Rational Design of an Antimicrobial Peptide Based on Structural Insight into the Interaction of Pseudomonas aeruginosa Initiation Factor 1 with Its Cognate 30S Ribosomal Subunit
Author:
Affiliation:
1. Department of Chemistry, The University of Texas Rio Grande Valley, Edinburg, Texas 78539, United States
Funder
Welch Foundation
University of Texas Rio Grande Valley
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Infectious Diseases
Link
https://pubs.acs.org/doi/pdf/10.1021/acsinfecdis.1c00256
Reference31 articles.
1. Antibiotics Special Issue: Challenges and Opportunities in Antibiotic Discovery and Development
2. Emerging Strategies to Combat ESKAPE Pathogens in the Era of Antimicrobial Resistance: A Review
3. Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen
4. Emerging therapies against infections with Pseudomonas aeruginosa
5. The Epidemiology, Pathogenesis and Treatment of Pseudomonas aeruginosa Infections
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1. A rationally designed antimicrobial peptide from structural and functional insights of Clostridioides difficile translation initiation factor 1;Microbiology Spectrum;2024-03-05
2. Heterologous expression and activity of α-helical antimicrobial peptide SW in Bacillus subtilis;Biochemical Engineering Journal;2024-03
3. A Rationally Designed Antimicrobial Peptide from Structural and Functional Insight ofClostridium difficileTranslation Initiation Factor 1;2023-06-30
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