CSF1R inhibitor JNJ-40346527 attenuates microglial proliferation and neurodegeneration in P301S mice

Autor: Mancuso, Renzo, Fryatt, Gemma, Cleal, Madeleine, Obst, Juliane, Pipi, Elena, Monzón-Sandoval, Jimena, Ribe, Elena, Winchester, Laura, Webber, Caleb, Nevado, Alejo, Jacobs, Tom, Austin, Nigel, Theunis, Clara, Grauwen, Karolien, Ruiz, Eva Daniela, Mudher, Amrit, Vicente-Rodriguez, Marta, Parker, Christine A., Simmons, Camilla, Cash, Diana, Richardson, Jill, Bullmore, Edward T., Bhatti, Junaid, Chamberlain, Samuel J., Correia, Marta M., Crofts, Anna L., Dickinson, Amber, Foster, Andrew C., Kitzbichler, Manfred G., Knight, Clare, Lynall, Mary-Ellen, Maurice, Christina, O'Donnell, Ciara, Pointon, Linda J., Hyslop, Peter St. George, Turner, Lorinda, Vertes, Petra, Widmer, Barry, Williams, Guy B., Morgan, B. Paul, Leckey, Claire A., Morgan, Angharad R., O'Hagan, Caroline, Touchard, Samuel, Cavanagh, Jonathan, Deith, Catherine, Farmer, Scott, McClean, John, McColl, Alison, McPherson, Andrew, Scouller, Paul, Sutherland, Murray, Boddeke, H. W. G. M. (Erik), Richardson, Jill C., Khan, Shahid, Murphy, Phil, Patel, Jai, Jones, Declan, de Boer, Peter, Kemp, John, Drevets, Wayne C., Nye, Jeffrey S., Wittenberg, Gayle, Isaac, John, Bhattacharya, Anindya, Carruthers, Nick, Kolb, Hartmuth, Pariante, Carmine M., Turkheimer, Federico, Barker, Gareth J., Byrom, Heidi, Cattaneo, Annamaria, Gee, Antony, Hastings, Caitlin, Mariani, Nicole, McLaughlin, Anna, Mondelli, Valeria, Nettis, Maria, Nikkheslat, Naghmeh, Randall, Karen, Sheridan, Hannah, Singh, Nisha, VAn Loo, Victoria, Wood, Tobias C, Worrell, Courtney, Zajkowska, Zuzanna, Plath, Niels, Egebjerg, Jan, Eriksson, Hans, Gastambide, Francois, Adams, Karen Husted, Jeggo, Ross, Thomsen, Christian, Pederson, Jan Torleif, Campbell, Brian, Möller, Thomas, Nelson, Bob, Zorn, Stevin, O'Connor, Jason, Attenburrow, Mary Jane, Baird, Alison, Benjamin, Jithen, Clare, Stuart, Cowen, Philip, Huang, I-Shu (Dante), Hurley, Samuel, Jones, Helen, Lovestone, Simon, Mada, Francisca, Nevado-Holgado, Alejo, Oladejo, Akintayo, Smith, Katy, Vyas, Anviti, Hughes, Zoe, Balice-Gordon, Rita, Duerr, James, Piro, Justin R, Sporn, Jonathan, Perry (PI), V Hugh, Gomez-Nicola, Diego, Reynolds, Richard, Harrison, Neil A., Cercignani, Mara, Clarke, Charlotte L, Hoskins, Elizabeth, Kohn, Charmaine, Murray, Rosemary, Wilcock, Lauren, Wlazly, Dominika, Mount, Howard, Jones, Declan N. C., Perry, V. Hugh

Neuroinflammation and microglial activation are significant processes in Alzheimer’s disease pathology. Recent genome-wide association studies have highlighted multiple immune-related genes in association with Alzheimer’s disease, and experimenta

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=core_ac_uk__::51ba1226d0cdf9b948ae30e9b823a15b
https://orca.cardiff.ac.uk/id/eprint/125159/7/awz241.pdf

Frequency of nuclear mutant huntingtin inclusion formation in neurons and glia is cell-type-specific

Autor: Jansen, Anne H. P., van Hal, Maurik, Op den Kelder, Ilse C., Meier, Romy T., de Ruiter, Anna-Aster, Schut, Menno H., Smith, Donna L., Grit, Corien, Brouwer, Nieske, Kamphuis, Willem, Boddeke, H. W. G. M., den Dunnen, Wilfred F. A., van Roon, Willeke M. C., Bates, Gillian P., Hol, Elly M., Reits, Eric A.

Publikováno v: GLIA, 65, 50-61. John Wiley and Sons Inc.
Glia, 65(1), 50-61. Wiley
Glia, 65(1), 50-61. John Wiley and Sons Inc.

Huntington's disease (HD) is an autosomal dominant inherited neurodegenerative disorder that is caused by a CAG expansion in the Huntingtin (HTT) gene, leading to HTT inclusion formation in the brain. The mutant huntingtin protein (mHTT) is ubiquitou

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::0387328b88b415234f036c81830e572c
https://pure.knaw.nl/portal/en/publications/80861db7-6e52-4c3d-b34c-c624dc737800

Chimeric OHSCs as culture system to study microglia phenotypes

Autor: van der Pijl, C. A., van Weering, H. R., Masuch, A., Biber, K. P. H., Eggen, B. J. L., Boddeke, H. W. G.

Publikováno v: Glia, 63, E106-E107. Wiley

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::92609689f311b231c8ecadd97ccd6c50
https://research.rug.nl/en/publications/bf840727-b7bb-4dfb-954b-2e40c2e77b0c

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The HSPB8-BAG3 chaperone complex is upregulated in astrocytes in the human brain affected by protein aggregation diseases

Autor: Seidel, K., Vinet, J., den Dunnen, W. F. A., Brunt, E. R., Meister, M., Boncoraglio, A., Zijlstra, M. P., Boddeke, H. W. G. M., Rueb, U., Kampinga, H. H., Carra, S.

Publikováno v: Neuropathology and Applied Neurobiology, 38(1), 39-53. WILEY-BLACKWELL

HSPB8 is a small heat shock protein that forms a complex with the co-chaperone BAG3. Overexpression of the HSPB8-BAG3 complex in cells stimulates autophagy and facilitates the clearance of mutated aggregation-prone proteins, whose accumulation is a h

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::1467d38c6024cfe2aebf547a75ff5a3e
https://pubmed.ncbi.nlm.nih.gov/21696420