The DOI matches its Crossref record; 96 of the 96 references it cites were found in a registry or an index.
Recent advances in arginine metabolism: roles and regulation of the arginases
Open accessAbstract
As arginine can serve as precursor to a wide range of compounds, including nitric oxide, creatine, urea, polyamines, proline, glutamate and agmatine, there is considerable interest in elucidating mechanisms underlying regulation of its metabolism. It is now becoming apparent that the two isoforms of arginase in mammals play key roles in regulation of most aspects of arginine metabolism in health and disease. In particular, work over the past several years has focused on the roles and regulation of the arginases in vascular disease, pulmonary disease, infectious disease, immune cell function and cancer. As most of these topics have been considered in recent review articles, this review will focus more closely on results of recent studies on expression of the arginases in endothelial and vascular smooth muscle cells, post‐translational modulation of arginase activity and applications of arginase inhibitors in vivo .
Overview
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
Verification
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?
In the citing paper
“At the site of vascular injury, arginase is induced, converting arginine to urea and ornithine (8).”
From Dietary nitrate, nitric oxide, and restenosis (2011) · cites this paper as [8]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Vascular endothelial cells synthesize nitric oxide from L-arginine
Palmer, R. M. J., Ashton, D., & Moncada, S. (1988) · Nature · doi:10.1038/333664a0 · Cited by 4,786
Arginine metabolism: nitric oxide and beyond
WU, G., & MORRIS, S. M. (1998) · Biochemical Journal · doi:10.1042/bj3360001 · Cited by 2,811
Self-citationNitric oxide: A cytotoxic activated macrophage effector molecule
Hibbs, J. B., Taintor, R. R., Vavrin, Z., & Rachlin, E. M. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(88)80015-9 · Cited by 2,034
Regulation of immune responses by L-arginine metabolism
Bronte, V., & Zanovello, P. (2005) · Nature Reviews Immunology · doi:10.1038/nri1668 · Cited by 1,775
Metcalf, B. W., Bey, P., Danzin, C., Jung, M. J., Casara, P., & Vevert, J. (1978) · Journal of the American Chemical Society · doi:10.1021/ja00476a050 · Cited by 1,005
Rodrı́guez, P. C., & Ochoa, A. C. (2008) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00608.x · Cited by 743
Xia, Y., Dawson, V. L., Dawson, T. M., Snyder, S. H., & Zweier, J. L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.13.6770 · Cited by 717
Arginine Metabolism: Boundaries of Our Knowledge
Morris, S. M. (2007) · Journal of Nutrition · doi:10.1093/jn/137.6.1602s · Cited by 649
El Kasmi, K. C., Qualls, J. E., Pesce, J. T., Smith, A. M., Thompson, R. W., Henao-Tamayo, M., Basaraba, R. J., König, T., Schleicher, U., Koo, M.-S., et al. (2008) · Nature Immunology · doi:10.1038/ni.1671 · Cited by 646 · cited 1×
“Thus, mouse strains with ablation of arginase I expression in macrophages have recently been developed to demonstrate the role of this enzyme in modulating host defense against intracellular pathogens (El Kasmi et al., 2008).”
BackgroundComparative 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
Research works printed but not linked: 2
- Abumrad NN, 2004, Metabolic and Therapeutic Aspects of Amino Acids in Clinical Nutrition, 595
- Wu G, 2004, Metabolic and Therapeutic Aspects of Amino Acids in Clinical Nutrition, 153
Cited by
Sorted by citations
Microglial M1/M2 polarization and metabolic states
Orihuela, R., McPherson, C. A., & Harry, G. J. (2016) · British Journal of Pharmacology · doi:10.1111/bph.13139 · Cited by 2,070
From Monocytes to M1/M2 Macrophages: Phenotypical vs. Functional Differentiation
Italiani, P., & Boraschi, D. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00514 · Cited by 2,067
