{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,14]],"date-time":"2026-02-14T05:56:37Z","timestamp":1771048597510,"version":"3.50.1"},"reference-count":59,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2025,11,12]],"date-time":"2025-11-12T00:00:00Z","timestamp":1762905600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"},{"start":{"date-parts":[[2025,11,12]],"date-time":"2025-11-12T00:00:00Z","timestamp":1762905600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"}],"funder":[{"name":"ARC Australian Laureate Fellowship","award":["FL210100071"],"award-info":[{"award-number":["FL210100071"]}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Sci Rep"],"DOI":"10.1038\/s41598-025-23271-w","type":"journal-article","created":{"date-parts":[[2025,11,12]],"date-time":"2025-11-12T18:46:03Z","timestamp":1762973163000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["The zinc bound form of the actinomycete derived natural product compound JBIR-141 induces a mitotic phenotype in fission yeast"],"prefix":"10.1038","volume":"15","author":[{"given":"Richard Alexander","family":"Lewis","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jacqueline","family":"Hayles","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael John","family":"Hall","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Joe","family":"Gray","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sofanit","family":"Mebrate","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Juanjuan","family":"Li","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nicholas Edward Ellis","family":"Allenby","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jeff","family":"Errington","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2025,11,12]]},"reference":[{"key":"23271_CR1","doi-asserted-by":"publisher","first-page":"357","DOI":"10.1242\/jcs.75.1.357","volume":"75","author":"JM Mitchison","year":"1985","unstructured":"Mitchison, J. M. & Nurse, P. Growth in cell length in the fission yeast Schizosaccharomyces Pombe. J. Cell. Sci. 75, 357\u2013376 (1985).","journal-title":"J. Cell. Sci."},{"key":"23271_CR2","doi-asserted-by":"publisher","first-page":"4","DOI":"10.1038\/s41437-019-0209-z","volume":"123","author":"P Nurse","year":"2019","unstructured":"Nurse, P. & Hayles, J. Using genetics to understand biology. Heredity (Edinb). 123, 4\u201313 (2019).","journal-title":"Heredity (Edinb)"},{"key":"23271_CR3","doi-asserted-by":"publisher","first-page":"871","DOI":"10.1038\/nature724","volume":"415","author":"V Wood","year":"2002","unstructured":"Wood, V. et al. The genome sequence of Schizosaccharomyces Pombe. Nature 415, 871\u2013880 (2002).","journal-title":"Nature"},{"key":"23271_CR4","doi-asserted-by":"publisher","first-page":"617","DOI":"10.1038\/nbt.1628","volume":"28","author":"DU Kim","year":"2010","unstructured":"Kim, D. U. et al. Analysis of a genome-wide set of gene deletions in the fission yeast Schizosaccharomyces Pombe. Nat. Biotechnol. 28, 617\u2013623 (2010).","journal-title":"Nat. Biotechnol."},{"key":"23271_CR5","doi-asserted-by":"publisher","first-page":"130053","DOI":"10.1098\/rsob.130053.PMID","volume":"3","author":"J Hayles","year":"2013","unstructured":"Hayles, J. et al. A genome-wide resource of cell cycle and cell shape genes of fission yeast. Open. Biol. 3, 130053. https:\/\/doi.org\/10.1098\/rsob.130053.PMID (2013).","journal-title":"Open. Biol."