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2. RNA Sequencing and Weighted Gene Co-Expression Network Analysis Highlight DNA Replication and Key Genes in Nucleolin-Depleted Hepatoblastoma Cells.

Author

Steinkellner, Hannes, Madritsch, Silvia, Kluge, Mara, Seipel, Teresa, Sarne, Victoria, Huber, Anna, Schosserer, Markus, Oberle, Raimund, Neuhaus, Winfried, Beribisky, Alexander V., and Laccone, Franco

Subjects
*CELL cycle regulation, *GENE expression, *DNA analysis, *DNA replication, *ORGANELLE formation
Abstract

Background/objectives: Nucleolin is a major component of the nucleolus and is involved in various aspects of ribosome biogenesis. However, it is also implicated in non-nucleolar functions such as cell cycle regulation and proliferation, linking it to various pathologic processes. The aim of this study was to use differential gene expression analysis and Weighted Gene Co-expression Network analysis (WGCNA) to identify nucleolin-related regulatory pathways and possible key genes as novel therapeutic targets for cancer, viral infections and other diseases. Methods: We used two different siRNAs to downregulate the expression of nucleolin in a human hepatoblastoma (HepG2) cell line. We carried out RNA-sequencing (RNA-Seq), performed enrichment analysis of the pathways of the differentially expressed genes (DEGs) and identified protein–protein interaction (PPI) networks. Results: Both siRNAs showed high knockdown efficiency in HepG2 cells, resulting in the disruption of the nucleolar architecture and the downregulation of rRNA gene expression, both downstream hallmarks of a loss of nucleolin function. RNA-Seq identified 44 robust DEGs in both siRNA cell models. The enrichment analysis of the pathways of the downregulated genes confirmed the essential role of nucleolin in DNA replication and cell cycle processes. In addition, we identified seven hub genes linked to NCL: MCM6, MCM3, FEN1, MYBL2, MSH6, CDC6 and RBM14; all are known to be implicated in DNA replication, cell cycle progression and oncogenesis. Conclusions: Our findings demonstrate the functional consequences of nucleolin depletion in HepG2 and confirm the importance of nucleolin in DNA replication and cell cycle processes. These data will further enhance our understanding of the molecular and pathologic mechanisms of nucleolin and provide new therapeutic perspectives in disease. [ABSTRACT FROM AUTHOR]

Published
2024
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4. MeCP2 is a naturally supercharged protein with cell membrane transduction capabilities.

Author

Beribisky, Alexander V., Huber, Anna, Sarne, Victoria, Spittler, Andreas, Sukhbaatar, Nyamdelger, Seipel, Teresa, Laccone, Franco, and Steinkellner, Hannes

Abstract

The intrinsically disordered protein MeCP2 is a global transcriptional regulator encoded by the MECP2 gene. Although the structured domains of MeCP2 have been the subject of multiple studies, its unstructured regions have not been that extensively characterized. In this work, we show that MeCP2 possesses properties akin to those of supercharged proteins. By utilizing its unstructured portions, MeCP2 can successfully transduce across cell membranes and localize to heterochromatic foci in the nuclei, displaying uptake levels a third lower than a MeCP2 construct fused to the cell‐penetrating peptide TAT. MeCP2 uptake can further be enhanced by the addition of compounds that promote endosomal escape following cellular trafficking by means of macropinocytosis. Using a combination of in silico prediction algorithms and live‐cell imaging experiments, we mapped the sequence in MeCP2 responsible for its cellular incorporation, which bears a striking resemblance to TAT itself. Transduced MeCP2 was shown to interact with HDAC3. These findings provide valuable insight into the properties of MeCP2 and may be beneficial for devising future protein‐based treatment strategies. [ABSTRACT FROM AUTHOR]

Published
2024
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5. Generation and Characterization of a Human Neuronal In Vitro Model for Rett Syndrome Using a Direct Reprogramming Method

