Publications
30 found
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Overwijn, Daan, Dörner, Kerstin, de Almeida, Caroline, Müller, Martin, Mironov, Aleksei, Ivanek, Robert, Skrinjar, Peter, Gut, Michelle Jennifer, Solheim, Isabel, Beuret, Nicole, Bock, Thomas, Zeug, Matthias, Smialek, Maciej, Brandkamp, Sina, Maier, Timm, Zavolan, Mihaela, Keller Valsecchi, Claudia Isabelle, & . (2026). PAIP1 couples mRNA export to cytoplasmic mRNP remodeling and poly(A) homeostasis [Posted-content]. In bioRxiv (Cold Spring Harbor Laboratory). Cold Spring Harbor Laboratory. https://doi.org/10.64898/2026.07.31.742013
Overwijn, Daan, Dörner, Kerstin, de Almeida, Caroline, Müller, Martin, Mironov, Aleksei, Ivanek, Robert, Skrinjar, Peter, Gut, Michelle Jennifer, Solheim, Isabel, Beuret, Nicole, Bock, Thomas, Zeug, Matthias, Smialek, Maciej, Brandkamp, Sina, Maier, Timm, Zavolan, Mihaela, Keller Valsecchi, Claudia Isabelle, & . (2026). PAIP1 couples mRNA export to cytoplasmic mRNP remodeling and poly(A) homeostasis [Posted-content]. In bioRxiv (Cold Spring Harbor Laboratory). Cold Spring Harbor Laboratory. https://doi.org/10.64898/2026.07.31.742013
Naduthodi, Mihris I.S., Barrett, James, Pritchard, Jessica, Van der Stappen, Philippe, Demulder, Manon, Garfagnini, Tommaso, Dowle, Adam, , Engel, Benjamin D., McCormick, Alistair, & Mackinder, Luke C.M. (2026). Molecular organization of the Chlorella sorokiniana pyrenoid. In BioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.64898/2026.07.17.739135
Naduthodi, Mihris I.S., Barrett, James, Pritchard, Jessica, Van der Stappen, Philippe, Demulder, Manon, Garfagnini, Tommaso, Dowle, Adam, , Engel, Benjamin D., McCormick, Alistair, & Mackinder, Luke C.M. (2026). Molecular organization of the Chlorella sorokiniana pyrenoid. In BioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.64898/2026.07.17.739135
Mookherjee, Debdatto, Rommel, Madeleine, Weidner, Ferdinand, Siketanc, Matej, , & Spang, Anne. (2026). Non-translated mRNA levels determine P-body properties [Posted-content]. In bioRxiv . Cold Spring Harbor Laboratory. https://doi.org/10.64898/2026.03.18.712576
Mookherjee, Debdatto, Rommel, Madeleine, Weidner, Ferdinand, Siketanc, Matej, , & Spang, Anne. (2026). Non-translated mRNA levels determine P-body properties [Posted-content]. In bioRxiv . Cold Spring Harbor Laboratory. https://doi.org/10.64898/2026.03.18.712576
Dörner, Kerstin, Gut, Michelle Jennifer, Overwijn, Daan, Cao, Fan, Siketanc, Matej, Heinrich, Stephanie, Beuret, Nicole, Meyer, Justin, Sharpe, Timothy, Lindorff-Larsen, Kresten, & . (2026). Fluorescent protein and peptide tags alter condensate formation and dynamics in vivo and in vitro. EMBO Reports, 27(1), 89–121. https://doi.org/10.1038/s44319-025-00626-y
Dörner, Kerstin, Gut, Michelle Jennifer, Overwijn, Daan, Cao, Fan, Siketanc, Matej, Heinrich, Stephanie, Beuret, Nicole, Meyer, Justin, Sharpe, Timothy, Lindorff-Larsen, Kresten, & . (2026). Fluorescent protein and peptide tags alter condensate formation and dynamics in vivo and in vitro. EMBO Reports, 27(1), 89–121. https://doi.org/10.1038/s44319-025-00626-y
