substrates, and Inhibitors

Reczkowski, R. S., & Ash, D. E. (1994) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1994.1276 · Cited by 168 · see citing works

Two Distinct Determinants of Ligand Specificity in T1R1/T1R3 (the Umami Taste Receptor)

Toda, Y., Nakagita, T., Hayakawa, T., Okada, S., Narukawa, M., Imai, H., Ishimaru, Y., & Misaka, T. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.494443 · Cited by 159 · see citing works

Targeting arginine metabolism pathway to treat arginine-dependent cancers

Qiu, F., Huang, J., & Sui, M. (2015) · Cancer Letters · doi:10.1016/j.canlet.2015.04.020 · Cited by 158 · see citing works

Channeling of Urea Cycle Intermediates in Situ in Permeabilized Hepatocytes

Cheung, C. W., Cohen, N. S., & Raijman, L. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84958-x · Cited by 156 · see citing works

Citrulline and nitrogen homeostasis: an overview

Breuillard, C., Cynober, L., & Moinard, C. (2015) · Amino Acids · doi:10.1007/s00726-015-1932-2 · Cited by 153 · see citing works

Analysis of Citrulline, Arginine, and Methylarginines Using High‐Performance Liquid Chromatography

Wu, G., & Meininger, C. J. (2008) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)00810-5 · Cited by 147 · see citing works

Homoarginine Levels Are Regulated by l -Arginine:Glycine Amidinotransferase and Affect Stroke Outcome

Choe, C., Atzler, D., Wild, P. S., Carter, A. M., Böger, R. H., Ojeda, F., Simova, O., Stockebrand, M. C., Lackner, K. J., Nabuurs, C. I. H. C., et al. (2013) · Circulation · doi:10.1161/circulationaha.112.000580 · Cited by 145 · see citing works

ARG2 impairs endothelial autophagy through regulation of MTOR and PRKAA/AMPK signaling in advanced atherosclerosis

Xiong, Y., Yepuri, G., Forbiteh, M., Yu, Y., Montani, J., Yang, Z., & Ming, X. (2014) · Autophagy · doi:10.4161/15548627.2014.981789 · Cited by 145 · see citing works

Arginine and Leucine regulate p70 S6 kinase and 4E-BP1 in intestinal epithelial cells

Ban, H., Shigemitsu, K., Yamatsuji, T., Haisa, M., Nakajo, T., Takaoka, M., Nobuhisa, T., Gündüz, M., Tanaka, N., & Naomoto, Y. (2004) · International Journal of Molecular Medicine · doi:10.3892/ijmm.13.4.537 · Cited by 142 · see citing works

Dimethylarginine Dimethylaminohydrolase-1 Is the Critical Enzyme for Degrading the Cardiovascular Risk Factor Asymmetrical Dimethylarginine

Hu, X., Atzler, D., Xu, X. Y., Zhang, P., Guo, H., Lu, Z., Fassett, J., Schwedhelm, E., Böger, R. H., Bache, R. J., et al. (2011) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.110.222638 · Cited by 138 · see citing works

Cloning and characterization of a Family C orphan G‐protein coupled receptor

Kuang, D., Yao, Y., Lam, J., Tsushima, R. G., & Hampson, D. R. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03025.x · Cited by 133 · see citing works

l-Arginine and its metabolites in kidney and cardiovascular disease

Popolo, A., Adesso, S., Pinto, A., Autore, G., & Marzocco, S. (2014) · Amino Acids · doi:10.1007/s00726-014-1825-9 · Cited by 126 · see citing works

Glutamine is an important precursor for de novo synthesis of arginine in humans

Ligthart‐Melis, G. C., van de Poll, M. C. G., Boelens, P. G., Dejong, C. H. C., Deutz, N. E. P., & van Leeuwen, P. A. M. (2008) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/87.5.1282 · Cited by 119 · see citing works

The GPCR , class C , group 6, subtype A ( GPRC6A ) receptor: from cloning to physiological function

Clemmensen, C., Smajilovic, S., Wellendorph, P., & Bräuner‐Osborne, H. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12365 · Cited by 103 · see citing works

