[{"conference":{"end_date":"2021-07-02","start_date":"2021-06-28","name":"iNCNC: Internet nanoGe Conference on Nanocrystals","location":"Virtual"},"_id":"15280","language":[{"iso":"eng"}],"date_published":"2021-06-08T00:00:00Z","author":[{"id":"302BADF6-85FC-11EA-9E3B-B9493DDC885E","full_name":"Balazs, Daniel","orcid":"0000-0001-7597-043X","last_name":"Balazs","first_name":"Daniel"},{"last_name":"Cimada da Silva","first_name":"Jessica","full_name":"Cimada da Silva, Jessica"},{"full_name":"Dunbar, Tyler","last_name":"Dunbar","first_name":"Tyler"},{"full_name":"Ibáñez, Maria","id":"43C61214-F248-11E8-B48F-1D18A9856A87","first_name":"Maria","orcid":"0000-0001-5013-2843","last_name":"Ibáñez"},{"full_name":"Hanrath, Tobias","first_name":"Tobias","last_name":"Hanrath"}],"publication":"Proceedings of the Internet NanoGe Conference on Nanocrystals","doi":"10.29363/nanoge.incnc.2021.050","ddc":["530"],"date_updated":"2026-07-06T13:07:52Z","month":"06","article_processing_charge":"No","title":"Controlled reactive assembly of colloidal nanocrystal superlattices: Mechanism and kinetics","date_created":"2024-04-03T08:28:26Z","fulldoi":"https://doi.org/10.29363/nanoge.incnc.2021.050","article_number":"050","citation":{"mla":"Balazs, Daniel, et al. “Controlled Reactive Assembly of Colloidal Nanocrystal Superlattices: Mechanism and Kinetics.” <i>Proceedings of the Internet NanoGe Conference on Nanocrystals</i>, 050, Fundació de la comunitat valenciana SCITO, 2021, doi:<a href=\"https://doi.org/10.29363/nanoge.incnc.2021.050\">10.29363/nanoge.incnc.2021.050</a>.","ieee":"D. Balazs, J. Cimada da Silva, T. Dunbar, M. Ibáñez, and T. Hanrath, “Controlled reactive assembly of colloidal nanocrystal superlattices: Mechanism and kinetics,” in <i>Proceedings of the Internet NanoGe Conference on Nanocrystals</i>, Virtual, 2021.","short":"D. Balazs, J. Cimada da Silva, T. Dunbar, M. Ibáñez, T. Hanrath, in:, Proceedings of the Internet NanoGe Conference on Nanocrystals, Fundació de la comunitat valenciana SCITO, 2021.","ama":"Balazs D, Cimada da Silva J, Dunbar T, Ibáñez M, Hanrath T. Controlled reactive assembly of colloidal nanocrystal superlattices: Mechanism and kinetics. In: <i>Proceedings of the Internet NanoGe Conference on Nanocrystals</i>. Fundació de la comunitat valenciana SCITO; 2021. doi:<a href=\"https://doi.org/10.29363/nanoge.incnc.2021.050\">10.29363/nanoge.incnc.2021.050</a>","chicago":"Balazs, Daniel, Jessica Cimada da Silva, Tyler Dunbar, Maria Ibáñez, and Tobias Hanrath. “Controlled Reactive Assembly of Colloidal Nanocrystal Superlattices: Mechanism and Kinetics.” In <i>Proceedings of the Internet NanoGe Conference on Nanocrystals</i>. Fundació de la comunitat valenciana SCITO, 2021. <a href=\"https://doi.org/10.29363/nanoge.incnc.2021.050\">https://doi.org/10.29363/nanoge.incnc.2021.050</a>.","apa":"Balazs, D., Cimada da Silva, J., Dunbar, T., Ibáñez, M., &#38; Hanrath, T. (2021). Controlled reactive assembly of colloidal nanocrystal superlattices: Mechanism and kinetics. In <i>Proceedings of the Internet NanoGe Conference on Nanocrystals</i>. Virtual: Fundació de la comunitat valenciana SCITO. <a href=\"https://doi.org/10.29363/nanoge.incnc.2021.050\">https://doi.org/10.29363/nanoge.incnc.2021.050</a>","ista":"Balazs D, Cimada da Silva J, Dunbar T, Ibáñez M, Hanrath T. 2021. Controlled reactive assembly of colloidal nanocrystal superlattices: Mechanism and kinetics. Proceedings of the Internet NanoGe Conference on Nanocrystals. iNCNC: Internet nanoGe Conference on Nanocrystals, 050."},"oa":1,"quality_controlled":"1","publication_status":"published","oa_version":"Published Version","publisher":"Fundació de la comunitat valenciana SCITO","day":"08","main_file_link":[{"url":"https://doi.org/10.29363/nanoge.incnc.2021.050","open_access":"1"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","corr_author":"1","type":"conference_abstract","year":"2021","department":[{"_id":"MaIb"},{"_id":"LifeSc"}],"status":"public"},{"related_material":{"record":[{"status":"public","id":"7800","relation":"earlier_version"},{"relation":"dissertation_contains","id":"12401","status":"public"},{"id":"19557","relation":"dissertation_contains","status":"public"}],"link":[{"relation":"press_release","url":"https://ist.ac.at/en/news/defective-gene-slows-down-brain-cells/"}]},"fulldoi":"https://doi.org/10.1038/s41467-021-23123-x","acknowledgement":"We thank A. Coll Manzano, F. Freeman, M. Ladron de Guevara, and A. Ç. Yahya for technical assistance, S. Deixler, A. Lepold, and A. Schlerka for the management of our animal colony, as well as M. Schunn and the Preclinical Facility team for technical assistance. We thank K. Heesom and her team at the University of Bristol Proteomics Facility for the proteomics sample preparation, data generation, and analysis support. We thank Y. B. Simon for kindly providing the plasmid for lentiviral labeling. Further, we thank M. Sixt for his advice regarding cell migration and the fruitful discussions. This work was supported by the ISTPlus postdoctoral fellowship (Grant Agreement No. 754411) to B.B., by the European Union’s Horizon 2020 research and innovation program (ERC) grant 715508 (REVERSEAUTISM), and by the Austrian Science Fund (FWF) to G.N. (DK W1232-B24 and SFB F7807-B) and to J.G.D (I3600-B27).","intvolume":"        12","volume":12,"ddc":["572"],"acknowledged_ssus":[{"_id":"PreCl"}],"doi":"10.1038/s41467-021-23123-x","publication_identifier":{"eissn":["2041-1723"]},"language":[{"iso":"eng"}],"abstract":[{"lang":"eng","text":"De novo loss of function mutations in the ubiquitin ligase-encoding gene Cullin3 lead to autism spectrum disorder (ASD). In mouse, constitutive haploinsufficiency leads to motor coordination deficits as well as ASD-relevant social and cognitive impairments. However, induction of Cul3 haploinsufficiency later in life does not lead to ASD-relevant behaviors, pointing to an important role of Cul3 during a critical developmental window. Here we show that Cul3 is essential to regulate neuronal migration and, therefore, constitutive Cul3 heterozygous mutant mice display cortical lamination abnormalities. At the molecular level, we found that Cul3 controls neuronal migration by tightly regulating the amount of Plastin3 (Pls3), a previously unrecognized player of neural migration. Furthermore, we found that Pls3 cell-autonomously regulates cell migration by regulating actin cytoskeleton organization, and its levels are inversely proportional to neural migration speed. Finally, we provide evidence that cellular phenotypes associated with autism-linked gene haploinsufficiency can be rescued by transcriptional activation of the intact allele in vitro, offering a proof of concept for a potential therapeutic approach for ASDs."