Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Berdien Siregar"'
Autor:
Jeroen van Ameijde, Rosa Crespo, Roosmarijn Janson, Jarek Juraszek, Berdien Siregar, Hanneke Verveen, Imke Sprengers, Tariq Nahar, Jeroen J. Hoozemans, Stefan Steinbacher, Roland Willems, Lore Delbroek, Marianne Borgers, Koen Dockx, Kristof Van Kolen, Marc Mercken, Gabriel Pascual, Wouter Koudstaal, Adrian Apetri
Publikováno v:
Acta Neuropathologica Communications, Vol 6, Iss 1, Pp 1-14 (2018)
Abstract Aggregation of tau protein and spreading of tau aggregates are pivotal pathological processes in a range of neurological disorders. Accumulating evidence suggests that immunotherapy targeting tau may be a viable therapeutic strategy. We have
Externí odkaz:
https://doaj.org/article/953e8ff91c8e4f18bdde6ccba2569d9c
Autor:
Adrian Apetri, Rosa Crespo, Jarek Juraszek, Gabriel Pascual, Roosmarijn Janson, Xueyong Zhu, Heng Zhang, Elissa Keogh, Trevin Holland, Jay Wadia, Hanneke Verveen, Berdien Siregar, Michael Mrosek, Renske Taggenbrock, Jeroenvan Ameijde, Hanna Inganäs, Margot van Winsen, Martin H. Koldijk, David Zuijdgeest, Marianne Borgers, Koen Dockx, Esther J. M. Stoop, Wenli Yu, Els C. Brinkman-van der Linden, Kimberley Ummenthum, Kristof van Kolen, Marc Mercken, Stefan Steinbacher, Donata de Marco, Jeroen J. Hoozemans, Ian A. Wilson, Wouter Koudstaal, Jaap Goudsmit
Publikováno v:
Acta Neuropathologica Communications, Vol 6, Iss 1, Pp 1-17 (2018)
Abstract Misfolding and aggregation of tau protein are closely associated with the onset and progression of Alzheimer’s Disease (AD). By interrogating IgG+ memory B cells from asymptomatic donors with tau peptides, we have identified two somaticall
Externí odkaz:
https://doaj.org/article/c0395ac19eb24ba4951a4cf53142723b
Autor:
Marianne Borgers, Jeroen J.M. Hoozemans, Roosmarijn Janson, Jarek Juraszek, Lore Delbroek, Berdien Siregar, Marc Mercken, Imke Sprengers, Adrian Apetri, Jeroen van Ameijde, Roland Willems, Kristof Van Kolen, Wouter Koudstaal, Koen Dockx, Gabriel Pascual, Tariq Nahar, Hanneke Verveen, Stefan Steinbacher, Rosa Crespo
Publikováno v:
Acta Neuropathologica Communications, Vol 6, Iss 1, Pp 1-14 (2018)
Acta Neuropathologica Communinications, 6(1):59. BioMed Central
Acta Neuropathologica Communications
van Ameijde, J, Crespo, R, Janson, R, Juraszek, J, Siregar, B, Verveen, H, Sprengers, I, Nahar, T, Hoozemans, J J, Steinbacher, S, Willems, R, Delbroek, L, Borgers, M, Dockx, K, van Kolen, K, Mercken, M, Pascual, G, Koudstaal, W & Apetri, A 2018, ' Enhancement of therapeutic potential of a naturally occurring human antibody targeting a phosphorylated Ser 422 containing epitope on pathological tau ', Acta Neuropathologica Communinications, vol. 6, no. 1, 59 . https://doi.org/10.1186/s40478-018-0562-9, https://doi.org/10.1186/s40478-018-0562-9
Acta Neuropathologica Communinications, 6(1):59. BioMed Central
Acta Neuropathologica Communications
van Ameijde, J, Crespo, R, Janson, R, Juraszek, J, Siregar, B, Verveen, H, Sprengers, I, Nahar, T, Hoozemans, J J, Steinbacher, S, Willems, R, Delbroek, L, Borgers, M, Dockx, K, van Kolen, K, Mercken, M, Pascual, G, Koudstaal, W & Apetri, A 2018, ' Enhancement of therapeutic potential of a naturally occurring human antibody targeting a phosphorylated Ser 422 containing epitope on pathological tau ', Acta Neuropathologica Communinications, vol. 6, no. 1, 59 . https://doi.org/10.1186/s40478-018-0562-9, https://doi.org/10.1186/s40478-018-0562-9
Aggregation of tau protein and spreading of tau aggregates are pivotal pathological processes in a range of neurological disorders. Accumulating evidence suggests that immunotherapy targeting tau may be a viable therapeutic strategy. We have previous
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82ad08e9acdefdbe11f8ec2bf4a53f53
http://link.springer.com/article/10.1186/s40478-018-0562-9
http://link.springer.com/article/10.1186/s40478-018-0562-9