Author

Huber, Anna, primary, Sarne, Victoria, additional, Beribisky, Alexander V., additional, Ackerbauer, Daniela, additional, Derdak, Sophia, additional, Madritsch, Silvia, additional, Etzler, Julia, additional, Huck, Sigismund, additional, Scholze, Petra, additional, Gorgulu, Ilayda, additional, Christodoulou, John, additional, Studenik, Christian R., additional, Neuhaus, Winfried, additional, Connor, Bronwen, additional, Laccone, Franco, additional, and Steinkellner, Hannes, additional

Published
2024
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15. Abstracts from the 20th International Symposium on Signal Transduction at the Blood-Brain Barriers

Author

Małecki, Andrzej, primary, Skipor-Lahuta, Janina, additional, Toborek, Michal, additional, Abbott, N. Joan, additional, Antonetti, David A., additional, Su, Enming Joe, additional, Lawrence, Daniel A., additional, Atış, Müge, additional, Akcan, Uğur, additional, Yılmaz, Canan Uğur, additional, Orhan, Nurcan, additional, Düzgün, Poyraz, additional, Ceylan, Umut Deniz, additional, Arıcan, Nadir, additional, Karahüseyinoğlu, Serçin, additional, Şahin, Gizem Nur, additional, Ahıshalı, Bülent, additional, Kaya, Mehmet, additional, Aydin, Sidar, additional, Klopstein, Armelle, additional, Engelhardt, Britta, additional, Baumann, Julia, additional, Tsao, Chih-Chieh, additional, Huang, Sheng-Fu, additional, Ogunshola, Omolara, additional, Boytsova, Elizaveta B., additional, Morgun, Andrey V., additional, Khilazheva, Elena D., additional, Pozhilenkova, Elena A., additional, Gorina, Yana V., additional, Martynova, Galina P., additional, Salmina, Alla B., additional, Bueno, David, additional, Garcia-Fernàndez, Jordi, additional, Castro, Victor, additional, Skowronska, Marta, additional, Chupel, Matheus Uba, additional, Minuzzi, Luciele Guerra, additional, Filaire, Edith, additional, Teixeira, Ana Maria, additional, Corsi, Mariangela, additional, Versele, Romain, additional, Fuso, Andrea, additional, Sevin, Emmanuel, additional, Di Lorenzo, Cherubino, additional, Businaro, Rita, additional, Fenart, Laurence, additional, Gosselet, Fabien, additional, Candela, Pietra, additional, Deli, Mária A., additional, Delaney, Conor, additional, O’Keefe, Eoin, additional, Farrell, Michael, additional, Doyle, Sarah, additional, Campbell, Matthew, additional, Drewes, Lester R., additional, Appelt-Menzel, A., additional, Cubukova, A., additional, Metzger, M., additional, Fischer, R., additional, Francisco, David M. F., additional, Bruggmann, Rémy, additional, Fries, Alexa, additional, Blecharz, Kinga G., additional, Wagner, Josephin, additional, Winkler, Lars, additional, Schneider, Ulf, additional, Vajkoczy, Peter, additional, Furuse, Mikio, additional, Gabbert, Lydia, additional, Dilling, Christina, additional, Sisario, Dmitri, additional, Soukhoroukov, Vladimir, additional, Burek, Malgorzata, additional, Guérit, S., additional, Fidan, E., additional, Devraj, K., additional, Czupalla, C. J., additional, Macas, J., additional, Thom, S., additional, Plate, K. H., additional, Gerhardt, H., additional, Liebner, S., additional, Harazin, András, additional, Bocsik, Alexandra, additional, Váradi, Judit, additional, Fenyvesi, Ferenc, additional, Tubak, Vilmos, additional, Vecsernyés, Miklós, additional, Helms, Hans Christian, additional, Waagepetersen, Helle Sønderby, additional, Nielsen, Carsten Uhd, additional, Brodin, Birger, additional, Hoyk, Zsófia, additional, Tóth, Melinda E., additional, Lénárt, Nikolett, additional, Dukay, Brigitta, additional, Kittel, Ágnes, additional, Vígh, Judit, additional, Veszelka, Szilvia, additional, Walter, Fruzsina, additional, Zvara, Ágnes, additional, Puskás, László, additional, Sántha, Miklós, additional, Engelhardt, Sabrina, additional, Ogunshola, Omolara O., additional, Huber, Anna, additional, Reitner, Alexander, additional, Osmen, Samar, additional, Hahn, Kathrin, additional, Bounzina, Neli, additional, Gerhartl, Anna, additional, Schönegger, Anna, additional, Steinkellner, Hannes, additional, Laccone, Franco, additional, Neuhaus, Winfried, additional, Hudson, Natalie, additional, Celkova, Lucia, additional, Iltzsche, Anne, additional, Drndarski, Svetlana, additional, Begley, David J, additional, Janiurek, Mette Mathiesen, additional, Kucharz, Krzysztof, additional, Christoffersen, Christina, additional, Nielsen, Lars Bo, additional, Lauritzen, Martin, additional, Johnson, Rebecca H, additional, Kho, Dan T, additional, O’Carroll, Simon J, additional, Angel, Catherine E, additional, Graham, E. Scott, additional, Pereira, Jennifer, additional, Karali, Christina Simoglou, additional, Cheng, Vinton, additional, Zarghami, Niloufar, additional, Soto, Manuel Sarmiento, additional, Couch, Yvonne, additional, Anthony, Daniel C., additional, Sibson, Nicola R., additional, Kealy, John, additional, Keep, Richard