ArticleChemMedChem2011
Inhibition of Mycobacterium tuberculosis methionine aminopeptidases by bengamide derivatives.
Article in ChemMedChem, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 37 citations in OpenAlex.
- Anti-Tuberculosis Potential of OJT008 against Active and Multi-Drug-Resistant Mycobacterium Tuberculosis: In Silico and In Vitro Inhibition of Methionine Aminopeptidase.International journal of molecular sciences · 2023Article
- Computational Approaches to Enzyme Inhibition by Marine Natural Products in the Search for New Drugs.Marine drugs · 2023Review
- Article
- The Development of the Bengamides as New Antibiotics against Drug-Resistant Bacteria.Marine drugs · 2022Review
- Identification of Antimycobacterial Natural Products from a Library of Marine Invertebrate Extracts.Medicines (Basel, Switzerland) · 2022Article
- Bengamide Analogues Show A Potent Antitumor Activity against Colon Cancer Cells: A Preliminary Study.Marine drugs · 2020Article
- Bengamides display potent activity against drug-resistant Mycobacterium tuberculosis.Scientific reports · 2019Article
- Targeting Metalloenzymes for Therapeutic Intervention.Chemical reviews · 2019Review
- The Bengamides: A Mini-Review of Natural Sources, Analogues, Biological Properties, Biosynthetic Origins, and Future Prospects.Journal of natural products · 2017Review
- Article
- Advances in Bacterial Methionine Aminopeptidase Inhibition.Current topics in medicinal chemistry · 2016Review
- Chemistry and biology of bengamides and bengazoles, bioactive natural products from Jaspis sponges.Marine drugs · 2014Review
- Structural analysis of bengamide derivatives as inhibitors of methionine aminopeptidases.Journal of medicinal chemistry · 2012Article
- Myxobacteria versus sponge-derived alkaloids: the bengamide family identified as potent immune modulating agents by scrutiny of LC-MS/ELSD libraries.Bioorganic & medicinal chemistry · 2012Article
- Analogs of N'-hydroxy-N-(4H,5H-naphtho[1,2-d]thiazol-2-yl)methanimidamide inhibit Mycobacterium tuberculosis methionine aminopeptidases.Bioorganic & medicinal chemistry · 2012Article
- Structural analysis of inhibition of Mycobacterium tuberculosis methionine aminopeptidase by bengamide derivatives.European journal of medicinal chemistry · 2012Article
- Characterization of clioquinol and analogues as novel inhibitors of methionine aminopeptidases from Mycobacterium tuberculosis.Tuberculosis (Edinburgh, Scotland) · 2011Article
- Methionine aminopeptidases: Potential therapeutic target for microsporidia and other microbes.The Journal of eukaryotic microbiologyReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Methionine aminopeptidase (MetAP) carries out an essential function of protein N-terminal processing in many bacteria and is a promising target for the development of novel antitubercular agents. Natural bengamides potently inhibit the proliferation of mammalian cells by targeting MetAP enzymes, and the X-ray crystal structure of human type 2 MetAP in complex with a bengamide derivative reveals the key interactions at the active site. By preserving the interactions with the conserved residues inside the binding pocket while exploring the differences between bacterial and human MetAPs around the binding pocket, seven bengamide derivatives were synthesized and evaluated for inhibition of MtMetAP1a and MtMetAP1c in different metalloforms, inhibition of M. tuberculosis growth in replicating and non-replicating states, and inhibition of human K562 cell growth. Potent inhibition of MtMetAP1a and MtMetAP1c and modest growth inhibition of M. tuberculosis were observed for some of these derivatives. Crystal structures of MtMetAP1c in complex with two of the derivatives provided valuable structural information for improvement of these inhibitors for potency and selectivity.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.