Autor:
Jeroen van Ameijde, Trevin Holland, Hanna Inganäs, Ian A. Wilson, Gabriel Pascual, Hanneke Verveen, Roosmarijn Janson, Donata de Marco, Jeroen J.M. Hoozemans, Esther J. M. Stoop, Stefan Steinbacher, Renske Taggenbrock, Berdien Siregar, Rosa Crespo, Jay Wadia, Wouter Koudstaal, Margot van Winsen, Koen Dockx, Adrian Constantin Apetri, Jaap Goudsmit, Wenli Yu, David Zuijdgeest, Marianne Borgers, Jarek Juraszek, Heng Zhang, Elissa Keogh, Kristof Van Kolen, Kimberley Ummenthum, Martin H. Koldijk, Marc Mercken, Xueyong Zhu, Els C. M. Brinkman-Van der Linden, Michael Mrosek
Publikováno v:
Acta Neuropathologica Communications, Vol 6, Iss 1, Pp 1-17 (2018)
Apetri, A, Crespo, R, Juraszek, J, Pascual, G, Janson, R, Zhu, X, Zhang, H, Keogh, E, Holland, T, Wadia, J, Verveen, H, Siregar, B, Mrosek, M, Taggenbrock, R, Ameijde, J, Inganäs, H, van Winsen, M, Koldijk, M H, Zuijdgeest, D, Borgers, M, Dockx, K, Stoop, E J M, Yu, W, Brinkman-van der Linden, E C, Ummenthum, K, van Kolen, K, Mercken, M, Steinbacher, S, de Marco, D, Hoozemans, J J, Wilson, I A, Koudstaal, W & Goudsmit, J 2018, ' A common antigenic motif recognized by naturally occurring human V H 5-51/V L 4-1 anti-tau antibodies with distinct functionalities ', Acta Neuropathologica Communinications, vol. 6, no. 1, 43, pp. 43 . https://doi.org/10.1186/s40478-018-0543-z, https://doi.org/10.1186/s40478-018-0543-z
Acta Neuropathologica Communinications, 6(1):43. BioMed Central
Apetri, A, Crespo, R, Juraszek, J, Pascual, G, Janson, R, Zhu, X, Zhang, H, Keogh, E, Holland, T, Wadia, J, Verveen, H, Siregar, B, Mrosek, M, Taggenbrock, R, Ameijde, J, Inganäs, H, van Winsen, M, Koldijk, M H, Zuijdgeest, D, Borgers, M, Dockx, K, Stoop, E J M, Yu, W, Brinkman-van der Linden, E C, Ummenthum, K, van Kolen, K, Mercken, M, Steinbacher, S, de Marco, D, Hoozemans, J J, Wilson, I A, Koudstaal, W & Goudsmit, J 2018, ' A common antigenic motif recognized by naturally occurring human V H 5-51/V L 4-1 anti-tau antibodies with distinct functionalities ', Acta Neuropathologica Communinications, vol. 6, no. 1, 43, pp. 43 . https://doi.org/10.1186/s40478-018-0543-z, https://doi.org/10.1186/s40478-018-0543-z
Acta Neuropathologica Communinications, 6(1):43. BioMed Central
Misfolding and aggregation of tau protein are closely associated with the onset and progression of Alzheimer's Disease (AD). By interrogating IgG + memory B cells from asymptomatic donors with tau peptides, we have identified two somatically mutated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c0cc3ef318c798400926689fc83aaa11
http://link.springer.com/article/10.1186/s40478-018-0543-z
http://link.springer.com/article/10.1186/s40478-018-0543-z
Autor:
Jeremy Macedo, Stuart T Perry, Elissa Keogh, Xinyi Li, Adrian Apetri, Trevin Holland, Frederique Bard, Jaap Goudsmit, Julie Kim, Jeroen J.M. Hoozemans, Berdien Siregar, Martha Costa, Wouter Koudstaal, Lauren Fletcher, Gabriel Pascual, Hanna Inganäs, Margot van Winsen
Publikováno v:
Li, X, Koudstaal, W, Fletcher, L, Costa, M, van Winsen, M, Siregar, B, Inganäs, H, Kim, J, Keogh, E, Macedo, J, Holland, T, Perry, S, Bard, F, Hoozemans, J J, Goudsmit, J, Apetri, A & Pascual, G 2019, ' Naturally occurring antibodies isolated from PD patients inhibit synuclein seeding in vitro and recognize Lewy pathology ', Acta Neuropathologica, vol. 137, no. 5, pp. 825-836 . https://doi.org/10.1007/s00401-019-01974-5
Acta Neuropathologica
Acta Neuropathologica, 137(5), 825-836. Springer Verlag
Acta neuropathologica, 137(5), 825-836. Springer Verlag
Acta Neuropathologica
Acta Neuropathologica, 137(5), 825-836. Springer Verlag
Acta neuropathologica, 137(5), 825-836. Springer Verlag
Deposition of α-synuclein into Lewy bodies and Lewy neurites is the hallmark of Parkinson’s disease (PD). It is hypothesized that α-synuclein pathology spreads by a “prion-like” mechanism (i.e., by seeded aggregation or templated misfolding).
