Structure of a unique binuclear manganese cluster in arginase

The CCP4 suite: programs for protein crystallography

Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,299 · see citing works

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,157 · see citing works

Improved methods for building protein models in electron density maps and the location of errors in these models

Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,650 · see citing works

Untersuchungen uber die Harnstoffbildung im Tierkörper

Krebs, H. A., & Henseleit, K. (1932) · Hoppe-Seyler´s Zeitschrift für physiologische Chemie · doi:10.1515/bchm2.1932.210.1-2.33 · Cited by 3,113 · see citing works

Raster3D Version 2.0. A program for photorealistic molecular graphics

Merritt, E. A., & Murphy, M. E. P. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994006396 · Cited by 2,531 · see citing works

Crystallographic R Factor Refinement by Molecular Dynamics

Brünger, A. T., Kuriyan, J., & Karplus, M. (1987) · Science · doi:10.1126/science.235.4787.458 · Cited by 1,965 · see citing works

The crystal structure of urease from Klebsiella aerogenes

Jabri, E., Carr, M., Hausinger, R. P., & Karplus, P. A. (1995) · Science · doi:10.1126/science.7754395 · Cited by 830 · see citing works

A fast algorithm for rendering space-filling molecule pictures

Bacon, D., & Anderson, W. (1988) · Journal of Molecular Graphics · doi:10.1016/s0263-7855(98)80030-1 · Cited by 617 · see citing works

Carbonic Anhydrase: Evolution of the Zinc Binding Site by Nature and by Design

Christianson, D. W., & Fierke, C. A. (1996) · Accounts of Chemical Research · doi:10.1021/ar9501232 · Cited by 476 · see citing works

Arginase Induction by Suppressors of Nitric Oxide Synthesis (IL-4, IL-10 and PGE2) in Murine Bone-Marrow-Derived Macrophages

Corraliza, I., Soler, G., Eichmann, K., & Modolell, M. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.1094 · Cited by 364 · see citing works

Multiple catalytic functions of brain nitric oxide synthase. Biochemical characterization, cofactor-requirement, and the role of N omega-hydroxy-L-arginine as an intermediate

Klatt, P., Schmidt, K., Uray, G., & Mayer, B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82401-2 · Cited by 256 · see citing works

Inhibition of Rat Liver Arginase by an Intermediate in NO Biosynthesis, NG-Hydroxy-L-arginine: Implications for the Regulation of Nitric Oxide Biosynthesis by Arginase

Daghigh, F., Fukuto, J. M., & Ash, D. E. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1909 · Cited by 170 · 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

Carboxylate-histidine-zinc interactions in protein structure and function

Christianson, D. W., & Alexander, R. (1989) · Journal of the American Chemical Society · doi:10.1021/ja00198a065 · Cited by 165 · see citing works

The heterogeneity of arginases in rat tissues

Herzfeld, A., & Raper, S. M. (1976) · Biochemical Journal · doi:10.1042/bj1530469 · Cited by 162 · see citing works

Macrophage activation by culture in an anoxic environment

Albina, J. E., Henry, W. L., Mastrofrancesco, B., Martin, B. A., & Reichner, J. S. (1995) · The Journal of Immunology · doi:10.4049/jimmunol.155.9.4391 · Cited by 119 · see citing works

EPR evidence for binuclear manganese(II) centers in rat liver arginase

Reczkowski, R. S., & Ash, D. E. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00053a064 · Cited by 112 · see citing works

Function of arginase in lactating mammary gland

Yip, M. C. M., & Knox, W. E. (1972) · Biochemical Journal · doi:10.1042/bj1270893 · Cited by 104 · see citing works

Mutagenesis of Rat Liver Arginase Expressed in Escherichia coli: Role of Conserved Histidines

Cavalli, R. C., Burke, C. J., Soprano, D. R., Kawamoto, S., & Ash, D. E. (1994) · Biochemistry · doi:10.1021/bi00201a012 · Cited by 81 · see citing works

