Newman DJ, Cragg GM (2020) Natural products as sources of new drugs over the nearly four decades from 01/1981 to 09/2019. J Nat Prod 83:770–803. https://doi.org/10.1021/acs.jnatprod.9b01285

Article  CAS  PubMed  Google Scholar 

Walsh G, Walsh E (2022) Biopharmaceutical benchmarks 2022. Nat Biotechnol 40:1722–1760. https://doi.org/10.1038/s41587-022-01582-x

Article  CAS  PubMed  PubMed Central  Google Scholar 

Valeur E, Guéret SM, Adihou H, Gopalakrishnan R, Lemurell M, Waldmann H, Grossmann TN, Plowright AT (2017) New modalities for challenging targets in drug discovery. Angew Chem Int Ed 56:10294–10323. https://doi.org/10.1002/anie.201611914

Article  CAS  Google Scholar 

Miyachi H, Kanamitsu K, Ishii M, Watanabe E, Katsuyama A, Otsuguro S, Yakushiji F, Watanabe M, Matsui K, Sato Y, Shuto S, Tadokoro T, Kita S, Matsumaru T, Matsuda A, Hirose T, Iwatsuki M, Shigeta Y, Nagano T, Kojima H, Ichikawa S, Sunazuka T, Maenaka K (2021) Structure, solubility, and permeability relationships in a diverse middle molecule library. Bioorg Med Chem Lett 37:127847. https://doi.org/10.1016/j.bmcl.2021.127847

Article  CAS  PubMed  Google Scholar 

Hayakawa Y, Adachi H, Kim JW, Shin-ya K, Seto H (1998) Adenopeptin, a new apoptosis inducer in transformed cells from Chrysosporium sp. Tetrahedron 54:15871–15878. https://doi.org/10.1016/S0040-4020(98)00996-X

Article  CAS  Google Scholar 

Aron AT, Gentry EC, McPhail KL, Nthias LF, Nothias-Esposito M, Bouslimani A, Petras D, Gauglitz JM, Sikora N, Vargas F, van der Hooft JJJ, Ernst M, Kang KB, Aceves CM, Caraballo-Rodríguez AM, Koester I, Weldon KC, Bertrand S, Roullier C, Sun K, Tehan RM, Boya CA, Martin HC, Gutiérrez M, Ulloa AM, Mora JAT, Mojica-Flores R, Lakey-Beitia J, Vásquez-Chaves V, Zhang Y, Calderon AI, Tayler N, Keyzers RA, Tugizimana F, Ndlovu N, Aksenov AA, Jarmusch A, Schmid R, Truman AW, Bandeira N, Wang M, Dorrestein PC (2020) Reproducible molecular networking of untargeted mass spectrometry data using GNPS. Nat Protoc 15:1954–1991. https://doi.org/10.1038/s41596-020-0317-5

Article  CAS  PubMed  Google Scholar 

Nothias LF, Petras D, Schmid R, Dührkop K, Rainer J, Sarvepalli A, Protsyuk I, Ernst M, Tsugawa H, Fleischauer M, Aicheler F, Aksenov AA, Alka O, Allard PM, Barsch A, Cachet X et al (2020) Feature-based molecular networking in the GNPS analysis environment. Nat Methods 17:905–908. https://doi.org/10.1038/s41592-020-0933-6

Article  CAS  PubMed  PubMed Central  Google Scholar 

Tatsuda D, Amemiya M, Nosaka C, Sawa R, Muramatsu H, Igarashi M, Yoshida J, Ohishi T, Kawada M (2023) Two new adenopeptins B and C inhibit sphere formation of pancreatic cancer cells. J Antibiot. https://doi.org/10.1038/s41429-023-00679-y

Article  Google Scholar 

Iijima M, Amemiya M, Sawa R, Kubota Y, Kunisada T, Momose I, Kawada M, Shibasaki M (2017) Acremopeptin, a new peptaibol from Acremonium sp. PF1450. J Antibiot 70:791–794. https://doi.org/10.1038/ja.2017.15

Article  CAS  Google Scholar 

Gupta S, Krasnoff SB, Roberts DW, Renwick JAA, Brinen LS, Clardy J (1991) Structures of the efrapeptins: potent inhibitors of mitochondrial ATPase from the fungus Tolypocladium niveum. J Am Chem Soc 113:707–709. https://doi.org/10.1021/ja00002a068

Article  CAS  Google Scholar 

Gupta S, Krasnoff SB, Roberts DW, Renwick JAA, Brinen LS, Clardy J (1992) Structure of efrapeptins from the fungus Tolypocladium niveum: peptide inhibitors of mitochondrial ATPase. J Org Chem 57:2306–2313. https://doi.org/10.1021/jo00034a022

