Joseph M. Rogers
University of Tokyo
35 Papers
308 Citations
Joseph M. Rogers is an academic researcher from University of Tokyo. The author has contributed to research in topics: Protein folding & Chemistry. The author has an hindex of 18, co-authored 32 publications. Previous affiliations of Joseph M. Rogers include University of Copenhagen & University of Cambridge.
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Papers
Gene expression changes in the course of normal brain aging are sexually dimorphic.
Nicole C. Berchtold,David H. Cribbs,Paul D. Coleman,Joseph M. Rogers,Elizabeth Head,Ronald C. Kim,Thomas G. Beach,Carol A. Miller,Juan C. Troncoso,John Q. Trojanowski,H. Ronald Zielke,Carl W. Cotman +11 more
TL;DR: Clear gender differences in brain aging were evident, suggesting that the brain undergoes sexually dimorphic changes in gene expression not only in development but also in later life, and that this balance is set differently in males and females.
Alzheimer's disease is associated with reduced expression of energy metabolism genes in posterior cingulate neurons.
Winnie S. Liang,Eric M. Reiman,Jon Valla,Travis Dunckley,Thomas G. Beach,Andrew Grover,Tracey L. Niedzielko,Lonnie Schneider,Diego Mastroeni,Richard J. Caselli,Walter A. Kukull,John C. Morris,Christine M. Hulette,Donald E. Schmechel,Joseph M. Rogers,Dietrich A. Stephan +15 more
TL;DR: Molecular evaluation of cells from metabolically affected brain regions could provide new information about the pathogenesis of AD and new targets at which to aim disease-slowing and prevention therapies.
571
High thermodynamic stability of parametrically designed helical bundles.
Po-Ssu Huang,Gustav Oberdorfer,Gustav Oberdorfer,Chunfu Xu,Xue Y. Pei,Brent L. Nannenga,Joseph M. Rogers,Frank DiMaio,Tamir Gonen,Ben F. Luisi,David Baker +10 more
TL;DR: Protein design expands the repertoire of coiled-coil structures to α-helical barrels and hyperstable helical bundles, and describes a procedure for designing proteins with backbones produced by varying the parameters in the Crick coiled coil–generating equations.
Interplay between partner and ligand facilitates the folding and binding of an intrinsically disordered protein.
Joseph M. Rogers,Vladimiras Oleinikovas,Sarah L. Shammas,Chi T. Wong,David De Sancho,Christopher M. Baker,Jane Clarke +6 more
TL;DR: A small disordered protein is examined and it is found that interactions with its (already structured) partner protein are what cause the relatively unstructured protein to fold, offering some explanation for the abundance of similar protein–protein interactions throughout biology.
159
Folding and Binding of an Intrinsically Disordered Protein: Fast, but Not ‘Diffusion-Limited’
TL;DR: This work uses a model system where the ‘BH3 region’ of PUMA, an IDP, forms a single, contiguous α-helix upon binding the folded protein Mcl-1, and shows that the system is not ‘diffusion-limited’, despite having a k+ in the often-quoted’ regime and displaying an inverse dependence on solvent viscosity.
132