Kuwayama, Naohiro, Powers, Emily Nicole, Siketanc, Matej, Sousa, Camila Ines, Reynaud, Kendra, Jovanovic, Marko, , Ingolia, Nicholas Thomas, & Brar, Gloria Ann. (2024). Analyses of translation factors Dbp1 and Ded1 reveal the cellular response to heat stress to be separable from stress granule formation. Cell Reports, 43(12). https://doi.org/10.1016/j.celrep.2024.115059
Kuwayama, Naohiro, Powers, Emily Nicole, Siketanc, Matej, Sousa, Camila Ines, Reynaud, Kendra, Jovanovic, Marko, , Ingolia, Nicholas Thomas, & Brar, Gloria Ann. (2024). Analyses of translation factors Dbp1 and Ded1 reveal the cellular response to heat stress to be separable from stress granule formation. Cell Reports, 43(12). https://doi.org/10.1016/j.celrep.2024.115059
Szentgyörgyi, Viktória, Lueck, Leon, Overwijn, Daan, Ritz, Danilo, Zoeller, Nadja, Schmidt, Alexander, , Anne Spang, Anne, & Bakhtiar, Shahrzad. (2024). Arf1-dependent LRBA recruitment to Rab4 endosomes is required for endolysosome homeostasis. Journal of Cell Biology, 223(11). https://doi.org/10.1083/jcb.202401167
Szentgyörgyi, Viktória, Lueck, Leon, Overwijn, Daan, Ritz, Danilo, Zoeller, Nadja, Schmidt, Alexander, , Anne Spang, Anne, & Bakhtiar, Shahrzad. (2024). Arf1-dependent LRBA recruitment to Rab4 endosomes is required for endolysosome homeostasis. Journal of Cell Biology, 223(11). https://doi.org/10.1083/jcb.202401167
Szentgyörgyi, Viktória, Lueck, Leon Maximilian, Overwijn, Daan, Zoeller, Nadia, , Spang, Anne, & Bakhtiar, Shahrzad. (2024). Endosomal LRBA regulates the endo-lysosomal pathway [Posted-content]. In bioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2024.02.07.579084
Szentgyörgyi, Viktória, Lueck, Leon Maximilian, Overwijn, Daan, Zoeller, Nadia, , Spang, Anne, & Bakhtiar, Shahrzad. (2024). Endosomal LRBA regulates the endo-lysosomal pathway [Posted-content]. In bioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2024.02.07.579084
Heinrich, Stephanie, , Marchand, Désirée, Derrer, Carina Patrizia, Zedan, Mostafa, Oswald, Alexandra, Malinovska, Liliana, Uliana, Federico, Khawaja, Sarah, Mancini, Roberta, Grunwald, David, & Weis, Karsten. (2024). Glucose stress causes mRNA retention in nuclear Nab2 condensates. Cell Reports, 43(1). https://doi.org/10.1016/j.celrep.2023.113593
Heinrich, Stephanie, , Marchand, Désirée, Derrer, Carina Patrizia, Zedan, Mostafa, Oswald, Alexandra, Malinovska, Liliana, Uliana, Federico, Khawaja, Sarah, Mancini, Roberta, Grunwald, David, & Weis, Karsten. (2024). Glucose stress causes mRNA retention in nuclear Nab2 condensates. Cell Reports, 43(1). https://doi.org/10.1016/j.celrep.2023.113593
Dörner, Kerstin, & . (2024). The Story of RNA Unfolded: The Molecular Function of DEAD- and DExH-Box ATPases and Their Complex Relationship with Membraneless Organelles. Annual Review of Biochemistry, 93(1), 79–108. https://doi.org/10.1146/annurev-biochem-052521-121259
Dörner, Kerstin, & . (2024). The Story of RNA Unfolded: The Molecular Function of DEAD- and DExH-Box ATPases and Their Complex Relationship with Membraneless Organelles. Annual Review of Biochemistry, 93(1), 79–108. https://doi.org/10.1146/annurev-biochem-052521-121259