Article  CAS  Google Scholar 

Fukushima K, Arai T, Mori Y, Tsuboi M, Suzuki M (1983) Studies on peptide antibiotics, leucinostatins II. The structures of leucinostatins A and B. J Antibiot 36:1613–1630. https://doi.org/10.7164/antibiotics.36.1613

Article  CAS  Google Scholar 

Marfey P (1984) Determination ofD-amino acids. II. Use of a bifunctional reagent, 1,5-difluoro-2,4-dinitrobenzene. Carlsberg Res Commun 49:591–596. https://doi.org/10.1007/BF02908688

Article  CAS  Google Scholar 

Jost M, Greie JC, Stemmer N, Wilking SD, Altendorf K, Sewald N (2002) The first total synthesis of efrapeptin C. Angew Chem Int Ed 41:4267–4269. https://doi.org/10.1002/1521-3773(20021115)41:22%3c4267::AID-ANIE4267%3e3.0.CO;2-K

Article  CAS  Google Scholar 

Weigelt S, Huber T, Hofmann F, Jost M, Ritzefeld M, Luy B, Freudenberger C, Majer Z, Vass E, Greie JC, Panella L, Kaptein B, Broxterman QB, Kessler H, Altendorf K, Hollósi M, Sewald N (2012) Synthesis and conformational analysis of efrapeptins. Chem Eur J 18:478-487. https://doi.org/10.1002/chem.201102134

Fujii K, Ikai Y, Mayumi T, Oka H, Suzuki M, Harada K-I (1997) Anal Chem 69:3346–3352. https://doi.org/10.1021/ac9701795

Article  CAS  Google Scholar 

Fujii K, Ikai Y, Oka H, Suzuki M, Harada K-I (1997) Anal Chem 69:5146–5151. https://doi.org/10.1021/ac970289b

Article  CAS  Google Scholar 

Abrahams JP, Buchanan SK, Van Raaij MJ, Fearnley IM, Leslie AGW, Walker JE (1996) The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin. Proc Natl Acad Sci U S A 93:9420–9424. https://doi.org/10.1073/pnas.93.18.9420

Article  CAS  PubMed  PubMed Central  Google Scholar 

Lucero H, Lescano WIM, Vallejos RH (1978) Inhibition of energy conservation reactions in chromatophores of Rhodospirillum rubrum by antibiotics. Arch Biochem Biophys 186:9–14. https://doi.org/10.1016/0003-9861(78)90457-5

Article  CAS  PubMed  Google Scholar 

Hitora Y, Maeda R, Honda K, Sadahiro Y, Ise Y, Angkouw ED, Mangindaan REP, Tsukamoto S (2021) Neopetrosidines A-D, pyridine alkaloids isolated from the marine sponge Neopetrosia chaliniformis and their cell cycle elongation activity. Bioorg Med Chem 50:116461. https://doi.org/10.1016/j.bmc.2021.116461

Article  CAS  PubMed  Google Scholar 

Sanuki Y, Araki T, Nakazono O, Tsurui K (2017) A rapid mitochondrial toxicity assay utilizing rapidly changing cell energy metabolism. J Toxicol Sci 42:349–358. https://doi.org/10.2131/jts.42.349

Article  CAS  PubMed  Google Scholar 

de Kok MJC, Schaapherder AF, Wüst RCI, Zuiderwijk M, Bakker JA, Lindeman JHN, Le Dévédec SE (2021) Circumventing the Crabtree effect in cell culture: a systematic review. Mitochondrion 59:83–95. https://doi.org/10.1016/j.mito.2021.03.014

Article  CAS  PubMed  Google Scholar 

Tsukamoto S, Yamanokuchi R, Yoshitomi M, Sato K, Ikeda T, Rotinsulu H, Mangindaan REP, de Voogd NJ, van Soest RWM, Yokosawa H (2010) Aaptamine, an alkaloid from the sponge Aaptos suberitoides, functions as a proteasome inhibitor. Bioorg Med Chem Lett 20:3341–3343. https://doi.org/10.1016/j.bmcl.2010.04.029

Article  CAS  PubMed  Google Scholar 

Kimura I, Hitora Y, Sadahiro Y, Kawahara T, Tsukamoto S (2023) A monoacylglyceryltrimethylhomoserine, 21F121-A, containing a branched acyl group from Penicillium glaucoroseum. J Nat Med 77:992–997. https://doi.org/10.1007/s11418-023-01735-5

Article  CAS  PubMed  Google Scholar