References

Roles of conserved residues in the arginase family

10.1016/s0167-4838(97)00131-3 · 1998 · External reference

Structure and Function of Arginases

10.1093/jn/134.10.2760s · 2004 · External reference

Role of L-arginine in nitric oxide synthesis and health in humans

10.1007/978-3-030-74180-8_10 · 2021 · External reference

Arginine metabolism: boundaries of our knowledge

10.1093/jn/137.6.1602s · 2007 · External reference

Arginase: shedding light on the mechanisms and opportunities in cardiovascular diseases

10.1038/s41420-022-01200-4 · 2022 · External reference

Arginase: an old enzyme with new tricks

10.1016/j.tips.2015.03.006 · 2015 · External reference

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

10.1161/jaha.113.000096 · 2013 · External reference

Isolation of human liver arginase cDNA and demonstration of nonhomology between the two human arginase genes

10.1016/s0006-291x(86)80333-3 · 1986 · External reference

The human gene for liver arginase (ARG1) is assigned to chromosome 6

1986 · External reference

Cloning and characterization of the human type II arginase gene

10.1006/geno.1996.0606 · 1996 · External reference

Structural and dynamic insights into the arginase isoforms: implications for selective inhibitor design

10.1021/acs.jmedchem.4c01429 · 2024 · External reference

10.1073/pnas.0504027102

10.1073/pnas.0504027102 · External reference

Regulation of enzymes of the urea cycle and arginine metabolism

10.1146/annurev.nutr.22.110801.140547 · 2002 · External reference

Mouse model for human arginase deficiency

10.1128/mcb.22.13.4491-4498.2002 · 2002 · External reference

Molecular cloning of cDNA for nonhepatic mitochondrial arginase (arginase II) and comparison of its induction with nitric oxide synthase in a murine macrophage-like cell line

10.1016/0014-5793(96)01015-0 · 1996 · External reference

Structural and functional characterization of C0021158, a high-affinity monoclonal antibody that inhibits Arginase 2 function via a novel non-competitive mechanism of action

10.1080/19420862.2020.1801230 · 2020 · External reference

Structure of a unique binuclear manganese cluster in arginase

10.1038/383554a0 · 1996 · External reference

Human arginase II: crystal structure and physiological role in male and female sexual arousal

10.1021/bi034340j · 2003 · External reference

Arginase: structure, mechanism, and physiological role in male and female sexual arousal

10.1021/ar040183k · 2005 · External reference

L-Arginine binding to liver arginase requires proton transfer to gateway residue His141 and stabilization of a salt bridge between Asp128 and Mn2+_A

10.1021/bi972874c · 1998 · External reference

Design of amino acid sulfonamides as transition-state analogue inhibitors of arginase

10.1021/ja036365b · 2003 · External reference

Insights on the participation of Glu256 and Asp204 in the oligomeric structure and cooperative effects of human arginase type I

2020 · External reference

Obesity-induced vascular dysfunction and arterial stiffening requires endothelial cell arginase 1

10.1093/cvr/cvx164 · 2017 · External reference

Crystal structure of human arginase I complexed with thiosemicarbazide reveals an unusual thiocarbonyl μ-sulfide ligand in the binuclear manganese cluster

10.1021/ja071567j · 2007 · External reference

Myeloid Cell-Derived Arginase in Cancer Immune Response

10.3389/fimmu.2020.00938 · 2020 · External reference

OxLDL triggers retrograde translocation of arginase2 in aortic endothelial cells via ROCK and mitochondrial processing peptidase

10.1161/circresaha.115.304262 · 2014 · External reference

Mitochondria-targeting sequence, a multi-role sorting sequence recognized at all steps of protein import into mitochondria

10.1093/oxfordjournals.jbchem.a022036 · 1998 · External reference

Translocation of proteins into mitochondria

10.1146/annurev.biochem.76.052705.163409 · 2007 · External reference

Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function

10.1021/bi970800v · 1997 · External reference

Replacing Mn2+ with Co2+ in human arginase I enhances cytotoxicity toward L-arginine auxotrophic cancer cell lines