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::568512c90629bc5d80646725059ad41b
https://research.vumc.nl/en/publications/29c62774-183b-4f2f-9648-e5d12035134f
https://research.vumc.nl/en/publications/29c62774-183b-4f2f-9648-e5d12035134f
Common antigenic motif recognized by human VH5-51/VL4-1 tau antibodies with distinct functionalities
Autor:
Margot van Winsen, Hanneke Verveen, Heng Zhang, Jarek Juraszek, Renske Taggenbrock, Els C. M. Brinkman-Van der Linden, Elissa Keogh, Gabriel Pascual, Stefan Steinbacher, Berdien Siregar, Jaap Goudsmit, Wenli Yu, Michael Mrosek, Adrian Constantin Apetri, Jeroen van Ameijde, Marianne Borgers, Martin H. Koldijk, Wouter Koudstaal, Jay Wadia, Trevin Holland, Kristof Van Kolen, Xueyong Zhu, Donata de Marco, Kimberley Ummenthum, Esther J. M. Stoop, Hanna Inganäs, Koen Dockx, Marc Mercken, Jeroen J.M. Hoozemans, Rosa Crespo, Roosmarijn Janson, Ian A. Wilson, David Zuijdgeest
Misfolding and aggregation of tau protein are closely associated with the onset and progression of Alzheimer’s Disease (AD). By interrogating IgG+ memory B cells from asymptomatic donors with tau peptides, we have identified two somatically mutated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75f55d99202634ace50c06b8d45d8562
Autor:
Apetri, Adrian, Crespo, Rosa, Juraszek, Jarek, Pascual, Gabriel, Janson, Roosmarijn, Xueyong Zhu, Zhang, Heng, Keogh, Elissa, Trevin Holland, Wadia, Jay, Verveen, Hanneke, Berdien Siregar, Mrosek, Michael, Taggenbrock, Renske, Jeroenvan Ameijde, Inganäs, Hanna, Winsen, Margot Van, Koldijk, Martin, Zuijdgeest, David, Borgers, Marianne, Dockx, Koen, Stoop, Esther, Wenli Yu, Linden, Els Brinkman-Van Der, Ummenthum, Kimberley, Kolen, Kristof Van, Mercken, Marc, Steinbacher, Stefan, Marco, Donata De, Hoozemans, Jeroen, Wilson, Ian, Koudstaal, Wouter, Goudsmit, Jaap
Figure S1. Peptide epitope mapping. Figure S2. Reactivity of CBTAU-27.1 and CBTAU-28.1 to PHF-tau. Figure S3. Affinity of CBTAU-27.1, CBTAU-28.1 and their affinity-matured mutants for their cognate tau peptides. Figure S4. Affinity-improved antibodie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3732c1200463249b4c6dad61e68049e9
Autor:
Jeroen J.M. Hoozemans, Jaap Goudsmit, Hanna Inganäs, Başak Kükrer, Kiana West, Imke Sprengers, Xinyi Li, Michelle Wagner, Heng Zhang, Carrie Arnold, Lucy Chammas, Elissa Keogh, Frederique Bard, Wouter Koudstaal, Veronica Moreno, Julie Kim, Tariq Nahar, Gabriel Pascual, Gerrard Perdok, Laura A. N. Peferoen, Jeroen van Ameijde, Xueyong Zhu, Els C Brinkman van der Linden, Trevin Holland, Jehangir Wadia, Nancy Luckashenak, Zara Fulton, Martha Costa, Martin Koldijk, Berdien Siregar, Lauren Fletcher, R. Anthony Williamson, Adrian Apetri, Wenli Yu, Ian A. Wilson, Otto Diefenbach
Publikováno v:
Pascual, G, Wadia, J S, Zhu, X, Keogh, E, Kükrer, B, van Ameijde, J, Inganäs, H, Siregar, B, Perdok, G, Diefenbach, O, Nahar, T, Sprengers, I, Koldijk, M H, der Linden, E C B V, Peferoen, L A, Zhang, H, Yu, W, Li, X, Wagner, M, Moreno, V, Kim, J, Costa, M, West, K, Fulton, Z, Chammas, L, Luckashenak, N, Fletcher, L, Holland, T, Arnold, C, Anthony Williamson, R, Hoozemans, J J, Apetri, A, Bard, F, Wilson, I A, Koudstaal, W & Goudsmit, J 2017, ' Immunological memory to hyperphosphorylated tau in asymptomatic individuals ', Acta Neuropathologica, vol. 133, no. 5, pp. 767-783 . https://doi.org/10.1007/s00401-017-1705-y
