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Relevant bibliographies by topics / Salicyl-AMS

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Academic literature on the topic 'Salicyl-AMS'

Author: Grafiati

Published: 5 June 2025

Last updated: 24 June 2025

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Journal articles on the topic "Salicyl-AMS"

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Lun, Shichun, Haidan Guo, John Adamson, et al. "Pharmacokinetic andIn VivoEfficacy Studies of the Mycobactin Biosynthesis Inhibitor Salicyl-AMS in Mice." Antimicrobial Agents and Chemotherapy 57, no. 10 (2013): 5138–40. http://dx.doi.org/10.1128/aac.00918-13.

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ABSTRACTMycobactin biosynthesis inMycobacterium tuberculosisfacilitates iron acquisition, which is required for growth and virulence. The mycobactin biosynthesis inhibitor salicyl-AMS [5′-O-(N-salicylsulfamoyl)adenosine] inhibitsM. tuberculosisgrowthin vitrounder iron-limited conditions. Here, we conducted a single-dose pharmacokinetic study and a monotherapy study of salicyl-AMS with mice. Intraperitoneal injection yielded much better pharmacokinetic parameter values than oral administration did. Monotherapy of salicyl-AMS at 5.6 or 16.7 mg/kg significantly inhibitedM. tuberculosisgrowth in the mouse lung, providing the firstin vivoproof of concept for this novel antibacterial strategy.

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Gupte, Amol, Murali Subramanian, Rory P. Remmel, and Courtney C. Aldrich. "Synthesis of deuterium-labelled 5′-O-[N-(Salicyl)sulfamoyl]adenosine (Sal-AMS-d4) as an internal standard for quantitation of Sal-AMS." Journal of Labelled Compounds and Radiopharmaceuticals 51, no. 2 (2008): 118–22. http://dx.doi.org/10.1002/jlcr.1490.

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3

Bythrow, Glennon V., Poornima Mohandas, Tezcan Guney, et al. "Kinetic Analyses of the Siderophore Biosynthesis Inhibitor Salicyl-AMS and Analogues as MbtA Inhibitors and Antimycobacterial Agents." Biochemistry 58, no. 6 (2018): 833–47. http://dx.doi.org/10.1021/acs.biochem.8b01153.

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4

Shelton, Catherine L., Kathleen M. Meneely, Trey A. Ronnebaum, et al. "Rational inhibitor design for Pseudomonas aeruginosa salicylate adenylation enzyme PchD." JBIC Journal of Biological Inorganic Chemistry, May 5, 2022. http://dx.doi.org/10.1007/s00775-022-01941-8.

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AbstractPseudomonas aeruginosa is an increasingly antibiotic-resistant pathogen that causes severe lung infections, burn wound infections, and diabetic foot infections. P. aeruginosa produces the siderophore pyochelin through the use of a non-ribosomal peptide synthetase (NRPS) biosynthetic pathway. Targeting members of siderophore NRPS proteins is one avenue currently under investigation for the development of new antibiotics against antibiotic-resistant organisms. Here, the crystal structure of the pyochelin adenylation domain PchD is reported. The structure was solved to 2.11 Å when co-crystallized with the adenylation inhibitor 5′-O-(N-salicylsulfamoyl)adenosine (salicyl-AMS) and to 1.69 Å with a modified version of salicyl-AMS designed to target an active site cysteine (4-cyano-salicyl-AMS). In the structures, PchD adopts the adenylation conformation, similar to that reported for AB3403 from Acinetobacter baumannii. Graphical abstract

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Bythrow, Glennon, Manal Farhat, Keith Levendosky, et al. "Mycobacterium abscessus Mutants with a Compromised Functional Link between the Type VII ESX-3 System and an Iron Uptake Mechanism Reliant on an Unusual Mycobactin Siderophore. Supplementary figures, captions, and tables." August 23, 2022. https://doi.org/10.5281/zenodo.6840955.

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Book chapters on the topic "Salicyl-AMS"

1

Kinarivala, Nihar, Lisa C. Standke, Tezcan Guney, et al. "Gram-scale preparation of the antibiotic lead compound salicyl-AMS, a potent inhibitor of bacterial salicylate adenylation enzymes." In Methods in Enzymology. Elsevier, 2020. http://dx.doi.org/10.1016/bs.mie.2020.04.051.

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