}],"isi":1,"has_accepted_license":"1","status":"public","tmp":{"image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"day":"24","oa_version":"Published Version","external_id":{"isi":["000658769900010"]},"keyword":["General Biochemistry","Genetics and Molecular Biology"],"issue":"1","citation":{"ieee":"J. Morandell <i>et al.</i>, “Cul3 regulates cytoskeleton protein homeostasis and cell migration during a critical window of brain development,” <i>Nature Communications</i>, vol. 12, no. 1. Springer Nature, 2021.","chicago":"Morandell, Jasmin, Lena A Schwarz, Bernadette Basilico, Saren Tasciyan, Georgi A Dimchev, Armel Nicolas, Christoph M Sommer, et al. “Cul3 Regulates Cytoskeleton Protein Homeostasis and Cell Migration during a Critical Window of Brain Development.” <i>Nature Communications</i>. Springer Nature, 2021. <a href=\"https://doi.org/10.1038/s41467-021-23123-x\">https://doi.org/10.1038/s41467-021-23123-x</a>.","ama":"Morandell J, Schwarz LA, Basilico B, et al. Cul3 regulates cytoskeleton protein homeostasis and cell migration during a critical window of brain development. <i>Nature Communications</i>. 2021;12(1). doi:<a href=\"https://doi.org/10.1038/s41467-021-23123-x\">10.1038/s41467-021-23123-x</a>","short":"J. Morandell, L.A. Schwarz, B. Basilico, S. Tasciyan, G.A. Dimchev, A. Nicolas, C.M. Sommer, C. Kreuzinger, C. Dotter, L. Knaus, Z. Dobler, E. Cacci, F.K. Schur, J.G. Danzl, G. Novarino, Nature Communications 12 (2021).","mla":"Morandell, Jasmin, et al. “Cul3 Regulates Cytoskeleton Protein Homeostasis and Cell Migration during a Critical Window of Brain Development.” <i>Nature Communications</i>, vol. 12, no. 1, 3058, Springer Nature, 2021, doi:<a href=\"https://doi.org/10.1038/s41467-021-23123-x\">10.1038/s41467-021-23123-x</a>.","ista":"Morandell J, Schwarz LA, Basilico B, Tasciyan S, Dimchev GA, Nicolas A, Sommer CM, Kreuzinger C, Dotter C, Knaus L, Dobler Z, Cacci E, Schur FK, Danzl JG, Novarino G. 2021. Cul3 regulates cytoskeleton protein homeostasis and cell migration during a critical window of brain development. Nature Communications. 12(1), 3058.","apa":"Morandell, J., Schwarz, L. A., Basilico, B., Tasciyan, S., Dimchev, G. A., Nicolas, A., … Novarino, G. (2021). Cul3 regulates cytoskeleton protein homeostasis and cell migration during a critical window of brain development. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-021-23123-x\">https://doi.org/10.1038/s41467-021-23123-x</a>"},"date_created":"2021-05-28T11:49:46Z","title":"Cul3 regulates cytoskeleton protein homeostasis and cell migration during a critical window of brain development","article_type":"original","article_processing_charge":"No","date_updated":"2026-11-07T23:30:14Z","month":"05","publication":"Nature Communications","file":[{"date_updated":"2021-05-28T12:39:43Z","success":1,"file_id":"9430","file_size":9358599,"date_created":"2021-05-28T12:39:43Z","content_type":"application/pdf","access_level":"open_access","checksum":"337e0f7959c35ec959984cacdcb472ba","relation":"main_file","file_name":"2021_NatureCommunications_Morandell.pdf","creator":"kschuh"}],"date_published":"2021-05-24T00:00:00Z","author":[{"id":"4739D480-F248-11E8-B48F-1D18A9856A87","full_name":"Morandell, Jasmin","last_name":"Morandell","first_name":"Jasmin"},{"first_name":"Lena A","last_name":"Schwarz","full_name":"Schwarz, Lena A","id":"29A8453C-F248-11E8-B48F-1D18A9856A87"},{"id":"36035796-5ACA-11E9-A75E-7AF2E5697425","full_name":"Basilico, Bernadette","last_name":"Basilico","orcid":"0000-0003-1843-3173","first_name":"Bernadette"},{"last_name":"Tasciyan","orcid":"0000-0003-1671-393X","first_name":"Saren","id":"4323B49C-F248-11E8-B48F-1D18A9856A87","full_name":"Tasciyan, Saren"},{"full_name":"Dimchev, Georgi A","id":"38C393BE-F248-11E8-B48F-1D18A9856A87","first_name":"Georgi A","orcid":"0000-0001-8370-6161","last_name":"Dimchev"},{"first_name":"Armel","last_name":"Nicolas","full_name":"Nicolas, Armel","id":"2A103192-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Christoph M","last_name":"Sommer","orcid":"0000-0003-1216-9105","full_name":"Sommer, Christoph M","id":"4DF26D8C-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Caroline","last_name":"Kreuzinger","full_name":"Kreuzinger, Caroline","id":"382077BA-F248-11E8-B48F-1D18A9856A87"},{"orcid":"0000-0002-9033-9096","last_name":"Dotter","first_name":"Christoph","id":"4C66542E-F248-11E8-B48F-1D18A9856A87","full_name":"Dotter, Christoph"},{"last_name":"Knaus","first_name":"Lisa","id":"3B2ABCF4-F248-11E8-B48F-1D18A9856A87","full_name":"Knaus, Lisa"},{"id":"D23090A2-9057-11EA-883A-A8396FC7A38F","full_name":"Dobler, Zoe","last_name":"Dobler","first_name":"Zoe"},{"last_name":"Cacci","first_name":"Emanuele","full_name":"Cacci, Emanuele"},{"first_name":"Florian KM","last_name":"Schur","orcid":"0000-0003-4790-8078","full_name":"Schur, Florian KM","id":"48AD8942-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Johann G","orcid":"0000-0001-8559-3973","last_name":"Danzl","full_name":"Danzl, Johann G","id":"42EFD3B6-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Novarino, Gaia","id":"3E57A680-F248-11E8-B48F-1D18A9856A87","first_name":"Gaia","orcid":"0000-0002-7673-7178","last_name":"Novarino"}],"ec_funded":1,"_id":"9429","project":[{"call_identifier":"H2020","name":"ISTplus - Postdoctoral Fellowships","_id":"260C2330-B435-11E9-9278-68D0E5697425","grant_number":"754411"},{"name":"Probing the Reversibility of Autism Spectrum Disorders by Employing in vivo and in vitro Models","call_identifier":"H2020","_id":"25444568-B435-11E9-9278-68D0E5697425","grant_number":"715508"},{"_id":"2548AE96-B435-11E9-9278-68D0E5697425","grant_number":"W1232","call_identifier":"FWF","name":"Molecular Drug Targets"},{"name":"Stem Cell Modulation in Neural Development and Regeneration/ P07-Neural stem cells in autism and epilepsy","_id":"05A0D778-7A3F-11EA-A408-12923DDC885E","grant_number":"F7807"},{"name":"Optical control of synaptic function via adhesion molecules","call_identifier":"FWF","_id":"265CB4D0-B435-11E9-9278-68D0E5697425","grant_number":"I03600"}],"department":[{"_id":"GaNo"},{"_id":"JoDa"},{"_id":"FlSc"},{"_id":"MiSi"},{"_id":"LifeSc"},{"_id":"Bio"}],"corr_author":"1","year":"2021","scopus_import":"1","type":"journal_article","file_date_updated":"2021-05-28T12:39:43Z","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","publication_status":"published","publisher":"Springer Nature","quality_controlled":"1","article_number":"3058","oa":1},{"has_accepted_license":"1","status":"public","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","short":"CC BY-NC-ND (4.0)","image":"/images/cc_by_nc_nd.png","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)"},"day":"11","oa_version":"Preprint","citation":{"short":"J. Morandell, L.A. Schwarz, B. Basilico, S. Tasciyan, A. Nicolas, C.M. Sommer, C. Kreuzinger, L. Knaus, Z. Dobler, E. Cacci, J.G. Danzl, G. Novarino, BioRxiv (n.d.).","ama":"Morandell J, Schwarz LA, Basilico B, et al. Cul3 regulates cytoskeleton protein homeostasis and cell migration during a critical window of brain development. <i>bioRxiv</i>. doi:<a href=\"https://doi.org/10.1101/2020.01.10.902064 \">10.1101/2020.01.10.902064 </a>","chicago":"Morandell, Jasmin, Lena A Schwarz, Bernadette Basilico, Saren Tasciyan, Armel Nicolas, Christoph M Sommer, Caroline Kreuzinger, et al. “Cul3 Regulates Cytoskeleton Protein Homeostasis and Cell Migration during a Critical Window of Brain Development.” <i>BioRxiv</i>, n.d. <a href=\"https://doi.org/10.1101/2020.01.10.902064 \">https://doi.org/10.1101/2020.01.10.902064 </a>.","ieee":"J. Morandell <i>et al.</i>, “Cul3 regulates cytoskeleton protein homeostasis and cell migration during a critical window of brain development,” <i>bioRxiv</i>. .","mla":"Morandell, Jasmin, et al. “Cul3 Regulates Cytoskeleton Protein Homeostasis and Cell Migration during a Critical Window of Brain Development.” <i>BioRxiv</i>, doi:<a href=\"https://doi.org/10.1101/2020.01.10.902064 \">10.1101/2020.01.10.902064 </a>.","ista":"Morandell J, Schwarz LA, Basilico B, Tasciyan S, Nicolas A, Sommer CM, Kreuzinger C, Knaus L, Dobler Z, Cacci E, Danzl JG, Novarino G. Cul3 regulates cytoskeleton protein homeostasis and cell migration during a critical window of brain development. bioRxiv, <a href=\"https://doi.org/10.1101/2020.01.10.902064 \">10.1101/2020.01.10.902064 </a>.","apa":"Morandell, J., Schwarz, L. A., Basilico, B., Tasciyan, S., Nicolas, A., Sommer, C. M., … Novarino, G. (n.d.). Cul3 regulates cytoskeleton protein homeostasis and cell migration during a critical window of brain development. <i>bioRxiv</i>. <a href=\"https://doi.org/10.1101/2020.01.10.902064 \">https://doi.org/10.1101/2020.01.10.902064 </a>"},"related_material":{"record":[{"relation":"later_version","id":"9429","status":"public"},{"status":"public","relation":"dissertation_contains","id":"8620"}]},"fulldoi":"https://doi.org/10.1101/2020.01.10.902064 ","das_tickbox":"1","ddc":["570"],"acknowledged_ssus":[{"_id":"PreCl"}],"doi":"10.1101/2020.01.10.902064 ","language":[{"iso":"eng"}],"abstract":[{"text":"De novo loss of function mutations in the ubiquitin ligase-encoding gene Cullin3 (CUL3) lead to autism spectrum disorder (ASD). Here, we used Cul3 mouse models to evaluate the consequences of Cul3 mutations in vivo. Our results show that Cul3 haploinsufficient mice exhibit deficits in motor coordination as well as ASD-relevant social and cognitive impairments. Cul3 mutant brain displays cortical lamination abnormalities due to defective neuronal migration and reduced numbers of excitatory and inhibitory neurons. In line with the observed abnormal columnar organization, Cul3 haploinsufficiency is associated with decreased spontaneous excitatory and inhibitory activity in the cortex. At the molecular level, employing a quantitative proteomic approach, we show that Cul3 regulates cytoskeletal and adhesion protein abundance in mouse embryos. Abnormal regulation of cytoskeletal proteins in Cul3 mutant neuronal cells results in atypical organization of the actin mesh at the cell leading edge, likely causing the observed migration deficits. In contrast to these important functions early in development, Cul3 deficiency appears less relevant at adult stages. In fact, induction of Cul3 haploinsufficiency in adult mice does not result in the behavioral defects observed in constitutive Cul3 haploinsufficient animals. Taken together, our data indicate that Cul3 has a critical role in the regulation of cytoskeletal proteins and neuronal migration and that ASD-associated defects and behavioral abnormalities are primarily due to Cul3 functions at early developmental stages.","lang":"eng"}],"project":[{"name":"Optical control of synaptic function via adhesion molecules","call_identifier":"FWF","_id":"265CB4D0-B435-11E9-9278-68D0E5697425","grant_number":"I03600"},{"call_identifier":"FWF","name":"Molecular Drug Targets","_id":"2548AE96-B435-11E9-9278-68D0E5697425","grant_number":"W1232"}],"department":[{"_id":"JoDa"},{"_id":"GaNo"},{"_id":"LifeSc"}],"corr_author":"1","type":"preprint","year":"2020","file_date_updated":"2020-07-14T12:48:03Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication_status":"draft","oa":1,"date_created":"2020-05-05T14:31:33Z","title":"Cul3 