Bisubstrate Inhibitors of Nicotinamide N-Methyltransferase (NNMT) with Enhanced Activity-Reference-Cited by-同舟云学术

Bisubstrate Inhibitors of Nicotinamide N-Methyltransferase (NNMT) with Enhanced Activity

Published:2019-07-02 Issue:14 Volume:62 Page:6597-6614
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Gao Yongzhi¹,van Haren Matthijs J.¹,Moret Ed E.,Rood Johannes J. M.,Sartini Davide²,Salvucci Alessia²,Emanuelli Monica²,Craveur Pierrick³,Babault Nicolas³⁴,Jin Jian⁴^ORCID,Martin Nathaniel I.¹^ORCID

Affiliation:

1. Biological Chemistry Group, Institute of Biology Leiden, Leiden University, Sylviusweg 72, 2333 BE Leiden, The Netherlands

2. Department of Clinical Sciences, Universitá Politecnica delle Marche, Via Ranieri 65, 60131 Ancona, Italy

3. Synsight, Genopole Entreprises, 4 Rue Pierre Fontaine, 91000 Évry, France

4. Center for Chemical Biology and Drug Discovery, Departments of Pharmacological Sciences and Oncological Sciences, Tisch Cancer Institute, Icahn School of Medicine at Mount Sinai, New York, New York 10029, United States

Funder

China Scholarship Council

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

http://pubs.acs.org/doi/pdf/10.1021/acs.jmedchem.9b00413

Reference58 articles.

1. Substrate specificity of nicotinamide methyltransferase isolated from porcine liver

2. A Rapid and Efficient Assay for the Characterization of Substrates and Inhibitors of Nicotinamide N-Methyltransferase

3. Nicotinamide N-methyltransferase catalyses the N-methylation of the endogenous β-carboline norharman: evidence for a novel detoxification pathway