10.1021/cb900267j · 2010 · External reference

A comparative study of the catalytic activity of human arginase I with Mn2+ and Co2+ metal ions

2020 · External reference

Insights into the interaction of human liver arginase with tightly and weakly bound manganese ions by chemical modification and site-directed mutagenesis studies

10.1016/s0003-9861(02)00204-7 · 2002 · External reference

Structure and function of non-native metal clusters in human arginase I

10.1021/bi301145n · 2012 · External reference

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

10.1111/j.1742-4658.2005.04874.x · 2005 · External reference

Non-chelating inhibition of manganese-containing arginase by borate

10.1016/j.jinorgbio.2004.05.005 · 2004 · External reference

An enzyme cascade with horseradish peroxidase readout for high-throughput screening and engineering of human arginase-1

2018 · External reference

Regulatory role of arginase I and II in nitric oxide, polyamine, and proline syntheses in endothelial cells

10.1152/ajpendo.2001.280.1.e75 · 2001 · External reference

Arginase Structure and Inhibition: Catalytic Site Plasticity reveals New Modulation Possibilities

10.1038/s41598-017-13366-4 · 2017 · External reference

Arginase as a potential target in the treatment of cardiovascular disease: reversal of arginine steal?

10.1093/cvr/cvt036 · 2013 · External reference

Arginase I is constitutively expressed in human granulocytes and participates in fungicidal activity

10.1182/blood-2004-07-2521 · 2005 · External reference

Suppression of T-cell functions by human granulocyte arginase

10.1182/blood-2006-11-010389 · 2006 · External reference

Expression of the liver form of arginase in erythrocytes

10.1016/s1096-7192(02)00034-3 · 2002 · External reference

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

10.1016/s0378-1119(97)00099-1 · 1997 · External reference

Arginase 2 deletion reduces hyperoxia-mediated retinal neurodegeneration through the regulation of polyamine metabolism

2014 · External reference

p38 mitogen-activated protein kinase is involved in arginase-II-mediated eNOS-uncoupling in endothelial cells

2013 · External reference

Mitochondrial expression of arginase II in male and female rat inner medullary collecting ducts

10.1369/jhc.4a6489.2005 · 2005 · External reference

Alternative activation of macrophages: mechanism and functions

10.1016/j.immuni.2010.05.007 · 2010 · External reference

Macrophage activation and polarization: nomenclature and experimental guidelines

10.1016/j.immuni.2014.06.008 · 2014 · External reference

Arginase II promotes macrophage inflammatory responses through mitochondrial reactive oxygen species, contributing to insulin resistance and atherogenesis

10.1161/jaha.112.000992 · 2012 · External reference

Arginase: a multifaceted enzyme important in health and disease

10.1152/physrev.00037.2016 · 2018 · External reference

Nitric oxide synthases: regulation and function

10.1093/eurheartj/ehr304 · 2012 · External reference

Arginase inhibition restores NOS coupling and reverses endothelial dysfunction and vascular stiffness in old rats

10.1152/japplphysiol.91393.2008 · 2009 · External reference

Inducible NO synthase dependent S-nitrosylation and activation of arginase1 contribute to age-related endothelial dysfunction

10.1161/circresaha.107.157727 · 2007 · External reference

Arginase and vascular aging

10.1152/japplphysiol.90627.2008 · 2008 · External reference

Intracellular l-arginine concentration does not determine NO production in endothelial cells: Implications on the “l-arginine paradox”

10.1016/j.bbrc.2011.09.112 · 2011 · External reference

Regulation of nitric oxide synthesis and apoptosis by arginase and arginine recycling

10.1093/jn/137.6.1616s · 2007 · External reference

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

10.1007/s000180050352 · 1999 · External reference

Insulin and the arginine paradox

10.1172/jci119166 · 1997 · External reference

The L-arginine paradox: importance of the L-arginine/asymmetrical dimethylarginine ratio

10.1016/j.pharmthera.2007.03.002 · 2007 · External reference

The caveolar nitric oxide synthase/arginine regeneration system for NO production in endothelial cells

