ArticleThe Journal of antibiotics2018
Isolation and structural elucidation of pelgipeptin E, a novel pore-forming pelgipeptin analog from Paenibacillus elgii with low hemolytic activity.
Article in The Journal of antibiotics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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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.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Natural and Synthetic AMPs from Latin America across Diversity Engineering and Applications.ACS infectious diseases · 2026Review
- The structure of lipopeptides impacts their antiviral activity and mode of action against SARS-CoV-2Applied and environmental microbiology · 2024Article
- Article
- Complete genome sequence of biocontrol strain Paenibacillus peoriae HJ-2 and further analysis of its biocontrol mechanism.BMC genomics · 2022Article
- Article
- Streptomyces sp SM01 isolated from Indian soil produces a novel antibiotic picolinamycin effective against multi drug resistant bacterial strains.Scientific reports · 2020Article
- Biological Control of Tomato Bacterial Wilt, Kimchi Cabbage Soft Rot, and Red Pepper Bacterial Leaf Spot UsingFrontiers in plant science · 2020Article
Corrections and comments
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Authors and funding
8 authors at 6 institutions in 1 country.
Funding
Abstract
Pelgipeptins are cyclic lipopeptides composed of nine amino acids and a short fatty acid chain. In the present study, we report a novel pelgipeptin peptide that was isolated from Paenibacillus elgii BC34-6 and named pelgipeptin E (PGP-E). The molecular mass of PGP-E was 1072 Da as determined by liquid chromatography-mass spectrometry and the amino acid sequence was elucidated by tandem mass spectrometry. The complete molecular structure of PGP-E was characterized using 2D NMR spectroscopy. PGP-E consisted of a cyclic peptide backbone of Dab1-Val2-Dab3-Phe4-Leu5-Dab6-Val7-Leu8-Ser9 and a lipid chain (-CH
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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.