regulates cytoskeleton protein homeostasis and cell migration during a critical window of brain development","article_processing_charge":"No","date_updated":"2026-11-07T23:30:55Z","month":"01","publication":"bioRxiv","file":[{"access_level":"open_access","content_type":"application/pdf","file_name":"2020.01.10.902064v1.full.pdf","creator":"rsix","checksum":"c6799ab5daba80efe8e2ed63c15f8c81","relation":"main_file","file_id":"7801","date_updated":"2020-07-14T12:48:03Z","date_created":"2020-05-05T14:31:19Z","file_size":2931370}],"date_published":"2020-01-11T00:00:00Z","author":[{"full_name":"Morandell, Jasmin","id":"4739D480-F248-11E8-B48F-1D18A9856A87","first_name":"Jasmin","last_name":"Morandell"},{"first_name":"Lena A","last_name":"Schwarz","full_name":"Schwarz, Lena A","id":"29A8453C-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Basilico","orcid":"0000-0003-1843-3173","first_name":"Bernadette","id":"36035796-5ACA-11E9-A75E-7AF2E5697425","full_name":"Basilico, Bernadette"},{"full_name":"Tasciyan, Saren","id":"4323B49C-F248-11E8-B48F-1D18A9856A87","first_name":"Saren","orcid":"0000-0003-1671-393X","last_name":"Tasciyan"},{"id":"2A103192-F248-11E8-B48F-1D18A9856A87","full_name":"Nicolas, Armel","last_name":"Nicolas","first_name":"Armel"},{"orcid":"0000-0003-1216-9105","last_name":"Sommer","first_name":"Christoph M","id":"4DF26D8C-F248-11E8-B48F-1D18A9856A87","full_name":"Sommer, Christoph M"},{"id":"382077BA-F248-11E8-B48F-1D18A9856A87","full_name":"Kreuzinger, Caroline","last_name":"Kreuzinger","first_name":"Caroline"},{"full_name":"Knaus, Lisa","id":"3B2ABCF4-F248-11E8-B48F-1D18A9856A87","first_name":"Lisa","last_name":"Knaus"},{"first_name":"Zoe","last_name":"Dobler","full_name":"Dobler, Zoe","id":"D23090A2-9057-11EA-883A-A8396FC7A38F"},{"last_name":"Cacci","first_name":"Emanuele","full_name":"Cacci, Emanuele"},{"first_name":"Johann G","orcid":"0000-0001-8559-3973","last_name":"Danzl","full_name":"Danzl, Johann G","id":"42EFD3B6-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Novarino","orcid":"0000-0002-7673-7178","first_name":"Gaia","id":"3E57A680-F248-11E8-B48F-1D18A9856A87","full_name":"Novarino, Gaia"}],"_id":"7800"},{"citation":{"mla":"Antoniou, Michael N., et al. <i>MOESM1 of Glyphosate Does Not Substitute for Glycine in Proteins of Actively Dividing Mammalian Cells</i>. 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Rao, and Cristina Vazquez Martin. “MOESM1 of Glyphosate Does Not Substitute for Glycine in Proteins of Actively Dividing Mammalian Cells.” Springer Nature, 2019. <a href=\"https://doi.org/10.6084/m9.figshare.9411761.v1\">https://doi.org/10.6084/m9.figshare.9411761.v1</a>.","short":"M.N. Antoniou, A. Nicolas, R. Mesnage, M. Biserni, F.V. Rao, C.V. Martin, (2019).","apa":"Antoniou, M. N., Nicolas, A., Mesnage, R., Biserni, M., Rao, F. V., &#38; Martin, C. V. (2019). MOESM1 of Glyphosate does not substitute for glycine in proteins of actively dividing mammalian cells. Springer Nature. <a href=\"https://doi.org/10.6084/m9.figshare.9411761.v1\">https://doi.org/10.6084/m9.figshare.9411761.v1</a>","ista":"Antoniou MN, Nicolas A, Mesnage R, Biserni M, Rao FV, Martin CV. 2019. MOESM1 of Glyphosate does not substitute for glycine in proteins of actively dividing mammalian cells, Springer Nature, <a href=\"https://doi.org/10.6084/m9.figshare.9411761.v1\">10.6084/m9.figshare.9411761.v1</a>."},"oa":1,"user_id":"6785fbc1-c503-11eb-8a32-93094b40e1cf","main_file_link":[{"open_access":"1","url":"https://doi.org/10.6084/m9.figshare.9411761.v1"}],"day":"09","publisher":"Springer Nature","oa_version":"Published Version","status":"public","department":[{"_id":"LifeSc"}],"year":"2019","type":"research_data_reference","_id":"9784","abstract":[{"lang":"eng","text":"Additional file 1: Table S1. Kinetics of MDA-MB-231 cell growth in either the presence or absence of 100Â mg/L glyphosate. Cell counts are given at day-1 of seeding flasks and following 6-days of continuous culture. Note: no differences in cell numbers were observed between negative control and glyphosate treated cultures."}],"doi":"10.6084/m9.figshare.9411761.v1","author":[{"full_name":"Antoniou, Michael N.","last_name":"Antoniou","first_name":"Michael N."},{"first_name":"Armel","last_name":"Nicolas","full_name":"Nicolas, Armel","id":"2A103192-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Mesnage, Robin","last_name":"Mesnage","first_name":"Robin"},{"last_name":"Biserni","first_name":"Martina","full_name":"Biserni, Martina"},{"first_name":"Francesco V.","last_name":"Rao","full_name":"Rao, Francesco V."},{"full_name":"Martin, Cristina Vazquez","first_name":"Cristina Vazquez","last_name":"Martin"}],"date_published":"2019-08-09T00:00:00Z","article_processing_charge":"No","date_updated":"2023-02-23T12:52:29Z","month":"08","fulldoi":"https://doi.org/10.6084/m9.figshare.9411761.v1","date_created":"2021-08-06T08:14:05Z","related_material":{"record":[{"status":"public","id":"6819","relation":"used_in_publication"}]},"title":"MOESM1 of Glyphosate does not substitute for glycine in proteins of actively dividing mammalian cells"},{"citation":{"ista":"Antoniou MN, Nicolas A, Mesnage R, Biserni M, Rao FV, Martin CV. 2019. Glyphosate does not substitute for glycine in proteins of actively dividing mammalian cells. BMC Research Notes. 12, 494.","apa":"Antoniou, M. N., Nicolas, A., Mesnage, R., Biserni, M., Rao, F. V., &#38; Martin, C. V. (2019). Glyphosate does not substitute for glycine in proteins of actively dividing mammalian cells. <i>BMC Research Notes</i>. BioMed Central. <a href=\"https://doi.org/10.1186/s13104-019-4534-3\">https://doi.org/10.1186/s13104-019-4534-3</a>","ama":"Antoniou MN, Nicolas A, Mesnage R, Biserni M, Rao FV, Martin CV. Glyphosate does not substitute for glycine in proteins of actively dividing mammalian cells. <i>BMC Research Notes</i>. 