Xu, S., Ilyas, I., Little, P. J., Li, H., Kamato, D., Zheng, X., Luo, S., Li, Z., Liu, P., Han, J., et al. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000096 · Cited by 1,205
M1 and M2 Macrophages: Oracles of Health and Disease
Mills, C. D. (2012) · Critical Reviews in Immunology · doi:10.1615/critrevimmunol.v32.i6.10 · Cited by 1,169
Nitric oxide synthase in innate and adaptive immunity: an update
Bogdan, C. (2015) · Trends in Immunology · doi:10.1016/j.it.2015.01.003 · Cited by 862
Nitric oxide and redox mechanisms in the immune response
Wink, D. A., Hines, H. B., Cheng, R. Y. S., Switzer, C. H., Flores-Santana, W., Vitek, M. P., Ridnour, L. A., & Colton, C. A. (2011) · Journal of Leukocyte Biology · doi:10.1189/jlb.1010550 · Cited by 765
Eelen, G., de Zeeuw, P., Treps, L., Harjes, U., Wong, B. W., & Carmeliet, P. (2017) · Physiological Reviews · doi:10.1152/physrev.00001.2017 · Cited by 614
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
Steggerda, S. M., Bennett, M. K., Chen, J., Emberley, E. D., Huang, T. C., Janes, J. R., Li, W., MacKinnon, A. L., Makkouk, A., Marguier, G. M., et al. (2017) · Journal for ImmunoTherapy of Cancer · doi:10.1186/s40425-017-0308-4 · Cited by 503
Arginine 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
Molecular mechanisms underlying the activation of eNOS
Fleming, I. (2010) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-009-0767-7 · Cited by 437
Morris, S. M. (2016) · The Journal of Nutrition · doi:10.3945/jn.115.226621 · Cited by 435
M1 and M2 Macrophages: The Chicken and the Egg of Immunity
Mills, C. D., & Ley, K. F. (2014) · Journal of Innate Immunity · doi:10.1159/000364945 · Cited by 422
Grams, R. J., Santos, W. L., Scorei, I. R., Abad-García, A., Rosenblum, C. A., Biţă, A., Cerecetto, H., Viñas, C., & Soriano-Ursua, M. A. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00663 · Cited by 395
Diversion of aspartate in ASS1-deficient tumours fosters de novo pyrimidine synthesis
Rabinovich, S., Adler, L., Yizhak, K., Sarver, A., Silberman, A., Agron, S., Stettner, N., Sun, Q., Brandis, A., Helbling, D., et al. (2015) · Nature · doi:10.1038/nature15529 · Cited by 382
Chen, F., Wu, W., Millman, A., Craft, J. F., Chen, E., Patel, N. B., Boucher, J. L., Urban, J. F., Kim, C. C., & Gause, W. C. (2014) · Nature Immunology · doi:10.1038/ni.2984 · Cited by 355
Arginase: an old enzyme with new tricks
Caldwell, R. B., Toque, H. A., Narayanan, S. P., & Caldwell, R. W. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.03.006 · Cited by 358
Potential of Chlorella as a Dietary Supplement to Promote Human Health
Bito, T., Okumura, E., Fujishima, M., & Watanabe, F. (2020) · Nutrients · doi:10.3390/nu12092524 · Cited by 336
Impacts of arginine nutrition on embryonic and fetal development in mammals
Wu, G., Bazer, F. W., Satterfield, M. C., Li, X., Wang, X., Johnson, G. A., Burghardt, R. C., Dai, Z., Wang, J., & Wu, Z. (2013) · Amino Acids · doi:10.1007/s00726-013-1515-z · Cited by 308
Complement, C1q, and C1q-Related Molecules Regulate Macrophage Polarization
Bohlson, S. S., Oâ€TMConner, S. D., Hulsebus, H. J., Ho, M.-M., & Fraser, D. A. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00402 · Cited by 299
Majumdar, R., Barchi, B., Turlapati, S. A., Gagne, M., Minocha, R., Long, S. L., & Minocha, S. C. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.00078 · Cited by 273
Ley, K. F. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1701135 · Cited by 257
Local Arginase 1 Activity Is Required for Cutaneous Wound Healing
Campbell, L., Saville, C. R., Murray, P. J., Cruickshank, S. M., & Hardman, M. J. (2013) · Journal of Investigative Dermatology · doi:10.1038/jid.2013.164 · Cited by 254
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 250
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
Molecular Mechanisms of Nitric Oxide in Cancer Progression, Signal Transduction, and Metabolism