Heinrich, Stephanie, & . (2022). Probing Liquid-Liquid Phase Separation of RNA-Binding Proteins In Vitro and In Vivo. In Scheiffele, Peter;Mauger, Oriane (Ed.), Alternative Splicing: Methods and Protocols (pp. 307–333). Springer. https://doi.org/10.1007/978-1-0716-2521-7_18
Heinrich, Stephanie, & . (2022). Probing Liquid-Liquid Phase Separation of RNA-Binding Proteins In Vitro and In Vivo. In Scheiffele, Peter;Mauger, Oriane (Ed.), Alternative Splicing: Methods and Protocols (pp. 307–333). Springer. https://doi.org/10.1007/978-1-0716-2521-7_18
Linsenmeier, Miriam, , Grigolato, Fulvio, Secchi, Eleonora, Weis, Karsten, & Arosio, Paolo. (2022). Dynamic arrest and aging of biomolecular condensates are modulated by low-complexity domains, RNA and biochemical activity. Nature Communications, 13(1), 3030. https://doi.org/10.1038/s41467-022-30521-2
Linsenmeier, Miriam, , Grigolato, Fulvio, Secchi, Eleonora, Weis, Karsten, & Arosio, Paolo. (2022). Dynamic arrest and aging of biomolecular condensates are modulated by low-complexity domains, RNA and biochemical activity. Nature Communications, 13(1), 3030. https://doi.org/10.1038/s41467-022-30521-2
Overwijn, Daan, & . (2022). DEAD-box ATPases as regulators of biomolecular condensates and membrane-less organelles. Trends in Biochemical Sciences, 48(3), 244–258. https://doi.org/10.1016/j.tibs.2022.10.001
Overwijn, Daan, & . (2022). DEAD-box ATPases as regulators of biomolecular condensates and membrane-less organelles. Trends in Biochemical Sciences, 48(3), 244–258. https://doi.org/10.1016/j.tibs.2022.10.001
Weis, Karsten, & . (2022). The Role of DEAD-Box ATPases in Gene Expression and the Regulation of RNA-Protein Condensates. Annual Review of Biochemistry, 91, 197–219. https://doi.org/10.1146/annurev-biochem-032620-105429
Weis, Karsten, & . (2022). The Role of DEAD-Box ATPases in Gene Expression and the Regulation of RNA-Protein Condensates. Annual Review of Biochemistry, 91, 197–219. https://doi.org/10.1146/annurev-biochem-032620-105429
Wollny, Damian, Vernot, Benjamin, Wang, Jie, , Safrastyan, Aram, Aron, Franziska, Micheel, Julia, He, Zhisong, Hyman, Anthony, Weis, Karsten, Camp, J. Gray, Tang, T.-Y Dora, & Treutlein, Barbara. (2022). Characterization of RNA content in individual phase-separated coacervate microdroplets. Nature Communications, 13(1), 2626. https://doi.org/10.1038/s41467-022-30158-1
Wollny, Damian, Vernot, Benjamin, Wang, Jie, , Safrastyan, Aram, Aron, Franziska, Micheel, Julia, He, Zhisong, Hyman, Anthony, Weis, Karsten, Camp, J. Gray, Tang, T.-Y Dora, & Treutlein, Barbara. (2022). Characterization of RNA content in individual phase-separated coacervate microdroplets. Nature Communications, 13(1), 2626. https://doi.org/10.1038/s41467-022-30158-1
Linsenmeier, Miriam, , Grigolato, Fulvio, Secchi, Eleonora, Weis, Karsten, & Arosio, Paolo. (2021). Dynamic arrest and aging of biomolecular condensates are regulated by low-complexity domains, RNA and biochemical activity. bioRxiv. https://doi.org/10.1101/2021.02.26.433003