},{"key":"23271_CR6","doi-asserted-by":"publisher","first-page":"3173","DOI":"10.1242\/jcs.194571","volume":"130","author":"RA Lewis","year":"2017","unstructured":"Lewis, R. A. et al. Screening and purification of natural products from actinomycetes that affect the cell shape of fission yeast. J. Cell. Sci. 130, 3173\u20133185 (2017).","journal-title":"J. Cell. Sci."},{"key":"23271_CR7","doi-asserted-by":"publisher","first-page":"431","DOI":"10.1007\/s13659-021-00304-1","volume":"11","author":"RA Lewis","year":"2021","unstructured":"Lewis, R. A. et al. Screening and purification of natural products from actinomycetes that induce a rounded morphological phenotype in fission yeast. Nat. Prod. Bioprospect. 11, 431\u2013445 (2021).","journal-title":"Nat. Prod. Bioprospect"},{"key":"23271_CR8","doi-asserted-by":"publisher","first-page":"2871","DOI":"10.1091\/mbc.E20-10-0623","volume":"31","author":"P Nurse","year":"2020","unstructured":"Nurse, P. Fission yeast cell cycle mutants and the logic of eukaryotic cell cycle control. Mol. Biol. Cell. 31, 2871\u20132873 (2020).","journal-title":"Mol. Biol. Cell."},{"key":"23271_CR9","unstructured":"Kepplinger, B. The Discovery And Characterisation Of novel Antibiotics From Amycolatopsis Isolate DEM30355 (University of Newcastle upon Tyne, 2016)."},{"key":"23271_CR10","doi-asserted-by":"publisher","first-page":"1327","DOI":"10.4161\/cc.28294","volume":"13","author":"Y Aoi","year":"2014","unstructured":"Aoi, Y. et al. Dissecting the first and second meiotic divisions using a marker-less drug hypersensitive fission yeast. Cell. Cycle. 13, 1327\u20131334 (2014).","journal-title":"Cell. Cycle"},{"key":"23271_CR11","doi-asserted-by":"publisher","unstructured":"Navarro, F. J. & Nurse, P. A systematic screen reveals new elements acting at the G2\/M cell cycle control. Genome Biol. 13, R36. https:\/\/doi.org\/10.1186\/gb-2012-13-5-r36.PMID (2012).","DOI":"10.1186\/gb-2012-13-5-r36.PMID"},{"key":"23271_CR12","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1016\/0014-5793(87)81247-4","volume":"217","author":"A Takai","year":"1987","unstructured":"Takai, A., Bialojan, C., Troschka, M. & Ruegg, J. C. Smooth muscle myosin phosphatase Inhibition and force enhancement by black sponge toxin. FEBS Lett. 217, 81\u201384 (1987).","journal-title":"FEBS Lett."},{"key":"23271_CR13","doi-asserted-by":"publisher","first-page":"676","DOI":"10.1128\/jb.85.3.676-690.1963","volume":"85","author":"WH Trejo","year":"1963","unstructured":"Trejo, W. H. & Bennett, R. E. Streptomyces species comprising the blue-spore series. J. Bacteriol. 85, 676\u2013690 (1963).","journal-title":"J. Bacteriol."},{"key":"23271_CR14","doi-asserted-by":"publisher","first-page":"5476","DOI":"10.1021\/acs.orglett.5b02842","volume":"17","author":"T Kawahara","year":"2015","unstructured":"Kawahara, T. et al. Foxo3a inhibitors of microbial origin, JBIR-141 and JBIR-142. Org. Lett. 17, 5476\u20135479 (2015).","journal-title":"Org. Lett."},{"key":"23271_CR15","doi-asserted-by":"publisher","first-page":"794","DOI":"10.1021\/np400124n","volume":"76","author":"LM Blair","year":"2013","unstructured":"Blair, L. M. & Sperry, J. Natural products containing a nitrogen-nitrogen bond. J. Nat. Prod. 76, 794\u2013812 (2013).","journal-title":"J. Nat. Prod."},{"key":"23271_CR16","doi-asserted-by":"publisher","first-page":"196","DOI":"10.7164\/antibiotics.46.196","volume":"46","author":"M Toriya","year":"1993","unstructured":"Toriya, M. et al. Zincphyrin, a novel coproporphyrin III with zinc from Streptomyces Sp. J. Antibiot. 