Metal Ion Interactions with Urease and UreD-Urease Apoproteins

Park, I., & Hausinger, R. P. (1996) · Biochemistry · doi:10.1021/bi952894j · Cited by 69 · see citing works

pH-Sensitive control of arginase by Mn(II) ions at submicromolar concentrations

Kuhn, N. J., Talbot, J., & Ward, S. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90031-d · Cited by 47 · see citing works

Nω-Hydroxy-L-Arginine, a Reactional Intermediate in Nitric Oxide Biosynthesis, Induces Cytostasis in Human and Murine Tumor Cells

Chénais, B., Yapo, A., Lepoivre, M., & Tenu, J. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.2429 · Cited by 42 · see citing works

Crystallization and oligomeric structure of rat liver arginase

Kanyo, Z. F., Chen, C.-Y., Daghigh, F., Ash, D. E., & Christianson, D. W. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90479-4 · Cited by 36 · see citing works

The interaction of macrophages and bacteria: A comparative study of the induction of tumoricidal activity and of reactive nitrogen intermediates

Keller, R., Gehri, R., Keist, R., Huf, E., & Kayser, F. H. (1991) · Cellular Immunology · doi:10.1016/0008-8749(91)90348-f · Cited by 31 · see citing works

Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors

Finnin, M. S., Donigian, J. R., Cohen, A., Richon, V. M., Rifkind, R. A., Marks, P. A., Breslow, R., & Pavletich, N. P. (1999) · Nature · doi:10.1038/43710 · Cited by 1,714 · see citing works

New developments in RiPP discovery, enzymology and engineering

Montalbán‐López, M., Scott, T. A., Ramesh, S., Rahman, I. R., van Heel, A. J., Viel, J. H., Bandarian, V., Dittmann, E., Genilloud, O., Goto, Y., et al. (2020) · Natural Product Reports · doi:10.1039/d0np00027b · Cited by 775 · see citing works

Structural Snapshots of Human HDAC8 Provide Insights into the Class I Histone Deacetylases

Somoza, J. R., Skene, R. J., Katz, B. A., Mol, C., Ho, J. D., Jennings, A. J., Luong, C., Arvai, A., Buggy, J. J., Chi, E., et al. (2004) · Structure · doi:10.1016/j.str.2004.04.012 · Cited by 710 · 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

Physiological implications of arginine metabolism in plants

Winter, G., Todd, C. D., Trovato, M., Forlani, G., & Funck, D. (2015) · Frontiers in Plant Science · doi:10.3389/fpls.2015.00534 · Cited by 652 · see citing works

Manganese Is Essential for Neuronal Health

Horning, K. J., Caito, S. W., Tipps, K. G., Bowman, A. B., & Aschner, M. (2015) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071714-034419 · Cited by 605 · see citing works

Th1/Th2-Regulated Expression of Arginase Isoforms in Murine Macrophages and Dendritic Cells

Munder, M., Eichmann, K., Morán, J. M., Centeno, F., Soler, G., & Modolell, M. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.7.3771 · Cited by 561 · see citing works

Principles of Mononucleating and Binucleating Ligand Design

Gavrilova, A. L., & Bosnich, B. (2004) · Chemical Reviews · doi:10.1021/cr020604g · Cited by 516 · see citing works

Boronic acid compounds as potential pharmaceutical agents

Yang, W., Gao, X., & Wang, B. (2003) · Medicinal Research Reviews · doi:10.1002/med.10043 · Cited by 500 · see citing works

A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels

Benini, S., Rypniewski, W. R., Wilson, K. S., Miletti, S., Ciurli, S., & Mangani, S. (1999) · Structure · doi:10.1016/s0969-2126(99)80026-4 · Cited by 502 · 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

Boron Containing Compounds as Protease Inhibitors

Smoum, R., Rubinstein, A., Dembitsky, V. M., & Srebnik, M. (2012) · Chemical Reviews · doi:10.1021/cr608202m · Cited by 451 · see citing works

