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Daniel G. Chain

Researcher at Columbia University

Publications -  9
Citations -  1222

Daniel G. Chain is an academic researcher from Columbia University. The author has contributed to research in topics: Protein kinase A & Proteasome. The author has an hindex of 7, co-authored 8 publications receiving 1134 citations.

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Ubiquitin C-Terminal Hydrolase Is an Immediate-Early Gene Essential for Long-Term Facilitation in Aplysia

TL;DR: Through induction of the hydrolase and the resulting up-regulation of the ubiquitin pathway, learning recruits a regulated form of proteolysis that removes inhibitory constraints on long-term memory storage.
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Potent Neuroprotective Properties against the Alzheimer β-Amyloid by an Endogenous Melatonin-related Indole Structure, Indole-3-propionic Acid *

TL;DR: In kinetic competition experiments using free radical-trapping agents, the capacity of IPA to scavenge hydroxyl radicals exceeded that of melatonin, an indoleamine considered to be the most potent naturally occurring scavenger of free radicals.
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Mechanisms for generating the autonomous cAMP-dependent protein kinase required for long-term facilitation in Aplysia.

TL;DR: The formation of a persistently active cAMP-dependent protein kinase (PKA) is critical for establishing long-term synaptic facilitation (LTF) in Aplysia and appears to be a key function of proteasomes in LTF.
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Development of indole-3-propionic acid (OXIGON™) for Alzheimer's disease

TL;DR: This review will summarize the known properties of IPA and outline the rationale behind its selection as a potential disease-modifying therapy for Alzheimer’s disease.
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Persistent activation of cAMP-dependent protein kinase by regulated proteolysis suggests a neuron-specific function of the ubiquitin system in Aplysia

TL;DR: It is shown that ubiquitin (Ub), Ub-conjugates and proteasomes are present in cell bodies, axon, neuropil and nerve terminals of Aplysia neurons, and evidence that the susceptibility of R subunits to degradation in neurons relative to muscle results from the greater capacity of neurons to degrade ubiquitinated proteins through the proteasome.