46, 196\u2013200 (1993).","journal-title":"J. Antibiot."},{"key":"23271_CR17","doi-asserted-by":"publisher","first-page":"1501","DOI":"10.7164\/antibiotics.37.1501","volume":"37","author":"HA Brooks","year":"1984","unstructured":"Brooks, H. A., Gardner, D. & Poyser, J. P. The structure and absolute stereochemistry of Zincophorin (antibiotic M144255): a monobasic carboxylic acid ionophore having a remarkable specificity for divalent cations. J. Antibiot. 37, 1501\u20131503 (1984).","journal-title":"J. Antibiot."},{"key":"23271_CR18","doi-asserted-by":"publisher","unstructured":"Walther, E. et al. Zincophorin \u2013 biosynthesis in streptomyces griseus and antibiotic properties. GMS Infect. Dis. 4 (Doc08). https:\/\/doi.org\/10.3205\/id000026 (2016).","DOI":"10.3205\/id000026"},{"key":"23271_CR19","doi-asserted-by":"publisher","first-page":"836","DOI":"10.7164\/antibiotics.37.836","volume":"37","author":"U Gr\u00e4fe","year":"1984","unstructured":"Gr\u00e4fe, U., Schade, W. & Roth, M. Griseochelin, a novel carboxylic acid antibiotic from Streptomyces griseus. J Antibiot. 37, 836\u2013846 (1984).","journal-title":"J Antibiot"},{"key":"23271_CR20","doi-asserted-by":"publisher","first-page":"1213","DOI":"10.7164\/antibiotics.42.1213","volume":"42","author":"JP Dirlam","year":"1989","unstructured":"Dirlam, J. P. et al. CP-78,545, a new Monocarboxylic acid ionophore antibiotic related to Zincophorin and produced by a Streptomyces. J. Antibiot. 42, 1213\u20131220 (1989).","journal-title":"J. Antibiot."},{"key":"23271_CR21","doi-asserted-by":"publisher","first-page":"e00554","DOI":"10.1128\/mSystems.00554-20","volume":"5","author":"JR Morey","year":"2020","unstructured":"Morey, J. R. & Kehl-Fie, T. E. Bioinformatic mapping of opine-like Zincophore biosynthesis in bacteria. mSystems 5, e00554\u2013e00520 (2020).","journal-title":"mSystems"},{"key":"23271_CR22","doi-asserted-by":"publisher","first-page":"8009","DOI":"10.1074\/jbc.RA118.002007","volume":"293","author":"JS McFarlane","year":"2018","unstructured":"McFarlane, J. S., Davis, C. L. & Lamb, A. L. Staphylopine, Pseudopaline and Yersinopine dehydrogenases: a structural and kinetic analysis of a new functional class of opine dehydrogenases. J. Biol. Chem. 293, 8009\u20138019 (2018).","journal-title":"J. Biol. Chem."},{"key":"23271_CR23","doi-asserted-by":"publisher","first-page":"1105","DOI":"10.1126\/science.aaf1018","volume":"362","author":"G Ghssein","year":"2016","unstructured":"Ghssein, G. et al. Biosynthesis of a broad-spectrum nicotianamine-like metallophore in Staphylococcus aureus. Science 362, 1105\u20131108 (2016).","journal-title":"Science"},{"key":"23271_CR24","doi-asserted-by":"publisher","first-page":"e0128","DOI":"10.1128\/mBio.01281-17","volume":"8","author":"KP Grim","year":"2017","unstructured":"Grim, K. P. et al. The metallophore Staphylopine enables Staphylococcus aureus to compete with the host for zinc and overcome nutritional immunity. mBio 8, e0128\u2013e0117 (2017).","journal-title":"mBio"},{"key":"23271_CR25","doi-asserted-by":"publisher","unstructured":"Chabaan, T., Mohsen, Y., Ezzeddine, Z. & Ghssein, G. Overview of Yersinia pestis metallophores: Yersiniabactin and Yersinopine. Biology 12 https:\/\/doi.org\/10.3390\/biology12040598 (2023).","DOI":"10.3390\/biology12040598"},{"key":"23271_CR26","doi-asserted-by":"publisher","first-page":"14644","DOI":"10.1038\/srep14644","volume":"5","author":"M Gi","year":"2015","unstructured":"Gi, M. et al. A novel siderophore system is essential for the growth of Pseudomonas aeruginosa in airway mucus. Sci. Rep. 5, 14644. https:\/\/doi.org\/10.1038\/srep14644 (2015).","journal-title":"Sci. Rep."