Arginine metabolism: nitric oxide and beyond
Open accessAbstract
Arginine is one of the most versatile amino acids in animal cells, serving as a precursor for the synthesis not only of proteins but also of nitric oxide, urea, polyamines, proline, glutamate, creatine and agmatine. Of the enzymes that catalyse rate-controlling steps in arginine synthesis and catabolism, argininosuccinate synthase, the two arginase isoenzymes, the three nitric oxide synthase isoenzymes and arginine decarboxylase have been recognized in recent years as key factors in regulating newly identified aspects of arginine metabolism. In particular, changes in the activities of argininosuccinate synthase, the arginases, the inducible isoenzyme of nitric oxide synthase and also cationic amino acid transporters play major roles in determining the metabolic fates of arginine in health and disease, and recent studies have identified complex patterns of interaction among these enzymes. There is growing interest in the potential roles of the arginase isoenzymes as regulators of the synthesis of nitric oxide, polyamines, proline and glutamate. Physiological roles and relationships between the pathways of arginine synthesis and catabolism in vivo are complex and difficult to analyse, owing to compartmentalized expression of various enzymes at both organ (e.g. liver, small intestine and kidney) and subcellular (cytosol and mitochondria) levels, as well as to changes in expression during development and in response to diet, hormones and cytokines. The ongoing development of new cell lines and animal models using cDNA clones and genes for key arginine metabolic enzymes will provide new approaches more clearly elucidating the physiological roles of these enzymes. Correspondence may be addressed to either Dr. G. Wu (e-mail g-wu@tamu.edu) or Dr. S. M. Morris, Jr. (e-mail sid@hoffman.mgen.pitt.edu) at the addresses given.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Peroxynitrite can mediate lipid nitration.
“For example, lipids are also a significant biological target for peroxynitrite, and although the species can abstract a hydrogen atom to initiate lipid peroxidation, a detrimental process that can lead to cytotoxicity in many cases (65, 766), peroxynitrite can also mediate lipid nitration (54, 1027).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [1027]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
Palmer, R. M. J., Ferrige, A. G., & Moncada, S. (1987) · Nature · doi:10.1038/327524a0 · Cited by 10,704 · see citing works
Nitric oxide synthases in mammals
Knowles, R. G., & Moncada, S. (1994) · Biochemical Journal · doi:10.1042/bj2980249 · Cited by 2,752 · see citing works
Stuehr, D. J., & Marletta, M. A. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.22.7738 · Cited by 1,126 · see citing works
Dissecting the Interaction between Nitric Oxide Synthase (NOS) and Caveolin
Garcı́a-Cardeña, G., Martasek, P., Masters, B. S. S., Skidd, P. M., Couet, J., Li, S., Lisanti, M. P., & Sessa, W. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.41.25437 · Cited by 821 · see citing works
Urea synthesis in enterocytes of developing pigs
Wu, G. (1995) · Biochemical Journal · doi:10.1042/bj3120717 · Cited by 138 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 24
- Stuehr, D. J. and Marletta, M. A. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 7738-7742
- Green, L. C., de Luzuriaga, K. R., Wagner, D. A., Rand, W., Istfan, N., Young, V. R. and Tannenbaum, S. R. (1981) Proc. Natl. Acad. Sci. U.S.A. 78, 7764-7768
- Wagner, D. A., Young, V. R. and Tannenbaum, S. R. (1983) Proc. Natl. Acad. Sci.