Metal Activation of Enzymes in Nucleic Acid Biochemistry

Cowan, J. A. (1998) · Chemical Reviews · doi:10.1021/cr960436q · Cited by 405 · see citing works

Oxygen Production in Nature: A Light-Driven Metalloradical Enzyme Process

Tommos, C., & Babcock, Ǵ. (1998) · Accounts of Chemical Research · doi:10.1021/ar9600188 · Cited by 406 · see citing works

Catalysis By Metal-Activated Hydroxide in Zinc and Manganese Metalloenzymes

Christianson, D. W., & Cox, J. D. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.33 · Cited by 376 · see citing works

Metalloaminopeptidases: Common Functional Themes in Disparate Structural Surroundings

Lowther, W. T., & Matthews, B. W. (2002) · Chemical Reviews · doi:10.1021/cr0101757 · Cited by 347 · see citing works

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 336 · see citing works

Structure and function of the methionine aminopeptidases

Lowther, W. T., & Matthews, B. W. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00271-x · Cited by 320 · see citing works

Nitric oxide biosynthesis, nitric oxide synthase inhibitors and arginase competition for L-arginine utilization

Boucher, J., Moali, C., & Tenu, J. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050352 · Cited by 316 · see citing works

Manganese homeostasis in the nervous system

Chen, P., Chakraborty, S., Mukhopadhyay, S., Lee, E., Paoliello, M. M. B., Bowman, A. B., & Aschner, M. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13170 · Cited by 278 · see citing works

Structure, mechanism, and inhibition of histone deacetylases and related metalloenzymes

Lombardi, P. M., Cole, K., Dowling, D., & Christianson, D. W. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.08.004 · Cited by 279 · see citing works

Targeting Metalloenzymes for Therapeutic Intervention

Chen, A. Y., Adamek, R. N., Dick, B. L., Credille, C. V., Morrison, C. N., & Cohen, S. M. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00201 · Cited by 275 · see citing works

Human type II arginase: sequence analysis and tissue-specific expression

Morris, S. M., Bhamidipati, D., & Kepka‐Lenhart, D. (1997) · Gene · doi:10.1016/s0378-1119(97)00099-1 · Cited by 216 · see citing works

Manganese Redox Enzymes and Model Systems: Properties, Structures, and Reactivity

Law, N. A., Caudle, M. T., & Pecoraro, V. L. (1998) · Advances in inorganic chemistry · doi:10.1016/s0898-8838(08)60152-x · Cited by 209 · see citing works

Structure and Function of Arginases

Ash, D. E. (2004) · Journal of Nutrition · doi:10.1093/jn/134.10.2760s · Cited by 204 · see citing works

Structural Studies of Human Histone Deacetylase 8 and Its Site-Specific Variants Complexed with Substrate and Inhibitors^,

Dowling, D. P., Gantt, S. L., Gattis, S. G., Fierke, C. A., & Christianson, D. W. (2008) · Biochemistry · doi:10.1021/bi801610c · Cited by 200 · see citing works

Histone deacetylase 10 structure and molecular function as a polyamine deacetylase

Hai, Y., Shinsky, S. A., Porter, N. J., & Christianson, D. W. (2017) · Nature Communications · doi:10.1038/ncomms15368 · Cited by 200 · see citing works

Biosynthesis of polyamines and polyamine-containing molecules

Michael, A. J. (2016) · Biochemical Journal · doi:10.1042/bcj20160185 · Cited by 180 · see citing works

Crystal structure of human arginase I at 1.29-Å resolution and exploration of inhibition in the immune response

Costanzo, L. D., Sabio, G., Mora, A., Rodrı́guez, P. C., Ochoa, A. C., Centeno, F., & Christianson, D. W. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504027102 · Cited by 190 · see citing works

Unusual zinc-binding mode of HDAC6-selective hydroxamate inhibitors

Porter, N. J., Mahendran, A., Breslow, R., & Christianson, D. W. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1718823114 · Cited by 190 · see citing works

