Discovery of novel fragments inhibiting O-acetylserine sulphhydrylase by combining scaffold hopping and ligand–based drug design-Reference-Cited by-同舟云学术

Discovery of novel fragments inhibiting O-acetylserine sulphhydrylase by combining scaffold hopping and ligand–based drug design

Published:2018-01-01 Issue:1 Volume:33 Page:1444-1452
ISSN:1475-6366
Container-title:Journal of Enzyme Inhibition and Medicinal Chemistry
language:en
Short-container-title:Journal of Enzyme Inhibition and Medicinal Chemistry

Author:

Magalhães Joana¹,Franko Nina²,Annunziato Giannamaria¹,Welch Martin³,Dolan Stephen K.³,Bruno Agostino⁴,Mozzarelli Andrea²⁵⁶,Armao Stefano⁷,Jirgensons Aigars⁸,Pieroni Marco¹,Costantino Gabriele¹⁹,Campanini Barbara²

Affiliation:

1. P4T group, Department of Food and Drug, University of Parma, Parma, Italy;

2. Laboratory of Biochemistry and Molecular Biology, Department of Food and Drug, University of Parma, Parma, Italy;

3. Department of Biochemistry, Cambridge University, Cambridge, United Kingdom;

4. Experimental Therapeutics Program, IFOM – The FIRC Institute for Molecular Oncology Foundation, Milano, Italy;

5. National Institute of Biostructures and Biosystems, Rome, Italy;

6. Institute of Biophysics, CNR, Pisa, Italy;

7. Centro Interdipartimentale “Biopharmanet-tec”, Università degli Studi di Parma, Parma, Italy;

8. Latvian Institute of Organic Synthesis, Riga, Latvia;

9. Centro Interdipartimentale Misure (CIM)’G. Casnati’, University of Parma, Parma, Italy

Funder

European Union’s Horizon 2020

innovation program/Marie Sklodowska-Curie

Publisher

Informa UK Limited

Subject

Drug Discovery,Pharmacology,General Medicine

Link

https://www.tandfonline.com/doi/pdf/10.1080/14756366.2018.1512596

Reference42 articles.

1. Inhibitors of the Sulfur Assimilation Pathway in Bacterial Pathogens as Enhancers of Antibiotic Therapy

2. Cysteine biosynthesis, oxidative stress and antibiotic resistance in Salmonella typhimurium

3. The multifaceted pyridoxal 5′-phosphate-dependent O-acetylserine sulfhydrylase

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