Linsenmeier, Miriam, , Grigolato, Fulvio, Secchi, Eleonora, Weis, Karsten, & Arosio, Paolo. (2021). Dynamic arrest and aging of biomolecular condensates are regulated by low-complexity domains, RNA and biochemical activity. bioRxiv. https://doi.org/10.1101/2021.02.26.433003
Pérez-Schindler, Joaquín, Kohl, Bastian, Schneider-Heieck, Konstantin, Leuchtmann, Aurel B., Henríquez-Olguín, Carlos, Adak, Volkan, Maier, Geraldine, Delezie, Julien, Sakoparnig, Thomas, Vargas-Fernández, Elyzabeth, Karrer-Cardel, Bettina, Ritz, Danilo, Schmidt, Alexander, , Jensen, Thomas E., Hiller, Sebastian, & Handschin, Christoph. (2021). RNA-bound PGC-1α controls gene expression in liquid-like nuclear condensates. Proceedings of the National Academy of Sciences of the United States of America, 118(36), e2105951118. https://doi.org/10.1073/pnas.2105951118
Pérez-Schindler, Joaquín, Kohl, Bastian, Schneider-Heieck, Konstantin, Leuchtmann, Aurel B., Henríquez-Olguín, Carlos, Adak, Volkan, Maier, Geraldine, Delezie, Julien, Sakoparnig, Thomas, Vargas-Fernández, Elyzabeth, Karrer-Cardel, Bettina, Ritz, Danilo, Schmidt, Alexander, , Jensen, Thomas E., Hiller, Sebastian, & Handschin, Christoph. (2021). RNA-bound PGC-1α controls gene expression in liquid-like nuclear condensates. Proceedings of the National Academy of Sciences of the United States of America, 118(36), e2105951118. https://doi.org/10.1073/pnas.2105951118
Wollny, Damian, Vernot, Benjamin, Wang, Jie, , Hyman, Anthony, Weis, Karsten, Camp, J. Gray, Dora Tang, T. -Y., & Treutlein, Barbara. (2021). Characterization of RNA content in individual phase-separated coacervate microdroplets. bioRxiv. https://doi.org/10.1101/2021.03.08.434405
Wollny, Damian, Vernot, Benjamin, Wang, Jie, , Hyman, Anthony, Weis, Karsten, Camp, J. Gray, Dora Tang, T. -Y., & Treutlein, Barbara. (2021). Characterization of RNA content in individual phase-separated coacervate microdroplets. bioRxiv. https://doi.org/10.1101/2021.03.08.434405
, Heinrich, Stephanie, De Los Rios, Paolo, & Weis, Karsten. (2020). Membraneless organelles: phasing out of equilibrium. Emerging topics in life sciences, 4(3), 331–342. https://doi.org/10.1042/etls20190190
, Heinrich, Stephanie, De Los Rios, Paolo, & Weis, Karsten. (2020). Membraneless organelles: phasing out of equilibrium. Emerging topics in life sciences, 4(3), 331–342. https://doi.org/10.1042/etls20190190
, Sachdev, Ruchika, Heinrich, Stephanie, Wang, Juan, Vallotton, Pascal, Fontoura, Beatriz M. A., & Weis, Karsten. (2019). DEAD-box ATPases are global regulators of phase-separated organelles. Nature, 573(7772), 144–148. https://doi.org/10.1038/s41586-019-1502-y
, Sachdev, Ruchika, Heinrich, Stephanie, Wang, Juan, Vallotton, Pascal, Fontoura, Beatriz M. A., & Weis, Karsten. (2019). DEAD-box ATPases are global regulators of phase-separated organelles. Nature, 573(7772), 144–148. https://doi.org/10.1038/s41586-019-1502-y