Structural chemistry and biology of manganese metalloenzymes

Christianson, D. W. (1997) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(97)88477-5 · Cited by 190 · see citing works

Inducible NO Synthase–DependentS-Nitrosylation and Activation of Arginase1 Contribute to Age-Related Endothelial Dysfunction

Santhanam, L., Lim, H. K., Lim, H. K., Miriel, V. A., Brown, T. R., Patel, M. D., Balanson, S., Ryoo, S., Anderson, M., Irani, K., et al. (2007) · Circulation Research · doi:10.1161/circresaha.107.157727 · Cited by 184 · see citing works

Crystal Structure of the Oxygen-Evolving Complex of Photosystem II

Barber, J. P. (2008) · Inorganic Chemistry · doi:10.1021/ic701835r · Cited by 184 · see citing works

Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli

Wilce, M. C. J., Bond, C. S., Dixon, N. E., Freeman, H. C., Guss, J. M., Lilley, P. E., & Wilce, M. C. J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3472 · Cited by 182 · 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

Hepatic metal ion transporter ZIP8 regulates manganese homeostasis and manganese-dependent enzyme activity

Lin, W. Y., Vann, D. R., Doulias, P., Wang, T., Landesberg, G. P., Li, X., Ricciotti, E., Scalia, R. G., He, M., Hand, N. J., et al. (2017) · Journal of Clinical Investigation · doi:10.1172/jci90896 · Cited by 173 · see citing works

Metalloproteomics, metalloproteomes, and the annotation of metalloproteins

Maret, W. (2010) · Metallomics · doi:10.1039/b915804a · Cited by 172 · see citing works

Mouse Model for Human Arginase Deficiency

Iyer, R. K., Yoo, P. K., Kern, R. M., Rozengurt, N., Tsoa, R. W., O’Brien, W. E., Yu, H., Grody, W. W., & Cederbaum, S. D. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.13.4491-4498.2002 · Cited by 171 · see citing works

Arginase-boronic acid complex highlights a physiological role in erectile function.

Christianson, D. W., Cox, J. D., Kim, N. N., & Traish, A. M. (1999) · Nature Structural Biology · doi:10.1038/14929 · Cited by 170 · see citing works

The leishmanicidal flavonols quercetin and quercitrin target Leishmania (Leishmania) amazonensis arginase

da Silva, E. R., Maquiaveli, C. D. C., & Magalhães, P. P. (2012) · Experimental Parasitology · doi:10.1016/j.exppara.2012.01.015 · Cited by 168 · see citing works

Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis

Whittington, D. A., Rusche, K. M., Shin, H., Fierke, C. A., & Christianson, D. W. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1432990100 · Cited by 167 · see citing works

Arginase: Structure, Mechanism, and Physiological Role in Male and Female Sexual Arousal

Christianson, D. W. (2005) · Accounts of Chemical Research · doi:10.1021/ar040183k · Cited by 168 · see citing works

Arginase and vascular aging

Santhanam, L., Christianson, D. W., Nyhan, D. P., & Berkowitz, D. E. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.90627.2008 · Cited by 166 · see citing works

Polyamine metabolism in Leishmania: from arginine to trypanothione

Colotti, G., & Ilari, A. (2010) · Amino Acids · doi:10.1007/s00726-010-0630-3 · Cited by 165 · see citing works

Regulation of Plant Arginase by Wounding, Jasmonate, and the Phytotoxin Coronatine

Chen, H., McCaig, B. C., Melotto, M., He, S. Y., & Howe, G. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407151200 · Cited by 162 · see citing works

Global folds of proteins with low densities of NOEs using residual dipolar couplings: application to the 370-residue maltodextrin-binding protein

Mueller, G. A., Choy, W., Yang, D., Forman-Kay, J. D., Venters, R. A., & Kay, L. E. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3842 · Cited by 163 · see citing works