- Ignarro, L. J., Buga, G. M., Wood, K. S., Byrus, R. E. and Chaudhuri, G. (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 9265-9269
- Wakabayashi, Y. (1995) in Amino Acid Metabolism and Therapy in Health and Nutritional Disease (Cynober, L. A., ed.), pp. 89-98, CRC Press, London 48
- Phang, J. M., Yeh, G. C. and Scriver, C. R. (1995) in The Metabolic and Molecular Bases of Inherited Disease (Scriver, C. R., Beaudet, A. L., Sly, W. S. and Valle, D., eds.), pp. 1125-1146, McGraw-Hill Inc., New York 49
- Castillo, L., Chapman, T. E., Sanchez, M., Yu, Y. M., Burke, J. F., Ajami, A. M., Vogt, J. and Young, V. R. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 7749-7753
- Castillo, L., Beaumier, L., Ajami, A. M. and Young, V. R. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 11460-11465
- Bergman, E. N. and Heitmann, R. N. (1978) Fed. Proc. Fed. Am. Soc. Exp. Biol. 37, 1228-1232
- Valle, D. and Simell, O. (1995) in The Metabolic and Molecular Bases of Inherited Disease (Scriver, C. R., Beaudet, A. L., Sly, W. S. and Valle, D., eds.), pp. 1147-1185, McGraw-Hill Inc., New York
- Raiha, N. C. R. (1976) in The Urea Cycle (Grisolia, S., Baguena, R. and Mayor, F., eds.), pp. 261-272, John Wiley & Sons, New York 128
- Brusilow, S. W. and Horwich, A. L. (1995) in The Metabolic and Molecular Bases of Inherited Diseases, 7th edn. (Scriver, C. R., Beaudet, A. L., Sly, W. S. and Valle, D., eds.), pp. 1187-1232, McGraw-Hill, Inc., New York 131
- Morris, Jr., S. M. (1998) in Cellular and Molecular Biology of Nitric Oxide (Laskin, J. and Laskin, D., eds.), pp. 57-85, Marcel Dekker, Inc., New York 139
- Morris, Jr., S. M., Nakayama, D. K., Nussler, A. K., Liu, Z. Z., Davies, P., Pitt, B. R., Simmons, R. L. and Billiar, T. R. (1994) in The Biology of Nitric Oxide, Vol. 4 : Enzymology, Biochemistry and Immunology (Moncada, S., Freelisch, M., Busse, R. and Higgs, E. A., eds.), pp. 301-303, Portland Press, London 140
- Hecker, M., Sessa, W. C., Harris, H. J., Anggard, E. E. and Vane, J. R. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 8612-8616 141
- Sessa, W. C., Hecker, M., Mitchell, J. A. and Vane, J. R. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 8607-8611 154
- Bogle, R. G., Moncada, S., Pearson, J. D. and Mann, G. E. (1992) Br. J. Pharmacol. 105, 768-770 171
- Bogle, R. G., Baydoun, A. R. and Pearson, J. D. (1992) Biochem. J. 284, 15-18 180
- Iyengar, R., Stuehr, D. J. and Marletta, M. A. (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 6369-6373 189
- Vadon, S., Custot, J., Boucher, J.-L. and Mansuy, D. (1996) J. Chem. Soc. Perkin Trans. 1, 645-648 197
- Morris, Jr., S. M., Kepka-Lenhart, D. and Chen, L.-C. (1998) Am. J. Physiol., in the press 203
- Kuo, F. C., Hwu, W. L., Valle, D. and Darnell, J. E. (1991) Proc. Natl. Acad. Sci.
- Morrissey, J. J. and Klahr, S. (1997) Trans. Assoc. Am. Physicians 109, 51-57 278
- Kunz, D., Muhl, H., Walker, G. and Pfeilschifter, J. (1994) Proc. Natl. Acad. Sci.