2019;12. doi:<a href=\"https://doi.org/10.1186/s13104-019-4534-3\">10.1186/s13104-019-4534-3</a>","short":"M.N. Antoniou, A. Nicolas, R. Mesnage, M. Biserni, F.V. Rao, C.V. Martin, BMC Research Notes 12 (2019).","chicago":"Antoniou, Michael N., Armel Nicolas, Robin Mesnage, Martina Biserni, Francesco V. Rao, and Cristina Vazquez Martin. “Glyphosate Does Not Substitute for Glycine in Proteins of Actively Dividing Mammalian Cells.” <i>BMC Research Notes</i>. BioMed Central, 2019. <a href=\"https://doi.org/10.1186/s13104-019-4534-3\">https://doi.org/10.1186/s13104-019-4534-3</a>.","ieee":"M. N. Antoniou, A. Nicolas, R. Mesnage, M. Biserni, F. V. Rao, and C. V. Martin, “Glyphosate does not substitute for glycine in proteins of actively dividing mammalian cells,” <i>BMC Research Notes</i>, vol. 12. BioMed Central, 2019.","mla":"Antoniou, Michael N., et al. “Glyphosate Does Not Substitute for Glycine in Proteins of Actively Dividing Mammalian Cells.” <i>BMC Research Notes</i>, vol. 12, 494, BioMed Central, 2019, doi:<a href=\"https://doi.org/10.1186/s13104-019-4534-3\">10.1186/s13104-019-4534-3</a>."},"oa_version":"Published Version","external_id":{"pmid":["31395095"]},"day":"08","tmp":{"image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"has_accepted_license":"1","status":"public","abstract":[{"lang":"eng","text":"Glyphosate (N-phosphonomethyl glycine) and its commercial herbicide formulations have been shown to exert toxicity via various mechanisms. It has been asserted that glyphosate substitutes for glycine in polypeptide chains leading to protein misfolding and toxicity. However, as no direct evidence exists for glycine to glyphosate substitution in proteins, including in mammalian organisms, we tested this claim by conducting a proteomics analysis of MDA-MB-231 human breast cancer cells grown in the presence of 100 mg/L glyphosate for 6 days. Protein extracts from three treated and three untreated cell cultures were analysed as one TMT-6plex labelled sample, to highlight a specific pattern (+/+/+/−/−/−) of reporter intensities for peptides bearing true glyphosate treatment induced-post translational modifications as well as allowing an investigation of the total proteome."}],"language":[{"iso":"eng"}],"publication_identifier":{"eissn":["1756-0500"]},"doi":"10.1186/s13104-019-4534-3","ddc":["570"],"volume":12,"intvolume":"        12","related_material":{"record":[{"relation":"research_data","id":"9784","status":"public"}]},"fulldoi":"https://doi.org/10.1186/s13104-019-4534-3","quality_controlled":"1","oa":1,"article_number":"494","publication_status":"published","publisher":"BioMed Central","file_date_updated":"2020-07-14T12:47:40Z","user_id":"3E5EF7F0-F248-11E8-B48F-1D18A9856A87","type":"journal_article","scopus_import":1,"year":"2019","department":[{"_id":"LifeSc"}],"pmid":1,"_id":"6819","date_published":"2019-08-08T00:00:00Z","author":[{"full_name":"Antoniou, Michael N.","first_name":"Michael N.","last_name":"Antoniou"},{"full_name":"Nicolas, Armel","id":"2A103192-F248-11E8-B48F-1D18A9856A87","first_name":"Armel","last_name":"Nicolas"},{"first_name":"Robin","last_name":"Mesnage","full_name":"Mesnage, Robin"},{"full_name":"Biserni, Martina","first_name":"Martina","last_name":"Biserni"},{"full_name":"Rao, Francesco V.","last_name":"Rao","first_name":"Francesco V."},{"full_name":"Martin, Cristina Vazquez","first_name":"Cristina Vazquez","last_name":"Martin"}],"publication":"BMC Research Notes","file":[{"date_created":"2019-08-23T11:10:35Z","file_size":1177482,"date_updated":"2020-07-14T12:47:40Z","file_id":"6829","file_name":"2019_BMC_Antoniou.pdf","creator":"dernst","checksum":"4a2bb7994b7f2c432bf44f5127ea3102","relation":"main_file","access_level":"open_access","content_type":"application/pdf"}],"date_updated":"2023-02-23T14:08:14Z","month":"08","article_processing_charge":"No","title":"Glyphosate does not substitute for glycine in proteins of actively dividing mammalian cells","date_created":"2019-08-18T22:00:39Z"},{"type":"journal_article","year":"2019","department":[{"_id":"GaNo"},{"_id":"LifeSc"}],"publication_status":"published","publisher":"Elsevier","page":"S11-S12","user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","quality_controlled":"1","article_type":"original","title":"S.16.05 Illuminating the role of the e3 ubiquitin ligase cullin3 in brain development and autism","date_created":"2020-01-30T10:07:41Z","month":"12","date_updated":"2023-09-07T14:56:17Z","article_processing_charge":"No","date_published":"2019-12-13T00:00:00Z","author":[{"id":"4739D480-F248-11E8-B48F-1D18A9856A87","full_name":"Morandell, Jasmin","last_name":"Morandell","first_name":"Jasmin"},{"first_name":"Armel","last_name":"Nicolas","full_name":"Nicolas, Armel","id":"2A103192-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Schwarz","first_name":"Lena A","id":"29A8453C-F248-11E8-B48F-1D18A9856A87","full_name":"Schwarz, Lena A"},{"id":"3E57A680-F248-11E8-B48F-1D18A9856A87","full_name":"Novarino, Gaia","orcid":"0000-0002-7673-7178","last_name":"Novarino","first_name":"Gaia"}],"publication":"European Neuropsychopharmacology","_id":"7415","status":"public","oa_version":"None","external_id":{"isi":["000502657500021"]},"day":"13","citation":{"mla":"Morandell, Jasmin, et al. “S.16.05 Illuminating the Role of the E3 Ubiquitin Ligase Cullin3 in Brain Development and Autism.” <i>European Neuropsychopharmacology</i>, vol. 29, no. Supplement 6, Elsevier, 2019, pp. S11–12, doi:<a href=\"https://doi.org/10.1016/j.euroneuro.2019.09.040\">10.1016/j.euroneuro.2019.09.040</a>.","ieee":"J. Morandell, A. Nicolas, L. A. Schwarz, and G. Novarino, “S.16.05 Illuminating the role of the e3 ubiquitin ligase cullin3 in brain development and autism,” <i>European Neuropsychopharmacology</i>, vol. 29, no. Supplement 6. Elsevier, pp. S11–S12, 2019.","chicago":"Morandell, Jasmin, Armel Nicolas, Lena A Schwarz, and Gaia Novarino. “S.16.05 Illuminating the Role of the E3 Ubiquitin Ligase Cullin3 in Brain Development and Autism.” <i>European Neuropsychopharmacology</i>. Elsevier, 2019. <a href=\"https://doi.org/10.1016/j.euroneuro.2019.09.040\">https://doi.org/10.1016/j.euroneuro.2019.09.040</a>.","short":"J. Morandell, A. Nicolas, L.A. Schwarz, G. Novarino, European Neuropsychopharmacology 29 (2019) S11–S12.","ama":"Morandell J, Nicolas A, Schwarz LA, Novarino G. S.16.05 Illuminating the role of the e3 ubiquitin ligase cullin3 in brain development and autism. <i>European Neuropsychopharmacology</i>. 