Zobrazeno 1 - 10
of 34
pro vyhledávání: '"Jaime Vaquer"'
Autor:
Peter Kunach, Jaime Vaquer-Alicea, Matthew S. Smith, Jim Monistrol, Robert Hopewell, Luc Moquin, Joseph Therriault, Cecile Tissot, Nesrine Rahmouni, Gassan Massarweh, Jean-Paul Soucy, Marie-Christine Guiot, Brian K. Shoichet, Pedro Rosa-Neto, Marc I. Diamond, Sarah H. Shahmoradian
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-7 (2024)
Abstract Positron Emission Tomography (PET) ligands have advanced Alzheimer’s disease (AD) diagnosis and treatment. Using autoradiography and cryo-EM, we identify AD brain tissue with elevated tau burden, purify filaments, and determine the structu
Externí odkaz:
https://doaj.org/article/5efd6927183340d0a34822a15bd6da61
Autor:
Dailu Chen, Sofia Bali, Ruhar Singh, Aleksandra Wosztyl, Vishruth Mullapudi, Jaime Vaquer-Alicea, Parvathy Jayan, Shamiram Melhem, Harro Seelaar, John C. van Swieten, Marc I. Diamond, Lukasz A. Joachimiak
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-17 (2023)
The authors used multi-disciplinary approaches to understand the structural mechanism underlying spontaneous aggregation of tau encoding an S320F FTD-tau mutant. Understanding the mechanisms of tau aggregation will help identify novel methods to regu
Externí odkaz:
https://doaj.org/article/b84963259f3d4cf7b3feeba89b86ffa0
Autor:
Vishruth Mullapudi, Jaime Vaquer-Alicea, Vaibhav Bommareddy, Anthony R. Vega, Bryan D. Ryder, Charles L. White, Marc. I. Diamond, Lukasz A. Joachimiak
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-19 (2023)
The authors developed a computational approach to probe the stability of amyloid fibrils and discover networks of hotspot interactions. Understanding the mechanisms of amyloid folding will help identify novel methods to treat protein (mis)folding dis
Externí odkaz:
https://doaj.org/article/34f3c028b8a641bd82ea0612f902b308
Autor:
Jiang Zhu, Sara Pittman, Dhruva Dhavale, Rachel French, Jessica N. Patterson, Mohamed Salman Kaleelurrrahuman, Yuanzi Sun, Jaime Vaquer-Alicea, Gianna Maggiore, Christoph S. Clemen, William J. Buscher, Jan Bieschke, Paul Kotzbauer, Yuna Ayala, Marc I. Diamond, Albert A. Davis, Conrad Weihl
Publikováno v:
Molecular Neurodegeneration, Vol 17, Iss 1, Pp 1-25 (2022)
Abstract Background Neuronal uptake and subsequent spread of proteopathic seeds, such as αS (alpha-synuclein), Tau, and TDP-43, contribute to neurodegeneration. The cellular machinery participating in this process is poorly understood. One proteinop
Externí odkaz:
https://doaj.org/article/47c9b932aac447af8c16f13a657d0a0e
Autor:
Brian D. Hitt, Jaime Vaquer-Alicea, Victor A. Manon, Joshua D. Beaver, Omar M. Kashmer, Jan N. Garcia, Marc I. Diamond
Publikováno v:
Acta Neuropathologica Communications, Vol 9, Iss 1, Pp 1-10 (2021)
Abstract Tau protein forms self-replicating assemblies (seeds) that may underlie progression of pathology in Alzheimer’s disease (AD) and related tauopathies. Seeding in recombinant protein preparations and brain homogenates has been quantified wit
Externí odkaz:
https://doaj.org/article/26fecdf55fb444eaa83ce6638c777ea8
Autor:
Bryan D. Ryder, Irina Matlahov, Sofia Bali, Jaime Vaquer-Alicea, Patrick C. A. van der Wel, Lukasz A. Joachimiak
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
The Hsp70/Hsp40 system plays an important role in maintaining cellular proteostasis but so far it is not well understood how Hsp70 proteins are recruited to specific Hsp40 co-chaperones. Here, the authors combine biochemical and biophysical approache
Externí odkaz:
https://doaj.org/article/60d78f39be754f40b8a931a46a1f1dfb
Autor:
Nguyen, Binh An, Afrin, Shumaila, Yakubovska, Anna, Singh, Virender, Pedretti, Rose, Bassett, Parker, Pekala, Maja, Alicea, Jaime Vaquer, Kunach, Peter, Wang, Lanie, Lemoff, Andrew, Kluve-Beckerman, Barbara, Saelices, Lorena
Publikováno v:
In Structure 5 December 2024 32(12):2244-2250
Autor:
Victor A. Manon, Marc I. Diamond, Jaime Vaquer-Alicea, Omar M. Kashmer, Joshua D. Beaver, Jan N. Garcia, Brian D. Hitt
Publikováno v:
Acta Neuropathologica Communications, Vol 9, Iss 1, Pp 1-10 (2021)
Acta Neuropathologica Communications
Acta Neuropathologica Communications
Tau protein forms self-replicating assemblies (seeds) that may underlie progression of pathology in Alzheimer’s disease (AD) and related tauopathies. Seeding in recombinant protein preparations and brain homogenates has been quantified with “bios
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::048273ce8e715f9109e003911c381ef8
https://doaj.org/article/26fecdf55fb444eaa83ce6638c777ea8
https://doaj.org/article/26fecdf55fb444eaa83ce6638c777ea8
Publikováno v:
Acta Neuropathologica
Tauopathies consist of over 25 different neurodegenerative diseases that include argyrophilic grain disease (AGD), progressive supranuclear palsy (PSP), corticobasal degeneration (CBD), and Pick’s disease (PiD). Tauopathies are defined by brain acc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc94b5f8d3fe7ac31cee02e044d985b5
http://europepmc.org/articles/PMC8217038
http://europepmc.org/articles/PMC8217038
Autor:
Vishruth Mullapudi, Jaime Vaquer-Alicea, Vaibhav Bommareddy, Anthony R. Vega, Bryan D. Ryder, Charles L. White, Marc. I. Diamond, Lukasz A. Joachimiak
Cryogenic electron microscopy has revealed unprecedented molecular insight into the conformation of β-sheet-rich protein amyloids linked to neurodegenerative diseases. It remains unknown how a protein can adopt a diversity of folds and form multiple
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2845e038c1ac152928bec3ac55666536
https://doi.org/10.1101/2022.07.01.498342
https://doi.org/10.1101/2022.07.01.498342