F., additional, Routhe, Lisa J., additional, Xiang, Jianming, additional, Ye, Hong, additional, Hua, Ya, additional, Moos, Torben, additional, Xi, Guohua, additional, Kristensen, M., additional, Bach, A., additional, Strømgaard, K., additional, Kutuzov, Nikolay, additional, Lopes-Pinheiro, Melissa A., additional, Lim, Jamie, additional, Kamermans, Alwin, additional, van Horssen, Jack, additional, Unger, Wendy W.J., additional, Fontijn, Ruud, additional, de Vries, Helga E., additional, Majerova, Petra, additional, Garruto, Ralph M., additional, Marchetti, Luca, additional, Francisco, David, additional, Gruber, Isabelle, additional, Lyck, Ruth, additional, Mészáros, Mária, additional, Porkoláb, Gergő, additional, Kiss, Lóránd, additional, Pilbat, Ana-Maria, additional, Török, Zsolt, additional, Bozsó, Zsolt, additional, Fülöp, Lívia, additional, Michalicova, Alena, additional, Galba, Jaroslav, additional, Mihaljevic, Sandra, additional, Novak, Michal, additional, Kovac, Andrej, additional, Morofuji, Yoichi, additional, Fujimoto, Takashi, additional, Watanabe, Daisuke, additional, Nakagawa, Shinsuke, additional, Ujifuku, Kenta, additional, Horie, Nobutaka, additional, Izumo, Tsuyoshi, additional, Anda, Takeo, additional, Matsuo, Takayuki, additional, Niu, Fang, additional, Buch, Shilpa, additional, Nyúl-Tóth, Ádám, additional, Kozma, Mihály, additional, Nagyőszi, Péter, additional, Nagy, Krisztina, additional, Fazakas, Csilla, additional, Haskó, János, additional, Molnár, Kinga, additional, Farkas, Attila E., additional, Galajda, Péter, additional, Wilhelm, Imola, additional, Krizbai, István A., additional, Kelly, Eoin, additional, Wallace, Eugene, additional, Greene, Chris, additional, Hughes, Stephanie, additional, Doyle, Niamh, additional, Humphries, Marian M., additional, Grant, Gerald A., additional, Friedman, Alon, additional, Veksler, Ronel, additional, Molloy, Michael G., additional, Meaney, James F., additional, Pender, Niall, additional, Doherty, Colin P., additional, Park, Minseon, additional, Liskiewicz, Arkadiusz, additional, Przybyla, Marta, additional, Kasprowska-Liśkiewicz, Daniela, additional, Nowacka-Chmielewska, Marta, additional, Malecki, Andrzej, additional, Pombero, Ana, additional, Garcia-Lopez, Raquel, additional, Martinez-Morga, Marta, additional, Martinez, Salvador, additional, Prager, Ofer, additional, Solomon-Kamintsky, Lyna, additional, Schoknecht, Karl, additional, Bar-Klein, Guy, additional, Milikovsky, Dan, additional, Vazana, Udi, additional, Rosenbach, Dror, additional, Kovács, Richard, additional, Radak, Zsolt, additional, Rodríguez-Lorenzo, Sabela, additional, Bruggmann, Remy, additional, Kooij, Gijs, additional, de Vries, Helga E, additional, Oxana, Semyachkina-Glushkovskaya, additional, Denis, Bragin, additional, Elena, Vodovozova, additional, Anna, Alekseeva, additional, Alla, Salmina, additional, Vladimir, Salmin, additional, Andrey, Morgun, additional, Nataliya, Malinovskaya, additional, Elena, Khilazheva, additional, Elizaveta, Boytsova, additional, Alexander, Shirokov, additional, Nikita, Navolokin, additional, Alla, Bucharskaya, additional, Yirong, Yang, additional, Arkady, Abdurashitov, additional, Artem, Gekalyuk, additional, Mariya, Ulanova, additional, Anastasia, Shushunova, additional, Madina, Bodrova, additional, Artem, Sagatova, additional, Alexander, Khorovodov, additional, Esmat, Shareef Ali, additional, Valery, Pavlov, additional, Artem, Tuchin, additional, Jürgen, Kurths, additional, de Abreu, Marcelle Silva, additional, Calpena, Ana C., additional, Espina, Marta, additional, García, Maria Luisa, additional, Romero, Ignacio A., additional, Male, David, additional, Storck, Steffen, additional, Hartz, Anika, additional, Pahnke, Jens, additional, Surma, Claus U., additional, Surma, M., additional, Giżejewski, Z., additional, Zieliński, H., additional, Szczepkowska, Aleksandra, additional, Kowalewska, Marta, additional, Krawczynska, Agata, additional, Herman, Andrzej P., additional, Skipor, Janina, additional, Kachappilly, Nicole, additional, Veenstra, Mike, additional, Rivera, Rosiris Leon, additional, Williams, Dionna W., additional, Morgello, Susan, additional, Berman, Joan W., additional, Wyneken, Ursula, additional, Batiz, Luis Federico, additional, Temizyürek, Arzu, additional, Khodadust, Rouhollah, additional, Küçük, Mutlu, additional, Gürses, Candan, additional, Emik, Serkan, additional, Zielińska, Magdalena, additional, Obara-Michlewska, Marta, additional, Milewski, Krzysztof, additional, Skonieczna, Edyta, additional, Fręśko, Inez, additional, Neuwelt, Edward A., additional, Maria, Ana Raquel Santa, additional, Bras, Ana Rita, additional, Lipka, Dóra, additional, Valkai, Sándor, additional, Kincses, András, additional, Dér, András, additional, and Deli, Maria A., additional