Role of Neutral Amino Acid Transport and Protein Breakdown for Substrate Supply of Nitric Oxide Synthase in Human Endothelial Cells

Simon, A., Plies, L., Habermeier, A., Martiné, U., Reining, M., & Closs, E. I. (2003) · Circulation Research · doi:10.1161/01.res.0000097761.19223.0d · Cited by 102 · see citing works

Low homoarginine concentration is a novel risk factor for heart disease

Pilz, S., Meinitzer, A., Tomaschitz, A., Drechsler, C., Ritz, E., Krane, V., Wanner, C., Boehm, B. O., & Marz, W. (2011) · Heart · doi:10.1136/hrt.2010.220731 · Cited by 102 · see citing works

Broad-spectrum l-amino acid sensing by class 3 G-protein-coupled receptors

Conigrave, A. D., & Hampson, D. R. (2006) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2006.10.012 · Cited by 101 · see citing works

Argininosuccinate Synthase Expression Is Required to Maintain Nitric Oxide Production and Cell Viability in Aortic Endothelial Cells

Goodwin, B. L., Solomonson, L. P., & Eichler, D. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308160200 · Cited by 100 · see citing works

Mitochondrial Arginase II Modulates Nitric-Oxide Synthesis through Nonfreely Exchangeable l-Arginine Pools in Human Endothelial Cells

Topal, G., Brunet, A., Walch, L., Boucher, J., & David‐Dufilho, M. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.103747 · Cited by 100 · see citing works

Multiligand Specificity and Wide Tissue Expression of GPRC6A Reveals New Endocrine Networks

Pi, M., & Quarles, L. D. (2012) · Endocrinology · doi:10.1210/en.2011-2117 · Cited by 95 · see citing works

Safety and Effectiveness of Arginine in Adults

McNeal, C. J., Meininger, C. J., Reddy, D., Wilborn, C., & Wu, G. (2016) · Journal of Nutrition · doi:10.3945/jn.116.234740 · Cited by 93 · see citing works

Arginase‐II Induces Vascular Smooth Muscle Cell Senescence and Apoptosis Through p66Shc and p53 Independently of Its l ‐Arginine Ureahydrolase Activity: Implications for Atherosclerotic Plaque Vulnerability

Xiong, Y., Yu, Y., Montani, J., Yang, Z., & Ming, X. (2013) · Journal of the American Heart Association · doi:10.1161/jaha.113.000096 · Cited by 91 · see citing works

Homoarginine, arginine, and relatives: analysis, metabolism, transport, physiology, and pathology

Tsikas, D., & Wu, G. (2015) · Amino Acids · doi:10.1007/s00726-015-2055-5 · Cited by 90 · see citing works

Homoarginine and Cardiovascular Outcome in the Population-Based Dallas Heart Study

Atzler, D., Gore, M. O., Ayers, C. R., Choe, C., Böger, R. H., de Lemos, J. A., McGuire, D. K., & Schwedhelm, E. (2014) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.114.304398 · Cited by 89 · see citing works

Glutamine is a key regulator for amino acid-controlled cell growth through the mTOR signaling pathway in rat intestinal epithelial cells.

Nakajo, T., Yamatsuji, T., Ban, H., Shigemitsu, K., Haisa, M., Motoki, T., Noma, K., Nobuhisa, T., Matsuoka, J., Gunduz, M., et al. (2004) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2004.11.015 · Cited by 88 · see citing works

Arginine-induced stimulation of protein synthesis and survival in IPEC-J2 cells is mediated by mTOR but not nitric oxide

Bauchart‐Thevret, C., Cui, L., Wu, G., & Burrin, D. G. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00068.2010 · Cited by 88 · see citing works

Promiscuous activity of arginine:glycine amidinotransferase is responsible for the synthesis of the novel cardiovascular risk factor homoarginine

Davids, M., Ndika, J., Salomons, G. S., Blom, H. J., & Teerlink, T. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.08.020 · Cited by 87 · see citing works

Arginyltransferase ATE1 Catalyzes Midchain Arginylation of Proteins at Side Chain Carboxylates In Vivo

