Binding Database

BindingDB

The first public molecular recognition database, BindingDB supports research, education and practice in drug discovery, pharmacology and related fields.

BindingDB contains 3.2M data for 1.4M Compounds and 11.4K Targets. Of those, 1.6M data for 752K Compounds and 4.8K Targets were curated by BindingDB curators. BindingDB is a FAIRsharing resource.

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15 articles for thisTarget

The following articles (labelled with PubMed ID or TBD) are for your review

PMID

Data

Article Title

Organization

Discovery of 4-Amino-8-quinoline Carboxamides as Novel, Submicromolar Inhibitors of NAD-Hydrolyzing Enzyme CD38.

Glaxosmithkline

Discovery, Synthesis, and Biological Evaluation of Thiazoloquin(az)olin(on)es as Potent CD38 Inhibitors.

Glaxosmithkline

Discovery of Potent Inhibitors of Schistosoma mansoni NAD¿ Catabolizing Enzyme.

University of Strasburg

Cyclic adenosine 5'-diphosphate ribose analogs without a"southern" ribose inhibit ADP-ribosyl cyclase-hydrolase CD38.

University of Bath

Flavonoids as inhibitors of human CD38.

University of Strasburg

Discovery of a First-in-Class CD38 Inhibitor for the Treatment of Mitochondrial Myopathy.

Immunophage Biotech Co.

Orally Bioavailable Enzymatic Inhibitor of CD38,

Mitobridge (An Astellas)

Discovery of indoles as potent and selective inhibitors of the deacetylase SIRT1.

Elixir Pharmaceuticals

Cyclic ADP Ribose Hydrolase (CD38) Inhibitors.

Temple University

2,4-Diamino-8-quinazoline carboxamides as novel, potent inhibitors of the NAD hydrolyzing enzyme CD38: Exploration of the 2-position structure-activity relationships.

Glaxosmithkline Research and Development

PHENYLALANINE-BASED LAT1 INHIBITORS AND USES THEREOF

Maxymune Therapeutics

LONG-CHAIN COMPOUND THAT ACTS ON ACLY, PREPARATION METHOD THEREFOR AND USE THEREOF

Shanghaiinstitute of Materia Medica

Dizocilpine derivatives as peripheral NMDA receptor antagonists

Institut National De La Sante Et De La Recherche Medicale (Inserm

Structure-based design, synthesis, evaluation, and crystal structures of transition state analogue inhibitors of inosine monophosphate cyclohydrolase.

The Scripps Research Institute