O-alkylhydroxylamines as rationally-designed mechanism-based inhibitors of indoleamine 2,3-dioxygenase-1.

Abnormal kynurenine pathway of tryptophan catabolism in cardiovascular diseases. Cell Mol Life Sci (2017) 0.75

Erylusamides: Novel Atypical Glycolipids from Erylus cf. deficiens. Mar Drugs (2016) 0.75

Fused Heterocyclic Compounds as Potent Indoleamine-2,3-dioxygenase 1 Inhibitors. ACS Med Chem Lett (2016) 0.75

Structure validation by Calpha geometry: phi,psi and Cbeta deviation. Proteins (2003) 32.38

New colorimetric cytotoxicity assay for anticancer-drug screening. J Natl Cancer Inst (1990) 23.46

Cancer immunoediting: integrating immunity's roles in cancer suppression and promotion. Science (2011) 15.79

Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation. J Mol Biol (1999) 15.00

Immunosuppressive networks in the tumour environment and their therapeutic relevance. Nat Rev Cancer (2005) 10.06

The immunobiology of cancer immunosurveillance and immunoediting. Immunity (2004) 9.39

Force fields for protein simulations. Adv Protein Chem (2003) 8.70

Ligand efficiency: a useful metric for lead selection. Drug Discov Today (2004) 6.60

Heme-Containing Oxygenases. Chem Rev (1996) 5.82

Indoleamine 2,3-dioxygenase and tumor-induced tolerance. J Clin Invest (2007) 5.05

Inhibition of indoleamine 2,3-dioxygenase, an immunoregulatory target of the cancer suppression gene Bin1, potentiates cancer chemotherapy. Nat Med (2005) 4.92

Halogen bonding: the sigma-hole. Proceedings of "Modeling interactions in biomolecules II", Prague, September 5th-9th, 2005. J Mol Model (2006) 4.28

A medicinal chemist's guide to molecular interactions. J Med Chem (2010) 3.39

The maximal affinity of ligands. Proc Natl Acad Sci U S A (1999) 3.24

Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan. Cancer Res (2007) 2.78

The role of ligand efficiency metrics in drug discovery. Nat Rev Drug Discov (2014) 1.98

Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase. Proc Natl Acad Sci U S A (2006) 1.91

Targeting the mechanisms of tumoral immune tolerance with small-molecule inhibitors. Nat Rev Cancer (2006) 1.71

Indoleamine 2,3-dioxygenase-2; a new enzyme in the kynurenine pathway. Int J Biochem Cell Biol (2008) 1.64

Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based inhibitors. J Med Chem (2008) 1.18

Reaction of myoglobin with phenylhydrazine: a molecular doorstop. Biochemistry (1984) 1.15

Evidence for a ferryl intermediate in a heme-based dioxygenase. Proc Natl Acad Sci U S A (2009) 1.13

Density functional theory study on a missing piece in understanding of heme chemistry: the reaction mechanism for indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase. J Am Chem Soc (2008) 1.13

Discovery of potent competitive inhibitors of indoleamine 2,3-dioxygenase with in vivo pharmacodynamic activity and efficacy in a mouse melanoma model. J Med Chem (2009) 1.09

Structure based development of phenylimidazole-derived inhibitors of indoleamine 2,3-dioxygenase. J Med Chem (2008) 1.07

Expression and purification of recombinant human indoleamine 2, 3-dioxygenase. Protein Expr Purif (2000) 1.06

Marrying immunotherapy with chemotherapy: why say IDO? Cancer Res (2005) 1.04

Indoleamine 2,3-dioxygenase inhibitors: a patent review (2008 - 2012). Expert Opin Ther Pat (2013) 1.02

N-Phenylprotoporphyrin IX formation in the hemoglobin-phenylhydrazine reaction. Evidence for a protein-stabilized iron-phenyl intermediate. J Biol Chem (1982) 1.01

Enzyme kinetic and spectroscopic studies of inhibitor and effector interactions with indoleamine 2,3-dioxygenase. 1. Norharman and 4-phenylimidazole binding to the enzyme as inhibitors and heme ligands. Biochemistry (1989) 0.98

Geranylgeranyl diphosphate-based inhibitors of post-translational geranylgeranylation of cellular proteins. J Med Chem (1996) 0.95

Inactivation of catalase by phenylhydrazine. Formation of a stable aryl-iron heme complex. J Biol Chem (1983) 0.93

Prediction of binding modes for ligands in the cytochromes P450 and other heme-containing proteins. Proteins (2005) 0.91

Complete reaction mechanism of indoleamine 2,3-dioxygenase as revealed by QM/MM simulations. J Phys Chem B (2012) 0.90

Challenges in the Discovery of Indoleamine 2,3-Dioxygenase 1 (IDO1) Inhibitors. J Med Chem (2015) 0.89

The reaction of phenylhydrazine with microsomal cytochrome P-450. Catalysis of heme modification. J Biol Chem (1982) 0.88

Rational design of 4-aryl-1,2,3-triazoles for indoleamine 2,3-dioxygenase 1 inhibition. J Med Chem (2012) 0.85

S-benzylisothiourea derivatives as small-molecule inhibitors of indoleamine-2,3-dioxygenase. Bioorg Med Chem Lett (2010) 0.84

Structure-activity relationship and enzyme kinetic studies on 4-aryl-1H-1,2,3-triazoles as indoleamine 2,3-dioxygenase (IDO) inhibitors. Eur J Med Chem (2011) 0.83

Discovery of tryptanthrin derivatives as potent inhibitors of indoleamine 2,3-dioxygenase with therapeutic activity in Lewis lung cancer (LLC) tumor-bearing mice. J Med Chem (2013) 0.83

Crystal Structures and Structure-Activity Relationships of Imidazothiazole Derivatives as IDO1 Inhibitors. ACS Med Chem Lett (2014) 0.83

The Tumor-Selective Cytotoxic Agent β-Lapachone is a Potent Inhibitor of IDO1. Int J Tryptophan Res (2013) 0.77

Discovery and structure-activity relationships of phenyl benzenesulfonylhydrazides as novel indoleamine 2,3-dioxygenase inhibitors. Bioorg Med Chem Lett (2014) 0.76

Discovery and characterisation of hydrazines as inhibitors of the immune suppressive enzyme, indoleamine 2,3-dioxygenase 1 (IDO1). Bioorg Med Chem (2013) 0.76

Thiosemicarbazide, a fragment with promising indolamine-2,3-dioxygenase (IDO) inhibition properties. Eur J Med Chem (2014) 0.76

Evidence for a ferryl intermediate in a heme-based dioxygenase. Proc Natl Acad Sci U S A (2009) 1.13

IDO2 is critical for IDO1-mediated T-cell regulation and exerts a non-redundant function in inflammation. Int Immunol (2014) 1.13

Transformation-selective apoptotic program triggered by farnesyltransferase inhibitors requires Bin1. Oncogene (2003) 0.82