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David A. Lutz

Researcher at Dartmouth College

Publications -  50
Citations -  948

David A. Lutz is an academic researcher from Dartmouth College. The author has contributed to research in topics: Forest management & Neurite. The author has an hindex of 17, co-authored 43 publications receiving 648 citations. Previous affiliations of David A. Lutz include Wake Forest University & University of Virginia.

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A Fragment of Adhesion Molecule L1 Binds to Nuclear Receptors to Regulate Synaptic Plasticity and Motor Coordination

TL;DR: It is shown that the LXXLL and FXXLF motifs in the extracellular and transmembrane domain of this L1 fragment mediate the interaction with the nuclear estrogen receptors α and β, peroxisome proliferator-activated receptor γ, and retinoid X receptor β.
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A fragment of adhesion molecule L1 is imported into mitochondria and regulates mitochondrial metabolism and trafficking

TL;DR: Evidence is provided that a transmembrane fragment of the cell adhesion molecule L1 is imported into neuronal mitochondria, and is important for regulation of mitochondrial metabolism, fusion, fission and trafficking.
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Small-scale forestry and carbon offset markets: An empirical study of Vermont Current Use forest landowner willingness to accept carbon credit programs

TL;DR: It is suggested that aggregated forest carbon offset projects incorporating small forest landowners could be piloted successfully in Vermont by non-profit organizations while maintaining relatively strict guidelines of existing carbon offset protocols.
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Biomass Energy and Climate Neutrality: The Case of the Northern Forest

TL;DR: In this paper, the authors test the assumption that harvesting timber for energy production is assumed to have a carbon-neutral effect on climate and show that accounting for carbon means that timber bioenergy production causes negative externalities that lead to longer rotations.
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Generation of Amyloid-β Is Reduced by the Interaction of Calreticulin with Amyloid Precursor Protein, Presenilin and Nicastrin

TL;DR: Findings indicate that the interaction of calreticulin with amyloid precursor protein and the γ-secretase complex regulates the proteolytic processing of amyloids precursor protein by the ε-secret enzyme complex, pointing to cal reticulin as a potential target for therapy in Alzheimer's disease.