Restricted Location of PSEN2/γ-Secretase Determines Substrate Specificity and Generates an Intracellular Aβ Pool von Sannerud, Ragna, Esselens, Cary, Ejsmont, Paulina, Mattera, Rafael, Rochin, Leila, Tharkeshwar, Arun Kumar, De Baets, Greet, De Wever, Veerle, Habets, Roger, Baert, Veerle, Vermeire, Wendy, Michiels, Christine, Groot, Arjan J., Wouters, Rosanne, Dillen, Katleen, Vints, Katlijn, Baatsen, Pieter, Munck, Sebastian, Derua, Rita, Waelkens, Etienne, Basi, Guriqbal S., Mercken, Mark, Vooijs, Marc, Bollen, Mathieu, Schymkowitz, Joost, Rousseau, Frederic, Bonifacino, Juan S., Van Niel, Guillaume, De Strooper, Bart, Annaert, Wim

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Aikido's self-regulation and co-regulation: a promising embodied pedagogy for intercultural communication training von De Baets, Greet Angèle, Van Praet, Ellen

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AmyPro: a database of proteins with validated amyloidogenic regions von Varadi, Mihaly, De Baets, Greet, Vranken, Wim F, Tompa, Peter, Pancsa, Rita

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Drosophila screen connects nuclear transport genes to DPR pathology in c9ALS/FTD von Boeynaems, Steven, Bogaert, Elke, Michiels, Emiel, Gijselinck, Ilse, Sieben, Anne, Jovičić, Ana, De Baets, Greet, Scheveneels, Wendy, Steyaert, Jolien, Cuijt, Ivy, Verstrepen, Kevin J., Callaerts, Patrick, Rousseau, Frederic, Schymkowitz, Joost, Cruts, Marc, Van Broeckhoven, Christine, Van Damme, Philip, Gitler, Aaron D., Robberecht, Wim, Van Den Bosch, Ludo

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High‐throughput discovery of functional disordered regions: investigation of transactivation domains von Ravarani, Charles NJ, Erkina, Tamara Y, De Baets, Greet, Dudman, Daniel C, Erkine, Alexandre M, Babu, M Madan

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Increased Aggregation Is More Frequently Associated to Human Disease-Associated Mutations Than to Neutral Polymorphisms von De Baets, Greet, Van Doorn, Loic, Rousseau, Frederic, Schymkowitz, Joost

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Solubis: a webserver to reduce protein aggregation through mutation von Van Durme, Joost, De Baets, Greet, Van Der Kant, Rob, Ramakers, Meine, Ganesan, Ashok, Wilkinson, Hannah, Gallardo, Rodrigo, Rousseau, Frederic, Schymkowitz, Joost

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Structural hot spots for the solubility of globular proteins von Ganesan, Ashok, Siekierska, Aleksandra, Beerten, Jacinte, Brams, Marijke, Van Durme, Joost, De Baets, Greet, Van der Kant, Rob, Gallardo, Rodrigo, Ramakers, Meine, Langenberg, Tobias, Wilkinson, Hannah, De Smet, Frederik, Ulens, Chris, Rousseau, Frederic, Schymkowitz, Joost

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An evolutionary trade-off between protein turnover rate and protein aggregation favors a higher aggregation propensity in fast degrading proteins von De Baets, Greet, Reumers, Joke, Delgado Blanco, Javier, Dopazo, Joaquin, Schymkowitz, Joost, Rousseau, Frederic

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Assessing computational predictions of the phenotypic effect of cystathionine‐beta‐synthase variants von Kasak, Laura, Bakolitsa, Constantina, Hu, Zhiqiang, Yu, Changhua, Rine, Jasper, Dimster‐Denk, Dago F., Pandey, Gaurav, Baets, Greet, Bromberg, Yana, Cao, Chen, Capriotti, Emidio, Casadio, Rita, Durme, Joost, Giollo, Manuel, Karchin, Rachel, Katsonis, Panagiotis, Leonardi, Emanuela, Lichtarge, Olivier, Martelli, Pier Luigi, Masica, David, Mooney, Sean D., Olatubosun, Ayodeji, Radivojac, Predrag, Rousseau, Frederic, Pal, Lipika R., Savojardo, Castrense, Schymkowitz, Joost, Thusberg, Janita, Tosatto, Silvio C.E., Vihinen, Mauno, Väliaho, Jouni, Repo, Susanna, Moult, John, Brenner, Steven E., Friedberg, Iddo

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Reduced Levels of Misfolded and Aggregated Mutant p53 by Proteostatic Activation von Naus, Evelyne, Derweduwe, Marleen, Lampi, Youlia, Claeys, Annelies, Pauwels, Jarne, Langenberg, Tobias, Claes, Filip, Xu, Jie, Haemels, Veerle, Atak, Zeynep Kalender, van der Kant, Rob, Van Durme, Joost, De Baets, Greet, Ligon, Keith L, Fiers, Mark, Gevaert, Kris, Aerts, Stein, Rousseau, Frederic, Schymkowitz, Joost, De Smet, Frederik

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Je Suis Pas Tatamisé: Five Spectrums of Variation in the Narratives of 20 Aikido Experts Worldwide in 2020 von De Baets, Greet

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Horizontal gene transfer from human host to HIV-1 reverse transcriptase confers drug resistance and partly compensates for replication deficits von Megens, Sarah, Vaira, Dolores, De Baets, Greet, Dekeersmaeker, Nathalie, Schrooten, Yoeri, Li, Guangdi, Schymkowitz, Joost, Rousseau, Frederic, Vandamme, Anne-Mieke, Moutschen, Michel, Van Laethem, Kristel