Wang, J., Han, X., Wong, C. C. L., Cheng, H., Aslanian, A., Xu, T., Leavis, P. C., Röder, H., Hedstrom, L., Yates, J. R., et al. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.12.017 · Cited by 86 · see citing works

Catabolism and safety of supplemental l-arginine in animals

Wu, Z., Hou, Y., Hu, S., Bazer, F. W., Meininger, C. J., McNeal, C. J., & Wu, G. (2016) · Amino Acids · doi:10.1007/s00726-016-2245-9 · Cited by 86 · see citing works

The biochemistry, measurement and current clinical significance of asymmetric dimethylarginine

Blackwell, S. (2009) · Annals of Clinical Biochemistry International Journal of Laboratory Medicine · doi:10.1258/acb.2009.009196 · Cited by 84 · see citing works

Reference Intervals for Plasma L-Arginine and the L-Arginine:Asymmetric Dimethylarginine Ratio in the Framingham Offspring Cohort

Lüneburg, N., Xanthakis, V., Schwedhelm, E., SULLIVAN, L. M., Maas, R., Anderssohn, M., Riederer, U., Glazer, N. L., Vasan, R. S., & Böger, R. H. (2011) · Journal of Nutrition · doi:10.3945/jn.111.148197 · Cited by 84 · see citing works

Arginine deprivation in cancer therapy

Feun, L. G., Kuo, M. T., & Savaraj, N. (2014) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0000000000000122 · Cited by 84 · see citing works

A direct screen for c-di-GMP modulators reveals a Salmonella Typhimurium periplasmic ʟ-arginine–sensing pathway

Mills, E., Petersen, E. M., Kulasekara, B. R., & Miller, S. I. (2015) · Science Signaling · doi:10.1126/scisignal.aaa1796 · Cited by 84 · see citing works

L-Homoarginine and cardiovascular disease

Atzler, D., Schwedhelm, E., & Choe, C. (2014) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0000000000000123 · Cited by 81 · see citing works

Protein arginine methyltransferases (PRMTs): Role in chromatin organization

Jahan, S., & Davie, J. R. (2014) · Advances in Biological Regulation · doi:10.1016/j.jbior.2014.09.003 · Cited by 80 · see citing works

Minireview: Nutrient Sensing by G Protein-Coupled Receptors

Wauson, E., Lorente-Rodríguez, A., & Cobb, M. H. (2013) · Molecular Endocrinology · doi:10.1210/me.2013-1100 · Cited by 79 · see citing works

AGXT2: a promiscuous aminotransferase

Rodionov, R. N., Jarzebska, N., Weiss, N., & Lentz, S. R. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2014.09.005 · Cited by 79 · see citing works

Homoarginine in the renal and cardiovascular systems

Pilz, S., Meinitzer, A., Gaksch, M., Grübler, M. R., Verheyen, N., Drechsler, C., Hartaigh, B. Ó., Lang, F. J. W., Alesutan, I., Voelkl, J. G. J., et al. (2015) · Amino Acids · doi:10.1007/s00726-015-1993-2 · Cited by 77 · see citing works

On the substrate specificity of nitric oxide synthase

Hecker, M., Walsh, D. T., & Vane, J. R. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)81434-a · Cited by 76 · see citing works

Arginyltransferase, Its Specificity, Putative Substrates, Bidirectional Promoter, and Splicing-derived Isoforms

Hu, R., Brower, C. S., Wang, H., Davydov, I. V., Sheng, J., Zhou, J., Kwon, Y. T., & Varshavsky, A. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604355200 · Cited by 76 · see citing works

Cloning of human agmatinase. An alternate path for polyamine synthesis induced in liver by hepatitis B virus

Mistry, S. K., Burwell, T., Chambers, R. M., Rudolph‐Owen, L. A., Spaltmann, F., Cook, W. J., & Morris, S. M. (2002) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00386.2001 · Cited by 73 · see citing works

Parenteral or Enteral Arginine Supplementation Safety and Efficacy

Rosenthal, M. D., Carrott, P. W., Patel, J. J., Kiraly, L. N., & Martindale, R. G. (2016) · Journal of Nutrition · doi:10.3945/jn.115.228544 · Cited by 73 · see citing works

