Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Erik C. Gunther"'
Autor:
Timothy O, Cox, Erik C, Gunther, A Harrison, Brody, Marius T, Chiasseu, Austin, Stoner, Levi M, Smith, Laura T, Haas, Jayne, Hammersley, Gareth, Rees, Bhupinder, Dosanjh, Maria, Groves, Matthew, Gardener, Claire, Dobson, Tristan, Vaughan, Iain, Chessell, Andrew, Billinton, Stephen M, Strittmatter
Publikováno v:
Annals of Clinical and Translational Neurology
Objective Amyloid‐beta oligomers (Aßo) trigger the development of Alzheimer's disease (AD) pathophysiology. Cellular prion protein (PrPC) initiates synaptic damage as a high affinity receptor for Aßo. Here, we evaluated the preclinical therapeuti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d36f7f5c180265d45d862a4329636ad4
https://pubmed.ncbi.nlm.nih.gov/30911579
https://pubmed.ncbi.nlm.nih.gov/30911579
Autor:
Mikhail A, Kostylev, Marcus D, Tuttle, Suho, Lee, Lauren E, Klein, Hideyuki, Takahashi, Timothy O, Cox, Erik C, Gunther, Kurt W, Zilm, Stephen M, Strittmatter
Publikováno v:
Molecular cell. 72(3)
Protein phase separation by low complexity, intrinsically disordered domains generates membraneless organelles and links to neurodegeneration. Cellular prion protein (PrP(C)) contains such domains, causes spongiform degeneration and is a receptor for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::59bdf1d83fd77c85506f509141a96ca1
https://pubmed.ncbi.nlm.nih.gov/30401430
https://pubmed.ncbi.nlm.nih.gov/30401430
Autor:
Amanda T. Jeng, Jinhee Yang, Stephen M. Strittmatter, Haakon B. Nygaard, Mikhail A. Kostylev, Sophie A. Robinson, Santiago V. Salazar, Adam C. Kaufman, Christopher H. van Dyck, Laura T. Haas, Erik C. Gunther
Publikováno v:
Annals of Neurology. 77:953-971
Objective Currently no effective disease-modifying agents exist for the treatment of Alzheimer disease (AD). The Fyn tyrosine kinase is implicated in AD pathology triggered by amyloid-s oligomers (Aso) and propagated by Tau. Thus, Fyn inhibition may
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d2b3ea648255ef3232fc7fdf976b63db
https://doi.org/10.1002/ana.24394
https://doi.org/10.1002/ana.24394
Autor:
Timothy O. Cox, Stephen M. Strittmatter, Suho Lee, Lauren E. Klein, Kurt W. Zilm, Hideyuki Takahashi, Mikhail A. Kostylev, Erik C. Gunther, Marcus D. Tuttle
Publikováno v:
Molecular Cell. 72:426-443.e12
Protein phase separation by low-complexity, intrinsically disordered domains generates membraneless organelles and links to neurodegeneration. Cellular prion protein (PrPC) contains such domains, causes spongiform degeneration, and is a receptor for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::41ff8c5390eaec25506bd233dc155ae7
https://doi.org/10.1016/j.molcel.2018.10.009
https://doi.org/10.1016/j.molcel.2018.10.009
Publikováno v:
Journal of Molecular Medicine. 88:331-338
Prefibrillar oligomers of the beta-amyloid peptide (A beta) are recognized as potential mediators of Alzheimer's disease (AD) pathophysiology. Deficits in synaptic function, neurotoxicity, and the progression of AD have all been linked to the oligome
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::573000d8d3c0e12101e666a28ceb646d
https://doi.org/10.1007/s00109-009-0568-7
https://doi.org/10.1007/s00109-009-0568-7
Autor:
Laura T. Haas, Mikhail A. Kostylev, Alexander O. Vortmeyer, Haakon B. Nygaard, Adam C. Kaufman, Pujan R. Patel, Stephen M. Strittmatter, Erik C. Gunther
Alzheimer disease (AD) is characterized by amyloid-β accumulation, with soluble oligomers (Aβo) being the most synaptotoxic. However, the multivalent and unstable nature of Aβo limits molecular characterization and hinders research reproducibility
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd841b7c2d5b134d11d66e27e74316fd
https://europepmc.org/articles/PMC4498078/
https://europepmc.org/articles/PMC4498078/
Autor:
Adam C, Kaufman, Santiago V, Salazar, Laura T, Haas, Jinhee, Yang, Mikhail A, Kostylev, Amanda T, Jeng, Sophie A, Robinson, Erik C, Gunther, Christopher H, van Dyck, Haakon B, Nygaard, Stephen M, Strittmatter
Publikováno v:
Annals of neurology. 77(6)
Currently no effective disease-modifying agents exist for the treatment of Alzheimer disease (AD). The Fyn tyrosine kinase is implicated in AD pathology triggered by amyloid-ß oligomers (Aßo) and propagated by Tau. Thus, Fyn inhibition may prevent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d198d07545b93a5dbd55465585f18557
https://pubmed.ncbi.nlm.nih.gov/25707991
https://pubmed.ncbi.nlm.nih.gov/25707991
Autor:
Adam C. Kaufman, Jacqueline K. Heiss, Meghan E. Kerrisk, Stephen M. Strittmatter, Mikhail A. Kostylev, Anthony J. Koleske, Erik C. Gunther, Thomas Wisniewski, Massimiliano Stagi, Alexander O. Vortmeyer, Hideyuki Takahashi, Ji Won Um, Haakon B. Nygaard
Publikováno v:
Neuron. 80(2)
Soluble amyloid-β oligomers (Aβo) trigger Alzheimer's disease (AD) pathophysiology and bind with high affinity to cellular prion protein (PrP(C)). At the postsynaptic density (PSD), extracellular Aβo bound to lipid-anchored PrP(C) activates intrac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f3463072bf51aad947d1860772ea73b
Autor:
Massimiliano Stagi, Alexander O. Vortmeyer, Thomas Wisniewski, Mikhail A. Kostylev, Erik C. Gunther, Stephen M. Strittmatter, Ji Won Um, Jacqueline K. Heiss, Haakon B. Nygaard
Publikováno v:
Nature neuroscience. 15(9)
Amyloid-beta (Aβ) oligomers are thought to trigger Alzheimer's disease pathophysiology. Cellular prion protein (PrP(C)) selectively binds oligomeric Aβ and can mediate Alzheimer's disease-related phenotypes. We examined the specificity, distributio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aee8fc3cb649eb568edc66eeae5a6630
https://pubmed.ncbi.nlm.nih.gov/23326857
https://pubmed.ncbi.nlm.nih.gov/23326857
Autor:
David A. Gimbel, Zachary A. Gimbel, Juha Lauren, Erik C. Gunther, Stephen M. Strittmatter, Haakon B. Nygaard, Erin E. Coffey
Soluble oligomers of the amyloid-β (Aβ) peptide are thought to play a key role in the pathophysiology of Alzheimer's disease (AD). Recently, we reported that synthetic Aβ oligomers bind to cellular prion protein (PrPC) and that this interaction is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb0ead8f31c9862f608eb9a0cd3a1589
https://europepmc.org/articles/PMC3323924/
https://europepmc.org/articles/PMC3323924/