@inproceedings{15280,
  author       = {Balazs, Daniel and Cimada da Silva, Jessica and Dunbar, Tyler and Ibáñez, Maria and Hanrath, Tobias},
  booktitle    = {Proceedings of the Internet NanoGe Conference on Nanocrystals},
  location     = {Virtual},
  publisher    = {Fundació de la comunitat valenciana SCITO},
  title        = {{Controlled reactive assembly of colloidal nanocrystal superlattices: Mechanism and kinetics}},
  doi          = {10.29363/nanoge.incnc.2021.050},
  year         = {2021},
}

@article{9429,
  abstract     = {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.},
  author       = {Morandell, Jasmin and Schwarz, Lena A and Basilico, Bernadette and Tasciyan, Saren and Dimchev, Georgi A and Nicolas, Armel and Sommer, Christoph M and Kreuzinger, Caroline and Dotter, Christoph and Knaus, Lisa and Dobler, Zoe and Cacci, Emanuele and Schur, Florian KM and Danzl, Johann G and Novarino, Gaia},
  issn         = {2041-1723},
  journal      = {Nature Communications},
  keywords     = {General Biochemistry, Genetics and Molecular Biology},
  number       = {1},
  publisher    = {Springer Nature},
  title        = {{Cul3 regulates cytoskeleton protein homeostasis and cell migration during a critical window of brain development}},
  doi          = {10.1038/s41467-021-23123-x},
  volume       = {12},
  year         = {2021},
}

@unpublished{7800,
  abstract     = {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.},
  author       = {Morandell, Jasmin and Schwarz, Lena A and Basilico, Bernadette and Tasciyan, Saren and Nicolas, Armel and Sommer, Christoph M and Kreuzinger, Caroline and Knaus, Lisa and Dobler, Zoe and Cacci, Emanuele and Danzl, Johann G and Novarino, Gaia},
  booktitle    = {bioRxiv},
  title        = {{Cul3 regulates cytoskeleton protein homeostasis and cell migration during a critical window of brain development}},
  doi          = {10.1101/2020.01.10.902064 },
  year         = {2020},
}

@misc{9784,
  abstract     = {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.},
  author       = {Antoniou, Michael N. and Nicolas, Armel and Mesnage, Robin and Biserni, Martina and Rao, Francesco V. and Martin, Cristina Vazquez},
  publisher    = {Springer Nature},
  title        = {{MOESM1 of Glyphosate does not substitute for glycine in proteins of actively dividing mammalian cells}},
  doi          = {10.6084/m9.figshare.9411761.v1},
  year         = {2019},
}

@article{6819,
  abstract     = {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.},
  author       = {Antoniou, Michael N. and Nicolas, Armel and Mesnage, Robin and Biserni, Martina and Rao, Francesco V. and Martin, Cristina Vazquez},
  issn         = {1756-0500},
  journal      = {BMC Research Notes},
  publisher    = {BioMed Central},
  title        = {{Glyphosate does not substitute for glycine in proteins of actively dividing mammalian cells}},
  doi          = {10.1186/s13104-019-4534-3},
  volume       = {12},
  year         = {2019},
}

@article{7415,
  author       = {Morandell, Jasmin and Nicolas, Armel and Schwarz, Lena A and Novarino, Gaia},
  issn         = {0924-977X},
  journal      = {European Neuropsychopharmacology},
  number       = {Supplement 6},
  pages        = {S11--S12},
  publisher    = {Elsevier},
  title        = {{S.16.05 Illuminating the role of the e3 ubiquitin ligase cullin3 in brain development and autism}},
  doi          = {10.1016/j.euroneuro.2019.09.040},
  volume       = {29},
  year         = {2019},
}

@article{1678,
  abstract     = {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.},
  author       = {Inglés Prieto, Álvaro and Gschaider-Reichhart, Eva and Muellner, Markus and Nowak, Matthias and Nijman, Sebastian and Grusch, Michael and Janovjak, Harald L},
  journal      = {Nature Chemical Biology},
  number       = {12},
  pages        = {952 -- 954},
  publisher    = {Nature Publishing Group},
  title        = {{Light-assisted small-molecule screening against protein kinases}},
  doi          = {10.1038/nchembio.1933},
  volume       = {11},
  year         = {2015},
}

@article{1848,
  abstract     = {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.},
  author       = {Schwamb, Bettina and Pick, Robert and Fernández, Sara and Völp, Kirsten and Heering, Jan and Dötsch, Volker and Bösser, Susanne and Jung, Jennifer and Beinoravičiute Kellner, Rasa and Wesely, Josephine and Zörnig, Inka and Hammerschmidt, Matthias and Nowak, Matthias and Penzel, Roland and Zatloukal, Kurt and Joos, Stefan and Rieker, Ralf and Agaimy, Abbas and Söder, Stephan and Reid Lombardo, Kmarie and Kendrick, Michael and Bardsley, Michael and Hayashi, Yujiro and Asuzu, David and Syed, Sabriya and Ördög, Tamás and Zörnig, Martin},
  journal      = {International Journal of Cancer},
  number       = {6},
  pages        = {1318 -- 1329},
  publisher    = {Wiley},
  title        = {{FAM96A is a novel pro-apoptotic tumor suppressor in gastrointestinal stromal tumors}},
  doi          = {10.1002/ijc.29498},
  volume       = {137},
  year         = {2015},
}

@article{2410,
  abstract     = {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. },
  author       = {Fernandes Redondo, Rodrigo A and Kupczok, Anne and Stift, Gertraud and Bollback, Jonathan P},
  journal      = {Genome Announcements},
  number       = {3},
  publisher    = {American Society for Microbiology},
  title        = {{Complete genome sequence of the novel phage MG-B1 infecting bacillus weihenstephanensis}},
  doi          = {10.1128/genomeA.00216-13},
  volume       = {1},
  year         = {2013},
}