Browse result page of AntiTbPdb
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ID | Name | Sequence | N-Terminal Modification | C-Terminal Modification | Chemical Modification | Linear/Cyclic | Length | Chirality | Nature | Source | Origin | Species | Strain | Inhibition Concentration | In vitro/ In vivo | Cell Line | Intracellular Inhibition | Cytotoxicity | Animal Model | Effective Dose in model organism | Immune Responce | Mechanism of Action | Target | Combination Therapy | Other Activities | Year of Publication | Pubmed ID/ Patent No. |
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antitb_1014 | Ecumicin | (N,N-Me2-Val)-(Val)-(N-Me-allo-Ilu)-(Thr)-(N-Me-Thr)-(Val)-(N-Me-Leu)-(Val)-(N-Me-Val)-(N-Me-4-OMe-Trp)-(Val)-(Ph-threo-Ser)-(Val) | Free | Free | N-methylation pattern, N-Me-Val = N-methyl-valine, N,N-Me2-Val = N,N-dimethyl-valine, N-Me-Thr = N-methyl-threonine, N-Me-Leu = N-methyl-leucine, N-Me-allo-Ilu = N-methyl-isoleucine, N-Me-4-OMe-Trp = N-methyl-4-methoxy-tryptophan, Ph-threo-Ser = Phe | Macrocyclic | 13 | L | NA | Natural | Produced by a genetically distinct Nonomuraea species, strain MJM5123. | Mycobacterium chelonae | Mycobacterium chelonae (ATCC 35752) | MIC = 0.97 μM | In vitro | None | NA | NA | None | None | NA | Ecumicin markedly enhanced the ATPase activity of wild-type (WT) ClpC1 but prevented activation of proteolysis by ClpC1. so toxic proteins which are normally degraded by the ClpC1P1P2 complex, accumulate in the presence of ecumicin | ClpC1 ATPase complex | None | NA | 2015 | 25421483 |