OATD-02 Validates the Benefits of Pharmacological Inhibition of Arginase 1 and 2 in Cancer
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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 · doi-reference
Synthesis and evaluation of new ω-borono-α-amino acids as rat liver arginase inhibitors
10.1016/j.bmc.2005.01.053 · doi-reference
Can arginase inhibitors be the answer to therapeutic challenges in Alzheimer's disease?
10.1007/s13311-018-0669-5 · doi-reference
Arginine deprivation and immune suppression in a mouse model of Alzheimer's disease
10.1523/jneurosci.4668-14.2015 · doi-reference
Altered arginine metabolism in Alzheimer's disease brains
10.1016/j.neurobiolaging.2014.03.013 · doi-reference
Is the urea cycle involved in Alzheimer's disease?
10.3233/jad-2010-100630 · doi-reference
Arginase and pulmonary diseases
10.1007/s00210-008-0286-7 · doi-reference
Arginase-1-expressing macrophages suppress Th2 cytokine-driven inflammation and fibrosis
10.1371/journal.ppat.1000371 · doi-reference
Functions of arginase isoforms in macrophage inflammatory responses: impact on cardiovascular diseases and metabolic disorders
10.3389/fimmu.2014.00533 · doi-reference
Arginase inhibition improves endothelial function in patients with coronary artery disease and type 2 diabetes mellitus
10.1161/circulationaha.112.140335 · doi-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 · doi-reference
Increased arginase levels in heart failure represent a therapeutic target to rescue microvascular perfusion
10.3233/ch-2012-1617 · doi-reference
Arginase 1 mediates increased blood pressure and contributes to vascular endothelial dysfunction in deoxycorticosterone acetate-salt hypertension
10.3389/fimmu.2013.00219 · doi-reference
The immune regulation in cancer by the amino acid metabolizing enzymes ARG and IDO
10.1016/j.coph.2017.05.002 · doi-reference
Regulation of immune responses by L-arginine metabolism
10.1038/nri1668 · doi-reference
L-arginine modulates T cell metabolism and enhances survival and anti-tumor activity
10.1016/j.cell.2016.09.031 · doi-reference
Regulatory T cells use arginase 2 to enhance their metabolic fitness in tissues
10.1172/jci.insight.129756 · doi-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 · doi-reference
Arginine regulation by myeloid derived suppressor cells and tolerance in cancer: mechanisms and therapeutic perspectives
10.1111/j.1600-065x.2008.00608.x · doi-reference
Immune control by amino acid catabolism: a new paradigm for tumor therapy
10.1038/s41568-019-0106-z · doi-reference
Metabolic barriers to cancer immunotherapy
10.1038/s41577-021-00541-y · doi-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 · doi-reference
Insights into the arginine paradox: evidence against the importance of subcellular location of arginase and eNOS
10.1152/ajpheart.00755.2012 · doi-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 · doi-reference
Endothelial nitric oxide production is tightly coupled to the citrulline-NO cycle
10.1016/j.niox.2007.07.001 · doi-reference
Threeneo-Clerodane Diterpenoids fromTinospora cordifoliaStems and their Arginase Inhibitory Activities
10.1248/cpb.c24-00240 · doi-reference
Arginase 1/2 inhibitor OATD-02: from discovery to first-in-man setup in cancer immunotherapy
10.1158/1535-7163.mct-22-0721 · doi-reference
Antitumor activity of the glutaminase inhibitor CB-839 in triple-negative breast cancer
10.1158/1535-7163.mct-13-0870 · doi-reference
Inhibition of arginase by CB-1158 blocks myeloid cell-mediated immune suppression in the tumor microenvironment
10.1186/s40425-017-0308-4 · doi-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 · doi-reference
Synthesis of quaternary α-amino acid based arginase inhibitors via the Ugi reaction
10.1016/j.bmcl.2013.06.092 · doi-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 · doi-reference
Classical and slow-binding inhibitors of human type II arginase
10.1021/bi010783g · doi-reference
Inhibition of human arginase I by substrate and product analogues
10.1016/j.abb.2010.02.004 · doi-reference
Biochemical and functional profile of a newly developed potent and isozyme-selective arginase inhibitor
10.1016/s0022-3565(24)35048-7 · doi-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 · doi-reference
The caveolar nitric oxide synthase/arginine regeneration system for NO production in endothelial cells
10.1242/jeb.00361 · doi-reference
The L-arginine paradox: importance of the L-arginine/asymmetrical dimethylarginine ratio
10.1016/j.pharmthera.2007.03.002 · doi-reference
Insulin and the arginine paradox
10.1172/jci119166 · doi-reference