Acta Neuropathologica
Acta neuropathologica, 133(5), 767-783. Springer Verlag
Acta Neuropathologica, 133(5), 767-783. Springer Verlag
Acta Neuropathologica
Acta neuropathologica, 133(5), 767-783. Springer Verlag
Acta Neuropathologica, 133(5), 767-783. Springer Verlag
Several reports have described the presence of antibodies against Alzheimer’s disease-associated hyperphosphorylated forms of tau in serum of healthy individuals. To characterize the specificities that can be found, we interrogated peripheral IgG+
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad0dd5aca2d919eb046a2d3d9e6c9b9b
https://research.vumc.nl/en/publications/c1c61a6a-74cf-4ea9-b3c5-e6a59cbe6284
https://research.vumc.nl/en/publications/c1c61a6a-74cf-4ea9-b3c5-e6a59cbe6284
Autor:
Hanna Inganäs, Heng Zhang, Jeroen J.M. Hoozemans, Berdien Siregar, Elissa Keogh, Esther J. M. Stoop, Ian A. Wilson, Wouter Koudstaal, Xueyong Zhu, Gabriel Pascual, Jaap Goudsmit, Jehangir Wadia, Adrian Apetri
Publikováno v:
Structure, 26(12), 1626-1634.e4. Cell Press
Zhang, H, Zhu, X, Pascual, G, Wadia, J S, Keogh, E, Hoozemans, J J, Siregar, B, Inganäs, H, Stoop, E J M, Goudsmit, J, Apetri, A, Koudstaal, W & Wilson, I A 2018, ' Structural Basis for Recognition of a Unique Epitope by a Human Anti-tau Antibody ', Structure, vol. 26, no. 12, pp. 1626-1634.e4 . https://doi.org/10.1016/j.str.2018.08.012
Structure (London, England, 26(12), 1626-1634.e4. Cell Press
Zhang, H, Zhu, X, Pascual, G, Wadia, J S, Keogh, E, Hoozemans, J J, Siregar, B, Inganäs, H, Stoop, E J M, Goudsmit, J, Apetri, A, Koudstaal, W & Wilson, I A 2018, ' Structural Basis for Recognition of a Unique Epitope by a Human Anti-tau Antibody ', Structure, vol. 26, no. 12, pp. 1626-1634.e4 . https://doi.org/10.1016/j.str.2018.08.012
Structure (London, England, 26(12), 1626-1634.e4. Cell Press
Aggregation of the hyperphosphorylated protein tau into neurofibrillary tangles and neuropil threads is a hallmark of Alzheimer disease (AD). Identification and characterization of the epitopes recognized by anti-tau antibodies might shed light on th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2f4c1b4a75bc6ff8b28c6288aca8a5e
https://doi.org/10.1016/j.str.2018.08.012
https://doi.org/10.1016/j.str.2018.08.012
Autor:
Philip G. de Groot, Rolf T. Urbanus, Martijn F.B.G. Gebbink, Berdien Siregar, Miranda E.A.T. van Berkel, Coen Maas, Bas de Laat
Publikováno v:
Arthritis & Rheumatism, 63(12), 3960-3968. Wiley
Objective The presence of autoantibodies against a cryptic epitope in domain I of beta 2-glycoprotein I (beta 2GPI) is strongly associated with thrombotic events in patients with the antiphospholipid syndrome. We hypothesized that a conformational ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd15ceaa28af318f1571653b842667fd
https://pubmed.ncbi.nlm.nih.gov/21898342
https://pubmed.ncbi.nlm.nih.gov/21898342