Somasundaram, V., Basudhar, D., Bharadwaj, G., No, J. H., Ridnour, L. A., Cheng, R. Y. S., Fujita, M., Thomas, D. D., Anderson, S. K., McVicar, D. W., et al. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7527 · Cited by 217
Arginine and Citrulline and the Immune Response in Sepsis
Wijnands, K. A. P., Castermans, T. M. R., Hommen, M., Meesters, D. M., & Poeze, M. (2015) · Nutrients · doi:10.3390/nu7031426 · Cited by 217
Inflammatory cytokines in pulmonary hypertension
Groth, A., Vrugt, B., Brock, M., Speich, R., Ulrich, S., & Huber, L. (2014) · Respiratory Research · doi:10.1186/1465-9921-15-47 · Cited by 198
Aghdam, M. S., & Bodbodak, S. (2013) · Scientia Horticulturae · doi:10.1016/j.scienta.2013.03.028 · Cited by 197
Mechanisms of Fish Macrophage Antimicrobial Immunity
Grayfer, L., Kerimoğlu, B., Yaparla, A., Hodgkinson, J. W., Xie, J., & Belosevic, M. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01105 · Cited by 191
Botts, S. R., Fish, J. E., & Howe, K. L. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.787541 · Cited by 181
Polyamine metabolism in Leishmania: from arginine to trypanothione
Colotti, G., & Ilari, A. (2010) · Amino Acids · doi:10.1007/s00726-010-0630-3 · Cited by 166
Metabolic Pathways Fueling the Endothelial Cell Drive
Li, X., Kumar, A., & Carmeliet, P. (2019) · Annual Review of Physiology · doi:10.1146/annurev-physiol-020518-114731 · Cited by 172
Macrophage-mediated injury and repair after ischemic kidney injury
Huen, S. C., & Cantley, L. G. (2014) · Pediatric Nephrology · doi:10.1007/s00467-013-2726-y · Cited by 166
The Proline Regulatory Axis and Cancer
Phang, J. M., Liu, W., Hancock, C. N., & Christian, K. J. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00060 · Cited by 164
Burleigh, A., Chanalaris, A., Gardiner, M. D., Driscoll, C., Boruc, O., Saklatvala, J., & Vincent, T. L. (2012) · Arthritis & Rheumatism · doi:10.1002/art.34420 · Cited by 161
Chandra, S., Romero, M. J., Shatanawi, A., Alkilany, A. M., Caldwell, R., & Caldwell, R. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01584.x · Cited by 162
Ino, Y., Yamazaki–Itoh, R., Oguro, S., Shimada, K., Kosuge, T., Závada, J., Kanai, Y., & Hiraoka, N. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055146 · Cited by 160
Postharvest Heat Treatment for Mitigation of Chilling Injury in Fruits and Vegetables
Aghdam, M. S., & Bodbodak, S. (2013) · Food and Bioprocess Technology · doi:10.1007/s11947-013-1207-4 · Cited by 146
Arginase Inhibitors: A Rational Approach Over One Century
Pudlo, M., Demougeot, C., & Girard, C. (2016) · Medicinal Research Reviews · doi:10.1002/med.21419 · Cited by 151
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
Schleicher, U., Paduch, K., Debus, A., Obermeyer, S., König, T., Kling, J. C., Ribechini, E., Dudziak, D., Mougiakakos, D., Murray, P. J., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.04.001 · Cited by 136
Biology of Bony Fish Macrophages
Hodgkinson, J. W., Grayfer, L., & Belosevic, M. (2015) · Biology · doi:10.3390/biology4040881 · Cited by 138
The significant role of amino acid metabolic reprogramming in cancer
Liu, X., Ren, B., Ren, J., Gu, M., You, L., & Zhao, Y.-P. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01760-1 · Cited by 147
Arginine and nitric oxide synthase: Regulatory mechanisms and cardiovascular aspects
Lorin, J., Zeller, M., Guilland, J.-C., Cottin, Y., Vergely, C., & Rochette, L. (2013) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201300033 · Cited by 126
Opportunities for Small Molecules in Cancer Immunotherapy
van der Zanden, S. Y., Luimstra, J. J., Neefjes, J., Borst, J., & Ovaa, H. (2020) · Trends in Immunology · doi:10.1016/j.it.2020.04.004 · Cited by 119
Zhu, X., Pribis, J. P., Rodrı́guez, P. C., Morris, S. M., Yoram Vodovotz, B., Billiar, T. R., & Ochoa, J. B. (2013) · Annals of Surgery · doi:10.1097/sla.0b013e31828611f8 · Cited by 118