Cited by
Sorted by citations
Nitric oxide and the immune response
Bogdan, C. (2001) · Nature Immunology · doi:10.1038/ni1001-907 · Cited by 3,447 · see citing works
Amino acids: Metabolism, functions, and nutrition
Wu, G. (2009) · Amino Acids · doi:10.1007/s00726-009-0269-0 · Cited by 3,004 · see citing works
Self-citationThe transcription factor Myc controls metabolic reprogramming upon T lymphocyte activation
Wang, R., Dillon, C. P., Shi, L. Z., Milasta, S., Carter, R., Finkelstein, D., McCormick, L. L., Fitzgerald, P., Chi, H., Munger, J., et al. (2011) · Immunity · doi:10.1016/j.immuni.2011.09.021 · Cited by 2,140 · see citing works
The metabolic signature of macrophage responses
Viola, A., Munari, F., Sánchez-Rodríguez, R., Scolaro, T., & Castegna, A. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01462 · Cited by 2,021 · see citing works
Regulation of immune responses by L-arginine metabolism
Bronte, V., & Zanovello, P. (2005) · Nature Reviews Immunology · doi:10.1038/nri1668 · Cited by 1,775 · 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
Self-citationNutrient-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
Nitric oxide in health and disease of the respiratory system
Ricciardolo, F. L. M., Sterk, P. J., Gaston, B., & Folkerts, G. (2004) · Physiological Reviews · doi:10.1152/physrev.00034.2003 · Cited by 903 · 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
Plant Proteins: Assessing Their Nutritional Quality and Effects on Health and Physical Function
Hertzler, S. R., Lieblein-Boff, J. C., Weiler, M., & Allgeier, C. (2020) · Nutrients · doi:10.3390/nu12123704 · Cited by 594 · see citing works
Strategies to increase nitric oxide signalling in cardiovascular disease
Lundberg, J. O., Gladwin, M. T., & Weitzberg, E. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4623 · Cited by 576 · see citing works
ARGINASE: A CRITICAL REGULATOR OF NITRIC OXIDE SYNTHESIS AND VASCULAR FUNCTION
Durante, W., Johnson, F. K., & Johnson, R. A. (2007) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2007.04638.x · Cited by 577 · see citing works
Vallance, P., & Leiper, J. (2004) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000128897.54893.26 · Cited by 553 · see citing works
Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541 · see citing works
Villalta, S. A., Nguyen, H. X., Deng, B., Gotoh, T., & Tidball, J. G. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn376 · Cited by 512 · see citing works
Arginase: A Multifaceted Enzyme Important in Health and Disease
Caldwell, R. W., Rodriguez, P. C., Toque, H. A., Narayanan, S. P., & Caldwell, R. B. (2018) · Physiological Reviews · doi:10.1152/physrev.00037.2016 · Cited by 495 · see citing works
Berkowitz, D. E., White, R., Li, D., Minhas, K. M., Cernetich, A., Kim, S., Burke, S., Shoukas, A. A., Nyhan, D., Champion, H. C., et al. (2003) · Circulation · doi:10.1161/01.cir.0000092948.04444.c7 · Cited by 486 · 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
Rochette, L., Lorin, J., Zeller, M., Guilland, J.-C., Lorgis, L., Cottin, Y., & Vergely, C. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.07.004 · Cited by 456 · see citing works
Anatomy of a Discovery: M1 and M2 Macrophages
Mills, C. D. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00212 · Cited by 449 · see citing works
Morris, S. M. (2016) · The Journal of Nutrition · doi:10.3945/jn.115.226621 · Cited by 435 · see citing works
Self-citationArginine deprivation and argininosuccinate synthetase expression in the treatment of cancer
Delage, B., Fennell, D. A., Nicholson, L., McNeish, I., Lemoine, N. R., Crook, T., & Szlosarek, P. W. (2010) · International Journal of Cancer · doi:10.1002/ijc.25202 · Cited by 441 · see citing works
The New Biology and Pharmacology of Glucagon
Müller, T. D., Finan, B., Clemmensen, C., DiMarchi, R. D., & Tschöp, M. H. (2017) · Physiological Reviews · doi:10.1152/physrev.00025.2016 · Cited by 419 · see citing works
