Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Omar M. Kashmer"'
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:
Dailu Chen, Kenneth W. Drombosky, Zhiqiang Hou, Levent Sari, Omar M. Kashmer, Bryan D. Ryder, Valerie A. Perez, DaNae R. Woodard, Milo M. Lin, Marc I. Diamond, Lukasz A. Joachimiak
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
The biophysical mechanisms of how disease-associated tau mutations drive amyloid formation are not well understood. Here the authors use biophysical approaches, cell models and MD simulations and find that the intrinsically disordered repeat domain o
Externí odkaz:
https://doaj.org/article/03b30e34ee8f4915b39c71a3c1b8c803
Publikováno v:
eLife, Vol 7 (2018)
Tauopathies have diverse presentation, progression, and neuropathology. They are linked to tau prion strains, self-replicating assemblies of unique quaternary conformation, whose origin is unknown. Strains can be propagated indefinitely in cultured c
Externí odkaz:
https://doaj.org/article/60876edfb743457c9a9a73b08f5b5bb0
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
Autor:
Amy N. Zwierzchowski-Zarate, Omar M. Kashmer, Josue E. Collazo-Lopez, Charles L. White, Marc I. Diamond
Tau aggregation causes neurodegenerative tauopathies, and trans-cellular propagation of tau assemblies of unique structure, i.e. strains, may underlie the diversity of these disorders. Polyanions have been reported to induce tau aggregation in vitro,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b7c5ceef562fbb75d97208f17c13378e
https://doi.org/10.1101/2022.01.29.478315
https://doi.org/10.1101/2022.01.29.478315
Autor:
Sourav Kolay, Anthony R. Vega, Dana A. Dodd, Valerie A. Perez, Omar M. Kashmer, Charles L. White, Marc I. Diamond
Tau assembly propagation from the extracellular to intracellular space of a cell may underlie neurodegenerative tauopathies. The first step involves tau binding to heparan sulfate proteoglycans on the cell surface, followed by macropinocytosis. Patho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0d197a6492d22879ad1494c98554b004
https://doi.org/10.1101/2022.01.03.474802
https://doi.org/10.1101/2022.01.03.474802
Autor:
Sourav Kolay, Anthony R. Vega, Dana A. Dodd, Valerie A. Perez, Omar M. Kashmer, Charles L. White, Marc I. Diamond
Publikováno v:
The Journal of biological chemistry. 298(6)
Tau assembly movement from the extracellular to intracellular space may underlie transcellular propagation of neurodegenerative tauopathies. This begins with tau binding to cell surface heparan sulfate proteoglycans, which triggers macropinocytosis.
Autor:
Pawel M. Wydorski, Hilda Mirbaha, Omar M. Kashmer, Bryan D. Ryder, Lukasz A. Joachimiak, Valerie A. Perez, Aydé Mendoza-Oliva, Zhiqiang Hou
Publikováno v:
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-17 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-17 (2021)
Molecular chaperones, including Hsp70/J-domain protein (JDP) families, play central roles in binding substrates to prevent their aggregation. How JDPs select different conformations of substrates remains poorly understood. Here, we report an interact
Autor:
Barbara E. Stopschinski, Sourena Nadji, Jordan G. Finnell, Sandi J. Estill-Terpack, Omar M. Kashmer, Hung S. Luu, Talitha L. Thomas, Eric Darvish, Anuja Modi, Brandon B. Holmes, Hilda Mirbaha, Marc I. Diamond, Linfeng Fan
Publikováno v:
J Biol Chem
Tau aggregation underlies neurodegeneration in Alzheimer's disease and related tauopathies. We and others have proposed that transcellular propagation of pathology is mediated by Tau prions, which are ordered protein assemblies that faithfully replic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af4aacf11971b9112d93f76e4b02728c
https://europepmc.org/articles/PMC7062170/
https://europepmc.org/articles/PMC7062170/
Publikováno v:
eLife, Vol 7 (2018)
eLife
eLife
Tauopathies have diverse presentation, progression, and neuropathology. They are linked to tau prion strains, self-replicating assemblies of unique quaternary conformation, whose origin is unknown. Strains can be propagated indefinitely in cultured c