Published
2017
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17. Identification and molecular characterisation of a homozygous missense mutation in the ADAMTS10 gene in a patient with Weill-Marchesani syndrome

Author

Steinkellner, Hannes; https://orcid.org/0000-0002-4438-6043, Etzler, Julia, Gogoll, Laura; https://orcid.org/0000-0002-0516-9409, Neesen, Jürgen, Stifter, Eva, Brandau, Oliver, Laccone, Franco, Steinkellner, Hannes; https://orcid.org/0000-0002-4438-6043, Etzler, Julia, Gogoll, Laura; https://orcid.org/0000-0002-0516-9409, Neesen, Jürgen, Stifter, Eva, Brandau, Oliver, and Laccone, Franco

Abstract

Weill-Marchesani syndrome is a rare disorder of the connective tissue. Functional variants in ADAMTS10 are associated with Weill-Marchesani syndrome-1. We identified a homozygous missense mutation, c.41T>A, of the ADAMTS10 gene in a 19-year-old female with typical symptoms of WMS1: proportionate short stature, brachydactyly, joint stiffness, and microspherophakia. The ADAMTS10 missense mutation was analysed in silico, with conflicting results as to its effects on protein function, but it was predicted to affect the leader sequence. Molecular characterisation in HEK293 Ebna cells revealed an intracellular mis-targeting of the ADAMTS10 protein with a reduced concentration of the polypeptide in the endoplasmic reticulum. A large reduction in glycosylation of the cytoplasmic fraction of the mutant ADAMTS10 protein versus the wild-type protein and a lack of secretion of the mutant protein are also evident in our results.In conclusion, we identified a novel missense mutation of the ADAMTS10 gene and confirmed the functional consequences suggested by the in silico analysis by conducting molecular studies.