McKnight, J. R., Satterfield, M. C., Jobgen, W. S., Smith, S. B., Spencer, T. E., Meininger, C. J., McNeal, C. J., & Wu, G. (2010) · Amino Acids · doi:10.1007/s00726-010-0598-z · Cited by 376 · see citing works
Self-citationXu, W., Kaneko, F. T., Zheng, S., Comhair, S. A. A., Janocha, A. J., Goggans, T., Thunnissen, F. B. J. M., Farver, C., Hazen, S. L., Jennings, C., et al. (2004) · The FASEB Journal · doi:10.1096/fj.04-2317fje · Cited by 369 · see citing works
Janaszak-Jasiecka, A., Płoska, A., Wierońska, J. M., Dobrucki, L. W., & Kalinowski, L. (2023) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-023-00423-2 · Cited by 358 · see citing works
Dietary L-arginine supplementation reduces fat mass in Zucker diabetic fatty rats
Fu, W. J., Haynes, T. E., Kohli, R., Hu, J., Shi, W., Spencer, T. E., Carroll, R. J., Meininger, C. J., & Wu, G. (2005) · The Journal of Nutrition · doi:10.1093/jn/135.4.714 · Cited by 353 · see citing works
Self-citationJobgen, W., Meininger, C. J., Jobgen, S. C., Li, P., Lee, M.-J., Smith, S. B., Spencer, T. E., Fried, S. K., & Wu, G. (2009) · The Journal of Nutrition · doi:10.3945/jn.108.096362 · Cited by 288 · see citing works
Self-citationDas, P., Lahiri, A., Lahiri, A., & Chakravortty, D. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000899 · Cited by 247 · see citing works
Targeting arginine-dependent cancers with arginine-degrading enzymes: opportunities and challenges
Phillips, M. M., Sheaff, M. T., & Szlosarek, P. W. (2013) · Cancer Research and Treatment · doi:10.4143/crt.2013.45.4.251 · Cited by 229 · see citing works
The Pharmacodynamics of L-Arginine
Böger, R. H. (2007) · The Journal of Nutrition · doi:10.1093/jn/137.6.1650s · Cited by 221 · see citing works
Dietary Nitrate and Physical Performance
Jones, A. M., Thompson, C., Wylie, L. J., & Vanhatalo, A. (2018) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-082117-051622 · Cited by 206 · see citing works
Medina, M. Á., Urdiales, J. L., Rodríguez-Caso, C., Ramírez, F. J., & Sánchez-Jiménez, F. (2003) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/713609209 · Cited by 198 · see citing works
The L-cell in nutritional sensing and the regulation of appetite
Spreckley, E. (2015) · Frontiers in Nutrition · doi:10.3389/fnut.2015.00023 · Cited by 198 · see citing works
Nitric oxide and vascular insulin resistance
Wu, G., & Meininger, C. J. (2009) · BioFactors · doi:10.1002/biof.3 · Cited by 190 · see citing works
Self-citationGray, M. J., Poljakovic, M., Kepka-Lenhart, D., & Morris, S. M. (2005) · Gene · doi:10.1016/j.gene.2005.04.004 · Cited by 191 · see citing works
Self-citationMechanisms of endothelial dysfunction in obesity.
Avogaro, A., & de Kreutzenberg, S. V. (2005) · Clinica Chimica Acta · doi:10.1016/j.cccn.2005.04.020 · Cited by 188 · see citing works
Arginase inhibition mediates cardioprotection during ischaemia–reperfusion
Jung, C., Gonon, A. T., Sjoquist, P.-O., Lundberg, J. O., & Pernow, J. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvp303 · Cited by 139 · see citing works
Bailey, S. J., Blackwell, J. R., Lord, T., Vanhatalo, A., Winyard, P. G., & Jones, A. M. (2015) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00192.2014 · Cited by 136 · see citing works
Bailey, S. J., Winyard, P. G., Vanhatalo, A., Blackwell, J. R., DiMenna, F. J., Wilkerson, D. P., & Jones, A. M. (2010) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00503.2010 · Cited by 132 · see citing works
Measuring splanchnic amino acid metabolism in vivo using stable isotopic tracers1,2
Stoll, B., & Burrin, D. G. (2006) · Journal of Animal Science · doi:10.2527/2006.8413_supple60x · Cited by 132 · see citing works
The role of arginine in infection and sepsis
Luiking, Y. C., Poeze, M., Ramsay, G., & Deutz, N. E. P. (2005) · Journal of Parenteral and Enteral Nutrition · doi:10.1177/01486071050290s1s70 · Cited by 131 · see citing works
