PMID

Data

Article Title

Organization

Identification of Novel Triazole-Based Nicotinamide Phosphoribosyltransferase (NAMPT) Inhibitors Endowed with Antiproliferative and Antiinflammatory Activity.

Universit£

Minimizing CYP2C9 Inhibition of Exposed-Pyridine NAMPT (Nicotinamide Phosphoribosyltransferase) Inhibitors.

Genentech

Application of virtual screening to the discovery of novel nicotinamide phosphoribosyltransferase (NAMPT) inhibitors with potential for the treatment of cancer and axonopathies.

Charles River Laboratories

Identification of benzothiophene amides as potent inhibitors of human nicotinamide phosphoribosyltransferase.

Second Military Medical University

Identification of nicotinamide phosphoribosyltransferase (NAMPT) inhibitors with no evidence of CYP3A4 time-dependent inhibition and improved aqueous solubility.

Genentech

Identification of amides derived from 1H-pyrazolo[3,4-b]pyridine-5-carboxylic acid as potent inhibitors of human nicotinamide phosphoribosyltransferase (NAMPT).

Forma Therapeutics

Thiazolocarboxamide Analogues as NAMPT Inhibitors.

Dart Neuroscience

Fragment-based identification of amides derived from trans-2-(pyridin-3-yl)cyclopropanecarboxylic acid as potent inhibitors of human nicotinamide phosphoribosyltransferase (NAMPT).

Genentech

Fragment-based design of 3-aminopyridine-derived amides as potent inhibitors of human nicotinamide phosphoribosyltransferase (NAMPT).

Genentech

Discovery of potent and efficacious cyanoguanidine-containing nicotinamide phosphoribosyltransferase (Nampt) inhibitors.

Forma Therapeutics

Nicotinamide phosphoribosyltransferase inhibitors, design, preparation, and structure-activity relationship.

Topotarget

Medicinal chemistry of nicotinamide phosphoribosyltransferase (NAMPT) inhibitors.

Universit£

Identification of 2,3-dihydro-1H-pyrrolo[3,4-c]pyridine-derived ureas as potent inhibitors of human nicotinamide phosphoribosyltransferase (NAMPT).

Genentech

Structure-based discovery of novel amide-containing nicotinamide phosphoribosyltransferase (nampt) inhibitors.

Forma Therapeutics

Discovery of potent and efficacious urea-containing nicotinamide phosphoribosyltransferase (NAMPT) inhibitors with reduced CYP2C9 inhibition properties.

Genentech

Structure-based identification of ureas as novel nicotinamide phosphoribosyltransferase (Nampt) inhibitors.

Forma Therapeutics

Analogues of 4-[(7-Bromo-2-methyl-4-oxo-3H-quinazolin-6-yl)methylprop-2-ynylamino]-N-(3-pyridylmethyl)benzamide (CB-30865) as potent inhibitors of nicotinamide phosphoribosyltransferase (Nampt).

Myrexis

Design, synthesis and X-ray crystallographic study of NAmPRTase inhibitors as anti-cancer agents.

School Of Life Science

Identification of small-molecule urea derivatives as novel NAMPT inhibitors via pharmacophore-based virtual screening.

Gazi University

Structure-Based Design of Potent Nicotinamide Phosphoribosyltransferase Inhibitors with Promising in Vitro and in Vivo Antitumor Activities.

Chinese Academy Of Sciences

Scaffold Morphing Identifies 3-Pyridyl Azetidine Ureas as Inhibitors of Nicotinamide Phosphoribosyltransferase (NAMPT).

Novartis Institute For Biomedical Research

Discovery of trans-3-(pyridin-3-yl)acrylamide-derived sulfamides as potent nicotinamide phosphoribosyltransferase (NAMPT) inhibitors for the potential treatment of cancer.

Chinese Academy Of Sciences

Nicotinamide Phosphoribosyltransferase (NAMPT) Is a New Target of Antitumor Agent Chidamide.

Second Military Medical University

Dual NAMPT/HDAC Inhibitors as a New Strategy for Multitargeting Antitumor Drug Discovery.

Second Military Medical University

SAR and characterization of non-substrate isoindoline urea inhibitors of nicotinamide phosphoribosyltransferase (NAMPT).

Abbvie

Small Molecule Inhibitors Simultaneously Targeting Cancer Metabolism and Epigenetics: Discovery of Novel Nicotinamide Phosphoribosyltransferase (NAMPT) and Histone Deacetylase (HDAC) Dual Inhibitors.

Second Military Medical University

Deciphering the binding of caveolin-1 to client protein endothelial nitric-oxide synthase (eNOS): scaffolding subdomain identification, interaction modeling, and biological significance.

St. Paul'S Hospital'S Centre Of Heart And Lung Innovation

2-styrylchromones as novel inhibitors of xanthine oxidase. A structure-activity study.

University Of Porto-Rua Anibal Cunha

Toward an optimal joint recognition of the S1' subsites of endothelin converting enzyme-1 (ECE-1), angiotensin converting enzyme (ACE), and neutral endopeptidase (NEP).

Cnrs

Novel non-nucleoside inhibitors of HIV-1 reverse transcriptase. 2. Tricyclic pyridobenzoxazepinones and dibenzoxazepinones.

Boehringer Ingelheim Pharmaceuticals