The human arginases and arginase deficiency

Iyer, R. K., Jenkinson, C. P., Vockley, J. G., Kern, R. M., Grody, W. W., & Cederbaum, S. D. (1998) · Journal of Inherited Metabolic Disease · doi:10.1023/a:1005313809037 · Cited by 158 · see citing works

A revised model of the active site of alternative oxidase

Andersson, M. E., & Nordlund, P. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00376-2 · Cited by 154 · see citing works

Structural Basis of the Antiproliferative Activity of Largazole, a Depsipeptide Inhibitor of the Histone Deacetylases

Cole, K. E., Dowling, D. P., Boone, M. A., Phillips, A. J., & Christianson, D. W. (2011) · Journal of the American Chemical Society · doi:10.1021/ja205972n · Cited by 153 · see citing works

Redox dynamics of manganese as a mitochondrial life-death switch

Smith, M. R., Fernandes, J., Go, Y., & Jones, D. P. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.10.126 · Cited by 150 · see citing works

Aminoboronic acids and esters: from synthetic challenges to the discovery of unique classes of enzyme inhibitors

Touchet, S., Carreaux, F., Carboni, B., Bouillon, A., & Boucher, J. (2011) · Chemical Society Reviews · doi:10.1039/c0cs00154f · Cited by 147 · see citing works

Boron Chemicals in Drug Discovery and Development: Synthesis and Medicinal Perspective

Das, B. C., Nandwana, N. K., Das, S., Nandwana, V., Shareef, M. A., Das, Y., Saito, M., Weiss, L. M., Almaguel, F. A., Hosmane, N. S., et al. (2022) · Molecules · doi:10.3390/molecules27092615 · Cited by 147 · see citing works

Structure, mechanism, and inhibition of the zinc-dependent histone deacetylases

Porter, N. J., & Christianson, D. W. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.01.004 · Cited by 146 · see citing works

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 147 · see citing works

Effects of the New Arginase Inhibitor Nω-Hydroxy-nor-l-Arginine on NO Synthase Activity in Murine Macrophages

Tenu, J., Lepoivre, M., Moali, C., Brollo, M., Mansuy, D., & Boucher, J. (1999) · Nitric Oxide · doi:10.1006/niox.1999.0255 · Cited by 141 · see citing works

Inhibition of Mn2+2-Arginase by Borate Leads to the Design of a Transition State Analogue Inhibitor, 2(S)-Amino-6-boronohexanoic Acid

Baggio, R. F., Elbaum, D., Kanyo, Z. F., Carroll, P. J., Cavalli, R. C., Ash, D. E., & Christianson, D. W. (1997) · Journal of the American Chemical Society · doi:10.1021/ja971312d · Cited by 139 · see citing works

Crystal structures of Bacillus caldovelox arginase in complex with substrate and inhibitors reveal new insights into activation, inhibition and catalysis in the arginase superfamily

Bewley, M. C., Jeffrey, P. D., Patchett, M. L., Kanyo, Z. F., & Baker, E. N. (1999) · Structure · doi:10.1016/s0969-2126(99)80056-2 · Cited by 138 · see citing works

Hyperargininemia due to liver arginase deficiency

Crombez, E. A., & Cederbaum, S. D. (2004) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2004.11.004 · Cited by 135 · see citing works

Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective

Clemente, G. S., van Waarde, A., Antunes, I. F., Dömling, A. S. S., & Elsinga, P. H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155291 · Cited by 138 · see citing works

Recent advances in the understanding of the biological chemistry of manganese

Yocum, C. F., & Pecoraro, V. L. (1999) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)80031-3 · Cited by 133 · see citing works

Crystal structure and mechanism of human L‐arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis

Humm, A., Fritsche, E., Steinbacher, S., & Huber, R. (1997) · The EMBO Journal · doi:10.1093/emboj/16.12.3373 · Cited by 127 · see citing works