Campbell, B., Roberts, M., Kerksick, C., Wilborn, C., Marcello, B., Taylor, L., Nassar, E., Leutholtz, B., Bowden, R., Rasmussen, C., et al. (2006) · Nutrition · doi:10.1016/j.nut.2006.06.003 · Cited by 128 · see citing works
Hoffman, B. G., Robertson, G., Zavaglia, B., Beach, M., Cullum, R., Lee, S., Soukhatcheva, G., Li, L., Wederell, E. D., Thiessen, N., et al. (2010) · Genome Research · doi:10.1101/gr.104356.109 · Cited by 115 · see citing works
Flam, B. R., Hartmann, P. J., Harrell-Booth, M., Solomonson, L. P., & Eichler, D. C. (2001) · Nitric Oxide · doi:10.1006/niox.2001.0340 · Cited by 103 · see citing works
Villalba, N., Sackheim, A. M., Nunez, I. A., Hill-Eubanks, D. C., Nelson, M. T., Wellman, G. C., & Freeman, K. (2017) · Journal of Neurotrauma · doi:10.1089/neu.2015.4340 · Cited by 99 · see citing works
Biochemical responses of healthy subjects during dietary supplementation with L-arginine
Evans, R. W., Fernstrom, J. D., Thompson, J., Morris, S. M., & Kuller, L. H. (2004) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2004.03.005 · Cited by 97 · see citing works
Self-citationCloning and Characterization of Human Agmatinase
Iyer, R. K., Kim, H. K., Tsoa, R. W., Grody, W. W., & Cederbaum, S. D. (2002) · Molecular Genetics and Metabolism · doi:10.1006/mgme.2001.3277 · Cited by 97 · see citing works
Davis, J. S., & Anstey, N. M. (2011) · Critical Care Medicine · doi:10.1097/ccm.0b013e3181ffd9f7 · Cited by 86 · see citing works
Gladwin, M. T. (2006) · Journal of Clinical Investigation · doi:10.1172/jci29807 · Cited by 85 · see citing works
McGee, D. J., Zabaleta, J., Viator, R. J., Testerman, T. L., Ochoa, A. C., & Mendz, G. L. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04105.x · Cited by 84 · see citing works
Theoretical analysis of biochemical pathways of nitric oxide release from vascular endothelial cells
Chen, K., & Popel, A. S. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.05.009 · Cited by 82 · see citing works
Protective Effects of Ghrelin on Fasting-Induced Muscle Atrophy in Aging Mice
Wu, C.-S., Wei, Q., Wang, H., Kim, D. M., Balderas, M., Wu, G., Lawler, J., Safe, S., Guo, S., Devaraj, S., et al. (2020) · The Journals of Gerontology: Series A · doi:10.1093/gerona/gly256 · Cited by 81 · see citing works
Self-citationAntihyperglycemic Effect of Catalpol in Streptozotocin-Induced Diabetic Rats
Huang, W.-J., Niu, H.-S., Lin, M.-H., Cheng, J.-T., & Hsu, F.-L. (2010) · Journal of Natural Products · doi:10.1021/np9008317 · Cited by 80 · see citing works
Alizadeh, M., Safaeiyan, A., Ostadrahimi, A., Estakhri, R., Daneghian, S., Ghaffari, A., & Gargari, B. P. (2012) · Annals of Nutrition and Metabolism · doi:10.1159/000335470 · Cited by 76 · see citing works
Safety of dietary supplementation with arginine in adult humans
McNeal, C. J., Meininger, C. J., Wilborn, C. D., Tekwe, C. D., & Wu, G. (2018) · Amino Acids · doi:10.1007/s00726-018-2594-7 · Cited by 72 · see citing works
Self-citationJourdan, M., Nair, K. S., Carter, R. E., Schimke, J., Ford, G. C., Marc, J., Aussel, C., & Cynober, L. (2015) · Clinical Nutrition · doi:10.1016/j.clnu.2014.04.019 · Cited by 73 · see citing works
l-Arginine transporters in cardiovascular disease: A novel therapeutic target
Chin-Dusting, J. P. F., Willems, L., & Kaye, D. M. (2007) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2007.08.001 · Cited by 69 · see citing works
Shen, L.-J., Lin, W.-C., Beloussow, K., & Shen, W.-C. (2003) · Cancer Letters · doi:10.1016/s030-43835(02)00693-6 · Cited by 66 · see citing works
Sandbakk, S. B., Sandbakk, Ø., Peacock, O., James, P., Welde, B., Stokes, K., Böhlke, N., & Tjønna, A. E. (2015) · Nitric Oxide · doi:10.1016/j.niox.2014.10.006 · Cited by 66 · see citing works
Immunonutrition in Critical Illness: What Is the Role?