2019;29(Supplement 6):S11-S12. doi:<a href=\"https://doi.org/10.1016/j.euroneuro.2019.09.040\">10.1016/j.euroneuro.2019.09.040</a>","apa":"Morandell, J., Nicolas, A., Schwarz, L. A., &#38; Novarino, G. (2019). S.16.05 Illuminating the role of the e3 ubiquitin ligase cullin3 in brain development and autism. <i>European Neuropsychopharmacology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.euroneuro.2019.09.040\">https://doi.org/10.1016/j.euroneuro.2019.09.040</a>","ista":"Morandell J, Nicolas A, Schwarz LA, Novarino G. 2019. S.16.05 Illuminating the role of the e3 ubiquitin ligase cullin3 in brain development and autism. European Neuropsychopharmacology. 29(Supplement 6), S11–S12."},"issue":"Supplement 6","intvolume":"        29","fulldoi":"https://doi.org/10.1016/j.euroneuro.2019.09.040","volume":29,"publication_identifier":{"issn":["0924-977X"]},"doi":"10.1016/j.euroneuro.2019.09.040","isi":1,"language":[{"iso":"eng"}]},{"ddc":["571"],"volume":11,"intvolume":"        11","acknowledgement":"This work was supported by grants from the European Union Seventh Framework Programme (CIG-303564 to H.J. and ERC-StG-311166 to S.M.B.N.), the Human Frontier Science Program (RGY0084_2012 to H.J.) and the Herzfelder Foundation (to M.G.). A.I.-P. was supported by a Ramon Areces fellowship, and E.R. by the graduate program MolecularDrugTargets (Austrian Science Fund (FWF): W 1232) and a FemTech fellowship (3580812 Austrian Research Promotion Agency).","fulldoi":"https://doi.org/10.1038/nchembio.1933","related_material":{"record":[{"status":"public","relation":"dissertation_contains","id":"418"}]},"abstract":[{"text":"High-throughput live-cell screens are intricate elements of systems biology studies and drug discovery pipelines. Here, we demonstrate an optogenetics-assisted method that avoids the need for chemical activators and reporters, reduces the number of operational steps and increases information content in a cell-based small-molecule screen against human protein kinases, including an orphan receptor tyrosine kinase. This blueprint for all-optical screening can be adapted to many drug targets and cellular processes.","lang":"eng"}],"language":[{"iso":"eng"}],"doi":"10.1038/nchembio.1933","has_accepted_license":"1","status":"public","citation":{"ieee":"Á. Inglés Prieto <i>et al.</i>, “Light-assisted small-molecule screening against protein kinases,” <i>Nature Chemical Biology</i>, vol. 11, no. 12. Nature Publishing Group, pp. 952–954, 2015.","chicago":"Inglés Prieto, Álvaro, Eva Gschaider-Reichhart, Markus Muellner, Matthias Nowak, Sebastian Nijman, Michael Grusch, and Harald L Janovjak. “Light-Assisted Small-Molecule Screening against Protein Kinases.” <i>Nature Chemical Biology</i>. Nature Publishing Group, 2015. <a href=\"https://doi.org/10.1038/nchembio.1933\">https://doi.org/10.1038/nchembio.1933</a>.","ama":"Inglés Prieto Á, Gschaider-Reichhart E, Muellner M, et al. Light-assisted small-molecule screening against protein kinases. <i>Nature Chemical Biology</i>. 2015;11(12):952-954. doi:<a href=\"https://doi.org/10.1038/nchembio.1933\">10.1038/nchembio.1933</a>","short":"Á. Inglés Prieto, E. Gschaider-Reichhart, M. Muellner, M. Nowak, S. Nijman, M. Grusch, H.L. Janovjak, Nature Chemical Biology 11 (2015) 952–954.","mla":"Inglés Prieto, Álvaro, et al. “Light-Assisted Small-Molecule Screening against Protein Kinases.” <i>Nature Chemical Biology</i>, vol. 11, no. 12, Nature Publishing Group, 2015, pp. 952–54, doi:<a href=\"https://doi.org/10.1038/nchembio.1933\">10.1038/nchembio.1933</a>.","ista":"Inglés Prieto Á, Gschaider-Reichhart E, Muellner M, Nowak M, Nijman S, Grusch M, Janovjak HL. 2015. Light-assisted small-molecule screening against protein kinases. Nature Chemical Biology. 11(12), 952–954.","apa":"Inglés Prieto, Á., Gschaider-Reichhart, E., Muellner, M., Nowak, M., Nijman, S., Grusch, M., &#38; Janovjak, H. L. (2015). Light-assisted small-molecule screening against protein kinases. <i>Nature Chemical Biology</i>. Nature Publishing Group. <a href=\"https://doi.org/10.1038/nchembio.1933\">https://doi.org/10.1038/nchembio.1933</a>"},"issue":"12","oa_version":"Submitted Version","day":"12","publist_id":"5471","month":"10","date_updated":"2026-04-08T14:11:53Z","title":"Light-assisted small-molecule screening against protein kinases","date_created":"2018-12-11T11:53:25Z","_id":"1678","ec_funded":1,"pubrep_id":"837","author":[{"id":"2A9DB292-F248-11E8-B48F-1D18A9856A87","full_name":"Inglés Prieto, Álvaro","orcid":"0000-0002-5409-8571","last_name":"Inglés Prieto","first_name":"Álvaro"},{"id":"3FEE232A-F248-11E8-B48F-1D18A9856A87","full_name":"Gschaider-Reichhart, Eva","orcid":"0000-0002-7218-7738","last_name":"Gschaider-Reichhart","first_name":"Eva"},{"last_name":"Muellner","first_name":"Markus","full_name":"Muellner, Markus"},{"id":"30845DAA-F248-11E8-B48F-1D18A9856A87","full_name":"Nowak, Matthias","last_name":"Nowak","first_name":"Matthias"},{"full_name":"Nijman, Sebastian","first_name":"Sebastian","last_name":"Nijman"},{"last_name":"Grusch","first_name":"Michael","full_name":"Grusch, Michael"},{"first_name":"Harald L","last_name":"Janovjak","orcid":"0000-0002-8023-9315","full_name":"Janovjak, Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87"}],"date_published":"2015-10-12T00:00:00Z","file":[{"file_name":"IST-2017-837-v1+1_ingles-prieto.pdf","creator":"system","checksum":"e9fb251dfcb7cd209b83f17867e61321","relation":"main_file","access_level":"open_access","content_type":"application/pdf","date_created":"2018-12-12T10:10:51Z","file_size":1308364,"date_updated":"2020-07-14T12:45:12Z","file_id":"4842"}],"publication":"Nature Chemical