10.1242/jeb.00361 · 2003 · External reference

A caveolar complex between the cationic amino acid transporter 1 and endothelial nitric-oxide synthase may explain the “arginine paradox”

10.1074/jbc.272.50.31213 · 1997 · External reference

Biochemical and functional profile of a newly developed potent and isozyme-selective arginase inhibitor

10.1016/s0022-3565(24)35048-7 · 1999 · External reference

Inhibition of human arginase I by substrate and product analogues

10.1016/j.abb.2010.02.004 · 2010 · External reference

Classical and slow-binding inhibitors of human type II arginase

10.1021/bi010783g · 2001 · External reference

The new α-amino acid Nω-hydroxy-nor-L-arginine: a high-affinity inhibitor of arginase well adapted to bind to its manganese cluster

10.1021/ja970285o · 1997 · External reference

Synthesis of quaternary α-amino acid based arginase inhibitors via the Ugi reaction

10.1016/j.bmcl.2013.06.092 · 2013 · External reference

Discovery of N-Substituted 3-Amino-4-(3-boronopropyl)pyrrolidine-3-carboxylic Acids as Highly Potent Third-Generation Inhibitors of Human Arginase I and II

10.1021/acs.jmedchem.9b00931 · 2019 · External reference

Inhibition of arginase by CB-1158 blocks myeloid cell-mediated immune suppression in the tumor microenvironment

10.1186/s40425-017-0308-4 · 2017 · External reference

Antitumor activity of the glutaminase inhibitor CB-839 in triple-negative breast cancer

10.1158/1535-7163.mct-13-0870 · 2014 · External reference

Arginase 1/2 inhibitor OATD-02: from discovery to first-in-man setup in cancer immunotherapy

10.1158/1535-7163.mct-22-0721 · 2023 · External reference

OATD-02, an orally bioavailable, potent dual arginase 1/2 inhibitor with excellent intracellular activity, enhances antitumor immunity

2021 · External reference

Investigation of mammal arginase inhibitory properties of natural ubiquitous polyphenols by using an optimized colorimetric microplate assay

2017 · External reference

Threeneo-Clerodane Diterpenoids fromTinospora cordifoliaStems and their Arginase Inhibitory Activities

10.1248/cpb.c24-00240 · 2024 · External reference

Arginine metabolism: nitric oxide and beyond

1998 · External reference

Endothelial nitric oxide production is tightly coupled to the citrulline-NO cycle

10.1016/j.niox.2007.07.001 · 2007 · External reference

Arginine, citrulline, and the citrulline-NO cycle in endothelial nitric oxide production

2016 · External reference

Targeting of endothelial nitric-oxide synthase to the cytoplasmic face of the Golgi complex or plasma membrane regulates Akt- versus calcium-dependent mechanisms for nitric oxide release

10.1074/jbc.m402155200 · 2004 · External reference

Insights into the arginine paradox: evidence against the importance of subcellular location of arginase and eNOS

10.1152/ajpheart.00755.2012 · 2013 · External reference

There is no direct competition between arginase and nitric oxide synthase for the common substrate l-arginine

10.1016/j.niox.2022.09.002 · 2022 · External reference

Metabolic barriers to cancer immunotherapy

10.1038/s41577-021-00541-y · 2021 · External reference

Immune control by amino acid catabolism: a new paradigm for tumor therapy

10.1038/s41568-019-0106-z · 2019 · External reference

Arginine regulation by myeloid derived suppressor cells and tolerance in cancer: mechanisms and therapeutic perspectives

10.1111/j.1600-065x.2008.00608.x · 2008 · External reference

Arginase I production in the tumor microenvironment by mature myeloid cells inhibits T-cell receptor expression and antigen-specific T-cell responses

10.1158/0008-5472.can-04-0465 · 2004 · External reference

Mitochondrial arginase-2 is a cell-autonomous regulator of CD8+ T cell function and antitumor efficacy

2019 · External reference

Regulatory T cells use arginase 2 to enhance their metabolic fitness in tissues

10.1172/jci.insight.129756 · 2019 · External reference

L-arginine modulates T cell metabolism and enhances survival and anti-tumor activity