Conversion of Arginine into Ornithine by Advanced Glycation in Senescent Human Collagen and Lens Crystallins

Sell, D. R., & Monnier, V. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408946200 · Cited by 65 · see citing works

Stable isotope dilution assay for liquid chromatography–tandem mass spectrometric determination of l-homoarginine in human plasma

Atzler, D., Mieth, M., Maas, R., Böger, R. H., & Schwedhelm, E. (2011) · Journal of Chromatography B · doi:10.1016/j.jchromb.2011.06.016 · Cited by 65 · see citing works

Arginine and Ornithine Are the Main Precursors for Citrulline Synthesis in Mice3

Marini, J. C. (2012) · Journal of Nutrition · doi:10.3945/jn.111.153825 · Cited by 65 · see citing works

Accessibility of endothelial and inducible nitric oxide synthase to the intracellular citrulline–arginine regeneration pathway

Shen, L., Beloussow, K., & Shen, W. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.09.003 · Cited by 60 · see citing works

Arginine Can Be Synthesized from Enteral Proline in Healthy Adult Humans

Tomlinson, C., Rafii, M., Ball, R. O., & Pencharz, P. B. (2011) · Journal of Nutrition · doi:10.3945/jn.110.137224 · Cited by 59 · see citing works

Regulation of Endothelial Nitric Oxide Synthase Activity by Protein-Protein Interaction

Su, Y. (2014) · Current Pharmaceutical Design · doi:10.2174/13816128113196660752 · Cited by 54 · see citing works

Glutamine: precursor or nitrogen donor for citrulline synthesis?

Marini, J. C., Didelija, I. C., Castillo, L., & Lee, B. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00080.2010 · Cited by 54 · see citing works

Homoarginine and mortality in an older population: the H oorn study

Pilz, S., Teerlink, T., Scheffer, P. G., Meinitzer, A., Rutters, F., Tomaschitz, A., Drechsler, C., Kienreich, K., Nijpels, G., Stehouwer, C. D. A., et al. (2013) · European Journal of Clinical Investigation · doi:10.1111/eci.12208 · Cited by 52 · see citing works

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Integrated molecular and behavioural data reveal deep circadian disruption in response to artificial light at night in male Great tits (Parus major)

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Changes of microbial and metabolome of the equine hindgut during oligofructose-induced laminitis

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Functional Amino Acids and Autophagy: Diverse Signal Transduction and Application

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Unlocking the Potential of Arginine Deprivation Therapy: Recent Breakthroughs and Promising Future for Cancer Treatment

Chu, Y., Lai, M., & Yeh, C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241310668 · Cited by 42 · see citing works

Potential anticancer activity of Mn (II) complexes containing arginine dithiocarbamate ligand on MCF-7 breast cancer cell lines

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Hepatic arginase 2 (Arg2) is sufficient to convey the therapeutic metabolic effects of fasting

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COVID-19: A Redox Disease—What a Stress Pandemic Can Teach Us About Resilience and What We May Learn from the Reactive Species Interactome About Its Treatment

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The Role of Fecal Microbiota in Liver Toxicity Induced by Perfluorooctane Sulfonate in Male and Female Mice

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Lighting up arginine metabolism reveals its functional diversity in physiology and pathology

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UHPLC Q-Exactive MS-Based Serum Metabolomics to Explore the Effect Mechanisms of Immunological Activity of Astragalus Polysaccharides With Different Molecular Weights

Li, K., Cui, L.-J., Cao, Y., Li, S., Shi, L., Qin, X., & Du, Y. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.595692 · Cited by 37 · see citing works

Metabolic Regulation of Immune Responses to Mycobacterium tuberculosis: A Spotlight on L-Arginine and L-Tryptophan Metabolism

Crowther, R. R., & Qualls, J. E. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.628432 · Cited by 37 · see citing works

A commensal protozoan attenuates Clostridioides difficile pathogenesis in mice via arginine-ornithine metabolism and host intestinal immune response

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Arginine is a disease modifier for polyQ disease models that stabilizes polyQ protein conformation

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Plasma Arginine and Citrulline are Elevated in Diabetic Retinopathy

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Endogenous Hemoprotein-Dependent Signaling Pathways of Nitric Oxide and Nitrite

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Efficacy and safety of pegzilarginase in arginase 1 deficiency (PEACE): a phase 3, randomized, double-blind, placebo-controlled, multi-centre trial

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iNOS in Macrophage Polarization: Pharmacological and Regulatory Insights

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Metabolic adaptation to calorie restriction

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Neuroprotection by agmatine: Possible involvement of the gut microbiome?