Biology","year":"2015","scopus_import":1,"type":"journal_article","corr_author":"1","department":[{"_id":"HaJa"},{"_id":"LifeSc"}],"project":[{"_id":"25548C20-B435-11E9-9278-68D0E5697425","grant_number":"303564","call_identifier":"FP7","name":"Microbial Ion Channels for Synthetic Neurobiology"},{"name":"In situ real-time imaging of neurotransmitter signaling using designer optical sensors","grant_number":"RGY0084/2012","_id":"255BFFFA-B435-11E9-9278-68D0E5697425"},{"call_identifier":"FWF","name":"Molecular Drug Targets","_id":"255A6082-B435-11E9-9278-68D0E5697425","grant_number":"W1232-B24"}],"oa":1,"quality_controlled":"1","publisher":"Nature Publishing Group","publication_status":"published","page":"952 - 954","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","file_date_updated":"2020-07-14T12:45:12Z"},{"date_created":"2018-12-11T11:54:20Z","title":"FAM96A is a novel pro-apoptotic tumor suppressor in gastrointestinal stromal tumors","article_type":"original","article_processing_charge":"No","publist_id":"5253","date_updated":"2025-09-23T08:46:31Z","month":"09","publication":"International Journal of Cancer","author":[{"first_name":"Bettina","last_name":"Schwamb","full_name":"Schwamb, Bettina"},{"first_name":"Robert","last_name":"Pick","full_name":"Pick, Robert"},{"first_name":"Sara","last_name":"Fernández","full_name":"Fernández, Sara"},{"full_name":"Völp, Kirsten","first_name":"Kirsten","last_name":"Völp"},{"full_name":"Heering, Jan","last_name":"Heering","first_name":"Jan"},{"full_name":"Dötsch, Volker","last_name":"Dötsch","first_name":"Volker"},{"last_name":"Bösser","first_name":"Susanne","full_name":"Bösser, Susanne"},{"first_name":"Jennifer","last_name":"Jung","full_name":"Jung, Jennifer"},{"last_name":"Beinoravičiute Kellner","first_name":"Rasa","full_name":"Beinoravičiute Kellner, Rasa"},{"last_name":"Wesely","first_name":"Josephine","full_name":"Wesely, Josephine"},{"full_name":"Zörnig, Inka","first_name":"Inka","last_name":"Zörnig"},{"first_name":"Matthias","last_name":"Hammerschmidt","full_name":"Hammerschmidt, Matthias"},{"last_name":"Nowak","first_name":"Matthias","id":"30845DAA-F248-11E8-B48F-1D18A9856A87","full_name":"Nowak, Matthias"},{"last_name":"Penzel","first_name":"Roland","full_name":"Penzel, Roland"},{"full_name":"Zatloukal, Kurt","first_name":"Kurt","last_name":"Zatloukal"},{"full_name":"Joos, Stefan","first_name":"Stefan","last_name":"Joos"},{"full_name":"Rieker, Ralf","first_name":"Ralf","last_name":"Rieker"},{"full_name":"Agaimy, Abbas","first_name":"Abbas","last_name":"Agaimy"},{"last_name":"Söder","first_name":"Stephan","full_name":"Söder, Stephan"},{"first_name":"Kmarie","last_name":"Reid Lombardo","full_name":"Reid Lombardo, Kmarie"},{"first_name":"Michael","last_name":"Kendrick","full_name":"Kendrick, Michael"},{"full_name":"Bardsley, Michael","last_name":"Bardsley","first_name":"Michael"},{"full_name":"Hayashi, Yujiro","last_name":"Hayashi","first_name":"Yujiro"},{"last_name":"Asuzu","first_name":"David","full_name":"Asuzu, David"},{"last_name":"Syed","first_name":"Sabriya","full_name":"Syed, Sabriya"},{"last_name":"Ördög","first_name":"Tamás","full_name":"Ördög, Tamás"},{"first_name":"Martin","last_name":"Zörnig","full_name":"Zörnig, Martin"}],"date_published":"2015-09-01T00:00:00Z","_id":"1848","pmid":1,"department":[{"_id":"LifeSc"}],"scopus_import":"1","year":"2015","type":"journal_article","page":"1318 - 1329","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","publisher":"Wiley","publication_status":"published","oa":1,"quality_controlled":"1","fulldoi":"https://doi.org/10.1002/ijc.29498","intvolume":"       137","volume":137,"doi":"10.1002/ijc.29498","language":[{"iso":"eng"}],"isi":1,"abstract":[{"text":"The ability to escape apoptosis is a hallmark of cancer-initiating cells and a key factor of resistance to oncolytic therapy. Here, we identify FAM96A as a ubiquitous, evolutionarily conserved apoptosome-activating protein and investigate its potential pro-apoptotic tumor suppressor function in gastrointestinal stromal tumors (GISTs). Interaction between FAM96A and apoptotic peptidase activating factor 1 (APAF1) was identified in yeast two-hybrid screen and further studied by deletion mutants, glutathione-S-transferase pull-down, co-immunoprecipitation and immunofluorescence. Effects of FAM96A overexpression and knock-down on apoptosis sensitivity were examined in cancer cells and zebrafish embryos. Expression of FAM96A in GISTs and histogenetically related cells including interstitial cells of Cajal (ICCs), “fibroblast-like cells” (FLCs) and ICC stem cells (ICC-SCs) was investigated by Northern blotting, reverse transcription—polymerase chain reaction, immunohistochemistry and Western immunoblotting. Tumorigenicity of GIST cells and transformed murine ICC-SCs stably transduced to re-express FAM96A was studied by xeno- and allografting into immunocompromised mice. FAM96A was found to bind APAF1 and to enhance the induction of mitochondrial apoptosis. FAM96A protein or mRNA was dramatically reduced or lost in 106 of 108 GIST samples representing three independent patient cohorts. Whereas ICCs, ICC-SCs and FLCs, the presumed normal counterparts of GIST, were found to robustly express FAM96A protein and mRNA, FAM96A expression was much reduced in tumorigenic ICC-SCs. Re-expression of FAM96A in GIST cells and transformed ICC-SCs increased apoptosis sensitivity and diminished tumorigenicity. Our data suggest FAM96A is a novel pro-apoptotic tumor suppressor that is lost during GIST tumorigenesis.","lang":"eng"}],"status":"public","main_file_link":[{"open_access":"1","url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4497860/"}],"day":"01","external_id":{"pmid":["25716227"],"isi":["000357808900012"]},"oa_version":"Submitted Version","issue":"6","citation":{"ieee":"B. Schwamb <i>et al.