Unknown

Dataset Information

0

Docking into Mycobacterium tuberculosis Thioredoxin Reductase Protein Yields Pyrazolone Lead Molecules for Methicillin-Resistant Staphylococcus aureus.


ABSTRACT: The thioredoxin/thioredoxin reductase system (Trx/TrxR) is an attractive drug target because of its involvement in a number of important physiological processes, from DNA synthesis to regulating signal transduction. This study describes the finding of pyrazolone compounds that are active against Staphylococcus aureus. Initially, the project was focused on discovering small molecules that may have antibacterial properties targeting the Mycobacterium tuberculosis thioredoxin reductase. This led to the discovery of a pyrazolone scaffold-containing compound series that showed bactericidal capability against S. aureus strains, including drug-resistant clinical isolates. The findings support continued development of the pyrazolone compounds as potential anti-S. aureus antibiotics.

SUBMITTER: Sweeney NL 

PROVIDER: S-EPMC5372984 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

Docking into Mycobacterium tuberculosis Thioredoxin Reductase Protein Yields Pyrazolone Lead Molecules for Methicillin-Resistant Staphylococcus aureus.

Sweeney Noreena L NL   Lipker Lauren L   Hanson Alicia M AM   Bohl Chris J CJ   Engel Katie E KE   Kalous Kelsey S KS   Stemper Mary E ME   Sem Daniel S DS   Schwan William R WR  

Antibiotics (Basel, Switzerland) 20170128 1


The thioredoxin/thioredoxin reductase system (Trx/TrxR) is an attractive drug target because of its involvement in a number of important physiological processes, from DNA synthesis to regulating signal transduction. This study describes the finding of pyrazolone compounds that are active against <i>Staphylococcus aureus</i>. Initially, the project was focused on discovering small molecules that may have antibacterial properties targeting the <i>Mycobacterium tuberculosis</i> thioredoxin reductas  ...[more]

Similar Datasets

| S-EPMC2798248 | biostudies-literature
| S-EPMC2805538 | biostudies-literature
| S-EPMC305758 | biostudies-literature
| S-EPMC6974526 | biostudies-literature
| S-EPMC6196236 | biostudies-literature
| S-EPMC2957988 | biostudies-literature
2012-07-31 | GSE31342 | GEO
| S-EPMC5204005 | biostudies-other
| S-EPMC5019056 | biostudies-literature
| S-EPMC2841211 | biostudies-literature