Linsenmeier, Miriam, Kopp, Marie R. G., Grigolato, Fulvio, Emmanouilidis, Leonidas, Liu, Dany, Zürcher, Dominik, , Weis, Karsten, Capasso Palmiero, Umberto, & Arosio, Paolo. (2019). Corrigendum: Dynamics of Synthetic Membraneless Organelles in Microfluidic Droplets. Angewandte Chemie International Edition, 58(50), 17902. https://doi.org/10.1002/anie.201913379
Linsenmeier, Miriam, Kopp, Marie R. G., Grigolato, Fulvio, Emmanouilidis, Leonidas, Liu, Dany, Zürcher, Dominik, , Weis, Karsten, Capasso Palmiero, Umberto, & Arosio, Paolo. (2019). Corrigendum: Dynamics of Synthetic Membraneless Organelles in Microfluidic Droplets. Angewandte Chemie International Edition, 58(50), 17902. https://doi.org/10.1002/anie.201913379
Linsenmeier, Miriam, Kopp, Marie R. G., Grigolato, Fulvio, Emmanoulidis, Leonidas, Liu, Dany, Zürcher, Dominik, , Weis, Karsten, Capasso Palmiero, Umberto, & Arosio, Paolo. (2019). Dynamics of Synthetic Membraneless Organelles in Microfluidic Droplets. Angewandte Chemie International Edition, 58(41), 14489–14494. https://doi.org/10.1002/anie.201907278
Linsenmeier, Miriam, Kopp, Marie R. G., Grigolato, Fulvio, Emmanoulidis, Leonidas, Liu, Dany, Zürcher, Dominik, , Weis, Karsten, Capasso Palmiero, Umberto, & Arosio, Paolo. (2019). Dynamics of Synthetic Membraneless Organelles in Microfluidic Droplets. Angewandte Chemie International Edition, 58(41), 14489–14494. https://doi.org/10.1002/anie.201907278
Sachdev, Ruchika, , Linsenmeier, Miriam, Vallotton, Pascal, Mugler, Christopher F., Arosio, Paolo, & Weis, Karsten. (2019). Pat1 promotes processing body assembly by enhancing the phase separation of the DEAD-box ATPase Dhh1 and RNA. eLife, 8, e41415. https://doi.org/10.7554/elife.41415
Sachdev, Ruchika, , Linsenmeier, Miriam, Vallotton, Pascal, Mugler, Christopher F., Arosio, Paolo, & Weis, Karsten. (2019). Pat1 promotes processing body assembly by enhancing the phase separation of the DEAD-box ATPase Dhh1 and RNA. eLife, 8, e41415. https://doi.org/10.7554/elife.41415
Faltova, Lenka, Küffner, Andreas M., , Weis, Karsten, & Arosio, Paolo. (2018). Multifunctional Protein Materials and Microreactors using Low Complexity Domains as Molecular Adhesives. ACS nano, 12(10), 9991–9999. https://doi.org/10.1021/acsnano.8b04304
Faltova, Lenka, Küffner, Andreas M., , Weis, Karsten, & Arosio, Paolo. (2018). Multifunctional Protein Materials and Microreactors using Low Complexity Domains as Molecular Adhesives. ACS nano, 12(10), 9991–9999. https://doi.org/10.1021/acsnano.8b04304
Mugler, Christopher Frederick, , Heinrich, Stephanie, Sachdev, Ruchika, Vallotton, Pascal, Koek, Adriana Y., Chan, Leon Y., & Weis, Karsten. (2016). ATPase activity of the DEAD-box protein Dhh1 controls processing body formation. eLife, 5, e18746. https://doi.org/10.7554/elife.18746
Mugler, Christopher Frederick, , Heinrich, Stephanie, Sachdev, Ruchika, Vallotton, Pascal, Koek, Adriana Y., Chan, Leon Y., & Weis, Karsten. (2016). ATPase activity of the DEAD-box protein Dhh1 controls processing body formation. eLife, 5, e18746. https://doi.org/10.7554/elife.18746
, & Ladurner, Andreas G. (2013). Catch me if you can: how the histone chaperone FACT capitalizes on nucleosome breathing. Nucleus, 4(6), 443–449. https://doi.org/10.4161/nucl.27235
