Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Greet, De Baets"'
Autor:
Evelyne Naus, Marleen Derweduwe, Youlia Lampi, Annelies Claeys, Jarne Pauwels, Tobias Langenberg, Filip Claes, Jie Xu, Veerle Haemels, Zeynep Kalender Atak, Rob van der Kant, Joost Van Durme, Greet De Baets, Keith L. Ligon, Mark Fiers, Kris Gevaert, Stein Aerts, Frederic Rousseau, Joost Schymkowitz, Frederik De Smet
Publikováno v:
Cells, Vol 12, Iss 6, p 960 (2023)
In malignant cancer, excessive amounts of mutant p53 often lead to its aggregation, a feature that was recently identified as druggable. Here, we describe that induction of a heat shock-related stress response mediated by Foldlin, a small-molecule to
Externí odkaz:
https://doaj.org/article/37999acd49cb4597b94c46b713bf272c
High‐throughput discovery of functional disordered regions: investigation of transactivation domains
Autor:
Charles NJ Ravarani, Tamara Y Erkina, Greet De Baets, Daniel C Dudman, Alexandre M Erkine, M Madan Babu
Publikováno v:
Molecular Systems Biology, Vol 14, Iss 5, Pp 1-14 (2018)
Abstract Over 40% of proteins in any eukaryotic genome encode intrinsically disordered regions (IDRs) that do not adopt defined tertiary structures. Certain IDRs perform critical functions, but discovering them is non‐trivial as the biological cont
Externí odkaz:
https://doaj.org/article/497103fb35b649449bde3680dc6289f5
Autor:
Ashok Ganesan, Aleksandra Siekierska, Jacinte Beerten, Marijke Brams, Joost Van Durme, Greet De Baets, Rob Van der Kant, Rodrigo Gallardo, Meine Ramakers, Tobias Langenberg, Hannah Wilkinson, Frederik De Smet, Chris Ulens, Frederic Rousseau, Joost Schymkowitz
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-15 (2016)
Mutations in aggregation prone regions of recombinant proteins often improve their solubility, although they might cause negative effects on their structure and function. Here, the authors identify proteins hot spots that can be exploited to optimize
Externí odkaz:
https://doaj.org/article/83b3c708399847f480f311a4edf53932
Publikováno v:
RecSys
Drug discovery is notorious for its low success rates [5]. Despite best research efforts, the majority of drugs fail at early stages of development, even before they enter clinical trials. This phenomenon stems from the inherent complexity of biologi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d11b9b4ce6488fb68583c26a00f8af36
https://doi.org/10.1145/3460231.3474598
https://doi.org/10.1145/3460231.3474598
Publikováno v:
PLoS Computational Biology, Vol 11, Iss 9, p e1004374 (2015)
Protein aggregation is a hallmark of over 30 human pathologies. In these diseases, the aggregation of one or a few specific proteins is often toxic, leading to cellular degeneration and/or organ disruption in addition to the loss-of-function resultin
Externí odkaz:
https://doaj.org/article/d978e5595e8a45f0a2f21798320c1adf
Autor:
Joost Schymkowitz, Emiel Michiels, Diether Lambrechts, Adriaan Vanderstichele, Filip Claes, Ignace Vergote, Aleksandra Siekierska, Siel Olbrecht, Mirian Saiz Rubio, Elisabeth Maritschnegg, Frédéric Amant, Meine Ramakers, Greet De Baets, Els Hermans, Frederic Rousseau, Jeroen Depreeuw, K. Peter R. Nilsson, Frederik De Smet, Annick Van den Broeck
Protein aggregation is an underappreciated mechanism that may contribute to the loss- and oncogenic-gain-of-function of mutant tumor suppressors such as p53 and axin. In the present study, we describe amyloid-like aggregation behaviour of the second
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e37b8f8d535bf76bd04b875c1ccc5edb
https://doi.org/10.1101/2020.11.30.402115
https://doi.org/10.1101/2020.11.30.402115
Autor:
Evelyne Naus, Greet De Baets, Rob van der Kant, Frederic Rousseau, Jarne Pauwels, Keith L. Ligon, Joost Schymkowitz, Zeynep Kalender Atak, Stein Aerts, Veerle Haemels, F. De Smet, Mark Fiers, Kris Gevaert, Jie Xu, Tobias Langenberg, Joost Van Durme, Filip Claes, Youlia Lampi
Publikováno v:
SSRN Electronic Journal.
In malignant cancer, excessive amounts of mutant p53 often lead to its aggregation, a feature that was recently identified as druggable. Here, we describe that the induction of a heat-shock response by Foldlin, a small-molecule tool compound, reduced
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::04b36fc34be4642c80877f29149018aa
https://doi.org/10.2139/ssrn.3720306
https://doi.org/10.2139/ssrn.3720306
Autor:
Greet De Baets, Joke Reumers, Javier Delgado Blanco, Joaquin Dopazo, Joost Schymkowitz, Frederic Rousseau
Publikováno v:
PLoS Computational Biology, Vol 7, Iss 6, p e1002090 (2011)
We previously showed the existence of selective pressure against protein aggregation by the enrichment of aggregation-opposing 'gatekeeper' residues at strategic places along the sequence of proteins. Here we analyzed the relationship between protein
Externí odkaz:
https://doaj.org/article/7f914652200e4405911b24ffec16df79
Autor:
Javier Delgado Blanco, Matty P. Weijenberg, Joost Schymkowitz, Mark S. Hipp, Shakti Ramkissoon, Frederik De Smet, Frédéric Amant, Piet A. van den Brandt, Tobias Langenberg, Keith L. Ligon, André D'Hoore, Filip Claes, Daphne Hompes, Evelyne Naus, Manon Van England, Lori A. Ramkissoon, Greet De Baets, Sandrina Lambrechts, Bert Houben, Xavier Sagaert, Mirian Saiz Rubio, Colinda C. J. M. Simons, Sarah Charbonneau, Stéphane Plaisance, Frederic Rousseau
Publikováno v:
The Journal of Pathology. 242:24-38
Although p53 protein aggregates have been observed in cancer cell lines and tumour tissue, their impact in cancer remains largely unknown. Here, we extensively screened for p53 aggregation phenotypes in tumour biopsies, and identified nuclear inclusi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::01a6071d28cee5d8b2c507a710ffc26d
https://doi.org/10.1002/path.4872
https://doi.org/10.1002/path.4872
Autor:
Wim Robberecht, Kristy C. Yuan, Greet De Baets, Maja Debulpaep, Janine Kirstein, Bert Houben, Barbara Moahamed, Angela S. Laird, Frederic Rousseau, Mikael Oliveberg, Stanislav Rudyak, Kerensa Broersen, Emiel Michiels, Nikolaos N. Louros, Serene S. L. Gwee, Filip Claes, Sara Hernandez, Meine Ramakers, Joost Van Durme, Jacinte Beerten, Rob van der Kant, Joost Schymkowitz
Publikováno v:
Protein engineering, design & selection : PEDS, 32(10), 443-457. Oxford University Press
The accumulation of toxic protein aggregates is thought to play a key role in a range of degenerative pathologies, but it remains unclear why aggregation of polypeptides into non-native assemblies is toxic and why cellular clearance pathways offer in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc5436fd137e8390bee55460977820cf
https://research.utwente.nl/en/publications/5d08f882-1c15-4b53-9004-7ca723b489d2
https://research.utwente.nl/en/publications/5d08f882-1c15-4b53-9004-7ca723b489d2