},{"key":"23271_CR27","doi-asserted-by":"publisher","first-page":"543","DOI":"10.1111\/mmi.13834","volume":"106","author":"MC Mastopasqua","year":"2017","unstructured":"Mastopasqua, M. C. et al. Growth of Pseudomonas aeruginosa in zinc poor environments is promoted by a nicotianamine-related metallophore. Mol. Microbiol. 106, 543\u2013561 (2017).","journal-title":"Mol. Microbiol."},{"key":"23271_CR28","doi-asserted-by":"publisher","first-page":"1711","DOI":"10.3390\/biology11121711","volume":"11","author":"G Ghssein","year":"2022","unstructured":"Ghssein, G. & Ezzeddine, Z. Review of Pseudomonas aeruginosa metallophores: pyoverdine, Pyochelin and Pseudopaline. Biology 11, 1711. https:\/\/doi.org\/10.3390\/biology11121711 (2022).","journal-title":"Biology"},{"key":"23271_CR29","doi-asserted-by":"publisher","first-page":"797","DOI":"10.7164\/antibiotics.57.797","volume":"57","author":"Y Hoshino","year":"2004","unstructured":"Hoshino, Y. et al. Transvalencin A, a Thiazolidine zinc complex antibiotic produced by a clinical isolate of Nocardia transvalensis. I Taxonomy, Fermentation, isolation and biological activities. J. Antibiot. 57, 797\u2013802 (2004).","journal-title":"J. Antibiot."},{"key":"23271_CR30","doi-asserted-by":"publisher","first-page":"803","DOI":"10.7164\/antibiotics.57.803","volume":"57","author":"Y Hoshino","year":"2004","unstructured":"Hoshino, Y. et al. Transvalencin A, a Thiazolidine zinc complex antibiotic produced by a clinical isolate of Nocardia transvalensis. II. Structure Elucidation. J. Antibiot. 57, 803\u2013807 (2004).","journal-title":"J. Antibiot."},{"key":"23271_CR31","doi-asserted-by":"publisher","first-page":"759","DOI":"10.1111\/mmi.12693","volume":"93","author":"AG Bobrov","year":"2014","unstructured":"Bobrov, A. G. et al. The yersinia pestis siderophore, yersiniabactin, and the ZnuABC system both contribute to zinc acquisition and the development of lethal septicaemic plague in mice. Mol. Microbiol. 93, 759\u2013775 (2014).","journal-title":"Mol. Microbiol."},{"key":"23271_CR32","doi-asserted-by":"publisher","first-page":"1524","DOI":"10.3390\/md11051524","volume":"11","author":"N Liu","year":"2013","unstructured":"Liu, N., Shang, F., Xi, L. & Huang, Y. Tetrazolemycins A and B, two new oxazole-thiazole siderophores from deep sea Streptomyces Olivaceus FXJ8.012. Mar. Drugs. 11, 1524\u20131533 (2013).","journal-title":"Mar. Drugs"},{"key":"23271_CR33","doi-asserted-by":"publisher","first-page":"323","DOI":"10.7164\/antibiotics.51.323","volume":"51","author":"S Kobayashi","year":"1998","unstructured":"Kobayashi, S. et al. B and C, novel Antimycoplasma agents from Pseudomonas sp. I. Taxonomy, fermentation, isolation, physico-chemical properties and biological activities. J. Antibiot. 51, 323\u2013327 (1998).","journal-title":"J. Antibiot."},{"key":"23271_CR34","doi-asserted-by":"publisher","first-page":"328","DOI":"10.7164\/antibiotics.51.328","volume":"51","author":"S Kobayashi","year":"1998","unstructured":"Kobayashi, S. et al. Micacocidin A, B and C, novel Antimycoplasma agents from Pseudomonas sp. II structure Elucidation. J. Antibiot. 51, 328\u2013332 (1998).","journal-title":"J. Antibiot."