McCarthy, M. S., & Martindale, R. G. (2018) · Nutrition in Clinical Practice · doi:10.1002/ncp.10102 · Cited by 58 · see citing works
Siervo, M., Stephan, B. C. M., Feelisch, M., & Bluck, L. J. C. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.05.032 · Cited by 52 · see citing works
Pharmaconutrition Review: Physiological Mechanisms
Pierre, J. F., Heneghan, A. F., Lawson, C. M., Wischmeyer, P. E., Kozar, R. A., & Kudsk, K. A. (2013) · Journal of Parenteral and Enteral Nutrition · doi:10.1177/0148607113493326 · Cited by 51 · see citing works
Clemmensen, C., Madsen, A. N., Smajilovic, S., Holst, B., & Bräuner-Osborne, H. (2012) · Amino Acids · doi:10.1007/s00726-011-1199-1 · Cited by 49 · see citing works
Pervin, M., Unno, K., Konishi, T., & Nakamura, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020508 · Cited by 41 · see citing works
van der Zwan, L. P., Scheffer, P. G., Dekker, J. M., Stehouwer, C. D. A., Heine, R. J., & Teerlink, T. (2011) · Clinical Science · doi:10.1042/cs20100595 · Cited by 40 · see citing works
Wang, H., Wang, Y., Li, X., Deng, X., Kong, Y., Wang, W., & Zhou, Y. (2022) · Cardiovascular Diabetology · doi:10.1186/s12933-022-01716-0 · Cited by 34 · see citing works
No effect of acute l-arginine supplementation on O2 cost or exercise tolerance
Vanhatalo, A., Bailey, S. J., DiMenna, F. J., Blackwell, J. R., Wallis, G. A., & Jones, A. M. (2013) · European Journal of Applied Physiology · doi:10.1007/s00421-013-2593-z · Cited by 32 · see citing works
Yu, E., Ruiz-Canela, M., Hu, F. B., Clish, C. B., Corella, D., Salas-Salvadó, J., Hruby, A., Fitó, M., Liang, L., Toledo, E., et al. (2017) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2016-3569 · Cited by 30 · see citing works
Oral L-Arginine Before Resistance Exercise Blunts Growth Hormone in Strength Trained Males
Forbes, S. C., Harber, V., & Bell, G. J. (2014) · International Journal of Sport Nutrition and Exercise Metabolism · doi:10.1123/ijsnem.2013-0106 · Cited by 25 · see citing works
Pinho, N., Bombaça, A. C., Wiśniewski, J. R., Dias-Lopes, G., Saboia-Vahia, L., Cupolillo, E., de Jesus, J. B., de Almeida, R. P., Padrón, G., Menna-Barreto, R., et al. (2022) · Antioxidants · doi:10.3390/antiox11020277 · Cited by 21 · see citing works
Lind, L., Larsson, A., & Teerlink, T. (2009) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2008.07.016 · Cited by 17 · see citing works
Menafra, D., de Angelis, C., Garifalos, F., Mazzella, M., Galdiero, G., Piscopo, M., Castoro, M., Verde, N., Pivonello, C., Simeoli, C., et al. (2022) · Journal of Endocrinological Investigation · doi:10.1007/s40618-021-01704-3 · Cited by 15 · see citing works
- Authors
- WU, G., & MORRIS, S. M.
- Affiliations
- Texas A&M University (US)
- University of Pittsburgh (US)
- Corresponding author
- WU, Guoyao
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1998-11-15
- Volume
- 336
- Issue
- 1
- Pages
- 1-17
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1219836
- OpenAlex
- W2419604885
- Cited by
- 2,811
- References
- 5
- Citations by year
- 2026: 57 · 2025: 102 · 2024: 128 · 2023: 110 · 2022: 117 · 2021: 140 · 2020: 139 · 2019: 102 · 2018: 113 · 2017: 112 · 2016: 115 · 2015: 127 · 2014: 102 · 2013: 117 · 2012: 124
- FWCI
- 4.92
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Agriculture
- American Heart Association (95013030)
- National Institutes of Health (5r01gm050897-03)
- National Institute of General Medical Sciences (GM50897, GM57384, R01GM057384)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Polyamine Metabolism and Applications
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- arginine metabolism, nitric oxide, argininosuccinate synthetase, inducible nitric oxide synthase, arginine decarboxylase, polyamines, proline biosynthesis, glutamate synthesis, urea synthesis, agmatine, cationic amino acid transporters, enzyme regulation, subcellular localization
- MeSH terms
- Amidinotransferases, Animals, Arginase, Arginine, Biological Transport, Carboxy-Lyases, Intestinal Mucosa, Kidney, Liver, Nitric Oxide, Nitric Oxide Synthase
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
