D
Donald L. Price
Researcher at Johns Hopkins University
Publications - 471
Citations - 93184
Donald L. Price is an academic researcher from Johns Hopkins University. The author has contributed to research in topics: Cholinergic neuron & Senile plaques. The author has an hindex of 128, co-authored 471 publications receiving 90448 citations. Previous affiliations of Donald L. Price include Johns Hopkins University School of Medicine & Dartmouth–Hitchcock Medical Center.
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Myelinogenesis in optic nerve. A morphological, autoradiographic, and biochemical analysis.
TL;DR: There is a strict correlation between the structural and biochemical changes occurring during myelination and the increasing amounts of proteolipid protein and myelin basic protein corresponded with the morphological appearance of myelin.
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Rodent models of TDP-43: recent advances.
William Tsao,Yun Ha Jeong,Sophie Lin,Jonathan P. Ling,Donald L. Price,Po Min Chiang,Philip C. Wong +6 more
TL;DR: Major findings from the initial sets of TDP-43 transgenic and knockout rodent models are summarized, their limitations are identified, and future directions toward clarification of disease mechanism(s) and testing of therapeutic strategies that ultimately may lead to novel therapy for this devastating disease are pointed to.
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Amyloid beta amyloidosis in Alzheimer's disease
TL;DR: Molecular genetic investigations have identified a variety of mutations in the amyloid precursor protein gene that segregate with early-onset familial Alzheimer's disease and with hereditary cerebral hemorrhage with amyloids, Dutch type.
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Fast axonal transport in motor nerve regeneration.
TL;DR: Results are interpreted to suggest that the mechanism of fast transport is the same in regenerating sprouts as in normal axons; during regeneration fast transport appears to add newly synthesized materials to the growing tip.
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Microtubule-neurofilament segregation produced by beta, beta'- iminodipropionitrile: evidence for the association of fast axonal transport with microtubules
TL;DR: These studies indicate that IDPN acts at the level of the axon to disrupt interactions between cytoskeletal elements and show that rapidly transported constituents are preferentially conveyed in association with microtubules.