His primary scientific interests are in Biochemistry, Amyloid, P3 peptide, Molecular biology and Fibril. David B. Teplow combines subjects such as Cell culture and Amyloid precursor protein with his study of Biochemistry. The concepts of his Amyloid study are interwoven with issues in Biophysics, Amyloid beta and Circular dichroism.
His P3 peptide research includes elements of Neuropil, Biochemistry of Alzheimer's disease, Neuroscience and Neurotoxicity. His study on Cleavage is often connected to PrP 27-30 Protein as part of broader study in Molecular biology. His work on Fibrillogenesis as part of general Fibril study is frequently connected to Polymerization, therefore bridging the gap between diverse disciplines of science and establishing a new relationship between them.
David B. Teplow focuses on Biochemistry, Amyloid, Peptide, Biophysics and Molecular biology. His research investigates the connection between Biochemistry and topics such as P3 peptide that intersect with issues in Biochemistry of Alzheimer's disease. His research integrates issues of Fibril, Amyloid beta, Oligomer and Protein folding in his study of Amyloid.
The various areas that David B. Teplow examines in his Peptide study include Stereochemistry, Mutant, Protein secondary structure and Random hexamer. Nucleation is closely connected to Crystallography in his research, which is encompassed under the umbrella topic of Biophysics. His study in Molecular biology is interdisciplinary in nature, drawing from both Complementary DNA, Gene, Presenilin and Proteolysis.
David B. Teplow mainly investigates Biophysics, Amyloid, Peptide, Oligomer and Protein structure. His Biophysics research includes elements of Crystallography, Neurotoxicity and Amyloid β1 42. His Amyloid research integrates issues from Plasma protein binding, Intracellular, Cell biology, Neurodegeneration and Cognitive decline.
His research on Peptide concerns the broader Biochemistry. His study in P3 peptide extends to Biochemistry with its themes. The concepts of his Protein structure study are interwoven with issues in Peptide sequence and Protein folding.
David B. Teplow mainly focuses on Amyloid, Crystallography, Biophysics, Peptide and Oligomer. His Amyloid research is multidisciplinary, incorporating perspectives in Neurotoxicity, Neurodegeneration, Molecular biology and Cell biology. His Crystallography research incorporates themes from Fibril, Amyloid β, Amyloid β1 42 and Nucleation.
His Biophysics study integrates concerns from other disciplines, such as Nucleus and Amyloidogenic Proteins. To a larger extent, he studies Biochemistry with the aim of understanding Peptide. His Oligomer study incorporates themes from Protein structure and Dimer.
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Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE.
Robert Vassar;Brian D. Bennett;Safura Babu-Khan;Steve Kahn.
Amyloid β-peptide is produced by cultured cells during normal metabolism
Christian Haass;Michael G. Schlossmacher;Michael G. Schlossmacher;Albert Y. Hung;Carmen Vigo-Pelfrey.
A cellular gene encodes scrapie PrP 27-30 protein
Bruno Oesch;Bruno Oesch;David Westaway;Monika Wälchli;Monika Wälchli;Michael P. McKinley.
Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways.
Gal Bitan;Marina D. Kirkitadze;Aleksey Lomakin;Sabrina S. Vollers.
Proceedings of the National Academy of Sciences of the United States of America (2003)
Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates.
Dominic M. Walsh;Dean M. Hartley;Yoko Kusumoto;Youcef Fezoui.
Journal of Biological Chemistry (1999)
The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Abeta protofibril formation.
Camilla Nilsberth;Anita Westlind-Danielsson;Anita Westlind-Danielsson;Christopher B. Eckman;Margaret M. Condron.
Nature Neuroscience (2001)
Amyloid β-Protein Fibrillogenesis: DETECTION OF A PROTOFIBRILLAR INTERMEDIATE
Dominic M. Walsh;Aleksey Lomakin;George B. Benedek;Margaret M. Condron.
Journal of Biological Chemistry (1997)
Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons.
Dean M. Hartley;Dominic M. Walsh;Chianping P. Ye;Thekla Diehl.
The Journal of Neuroscience (1999)
On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants
Aleksey Lomakin;Doo Soo Chung;George B. Benedek;Daniel A. Kirschner.
Proceedings of the National Academy of Sciences of the United States of America (1996)
Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease
Summer L. Bernstein;Nicholas F. Dupuis;Noel D. Lazo;Thomas Wyttenbach.
Nature Chemistry (2009)
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