E
Evelyn R. Stimson
Researcher at Harvard University
Publications - 27
Citations - 3064
Evelyn R. Stimson is an academic researcher from Harvard University. The author has contributed to research in topics: Amyloid & P3 peptide. The author has an hindex of 23, co-authored 27 publications receiving 2977 citations. Previous affiliations of Evelyn R. Stimson include University of California, Los Angeles & Brigham and Women's Hospital.
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Journal ArticleDOI
Aluminum, Iron, and Zinc Ions Promote Aggregation of Physiological Concentrations of β‐Amyloid Peptide
Patrick W. Mantyh,Joseph R. Ghilardi,Scott D. Rogers,Eric DeMaster,Clark J. Allen,Evelyn R. Stimson,John E. Maggio +6 more
TL;DR: High concentrations of certain metals may play a role in the pathogenesis of AD by promoting aggregation of human βA4, a 40‐mer whose neurotoxicity is related to its aggregation.
Journal ArticleDOI
Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism.
William P. Esler,Evelyn R. Stimson,Joan M. Jennings,Harry V. Vinters,Joseph R. Ghilardi,Jonathan P. Lee,and Patrick W. Mantyh,John E. Maggio +7 more
TL;DR: The present study illustrates that the protein misfolding diseases are kinetically vulnerable to intervention and inhibiting the initial weak docking interaction between depositing Abeta and the template is a viable therapeutic target to prevent the critical conformational transition in the conversion of Abeta ((solution)) to Abeta((amyloid)) and thus prevent stable amyloid accumulation.
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Amyloid β-Peptide Is Transported on Lipoproteins and Albumin in Human Plasma
Anja Leona Biere,Anja Leona Biere,Beth L. Ostaszewski,Beth L. Ostaszewski,Evelyn R. Stimson,Bradley T. Hyman,John E. Maggio,Dennis J. Selkoe,Dennis J. Selkoe +8 more
TL;DR: Aβ is normally bound to and transported by albumin and specific lipoproteins in human plasma under physiological conditions and is not significantly influenced by apolipoprotein E genotype.
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Reversible in vitro growth of Alzheimer disease beta-amyloid plaques by deposition of labeled amyloid peptide.
John E. Maggio,Evelyn R. Stimson,Joseph R. Ghilardi,Clark J. Allen,Charles E. Dahl,David C. Whitcomb,Steven R. Vigna,Harry V. Vinters,Mark E. Labenski,Patrick W. Mantyh +9 more
TL;DR: The use of radioiodinated beta A4 provides an in vitro system for the quantitative evaluation of agents or conditions that may inhibit or enhance the growth or dissolution of AD plaques and an extremely sensitive method for visualizing various types of amyloid deposits.
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Oligomerization of endogenous and synthetic amyloid beta-protein at nanomolar levels in cell culture and stabilization of monomer by Congo red.
Marcia B. Podlisny,Dominic M. Walsh,Patricia Amarante,Beth L. Ostaszewski,Evelyn R. Stimson,John E. Maggio,David B. Teplow,Dennis J. Selkoe +7 more
TL;DR: It is concluded that both endogenous and synthetic A beta can assemble into stable oligomers at physiological concentrations in cell culture, providing a manipulable system for studying the mechanism of early A beta aggregation and identifying inhibitors thereof under biologically relevant conditions.