Ghent University Academic Bibliography

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Rational design of amyloid-like fibrillary structures for tailoring food protein techno-functionality and their potential health implications

Koen JA Jansens, Ine Rombouts, Charlotte Grootaert (UGent) , Kristof Brijs, John Van Camp (UGent) , Paul Van der Meeren (UGent) , Frederic Rousseau, Joost Schymkowitz and Jan A Delcour

(2019) COMPREHENSIVE REVIEWS IN FOOD SCIENCE AND FOOD SAFETY. 18(1). p.84-105
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- Journal Article
- A1
- open access
Loss of DPP6 in neurodegenerative dementia : a genetic player in the dysfunction of neuronal excitability

Rita Cacace, Bavo Heeman, Sara Van Mossevelde, Arne De Roeck, Julie Hoogmartens, Peter De Rijk, Helena Gossye, Kristof De Vos, Wouter De Coster, Mojca Strazisar, et al.

(2019) ACTA NEUROPATHOLOGICA . 137(6). p.901-918
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- Book Chapter
Selective knockdowns in maize by sequence-specific protein aggregation

Camilla Betti (UGent) , Joost Schymkowitz, Frederic Rousseau and Eugenia Russinova (UGent)

(2018) Maize : methods and protocols. In Methods in Molecular Biology 1676. p.109-127
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Alzheimer's-causing mutations shift Aβ length by destabilizing γ-secretase-Aβn interactions

Maria Szaruga, Bogdan Munteanu, Sam Lismont, Sarah Veugelen, Katrien Horre, Marc Mercken, Takaomi C Saido, Natalie S Ryan, Tatjana De Vos (UGent) , Savvas Savvides (UGent) , et al.

(2017) CELL. 170(3). p.443-456
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- Journal Article
- A1
- open access
Phase separation of C9orf72 dipeptide repeats perturbs stress granule dynamics

Steven Boeynaems, Elke Bogaert, Denes Kovacs, Albert Konijnenberg, Evy Timmerman (UGent) , Alex Volkov, Mainak Guharoy, Mathias De Decker, Tom Jaspers, Veronica H Ryan, et al.

(2017) MOLECULAR CELL. 65(6). p.1044-1055
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Protein aggregation as an antibiotic design strategy

Natalia G Bednarska, Johan van Eldere, Rodrigo Gallardo, Ashok Ganesan, Meine Ramakers, Isabel Vogel, Pieter Baatsen, An Staes (UGent) , Marc Goethals (UGent) , Per Hammarström, et al.

(2016) MOLECULAR MICROBIOLOGY. 99(5). p.849-865
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- Journal Article
- A1
- open access
Sequence-specific protein aggregation generates defined protein knockdowns in plants

Camilla Betti (UGent) , Isabelle Vanhoutte (UGent) , Silvie Coutuer (UGent) , Riet De Rycke (UGent) , Kiril Mishev (UGent) , Marnik Vuylsteke (UGent) , Stijn Aesaert (UGent) , Debbie Rombaut (UGent) , Rodrigo Gallardo, Frederik De Smet, et al.

(2016) PLANT PHYSIOLOGY. 171(2). p.773-787
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Restricted location of PSEN2/γ-secretase determines substrate specificity and generates an intracellular Aβ pool

Ragna Sannerud, Cary Esselens, Paulina Ejsmont, Rafael Mattera, Leila Rochin, Arun Kumar Tharkeshwar Raghunath (UGent) , Greet De Baets, Veerle De Wever, Roger Habets, Veerle Baert, et al.

(2016) CELL. 166(1). p.193-208
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De novo design of a biologically active amyloid

Rodrigo Gallardo, Meine Ramakers, Frederik De Smet (UGent) , Filip Claes, Ladan Khodaparast, Laleh Khodaparast, José R Couceiro, Tobias Langenberg, Maxime Siemons, Sofie Nyström, et al.

(2016) SCIENCE. 354(6313).
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Sequence-dependent internalization of aggregating peptides

José R Couceiro, Rodrigo Gallardo, Frederik De Smet, Greet De Baets, Pieter Baatsen, Wim Annaert, Kenny Roose (UGent) , Xavier Saelens (UGent) , Joost Schymkowitz and Frederic Rousseau

(2015) JOURNAL OF BIOLOGICAL CHEMISTRY. 290(1). p.242-258

Academic Bibliography

Rational design of amyloid-like fibrillary structures for tailoring food protein techno-functionality and their potential health implications

Loss of DPP6 in neurodegenerative dementia : a genetic player in the dysfunction of neuronal excitability

Selective knockdowns in maize by sequence-specific protein aggregation

Alzheimer's-causing mutations shift Aβ length by destabilizing γ-secretase-Aβn interactions

Phase separation of C9orf72 dipeptide repeats perturbs stress granule dynamics

Protein aggregation as an antibiotic design strategy

Sequence-specific protein aggregation generates defined protein knockdowns in plants

Restricted location of PSEN2/γ-secretase determines substrate specificity and generates an intracellular Aβ pool

De novo design of a biologically active amyloid

Sequence-dependent internalization of aggregating peptides

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