},{"key":"23271_CR35","doi-asserted-by":"publisher","first-page":"608","DOI":"10.1128\/JB.01022-09","volume":"192","author":"D Kallifidas","year":"2010","unstructured":"Kallifidas, D. et al. The zinc-responsive regulator Zur controls expression of the coelibactin gene cluster in Streptomyces coelicolor. J. Bacteriol. 192, 608\u2013611 (2010).","journal-title":"J. Bacteriol."},{"key":"23271_CR36","doi-asserted-by":"publisher","first-page":"777","DOI":"10.1111\/j.1751-1097.1997.tb01924.x","volume":"65","author":"S Namiranian","year":"1997","unstructured":"Namiranian, S., Richardson, D. J., Russell, D. A. & Sodeaqu, J. R. Excited state properties of the siderophore Pyochelin and its complex with zinc ions. Photochem. Photobiol. 65, 777\u2013782 (1997).","journal-title":"Photochem. Photobiol."},{"key":"23271_CR37","doi-asserted-by":"publisher","first-page":"2126","DOI":"10.1139\/v87-354","volume":"65","author":"DA Cuppels","year":"1987","unstructured":"Cuppels, D. A., Stipanovic, R. D., Stoessl, A. & Stothers, J. B. The constitution and properties of a pyochelin-zinc complex. Can. J. Chem. 65, 2126\u20132130 (1987).","journal-title":"Can. J. Chem."},{"key":"23271_CR38","doi-asserted-by":"publisher","first-page":"2820","DOI":"10.1039\/c1dt11804h","volume":"41","author":"J Brandel","year":"2012","unstructured":"Brandel, J. et al. Pyochelin, a siderophore of Pseudomonas aeruginosa: physicochemical characterization of the iron (III), copper (II) and zinc (II) complexes. Dalton Trans. 41, 2820\u20132834 (2012).","journal-title":"Dalton Trans."},{"key":"23271_CR39","doi-asserted-by":"publisher","first-page":"419","DOI":"10.1111\/j.1758-2229.2009.00126.x","volume":"2","author":"A Braud","year":"2010","unstructured":"Braud, A., Geoffrey, V., Hoegy, F., Mislin, G. L. A. & Schalk, I. J. Presence of the siderophores Pyoverdine and Pyochelin in the extracellular medium reduces toxic metal accumulation in Pseudomonas aeruginosa and increases bacterial metal tolerance. Environ Microbiol Rep. 2, 419\u2013425 (2010).","journal-title":"Environ Microbiol Rep."},{"key":"23271_CR40","doi-asserted-by":"crossref","unstructured":"Cox, C. D., Jnr, R. & Moore, K. L. M. L. & Carter Cook Jnr, C. Pyochelin: novel structure of an iron-chelating growth promoter for Pseudomonas aeruginosa. Proc. Natl. Acad. Sci. U. S. A.  78 4256\u20134260.  (1981).","DOI":"10.1073\/pnas.78.7.4256"},{"key":"23271_CR41","doi-asserted-by":"publisher","first-page":"1293","DOI":"10.1016\/j.jinorgbio.2011.03.016","volume":"105","author":"B Yang","year":"2011","unstructured":"Yang, B., Hoegy, F., Mislin, G. L. A., Mesini, P. J. & Schalk, I. J. Terbium, a fluorescent probe for investigation of siderophore Pyochelin interactions with its outer membrane transporter FptA. J. Inorg. Biochem. 105, 1293\u20131298 (2011).","journal-title":"J. Inorg. Biochem."},{"key":"23271_CR42","doi-asserted-by":"publisher","first-page":"419","DOI":"10.1007\/s00775-006-0088-7","volume":"11","author":"C-F Tseng","year":"2006","unstructured":"Tseng, C-F. et al. Bacterial siderophores: the solution stoichiometry and coordination of the Fe(III) complexes of Pyochelin and related compounds. J. Bio Inorg. Chem. 11, 419\u2013432 (2006).","journal-title":"J. Bio Inorg. Chem."},{"key":"23271_CR43","doi-asserted-by":"publisher","first-page":"893","DOI":"10.1016\/j.jmb.2005.08.004","volume":"352","author":"D Cobessi","year":"2005","unstructured":"Cobessi, D., Celia, H. & Pattus, F. Crystal structure at high resolution of ferric-pyochelin and its membrane receptor FptA from Pseudomonas aeruginosa. J. Mol. Biol. 352, 893\u2013904 (2005).","journal-title":"J. Mol. Biol."