10.1016/j.cell.2016.09.031 · 2016 · External reference

Regulation of immune responses by L-arginine metabolism

10.1038/nri1668 · 2005 · External reference

The immune regulation in cancer by the amino acid metabolizing enzymes ARG and IDO

10.1016/j.coph.2017.05.002 · 2017 · External reference

Arginase-2-specific cytotoxic T cells specifically recognize functional regulatory T cells

2021 · External reference

Arginase-2 specific CD8+ T cells react toward malignant and regulatory cells

2024 · External reference

OATD-02 validates the benefits of pharmacological inhibition of arginase 1 and 2 in cancer

2022 · External reference

Arginase 1 mediates increased blood pressure and contributes to vascular endothelial dysfunction in deoxycorticosterone acetate-salt hypertension

10.3389/fimmu.2013.00219 · 2013 · External reference

Increased arginase levels in heart failure represent a therapeutic target to rescue microvascular perfusion

10.3233/ch-2012-1617 · 2013 · External reference

Arginase inhibition reduces infarct size via nitric oxide, protein kinase C epsilon and mitochondrial ATP-dependent K+ channels

10.1016/j.ejphar.2013.04.044 · 2013 · External reference

Arginase inhibition improves endothelial function in patients with coronary artery disease and type 2 diabetes mellitus

10.1161/circulationaha.112.140335 · 2012 · External reference

Functions of arginase isoforms in macrophage inflammatory responses: impact on cardiovascular diseases and metabolic disorders

10.3389/fimmu.2014.00533 · 2014 · External reference

Stable expression of human arginase 1 does not suppress inflammation or M1 macrophage polarization in THP-1 monocytes

2025 · External reference

Macrophage-fibroblast crosstalk drives Arg1-dependent lung fibrosis via ornithine loading

2024 · External reference

Extracellular PKM2 facilitates organ-tissue fibrosis progression

2021 · External reference

Arginase-1-expressing macrophages suppress Th2 cytokine-driven inflammation and fibrosis

10.1371/journal.ppat.1000371 · 2009 · External reference

Arginase and pulmonary diseases

10.1007/s00210-008-0286-7 · 2008 · External reference

Dysregulation of arginase and arginine pathways in neurodegenerative diseases: metabolic and cellular dysfunction and therapeutic implications

2024 · External reference

Is the urea cycle involved in Alzheimer's disease?

10.3233/jad-2010-100630 · 2010 · External reference

Altered arginine metabolism in Alzheimer's disease brains

10.1016/j.neurobiolaging.2014.03.013 · 2014 · External reference

Arginine deprivation and immune suppression in a mouse model of Alzheimer's disease

10.1523/jneurosci.4668-14.2015 · 2015 · External reference

L-Norvaline reverses cognitive decline and synaptic loss in a murine model of Alzheimer's disease

10.1007/s13311-018-0669-5 · 2018 · External reference

Can arginase inhibitors be the answer to therapeutic challenges in Alzheimer's disease?

10.1007/s13311-018-0669-5 · 2018 · External reference

Synthesis and evaluation of new ω-borono-α-amino acids as rat liver arginase inhibitors

10.1016/j.bmc.2005.01.053 · 2005 · External reference

Probing erectile function: S-(2-boronoethyl)-L-cysteine binds to arginase as a transition state analogue and enhances smooth muscle relaxation in human penile corpus cavernosum

10.1021/bi002317h · 2001 · External reference

Structural insights into human Arginase-1 pH dependence and its inhibition by the small molecule inhibitor CB-1158

2019 · External reference

Phase I study of the arginase inhibitor INCB001158 as a single agent and in combination with pembrolizumab in patients with advanced/metastatic solid tumors

2019 · External reference

Phase I study of the arginase inhibitor INCB001158 alone and in combination with pembrolizumab in patients with advanced/metastatic solid tumors

2019 · External reference

OATD-02 Validates the Benefits of Pharmacological Inhibition of Arginase 1 and 2 in Cancer

10.3390/cancers14163967 · 2022 · External reference