, & Ladurner, Andreas G. (2013). Catch me if you can: how the histone chaperone FACT capitalizes on nucleosome breathing. Nucleus, 4(6), 443–449. https://doi.org/10.4161/nucl.27235
, Stuwe, Tobias, Hassler, Markus, Halbach, Felix, Bowman, Andrew, Zhang, Elisa T., Nijmeijer, Bianca, Kotthoff, Christiane, Rybin, Vladimir, Amlacher, Stefan, Hurt, Ed, & Ladurner, Andreas G. (2013). Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature, 499(7456), 111–114. https://doi.org/10.1038/nature12242
, Stuwe, Tobias, Hassler, Markus, Halbach, Felix, Bowman, Andrew, Zhang, Elisa T., Nijmeijer, Bianca, Kotthoff, Christiane, Rybin, Vladimir, Amlacher, Stefan, Hurt, Ed, & Ladurner, Andreas G. (2013). Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature, 499(7456), 111–114. https://doi.org/10.1038/nature12242
, & Ladurner, Andreas G. (2011). The chaperone-histone partnership: for the greater good of histone traffic and chromatin plasticity. Current Opinion in Structural Biology, 21(6), 698–708. https://doi.org/10.1016/j.sbi.2011.10.003
, & Ladurner, Andreas G. (2011). The chaperone-histone partnership: for the greater good of histone traffic and chromatin plasticity. Current Opinion in Structural Biology, 21(6), 698–708. https://doi.org/10.1016/j.sbi.2011.10.003
Goetze, Hannah, Wittner, Manuel, Hamperl, Stephan, , Merz, Katharina, Stoeckl, Ulrike, & Griesenbeck, Joachim. (2010). Alternative chromatin structures of the 35S rRNA Genes in Saccharomyces cerevisiae provide a molecular basis for the selective recruitment of RNA polymerases I and II. Molecular and cellular biology, 30(8), 2028–2045. https://doi.org/10.1128/mcb.01512-09
Goetze, Hannah, Wittner, Manuel, Hamperl, Stephan, , Merz, Katharina, Stoeckl, Ulrike, & Griesenbeck, Joachim. (2010). Alternative chromatin structures of the 35S rRNA Genes in Saccharomyces cerevisiae provide a molecular basis for the selective recruitment of RNA polymerases I and II. Molecular and cellular biology, 30(8), 2028–2045. https://doi.org/10.1128/mcb.01512-09
, & Ladurner, Andreas. (2010). A mitotic beacon reveals its nucleosome anchor. Molecular cell, 39(6), 829–830. https://doi.org/10.1016/j.molcel.2010.09.001
, & Ladurner, Andreas. (2010). A mitotic beacon reveals its nucleosome anchor. Molecular cell, 39(6), 829–830. https://doi.org/10.1016/j.molcel.2010.09.001
Merz, Katharina, , Goetze, Hannah, Gmelch, Katharina, Stoeckl, Ulrike, & Griesenbeck, Joachim. (2008). Actively transcribed rRNA genes in S. cerevisiae are organized in a specialized chromatin associated with the high-mobility group protein Hmo1 and are largely devoid of histone molecules. Genes & development, 22(9), 1190–1204. https://doi.org/10.1101/gad.466908
Merz, Katharina, , Goetze, Hannah, Gmelch, Katharina, Stoeckl, Ulrike, & Griesenbeck, Joachim. (2008). Actively transcribed rRNA genes in S. cerevisiae are organized in a specialized chromatin associated with the high-mobility group protein Hmo1 and are largely devoid of histone molecules. Genes & development, 22(9), 1190–1204. https://doi.org/10.1101/gad.466908