},{"key":"23271_CR44","doi-asserted-by":"publisher","first-page":"1495","DOI":"10.1016\/j.jinorgbio.2006.04.007","volume":"100","author":"MC Miller","year":"2006","unstructured":"Miller, M. C., Parkin, S., Fetherston, J. D., Perry, R. D. & DeMoll, E. Crystal structure of ferric-yersiniabactin, a virulence factor of Yersinia pestis. J. Inorg. Biochem. 100, 1495\u20131500 (2006).","journal-title":"J. Inorg. Biochem."},{"key":"23271_CR45","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1016\/0039-9140(66)80121-2","volume":"13","author":"AH Heyn","year":"1966","unstructured":"Heyn, A. H. & Dave, N. G. Precipitation of metal-cupferron complexes from homogeneous solution-I: determination of copper. Talanta 13, 27\u201332 (1966).","journal-title":"Talanta"},{"key":"23271_CR46","doi-asserted-by":"publisher","first-page":"1233","DOI":"10.1016\/S0968-0896(01)00003-7","volume":"5","author":"M Shiino","year":"2001","unstructured":"Shiino, M., Watanabe, Y. & Umezawa, K. Synthesis of N-substituted N-nitrosohydroxylamines as inhibitors of mushroom tyrosinase. Bioorg. Med. Chem. 5, 1233\u20131240 (2001).","journal-title":"Bioorg. Med. Chem."},{"key":"23271_CR47","doi-asserted-by":"publisher","first-page":"160","DOI":"10.1042\/bj0940160","volume":"94","author":"GA Snow","year":"1965","unstructured":"Snow, G. A. The structure of mycobactin P, a growth factor for Mycobacterium johnei, and the significance of its iron complex. Biochem. J. 94, 160\u2013165 (1965).","journal-title":"Biochem. J."},{"key":"23271_CR48","doi-asserted-by":"publisher","first-page":"123","DOI":"10.1016\/j.tube.2015.01.004","volume":"95","author":"Z Fang","year":"2015","unstructured":"Fang, Z., Sampson, S. L., Warren, R. M., van Gey, N. C. & Newton-Foot, M. Iron acquisition strategies in mycobacteria. Tuberculosis (Edinb). 95, 123\u2013130 (2015).","journal-title":"Tuberculosis (Edinb)"},{"key":"23271_CR49","doi-asserted-by":"publisher","first-page":"631","DOI":"10.1016\/S1074-5521(98)90291-5","volume":"5","author":"LE Quadri","year":"1998","unstructured":"Quadri, L. E., Sello, J., Keating, T. A., Weinreb, P. H. & Walsh, C. T. Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin. Chem. Biol. 5, 631\u2013645 (1998).","journal-title":"Chem. Biol."},{"key":"23271_CR50","doi-asserted-by":"publisher","first-page":"944","DOI":"10.1128\/EC.3.4.944-954.2004","volume":"3","author":"R Bulmer","year":"2004","unstructured":"Bulmer, R. et al. The forkhead transcription factor Fkh2 regulates the cell division cycle of Schizosaccharomyces Pombe. Eukaryot. Cell. 3, 944\u2013954 (2004).","journal-title":"Eukaryot. Cell"},{"key":"23271_CR51","doi-asserted-by":"publisher","first-page":"5623","DOI":"10.1242\/jcs.01473","volume":"117","author":"V Buck","year":"2004","unstructured":"Buck, V. et al. Fkh2p and Sep1p regulate mitotic gene transcription in fission yeast. J. Cell. Sci. 117, 5623\u20135632 (2004).","journal-title":"J. Cell. Sci."