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Preclinical safety and antitumor activity of the arginine-degrading therapeutic enzyme pegzilarginase, a PEGylated, cobalt-substituted recombinant human arginase 1

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The role of arginase in aging: A systematic review

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Extracellular vesicles in metabolic perspective: mechanism and targeted therapy

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L‐lysine: Its antagonism with L‐arginine in controlling viral infection. Narrative literature review

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Serum Untargeted Metabolomics Reveal Potential Biomarkers of Progression of Diabetic Retinopathy in Asians

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Detection of arginase through the optical behaviour of liquid crystals due to the pH-dependent adsorption of stearic acid at the aqueous/liquid crystal interface

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Impact of acyl-homoserine lactones on the response of nitrogen cycling in sediment to florfenicol stress

Zhou, Q., Xie, X., Feng, F., Huang, S., & Sun, Y. (2021) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2021.147294 · Cited by 32 · 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

Role of the Transcriptional Regulator ArgR in the Connection between Arginine Metabolism and c-di-GMP Signaling in Pseudomonas putida

Barrientos‐Moreno, L., Molina‐Henares, M. A., Ramos‐González, M. I., & Espinosa‐Urgel, M. (2022) · Applied and Environmental Microbiology · doi:10.1128/aem.00064-22 · Cited by 31 · see citing works

Response of laying hens to L-arginine, L-citrulline and guanidinoacetic acid supplementation in reduced protein diet

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Pharmacokinetic Parameters of Watermelon (Rind, Flesh, and Seeds) Bioactive Components in Human Plasma: A Pilot Study to Investigate the Relationship to Endothelial Function

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Interplay Between Metabolic Pathways and Increased Oxidative Stress in Human Red Blood Cells

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The shifted balance of arginine metabolites in acute myocardial infarction patients and its clinical relevance

Mołek, P., Żmudzki, P., Włodarczyk, A., Nessler, J. M., & Zalewski, J. (2021) · Scientific Reports · doi:10.1038/s41598-020-80230-3 · Cited by 29 · see citing works

L-arginine: its role in human physiology, in some diseases and mainly in viral multiplication as a narrative literature review

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Catabolic pathway of arginine in Anabaena involves a novel bifunctional enzyme that produces proline from arginine

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Regulated Arginine Metabolism in Immunopathogenesis of a Wide Range of Diseases: Is There a Way to Pass between Scylla and Charybdis?

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Promotion of Anti-Tuberculosis Macrophage Activity by L-Arginine in the Absence of Nitric Oxide

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Urinary metabolic phenotyping of mucopolysaccharidosis type I combining untargeted and targeted strategies with data modeling

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ARG2, MAP4K5 and TSTA3 as Diagnostic Markers of Steroid-Induced Osteonecrosis of the Femoral Head and Their Correlation With Immune Infiltration

Yu, R., Zhang, J., Zhuo, Y., Xu, H., Ye, J., Tang, S., Liu, N., & Zhang, Y. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.691465 · Cited by 26 · see citing works

Gastroenteritis in children: Part II. Prevention and management.

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Metabolic control of type 2 immunity

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The Mechanisms of L-Arginine Metabolism Disorder in Endothelial Cells

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Quantitative, Targeted Analysis of Gut Microbiota Derived Metabolites Provides Novel Biomarkers of Early Diabetic Kidney Disease in Type 2 Diabetes Mellitus Patients

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Arginine Metabolism: Boundaries of Our Knowledge

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Arginine metabolism: nitric oxide and beyond

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Arginine: beyond protein

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Enzymes of Arginine Metabolism

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Arginine metabolism in vascular biology and disease

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