D
David J. Rosenman
Researcher at Rensselaer Polytechnic Institute
Publications - 11
Citations - 971
David J. Rosenman is an academic researcher from Rensselaer Polytechnic Institute. The author has contributed to research in topics: Green fluorescent protein & Residual dipolar coupling. The author has an hindex of 7, co-authored 11 publications receiving 838 citations. Previous affiliations of David J. Rosenman include University of California, Los Angeles.
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Journal ArticleDOI
Amyloid β Protein and Alzheimer’s Disease: When Computer Simulations Complement Experimental Studies
Jessica Nasica-Labouze,Phuong H. Nguyen,Fabio Sterpone,Olivia Berthoumieu,Nicolae-Viorel Buchete,Sébastien Côté,Alfonso De Simone,Andrew J. Doig,Peter Faller,Angel E. Garcia,Alessandro Laio,Mai Suan Li,Simone Melchionna,Normand Mousseau,Yuguang Mu,Anant K. Paravastu,Samuela Pasquali,David J. Rosenman,Birgit Strodel,Bogdan Tarus,John H. Viles,Tong Zhang,Tong Zhang,Chunyu Wang,Philippe Derreumaux,Philippe Derreumaux +25 more
TL;DR: Simulations Complement Experimental Studies Jessica Nasica-Labouze, Phuong H. Nguyen, Fabio Sterpone,† Olivia Berthoumieu,‡ Nicolae-Viorel Buchete, Sebastien Cote, Alfonso De Simone, Andrew J. Doig, and Philippe Derreumaux are authors of this paper.
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Aβ Monomers Transiently Sample Oligomer and Fibril-like Configurations: Ensemble Characterization Using a Combined MD/NMR Approach
TL;DR: De novo replica exchange molecular dynamics simulations on the microseconds-per-replica timescale are used to characterize the structural ensembles of A β42, Aβ40, and M35-oxidized Aβ42, three physiologically relevant isoforms with substantially different aggregation properties, and provide insight into the early stages of Aβ aggregation pathways.
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Characterization of Aβ Monomers through the Convergence of Ensemble Properties among Simulations with Multiple Force Fields.
TL;DR: Analysis of ensembles of different isoforms (Aβ42 and Aβ40) and mutants of Aβ generated with all-atom replica exchange molecular dynamics (REMD) simulations on the μs/replica time scale finds that the resulting ensemble demonstrate a strong convergence in structural properties.
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Familial Alzheimer’s mutations within APPTM increase Aβ42 production by enhancing accessibility of ε-cleavage site
TL;DR: A structural model is proposed in which FAD mutations (V44M and V44A) can open the T48 site γ-secretase for the initial ε-cleavage, and consequently shift cleavage preference towards Aβ42.
Journal ArticleDOI
Aß Monomers Transiently Sample Oligomer and Fibril-Like Configurations: Ensemble Characterization using a Combined MD/NMR Approach
TL;DR: De novo replica exchange molecular dynamics simulations on the µs/replica timescale are used to characterize the structural ensembles of As42, As40, and M35-oxidized As 42, three physiologically prevalent isoforms with substantially different aggregation properties, the latter of which has hitherto not been investigated with computational techniques.