Structure–activity relationships of the peptide deformylase inhibitor BB-3497: modification of the methylene spacer and the P1′ side chain
- 18 August 2003
- journal article
- research article
- Published by Elsevier BV in Bioorganic & Medicinal Chemistry Letters
- Vol. 13 (16), 2709-2713
- https://doi.org/10.1016/s0960-894x(03)00532-8
Abstract
No abstract availableKeywords
This publication has 15 references indexed in Scilit:
- Structure–activity relationships of the peptide deformylase inhibitor BB-3497: modification of the metal binding groupBioorganic & Medicinal Chemistry Letters, 2002
- The Crystal Structures of Four Peptide Deformylases Bound to the Antibiotic Actinonin Reveal Two Distinct Types: A Platform for the Structure-based Design of Antibacterial AgentsJournal of Molecular Biology, 2002
- Peptide Deformylase Inhibitors, Potential for a New Class of Broad Spectrum AntibacterialsCurrent Medicinal Chemistry - Anti-Infective Agents, 2002
- Resistance to anti-peptide deformylase drugsEmerging Therapeutic Targets, 2001
- Peptide deformylase as an emerging target for antiparasitic agentsEmerging Therapeutic Targets, 2001
- Peptide deformylase: a target for novel antibiotics?Emerging Therapeutic Targets, 2001
- Antibiotic Activity and Characterization of BB-3497, a Novel Peptide Deformylase InhibitorAntimicrobial Agents and Chemotherapy, 2001
- Iron center, substrate recognition and mechanism of peptide deformylaseNature Structural & Molecular Biology, 1998
- Structure of Peptide Deformylase and Identification of the Substrate Binding SitePublished by Elsevier BV ,1998
- Crystal Structure of the Escherichia coli Peptide Deformylase,Biochemistry, 1997