Active sites of transition-metal enzymes with a focus on nickel

Ermler, U., Grabarse, W., Shima, S., Goubeaud, M., & Thauer, R. K. (1998) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(98)80095-x · Cited by 125 · see citing works

Real-Time Monitoring of Arsenic Trioxide Release and Delivery by Activatable T1 Imaging

Zhao, Z., Wang, X., Zhang, Z., Zhang, H., Liu, H., Zhu, X., Li, H., Chi, X., Yin, Z., & Gao, J. (2015) · ACS Nano · doi:10.1021/nn506640h · Cited by 120 · see citing works

Quantitative analysis of dinuclear manganese(II) EPR spectra

Golombek, A. P., & Hendrich, M. P. (2003) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2003.07.001 · Cited by 117 · see citing works

Solvent Structure and Hammerhead Ribozyme Catalysis

Martick, M. M., Lee, T., York, D. M., & Scott, W. G. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.03.010 · Cited by 116 · see citing works

A Quantum Chemical Study of Hydrogen Abstraction from Manganese-Coordinated Water by a Tyrosyl Radical: A Model for Water Oxidation in Photosystem II

Blomberg, M. R. A., Siegbahn, P. E. M., Styring, S., Babcock, Ǵ., Åkermark, B., & Korall, P. (1997) · Journal of the American Chemical Society · doi:10.1021/ja9642323 · Cited by 115 · see citing works

Dietary flavonoids fisetin, luteolin and their derived compounds inhibit arginase, a central enzyme in Leishmania (Leishmania) amazonensis infection

Manjolin, L. C., dos Reis, M. B. G., Maquiaveli, C. D. C., Santos‐Filho, O. A., & da Silva, E. R. (2013) · Food Chemistry · doi:10.1016/j.foodchem.2013.05.025 · Cited by 114 · see citing works

Neutralization of NET-associated human ARG1 enhances cancer immunotherapy

Canè, S., Barouni, R. M., Fabbi, M., Cuozzo, J. W., Fracasso, G., Adamo, A., Ugel, S., Trovato, R., Sanctis, F. D., Giacca, M., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.abq6221 · Cited by 112 · see citing works

The structure of human ADP-ribosylhydrolase 3 (ARH3) provides insights into the reversibility of protein ADP-ribosylation

Mueller‐Dieckmann, C., Kernstock, S., Lisurek, M., von Kries, J. P., Haag, F., Weiss, M. S., & Koch‐Nolte, F. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606762103 · Cited by 112 · 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

DNA-dependent divalent cation binding in the nucleosome core particle

Davey, C. A., & Richmond, T. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172271399 · Cited by 110 · see citing works

Mechanism of Cis-Dihydroxylation and Epoxidation of Alkenes by Highly H2O2 Efficient Dinuclear Manganese Catalysts

de Boer, J. W., Browne, W. R., Brinksma, J., Alsters, P. L., Ronald Hage, B., & Feringa, B. L. (2007) · Inorganic Chemistry · doi:10.1021/ic7003613 · Cited by 106 · see citing works

Arginase-1 deficiency

Sin, Y. Y., Baron, G., Schulze, A., & Funk, C. D. (2015) · Journal of Molecular Medicine · doi:10.1007/s00109-015-1354-3 · Cited by 103 · see citing works

Chemical and structural biology of protein lysine deacetylases

Yoshida, M., Kudo, N., Kosono, S., & Ito, A. (2017) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.93.019 · Cited by 102 · see citing works

Arginase pathway in human endothelial cells in pathophysiological conditions

Bachetti, T. (2004) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2004.05.004 · Cited by 103 · see citing works

Toward the de Novo Design of a Catalytically Active Helix Bundle: A Substrate-Accessible Carboxylate-Bridged Dinuclear Metal Center

Costanzo, L. D., Wade, H., Geremia, S., Randaccio, L., Pavone, V., DeGrado, W. F., & Lombardi, A. (2001) · Journal of the American Chemical Society · doi:10.1021/ja010506x · Cited by 100 · see citing works