},{"key":"23271_CR52","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1038\/342039a0","volume":"342","author":"KL Gould","year":"1989","unstructured":"Gould, K. L. & Nurse, P. Tyrosine phosphorylation of the fission yeast cdc2\u2009+\u2009protein kinase regulates entry into mitosis. Nature 342, 39\u201345 (1989).","journal-title":"Nature"},{"key":"23271_CR53","doi-asserted-by":"publisher","first-page":"1074","DOI":"10.1038\/nature09543","volume":"468","author":"D Coudreuse","year":"2010","unstructured":"Coudreuse, D. & Nurse, P. Driving the cell cycle with a minimal CDK control network. Nature 468, 1074\u20131079 (2010).","journal-title":"Nature"},{"key":"23271_CR54","doi-asserted-by":"crossref","unstructured":"Ottilie, S., Chernoff, J., Hannig, G., Hoffman, C. S. & Erikson, R. L. A fission-yeast gene encoding a protein with features of protein-tyrosine-phosphatases. Proc. Natl. Acad. Sci. U. S. A. 88, 3455\u20133459 (1991).","DOI":"10.1073\/pnas.88.8.3455"},{"key":"23271_CR55","doi-asserted-by":"publisher","first-page":"409","DOI":"10.1091\/mbc.8.3.409","volume":"8","author":"K Shiozaki","year":"1997","unstructured":"Shiozaki, K., Shiozaki, M. & Russell, P. Mcs4 mitotic catastrophe suppressor regulates the fission yeast cell cycle through the Wik1-Wis1-Spc1 kinase cascade. Mol. Biol. Cell. 8, 409\u2013419 (1997).","journal-title":"Mol. Biol. Cell."},{"key":"23271_CR56","doi-asserted-by":"publisher","first-page":"4943","DOI":"10.1002\/j.1460-2075.1992.tb05601.x","volume":"11","author":"JB Millar","year":"1992","unstructured":"Millar, J. B., Russell, P., Dixon, J. E. & Guan, K. L. Negative regulation of mitosis by two functionally overlapping PTPases in fission yeast. EMBO J. 11, 4943\u20134952 (1992).","journal-title":"EMBO J."},{"key":"23271_CR57","first-page":"5571","volume":"12","author":"S Ottilie","year":"1992","unstructured":"Ottilie, S., Chernoff, J., Hannig, G., Hoffman, C. S. & Erikson, R. L. The fission yeast genes pyp1\u2009+\u2009and pyp2\u2009+\u2009encode protein tyrosine phosphatases that negatively regulate mitosis. Mol. Cell. Biol. 12, 5571\u20135580 (1992).","journal-title":"Mol. Cell. Biol."},{"key":"23271_CR58","doi-asserted-by":"publisher","first-page":"795","DOI":"10.1016\/0076-6879(91)94059-L","volume":"194","author":"S Moreno","year":"1991","unstructured":"Moreno, S., Klar, A. & Nurse, P. Molecular genetic analysis of Schizosaccharomyces Pombe. Methods Enzymol. 194, 795\u2013823 (1991).","journal-title":"Methods Enzymol."},{"key":"23271_CR59","unstructured":"Kieser, T., Bibb, M. J., Buttner, M. J., Chater, K. F. & Hopwood, D. A. Practical Streptomyces Genetics (The John Innes Foundation, 2000)."}],"container-title":["Scientific Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41598-025-23271-w.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-025-23271-w","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-025-23271-w.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,11,12]],"date-time":"2025-11-12T20:03:22Z","timestamp":1762977802000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41598-025-23271-w"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,11,12]]},"references-count":59,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2025,12]]}},"alternative-id":["23271"],"URL":"https:\/\/doi.org\/10.1038\/s41598-025-23271-w","relation":{},"ISSN":["2045-2322"],"issn-type":[{"value":"2045-2322","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,11,12]]},"assertion":[{"value":"12 June 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"6 October 2025","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"12 November 2025","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors have no competing interests. RAL, NEEA and JE hold shares, or share options, in Demuris Ltd\/Odyssey Therapeutics Inc.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"39721"}}