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SNPeffect 4.0: on-line prediction of molecular and structural effects of protein-coding variants von De Baets, Greet, Van Durme, Joost, Reumers, Joke, Maurer-Stroh, Sebastian, Vanhee, Peter, Dopazo, Joaquin, Schymkowitz, Joost, Rousseau, Frederic

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Loss of TBK1 is a frequent cause of frontotemporal dementia in a Belgian cohort von Gijselinck, Ilse, Van Mossevelde, Sara, van der Zee, Julie, Sieben, Anne, Philtjens, Stéphanie, Heeman, Bavo, Engelborghs, Sebastiaan, Vandenbulcke, Mathieu, De Baets, Greet, Bäumer, Veerle, Cuijt, Ivy, Van den Broeck, Marleen, Peeters, Karin, Mattheijssens, Maria, Rousseau, Frederic, Vandenberghe, Rik, De Jonghe, Peter, Cras, Patrick, De Deyn, Peter P, Martin, Jean-Jacques, Cruts, Marc, Van Broeckhoven, Christine

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A Genome-Wide Sequence–Structure Analysis Suggests Aggregation Gatekeepers Constitute an Evolutionary Constrained Functional Class von De Baets, Greet, Van Durme, Joost, Rousseau, Frederic, Schymkowitz, Joost

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Solubis: optimize your protein von De Baets, Greet, Van Durme, Joost, van der Kant, Rob, Schymkowitz, Joost, Rousseau, Frederic

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CAGI, the Critical Assessment of Genome Interpretation, establishes progress and prospects for computational genetic variant interpretation methods von Jain, Shantanu, Bakolitsa, Constantina, Brenner, Steven E., Radivojac, Predrag, Moult, John, Repo, Susanna, Hoskins, Roger A., Andreoletti, Gaia, Barsky, Daniel, Chellapan, Ajithavalli, Chu, Hoyin, Dabbiru, Navya, Kollipara, Naveen K., Ly, Melissa, Neumann, Andrew J., Pal, Lipika R., Odell, Eric, Pandey, Gaurav, Peters-Petrulewicz, Robin C., Srinivasan, Rajgopal, Yee, Stephen F., Yeleswarapu, Sri Jyothsna, Zuhl, Maya, Adebali, Ogun, Patra, Ayoti, Beer, Michael A., Hosur, Raghavendra, Peng, Jian, Bernard, Brady M., Berry, Michael, Dong, Shengcheng, Boyle, Alan P., Adhikari, Aashish, Chen, Jingqi, Hu, Zhiqiang, Wang, Robert, Wang, Yaqiong, Miller, Maximilian, Wang, Yanran, Bromberg, Yana, Turina, Paola, Capriotti, Emidio, Han, James J., Ozturk, Kivilcim, Carter, Hannah, Babbi, Giulia, Bovo, Samuele, Di Lena, Pietro, Martelli, Pier Luigi, Savojardo, Castrense, Casadio, Rita, Cline, Melissa S., De Baets, Greet, Bonache, Sandra, Díez, Orland, Gutiérrez-Enríquez, Sara, Fernández, Alejandro, Montalban, Gemma, Ootes, Lars, Özkan, Selen, Padilla, Natàlia, Riera, Casandra, De la Cruz, Xavier, Diekhans, Mark, Huwe, Peter J., Wei, Qiong, Xu, Qifang, Dunbrack, Roland L., Gotea, Valer, Elnitski, Laura, Margolin, Gennady, Fariselli, Piero, Kulakovskiy, Ivan V., Makeev, Vsevolod J., Penzar, Dmitry D., Vorontsov, Ilya E., Favorov, Alexander V., Forman, Julia R., Hasenahuer, Marcia, Fornasari, Maria S., Parisi, Gustavo, Avsec, Ziga, Çelik, Muhammed H., Nguyen, Thi Yen Duong, Gagneur, Julien, Shi, Fang-Yuan, Edwards, Matthew D., Guo, Yuchun, Tian, Kevin, Zeng, Haoyang, Gifford, David K., Göke, Jonathan, Zaucha, Jan, Gough, Julian, Ritchie, Graham R. S., Frankish, Adam, Mudge, Jonathan M., Harrow, Jennifer, Young, Erin L., Yu, Yao

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A comparative analysis of the aggregation behavior of amyloid-β peptide variants von Vandersteen, Annelies, Hubin, Ellen, Sarroukh, Rabia, De Baets, Greet, Schymkowitz, Joost, Rousseau, Frederic, Subramaniam, Vinod, Raussens, Vincent, Wenschuh, Holger, Wildemann, Dirk, Broersen, Kerensa

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Nuclear inclusion bodies of mutant and wild‐type p53 in cancer: a hallmark of p53 inactivation and proteostasis remodelling by p53 aggregation von De Smet, Frederik, Saiz Rubio, Mirian, Hompes, Daphne, Naus, Evelyne, De Baets, Greet, Langenberg, Tobias, Hipp, Mark S, Houben, Bert, Claes, Filip, Charbonneau, Sarah, Delgado Blanco, Javier, Plaisance, Stephane, Ramkissoon, Shakti, Ramkissoon, Lori, Simons, Colinda, van den Brandt, Piet, Weijenberg, Matty, Van England, Manon, Lambrechts, Sandrina, Amant, Frederic, D'Hoore, André, Ligon, Keith L, Sagaert, Xavier, Schymkowitz, Joost, Rousseau, Frederic

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