Structure of Histone Deacetylases

Marmorstein, R. (2001) · Structure · doi:10.1016/s0969-2126(01)00690-6 · Cited by 97 · see citing works

Inhibition of Leishmania (Leishmania) amazonensis and Rat Arginases by Green Tea EGCG, (+)-Catechin and (−)-Epicatechin: A Comparative Structural Analysis of Enzyme-Inhibitor Interactions

dos Reis, M. B. G., Manjolin, L. C., Maquiaveli, C. D. C., Santos‐Filho, O. A., & da Silva, E. R. (2013) · PLoS ONE · doi:10.1371/journal.pone.0078387 · Cited by 94 · see citing works

The New α-Amino Acid Nω-Hydroxy-nor- l -arginine: a High-Affinity Inhibitor of Arginase Well Adapted To Bind to Its Manganese Cluster

Custot, J., Moali, C., Brollo, M., Boucher, J., Delaforge, M., Mansuy, D., Tenu, J., & Zimmermann, J. (1997) · Journal of the American Chemical Society · doi:10.1021/ja970285o · Cited by 96 · see citing works

Roles of conserved residues in the arginase family

Perozich, J., Hempel, J. D., & Morris, S. M. (1998) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(97)00131-3 · Cited by 95 · see citing works

Comparative Characterization of Fungal Anthracenone and Naphthacenedione Biosynthetic Pathways Reveals an α-Hydroxylation-Dependent Claisen-like Cyclization Catalyzed by a Dimanganese Thioesterase

Li, Y., Chooi, Y., Sheng, Y., Valentine, J. S., & Tang, Y. (2011) · Journal of the American Chemical Society · doi:10.1021/ja206906d · Cited by 93 · see citing works

Vitamins and Trace Elements

Shenkin, A., & Roberts, N. B. (2012) · Elsevier eBooks · doi:10.1016/b978-1-4160-6164-9.00031-7 · Cited by 92 · see citing works

Structure of the manganese-bound manganese transport regulator of Bacillus subtilis

Glasfeld, A., Guédon, E., Helmann, J. D., & Brennan, R. G. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb951 · Cited by 93 · see citing works

Arginine and Polyamines Fate in Leishmania Infection

Muxel, S. M., Aoki, J. I., Fernandes, J. C. R., Laranjeira‐Silva, M. F., Zampieri, R. A., Acuña, S. M., Müller, K. E., Vanderlinde, R. H., & Floeter‐Winter, L. M. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02682 · Cited by 88 · see citing works

Unusual (μ-aqua)bis(μ-carboxylate) Bridge in Homometallic M(II) (M = Mn, Co and Ni) Two-Dimensional Compounds Based on the 1,2,3,4-Butanetetracarboxylic Acid: Synthesis, Structure, and Magnetic Properties

Cañadillas‐Delgado, L., Fabelo, Ó., Pasán, J., Delgado, F. S., Lloret, F., Julve, M., & Ruíz-Pérez, C. (2007) · Inorganic Chemistry · doi:10.1021/ic7006765 · Cited by 86 · see citing works

The Effects of the Metal Ion Substitution into the Active Site of Metalloenzymes: A Theoretical Insight on Some Selected Cases

Prejanò, M., Alberto, M. E., Russo, N., Toscano, M., & Marino, T. (2020) · Catalysts · doi:10.3390/catal10091038 · Cited by 83 · see citing works

The “open” and “closed” structures of the type-C inorganic pyrophosphatases from Bacillus subtilis and Streptococcus gordonii

Ahn, S., Milner, A. J., Fütterer, K., Konopka, M., Ilias, M., Young, T., & White, S. A. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5070 · Cited by 82 · see citing works

Structures of Metal-Substituted Human Histone Deacetylase 8 Provide Mechanistic Inferences on Biological Function,

Dowling, D., Gattis, S. G., Fierke, C. A., & Christianson, D. W. (2010) · Biochemistry · doi:10.1021/bi1005046 · Cited by 81 · see citing works