</i>, “FAM96A is a novel pro-apoptotic tumor suppressor in gastrointestinal stromal tumors,” <i>International Journal of Cancer</i>, vol. 137, no. 6. Wiley, pp. 1318–1329, 2015.","chicago":"Schwamb, Bettina, Robert Pick, Sara Fernández, Kirsten Völp, Jan Heering, Volker Dötsch, Susanne Bösser, et al. “FAM96A Is a Novel Pro-Apoptotic Tumor Suppressor in Gastrointestinal Stromal Tumors.” <i>International Journal of Cancer</i>. Wiley, 2015. <a href=\"https://doi.org/10.1002/ijc.29498\">https://doi.org/10.1002/ijc.29498</a>.","short":"B. Schwamb, R. Pick, S. Fernández, K. Völp, J. Heering, V. Dötsch, S. Bösser, J. Jung, R. Beinoravičiute Kellner, J. Wesely, I. Zörnig, M. Hammerschmidt, M. Nowak, R. Penzel, K. Zatloukal, S. Joos, R. Rieker, A. Agaimy, S. Söder, K. Reid Lombardo, M. Kendrick, M. Bardsley, Y. Hayashi, D. Asuzu, S. Syed, T. Ördög, M. Zörnig, International Journal of Cancer 137 (2015) 1318–1329.","ama":"Schwamb B, Pick R, Fernández S, et al. FAM96A is a novel pro-apoptotic tumor suppressor in gastrointestinal stromal tumors. <i>International Journal of Cancer</i>. 2015;137(6):1318-1329. doi:<a href=\"https://doi.org/10.1002/ijc.29498\">10.1002/ijc.29498</a>","mla":"Schwamb, Bettina, et al. “FAM96A Is a Novel Pro-Apoptotic Tumor Suppressor in Gastrointestinal Stromal Tumors.” <i>International Journal of Cancer</i>, vol. 137, no. 6, Wiley, 2015, pp. 1318–29, doi:<a href=\"https://doi.org/10.1002/ijc.29498\">10.1002/ijc.29498</a>.","ista":"Schwamb B, Pick R, Fernández S, Völp K, Heering J, Dötsch V, Bösser S, Jung J, Beinoravičiute Kellner R, Wesely J, Zörnig I, Hammerschmidt M, Nowak M, Penzel R, Zatloukal K, Joos S, Rieker R, Agaimy A, Söder S, Reid Lombardo K, Kendrick M, Bardsley M, Hayashi Y, Asuzu D, Syed S, Ördög T, Zörnig M. 2015. FAM96A is a novel pro-apoptotic tumor suppressor in gastrointestinal stromal tumors. International Journal of Cancer. 137(6), 1318–1329.","apa":"Schwamb, B., Pick, R., Fernández, S., Völp, K., Heering, J., Dötsch, V., … Zörnig, M. (2015). FAM96A is a novel pro-apoptotic tumor suppressor in gastrointestinal stromal tumors. <i>International Journal of Cancer</i>. Wiley. <a href=\"https://doi.org/10.1002/ijc.29498\">https://doi.org/10.1002/ijc.29498</a>"}},{"citation":{"mla":"Fernandes Redondo, Rodrigo A., et al. “Complete Genome Sequence of the Novel Phage MG-B1 Infecting Bacillus Weihenstephanensis.” <i>Genome Announcements</i>, vol. 1, no. 3, American Society for Microbiology, 2013, doi:<a href=\"https://doi.org/10.1128/genomeA.00216-13\">10.1128/genomeA.00216-13</a>.","chicago":"Fernandes Redondo, Rodrigo A, Anne Kupczok, Gertraud Stift, and Jonathan P Bollback. “Complete Genome Sequence of the Novel Phage MG-B1 Infecting Bacillus Weihenstephanensis.” <i>Genome Announcements</i>. American Society for Microbiology, 2013. <a href=\"https://doi.org/10.1128/genomeA.00216-13\">https://doi.org/10.1128/genomeA.00216-13</a>.","short":"R.A. Fernandes Redondo, A. Kupczok, G. Stift, J.P. Bollback, Genome Announcements 1 (2013).","ama":"Fernandes Redondo RA, Kupczok A, Stift G, Bollback JP. Complete genome sequence of the novel phage MG-B1 infecting bacillus weihenstephanensis. <i>Genome Announcements</i>. 2013;1(3). doi:<a href=\"https://doi.org/10.1128/genomeA.00216-13\">10.1128/genomeA.00216-13</a>","ieee":"R. A. Fernandes Redondo, A. Kupczok, G. Stift, and J. P. Bollback, “Complete genome sequence of the novel phage MG-B1 infecting bacillus weihenstephanensis,” <i>Genome Announcements</i>, vol. 1, no. 3. American Society for Microbiology, 2013.","apa":"Fernandes Redondo, R. A., Kupczok, A., Stift, G., &#38; Bollback, J. P. (2013). Complete genome sequence of the novel phage MG-B1 infecting bacillus weihenstephanensis. <i>Genome Announcements</i>. American Society for Microbiology. <a href=\"https://doi.org/10.1128/genomeA.00216-13\">https://doi.org/10.1128/genomeA.00216-13</a>","ista":"Fernandes Redondo RA, Kupczok A, Stift G, Bollback JP. 2013. Complete genome sequence of the novel phage MG-B1 infecting bacillus weihenstephanensis. Genome Announcements. 1(3)."},"issue":"3","oa_version":"Published Version","day":"13","has_accepted_license":"1","status":"public","abstract":[{"lang":"eng","text":"Here, we describe a novel virulent bacteriophage that infects Bacillus weihenstephanensis, isolated from soil in Austria. It is the first phage to be discovered that infects this species. Here, we present the complete genome sequence of this podovirus. "}],"language":[{"iso":"eng"}],"doi":"10.1128/genomeA.00216-13","ddc":["576"],"volume":1,"intvolume":"         1","fulldoi":"https://doi.org/10.1128/genomeA.00216-13","oa":1,"quality_controlled":"1","publisher":"American Society for Microbiology","publication_status":"published","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","file_date_updated":"2020-07-14T12:45:40Z","year":"2013","scopus_import":1,"type":"journal_article","corr_author":"1","department":[{"_id":"JoBo"},{"_id":"LifeSc"}],"_id":"2410","pubrep_id":"398","author":[{"last_name":"Fernandes Redondo","orcid":"0000-0002-5837-2793","first_name":"Rodrigo A","id":"409D5C96-F248-11E8-B48F-1D18A9856A87","full_name":"Fernandes Redondo, Rodrigo A"},{"first_name":"Anne","last_name":"Kupczok","full_name":"Kupczok, Anne","id":"2BB22BC2-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Gertraud","last_name":"Stift","full_name":"Stift, Gertraud","id":"2DB195CA-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Jonathan P","last_name":"Bollback","orcid":"0000-0002-4624-4612","full_name":"Bollback, Jonathan P","id":"2C6FA9CC-F248-11E8-B48F-1D18A9856A87"}],"date_published":"2013-06-13T00:00:00Z","publication":"Genome Announcements","file":[{"content_type":"application/pdf","access_level":"open_access","checksum":"0751ec74b695567e0cdf02aaf9c26829","relation":"main_file","creator":"system","file_name":"IST-2015-398-v1+1_Genome_Announc.-2013-Redondo-.pdf","file_id":"5291","date_updated":"2020-07-14T12:45:40Z","file_size":130026,"date_created":"2018-12-12T10:17:36Z"}],"month":"06","date_updated":"2024-10-09T20:55:15Z","publist_id":"4516","title":"Complete genome sequence of the novel phage MG-B1 infecting bacillus weihenstephanensis","date_created":"2018-12-11T11:57:30Z"}]