Metformin in cardiovascular diabetology: a focused review of its impact on endothelial function
Ding, Y., Zhou, Y., Ling, P., Feng, X., Luo, S., Zheng, X., Little, P. J., Xu, S., & Weng, J. (2021) · Theranostics · doi:10.7150/thno.64706 · Cited by 121
Nonessential amino acid metabolism in breast cancer
Geck, R. C., & Toker, A. (2016) · Advances in Biological Regulation · doi:10.1016/j.jbior.2016.01.001 · Cited by 115
Mussai, F., Egan, S. A., Hunter, S., Webber, H. T., Fisher, J. P. H., Wheat, R. L., McConville, C. M., Sbirkov, Y., Wheeler, K., Bendle, G. M., et al. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-3443 · Cited by 115
Arginase: shedding light on the mechanisms and opportunities in cardiovascular diseases
Li, Z., Wang, L., Ren, Y., Huang, Y., Liu, W., Lv, Z., Lü, Q., Yu, Y., & Xiong, Y. (2022) · Cell Death Discovery · doi:10.1038/s41420-022-01200-4 · Cited by 118
Obesity-induced vascular dysfunction and arterial stiffening requires endothelial cell arginase 1
Bhatta, A., Yao, L., Xu, Z., Toque, H. A., Chen, J., Atawia, R. T., Fouda, A. Y., Bagi, Z. A., Lucas, R., Caldwell, R. B., et al. (2017) · Cardiovascular Research · doi:10.1093/cvr/cvx164 · Cited by 108
Zhang, X., Sheng, J., Li, F., Meng, D., & Shen, L. (2011) · Postharvest Biology and Technology · doi:10.1016/j.postharvbio.2011.07.006 · Cited by 107
Yergin, C. G., Roggerson, K. M., Lee, H., Golden‐Mason, L., Rosen, H. R., & Hahn, Y. S. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1501881 · Cited by 107
Arginine and Arginases Modulate Metabolism, Tumor Microenvironment and Prostate Cancer Progression
Matos, A., Carvalho, M., Bicho, M., & Ribeiro, R. J. T. (2021) · Nutrients · doi:10.3390/nu13124503 · Cited by 109
Regulatory roles for L-arginine in reducing white adipose tissue
Tan, B. (2012) · Frontiers in bioscience · doi:10.2741/4047 · Cited by 106
Central Role of Metabolism in Endothelial Cell Function and Vascular Disease
Bierhansl, L., Conradi, L., Treps, L., Dewerchin, M. A., & Carmeliet, P. (2017) · Physiology · doi:10.1152/physiol.00031.2016 · Cited by 107
Akinyemi, A. J., Thomé, G. R., Morsch, V. M., Stefanello, N., Goularte, J. F., Belló‐Klein, A., Oboh, G., & Schetinger, M. R. C. (2015) · Journal of Functional Foods · doi:10.1016/j.jff.2015.06.011 · Cited by 98
Arginases and arginine deficiency syndromes
Morris, S. M. (2011) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e32834d1a08 · Cited by 97
Zhang, X., Shen, L., Li, F., Meng, D., & Sheng, J. (2011) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf201812r · Cited by 97
Krause, B. J., Carrasco‐Wong, I., Caniuguir, A., Jorge Carvajal, C., Farías, M., & Casanello, P. C. (2012) · Placenta · doi:10.1016/j.placenta.2012.09.015 · Cited by 96
Zhang, X., Shen, L., Li, F., Meng, D., & Sheng, J. (2013) · Postharvest Biology and Technology · doi:10.1016/j.postharvbio.2012.12.019 · Cited by 96
Marchese, L., Nascimento, J. D. F., Damasceno, F. S., Bringaud, F., Michels, P. A. M., & Silber, A. M. (2018) · Pathogens · doi:10.3390/pathogens7020036 · Cited by 95
Narayanan, S. P., Rojas, M., Suwanpradid, J., Toque, H. A., Caldwell, R. W., & Caldwell, R. B. (2013) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2013.06.002 · Cited by 96
Regulation of Lymphocytes by Nitric Oxide
Bogdan, C. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-869-0_24 · Cited by 95
Zarić, B. L., Radovanović, J., Gluvic, Z. M., Stewart, A. J., Essack, M., Motwalli, O., Gojobori, T., & Isenović, E. R. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.551758 · Cited by 94
Role of Arginase in Vessel Wall Remodeling
Durante, W. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00111 · Cited by 94
Arginase impedes the resolution of colitis by altering the microbiome and metabolome
Baier, J., Gänsbauer, M., Gießler, C., Arnold, H., Muske, M., Schleicher, U., Lukassen, S., Ekici, A. B., Rauh, M., Daniel, C., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci126923 · Cited by 87