Published
2015

21. Review: Friedreich Ataxia and Erythropoietin

Author

Boesch, Sylvia, primary, Sturm, Brigitte, additional, Nachbauer, Wolfgang, additional, Hering, Sascha, additional, Steinkellner, Hannes, additional, Schneider, Rainer, additional, Poewe, Werner, additional, and Scheiber-Mojdehkar, Barbara, additional

Published
2010
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23. Identification and molecular characterisation of a homozygous missense mutation in the ADAMTS10 gene in a patient with Weill-Marchesani syndrome.

Author

Steinkellner, Hannes, Etzler, Julia, Gogoll, Laura, Neesen, Jürgen, Stifter, Eva, Brandau, Oliver, and Laccone, Franco

Subjects
*WEILL-Marchesani syndrome, *CONNECTIVE tissue diseases, *GENETIC testing, *MISSENSE mutation, *POLYPEPTIDES, *GLYCOSYLATION
Abstract

Weill-Marchesani syndrome is a rare disorder of the connective tissue. Functional variants in ADAMTS10 are associated with Weill-Marchesani syndrome-1. We identified a homozygous missense mutation, c.41T>A, of the ADAMTS10 gene in a 19-year-old female with typical symptoms of WMS1: proportionate short stature, brachydactyly, joint stiffness, and microspherophakia. The ADAMTS10 missense mutation was analysed in silico, with conflicting results as to its effects on protein function, but it was predicted to affect the leader sequence. Molecular characterisation in HEK293 Ebna cells revealed an intracellular mis-targeting of the ADAMTS10 protein with a reduced concentration of the polypeptide in the endoplasmic reticulum. A large reduction in glycosylation of the cytoplasmic fraction of the mutant ADAMTS10 protein versus the wild-type protein and a lack of secretion of the mutant protein are also evident in our results.In conclusion, we identified a novel missense mutation of the ADAMTS10 gene and confirmed the functional consequences suggested by the in silico analysis by conducting molecular studies. [ABSTRACT FROM AUTHOR]

Published
2015
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26. MeCP2 is a naturally supercharged protein with cell membrane transduction capabilities.

Author

Beribisky AV, Huber A, Sarne V, Spittler A, Sukhbaatar N, Seipel T, Laccone F, and Steinkellner H

Subjects
Humans, HEK293 Cells, Protein Transport, Cell-Penetrating Peptides metabolism, Cell-Penetrating Peptides chemistry, Cell-Penetrating Peptides genetics, Methyl-CpG-Binding Protein 2 metabolism, Methyl-CpG-Binding Protein 2 genetics, Methyl-CpG-Binding Protein 2 chemistry, Cell Membrane metabolism, Cell Membrane chemistry, Histone Deacetylases metabolism, Histone Deacetylases chemistry, Histone Deacetylases genetics
Abstract

The intrinsically disordered protein MeCP2 is a global transcriptional regulator encoded by the MECP2 gene. Although the structured domains of MeCP2 have been the subject of multiple studies, its unstructured regions have not been that extensively characterized. In this work, we show that MeCP2 possesses properties akin to those of supercharged proteins. By utilizing its unstructured portions, MeCP2 can successfully transduce across cell membranes and localize to heterochromatic foci in the nuclei, displaying uptake levels a third lower than a MeCP2 construct fused to the cell-penetrating peptide TAT. MeCP2 uptake can further be enhanced by the addition of compounds that promote endosomal escape following cellular trafficking by means of macropinocytosis. Using a combination of in silico prediction algorithms and live-cell imaging experiments, we mapped the sequence in MeCP2 responsible for its cellular incorporation, which bears a striking resemblance to TAT itself. Transduced MeCP2 was shown to interact with HDAC3. These findings provide valuable insight into the properties of MeCP2 and may be beneficial for devising future protein-based treatment strategies., (© 2024 The Author(s). Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.)

Published
2024
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