The aminopeptidase from Aeromonas proteolytica: structure and mechanism of co-catalytic metal centers involved in peptide hydrolysis

Holz, R. C. (2002) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(01)00470-2 · Cited by 80 · see citing works

Landornamides: Antiviral Ornithine‐Containing Ribosomal Peptides Discovered through Genome Mining

Bösch, N. M., Borsa, M., Greczmiel, U., Morinaka, B. I., Gugger, M. F., Oxenius, A., Vagstad, A. L., & Piel, J. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.201916321 · Cited by 80 · see citing works

Spectroscopic and mechanistic studies of dinuclear metallohydrolases and their biomimetic complexes

Daumann, L. J., Schenk, G., Ollis, D. L., & Gahan, L. R. (2013) · Dalton Transactions · doi:10.1039/c3dt52287c · Cited by 79 · see citing works

Structure and mechanism of action of a novel phosphoglycerate mutase from Bacillus stearothermophilus

Jedrzejas, M. J., Chander, M., Setlow, P., & Gunasekaran, K. (2000) · The EMBO Journal · doi:10.1093/emboj/19.7.1419 · Cited by 79 · see citing works

Development of Novel Arginase Inhibitors for Therapy of Endothelial Dysfunction

Steppan, J., Nyhan, D. P., & Berkowitz, D. E. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00278 · Cited by 78 · see citing works

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 75 · see citing works

Binding of the Microbial Cyclic Tetrapeptide Trapoxin A to the Class I Histone Deacetylase HDAC8

Porter, N. J., & Christianson, D. W. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00330 · Cited by 73 · see citing works

Evolution of the arginase fold and functional diversity

Dowling, D., Costanzo, L. D., Gennadios, H. A., & Christianson, D. W. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-7554-z · Cited by 73 · see citing works

Expression, purification, assay, and crystal structure of perdeuterated human arginase I

Costanzo, L. D., Moulin, M., Haertlein, M., Meilleur, F., & Christianson, D. W. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.04.036 · Cited by 71 · see citing works

Revealing the structure of the Mn-cluster of photosystem II by X-ray crystallography

Barber, J. P., & Murray, J. W. (2007) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2007.08.013 · Cited by 71 · see citing works

Flavonoids as efficient scaffolds: Recent trends for malaria, leishmaniasis, Chagas disease, and dengue

Kamdem, B. P., & Ferreira, E. I. (2019) · Phytotherapy Research · doi:10.1002/ptr.6383 · Cited by 70 · see citing works

Genomic organisation and transcription characterisation of the gene encoding Leishmania (Leishmania) amazonensis arginase and its protein structure prediction

da Silva, E. R., Castilho, T. M., Pioker‐Hara, F. C., da Silva, C. H. T. D. P., & Floeter‐Winter, L. M. (2002) · International Journal for Parasitology · doi:10.1016/s0020-7519(02)00002-4 · Cited by 69 · see citing works

The structure of rat liver arginase

Kanyo, Z. F. (1996) · Scholarly Commons (University of Pennsylvania) · Cited by 3 · see citing works

Arginase: A Binuclear Manganese Metalloenzyme

Ash, D. E., Cox, J. D., & Christianson, D. W. (2000) · CRC Press eBooks · doi:10.1201/9781482289893-23 · Cited by 72 · see citing works

Arginase

Bewley, M. C., & Flanagan, J. M. (2004) · Encyclopedia of Inorganic and Bioinorganic Chemistry · doi:10.1002/9781119951438.eibc0595 · Cited by 1 · see citing works

Manganese-Containing Arginase - Computational Studies

Russo, N., Leopoldini, M., & Toscano, M. (2012) · Springer eBooks · doi:10.1007/978-3-642-16712-6_598

Structure and Function of Arginases

Ash, D. E. (2004) · Journal of Nutrition · doi:10.1093/jn/134.10.2760s · Cited by 204 · see citing works