Guo, D., Zhang, X., Zhang, S.-Q., Zhang, S., Zhang, X., Yan, J., Dong, S.-Y., Zhu, K., Yang, X.-R., Fan, J., et al. (2024) · Molecular Cancer · doi:10.1186/s12943-024-02062-3 · Cited by 97
Riess, C., Shokraie, F., Classen, C. F., Kreikemeyer, B., Fiedler, T., Junghanß, C., & Maletzki, C. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000495382 · Cited by 88
Nelson, M. P., Christmann, B. S., Werner, J. L., Metz, A. E., Trevor, J. L., Lowell, C. A., & Steele, C. H. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1002558 · Cited by 86
Role of Arginase 1 from Myeloid Cells in Th2-Dominated Lung Inflammation
Barron, L., Smith, A. M., Kasmi, K. C. E., Qualls, J. E., Huang, X., Cheever, A. W., Borthwick, L. A., Wilson, M. S., Murray, P. J., & Wynn, T. A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0061961 · Cited by 85
Arginase-2 Mediates Diabetic Renal Injury
Morris, S. M., Gao, T., Cooper, T. K., Kepka‐Lenhart, D., & Awad, A. S. (2011) · Diabetes · doi:10.2337/db11-0901 · Cited by 88
Angiotensin II and NADPH Oxidase Increase ADMA in Vascular Smooth Muscle Cells
Luo, Z., Teerlink, T., Griendling, K. K., Aslam, S., Welch, W. J., & Wilcox, C. S. (2010) · Hypertension · doi:10.1161/hypertensionaha.110.152959 · Cited by 83
Transcriptional regulation of macrophage arginase 1 expression and its role in atherosclerosis
Pourcet, B., & Pineda‐Torra, I. (2013) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2012.10.003 · Cited by 82
Inhibition of human arginase I by substrate and product analogues
Costanzo, L. D., Ilies, M., Thorn, K. J., & Christianson, D. W. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.02.004 · Cited by 81
Hypoxic upregulation of arginase II in human lung endothelial cells
Krotova, K. Y., Patel, J. M., Block, E. R., & Zharikov, S. I. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00068.2010 · Cited by 81
FoxO4 Promotes Early Inflammatory Response Upon Myocardial Infarction via Endothelial Arg1
Zhu, M., Goetsch, S. C., Wang, Z., Luo, R., Hill, J. A., Schneider, J. W., Morris, S. M., & Liu, Z. (2015) · Circulation Research · doi:10.1161/circresaha.115.306919 · Cited by 80
Burrack, K. S., Burrack, A., Oko, L. M., Montgomery, S. A., Borst, L. B., Gill, R. G., & Morrison, T. E. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1201240 · Cited by 83
Mechanisms of endothelial dysfunction in rheumatoid arthritis: lessons from animal studies
Totoson, P., Maguin‐Gaté, K., Prati, C., Wendling, D., & Demougeot, C. (2014) · Arthritis Research & Therapy · doi:10.1186/ar4450 · Cited by 79
Binding of α,α-Disubstituted Amino Acids to Arginase Suggests New Avenues for Inhibitor Design
Ilies, M., Costanzo, L. D., Dowling, D., Thorn, K. J., & Christianson, D. W. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200443b · Cited by 78
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
Pilanc, P., Wojnicki, K., Roura, A.-J., Cyranowski, S., Ellert‐Miklaszewska, A., Ochocka, N., Gielniewski, B., Grzybowski, M. M., Błaszczyk, R., Stańczak, P. S., et al. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.703465 · Cited by 72
Geck, R. C., Foley, J. R., Stewart, T. M., Asara, J. M., Casero, R. A., & Toker, A. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012376 · Cited by 75
Immunohistochemical study of arginase 1 and 2 in various tissues of rats
Choi, S., Park, C., Ahn, M., Lee, J. H., & Shin, T. (2011) · Acta Histochemica · doi:10.1016/j.acthis.2011.09.002 · Cited by 70
Evolutionary Aspects of Macrophages Polarization
Edholm, E., Rhoo, K. H., & Robert, J. (2017) · Results and problems in cell differentiation · doi:10.1007/978-3-319-54090-0_1 · Cited by 70
N -carbamylglutamate and L-arginine improved maternal and placental development in underfed ewes
