Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Marc F. Bolliger"'
Autor:
Matthieu Drouyer, Marc F. Bolliger, Evy Lobbestael, Chris Van den Haute, Marco Emanuele, Réginald Lefebvre, William Sibran, Tina De Wit, Coline Leghay, Eugénie Mutez, Nicolas Dzamko, Glenda M. Halliday, Shigeo Murayama, Alain Martoriati, Katia Cailliau, Jean-François Bodart, Marie-Christine Chartier-Harlin, Veerle Baekelandt, R. Jeremy Nichols, Jean-Marc Taymans
Publikováno v:
Neurobiology of Disease, Vol 157, Iss , Pp 105426- (2021)
LRRK2 is a highly phosphorylated multidomain protein and mutations in the gene encoding LRRK2 are a major genetic determinant of Parkinson's disease (PD). Dephosphorylation at LRRK2's S910/S935/S955/S973 phosphosite cluster is observed in several con
Externí odkaz:
https://doaj.org/article/1fd99d9a1cef4426b7f99882df3c1bd9
Autor:
Amanda M. Gysbers, Shigeo Murayama, Wilma D.J. van de Berg, Masaki Takao, Glenda M. Halliday, Akiko Uchino, Ye Zhao, Rina Bandopadhyay, Sandrine Wauters, Nicolas Dzamko, Marc F. Bolliger, Janice L. Holton, R. Jeremy Nichols, Junko Takahashi-Fujigasaki
Publikováno v:
Dzamko, N, Gysbers, A M, Bandopadhyay, R, Bolliger, M F, Uchino, A, Zhao, Y, Takao, M, Wauters, S, van de Berg, W D J, Takahashi-Fujigasaki, J, Nichols, R J, Holton, J L, Murayama, S & Halliday, G M 2017, ' LRRK2 levels and phosphorylation in Parkinson's disease brain and cases with restricted Lewy bodies ', Movement Disorders, vol. 32, no. 3, pp. 423-432 . https://doi.org/10.1002/mds.26892
Movement Disorders, 32(3), 423-432. John Wiley and Sons Inc.
Movement Disorders, 32(3), 423-432. John Wiley and Sons Inc.
Background: Leucine rich repeat kinase 2 (LRRK2) is a promising target for the treatment of Parkinson's disease; however, little is known about the expression of LRRK2 in human brain and if/how LRRK2 protein levels are altered in Parkinson's disease.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f416a8903f03aee488f521b64ef9cdf
https://research.vumc.nl/en/publications/01f33f01-5556-4736-a265-fe903678871c
https://research.vumc.nl/en/publications/01f33f01-5556-4736-a265-fe903678871c
Autor:
Marc F. Bolliger, Thomas C. Südhof, Jenna Nguyen, Antony A. Boucard, S. Michael Soltis, Axel T. Brunger, Demet Araç
Publikováno v:
The EMBO Journal. 31:1364-1378
The G protein-coupled receptor (GPCR) Proteolysis Site (GPS) of cell-adhesion GPCRs and polycystic kidney disease (PKD) proteins constitutes a highly conserved autoproteolysis sequence, but its catalytic mechanism remains unknown. Here, we show that
Autor:
Marc F. Bolliger, Mark R Etherton, Cory A. Blaiss, Christopher Walz, Thomas C. Südhof, Katsuhiko Tabuchi, Craig M. Powell, Jacqueline Blundell, Felipe Espinosa
Publikováno v:
The Journal of Neuroscience. 30:2115-2129
Neuroligins (NLs) are a family of neural cell-adhesion molecules that are involved in excitatory/inhibitory synapse specification. Multiple members of the NL family (including NL1) and their binding partners have been linked to cases of human autism
Autor:
Alice S. Carter, Geping Zhao, Jeff M. Milunsky, Thomas C. Südhof, Craig M. Powell, Jaewon Ko, Marc F. Bolliger, Tom A. Maher, Chen Zhang, Helen Tager-Flusberg, Stephanie Newton, Antony A. Boucard
Publikováno v:
The Journal of Neuroscience. 29:10843-10854
Neuroligins (NLs) are postsynaptic cell-adhesion molecules essential for normal synapse function. Mutations in neuroligin-4 (NL4) (gene symbol:NLGN4) have been reported in some patients with autism spectrum disorder (ASD) and other neurodevelopmental
Autor:
Sergio M. Gloor, Marco Wachtel, Regine Landmann, Hideyuki Ishihara, Marc F Bolliger, Karl Frei
Publikováno v:
Brain Research Reviews. 36:258-264
The blood-brain barrier (BBB) is formed by brain capillary endothelial cells. These cells have at least three properties which distinguish them from their peripheral counterparts: (1) tight junctions (TJs) of extremely low permeability; (2) low rates
C1q-like genes ( C1ql1–C1ql4 ) encode small, secreted proteins that are expressed in differential patterns in the brain but whose receptors and functions remain unknown. BAI3 protein, in contrast, is a member of the cell-adhesion class of G protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a2081fd0f5d28e2b3e77fe8f7b33d2f
https://europepmc.org/articles/PMC3038708/
https://europepmc.org/articles/PMC3038708/
Autor:
Thomas C. Südhof, Xinran Liu, Cory A. Blaiss, Marc F. Bolliger, Katsuhiko Tabuchi, Nils Brose, Craig M. Powell, Jacqueline Blundell
Publikováno v:
Genes, brain, and behavior. 8(1)
Neuroligins are postsynaptic cell-adhesion molecules that are thought to specify synapse properties. Previous studies showed that mutant mice carrying an autism-associated point mutation in neuroligin-3 (NL3) exhibit social interaction deficits, enha
Autor:
Antony A. Boucard, Marc F. Bolliger, Jimin Pei, Thomas C. Südhof, Stephan Maxeiner, Nick V. Grishin
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 105(17)
Neuroligins (NLs) are postsynaptic cell-adhesion molecules that are implicated in humans in autism spectrum disorders because the genes encoding NL3 and NL4 are mutated in rare cases of familial autism. NLs are highly conserved evolutionarily, except