Zhang, H., Sun, L., Wang, Z., Deng, M., Nie, H., Zhang, G., Ma, T., & Wang, F. (2016) · Reproduction · doi:10.1530/rep-16-0067 · Cited by 69
Bokhary, S. U. F., Wang, L., Zheng, Y., & Jin, P. (2020) · Postharvest Biology and Technology · doi:10.1016/j.postharvbio.2020.111229 · Cited by 68
Narayanan, S. P., Xu, Z., Putluri, N., Sreekumar, A., Lemtalsi, T., Caldwell, R. W., & Caldwell, R. B. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.23 · Cited by 68
Role of trypanosomatid's arginase in polyamine biosynthesis and pathogenesis
Balaña‐Fouce, R., Alvarez, E. C., Álvarez‐Velilla, R., Fernandez‐Prada, C., Pérez‐Pertejo, Y., & Reguera, R. M. (2011) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2011.10.007 · Cited by 68
Leiva, A., Pardo, F., Ramírez, M. A., Farías, M., Casanello, P. C., & Sobrevía, L. (2011) · Experimental Diabetes Research · doi:10.1155/2011/349286 · Cited by 68
Nguyen, T. L., Chun, W., Kim, A., Kim, N., Roh, H., Lee, Y., Yi, M., Kim, S., Park, C., & Kim, D. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02059 · Cited by 66
Akomolafe, S. F., Oboh, G., Oyeleye, S. I., & Boligon, A. A. (2016) · NFS Journal · doi:10.1016/j.nfs.2016.06.001 · Cited by 69
The Role of Asymmetric Dimethylarginine and Arginine in the Failing Heart and Its Vasculature
Visser, M., Paulus, W. J., Vermeulen, M. A. R., Richir, M. C., Davids, M., Wisselink, W., de Mol, B. A. J. M., & van Leeuwen, P. A. M. (2010) · European Journal of Heart Failure · doi:10.1093/eurjhf/hfq158 · Cited by 66
Myeloid-derived Suppressor Cells (MDSCs) in Gliomas and Glioma-Development
Kohanbash, G., & Okada, H. (2012) · Immunological Investigations · doi:10.3109/08820139.2012.689591 · Cited by 65
Patra, S., Ghosh, A., Roy, S. S., Bera, S., Das, M., Talukdar, D., Ray, S., Wallimann, T., & Ray, M. (2012) · Amino Acids · doi:10.1007/s00726-011-0974-3 · Cited by 64
Arginase Signalling as a Key Player in Chronic Wound Pathophysiology and Healing
Szondi, D. C., Wong, J. K. F., Vardy, L. A., & Cruickshank, S. M. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.773866 · Cited by 64
Lv, Y., Li, M., Weng, L., Huang, H., Mao, Y., Yang, D. A., Wei, Q., Zhao, M., Qin, W. D., Rui, K., et al. (2023) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-023-02888-7 · Cited by 69
Metabolic reprogramming and interventions in angiogenesis
Liu, Y., Wu, Z., Li, Y., Chen, Y., Zhao, X., Wu, M., & Xia, Y. (2024) · Journal of Advanced Research · doi:10.1016/j.jare.2024.05.001 · Cited by 70
When Is It Appropriate to Use Arginine in Critical Illness?
Patel, J. J., Miller, K. R., Rosenthal, C. M., & Rosenthal, M. D. (2016) · Nutrition in Clinical Practice · doi:10.1177/0884533616652576 · Cited by 63
Metadata
- Authors
- Morris Jr, S. M.
- Venue
- British Journal of Pharmacology
- Publisher
- Wiley
- Published
- 2009-07
- Volume
- 157
- Issue
- 6
- Pages
- 922-930
- ISSN
- 0007-1188 (ISSN-L)
- 1476-5381
- PMC
- PMC2737650
- OpenAlex
- W1996295305
- Cited by
- 485
- References
- 96
- Citations by year
- 2026: 19 · 2025: 22 · 2024: 24 · 2023: 24 · 2022: 20 · 2021: 35 · 2020: 33 · 2019: 24 · 2018: 31 · 2017: 23 · 2016: 35 · 2015: 30 · 2014: 32 · 2013: 43 · 2012: 33
- FWCI
- 20.32
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- British Journal of Pharmacology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (GM64509, GM57384, R01GM057384, R01GM064509)
- Topics
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- 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
- Keywords
- arginine metabolism, arginase, nitric oxide, endothelial cells, vascular smooth muscle cells, post-translational regulation, arginase inhibitors, vascular disease, lung disease, immune cell function, cancer
- MeSH terms
- Animals, Arginase, Arginine, Cytosol, Disease Models, Animal, Endothelium, Vascular, Humans, Isoenzymes, Muscle, Smooth, Vascular, Gene Expression Regulation, Enzymologic, Mitochondrial Proteins
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