Author

D. Moses

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 2 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Assay:protein structure· 2 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Assay:fluorescence / live-cell microscopy· 1 Organism:plant (other)· 1

Frequent Co-Authors

F. Yu· 3 shared S. Sukenik· 3 shared A. S. Holehouse· 2 shared K. Guadalupe· 2 shared N. M. Shamoon· 2 shared A. A. Covarrubias· 1 shared A. Das· 1 shared A. M. Jones· 1 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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3 shared papersBiophysics

F. Yu

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Structural biases in disordered proteins are prevalent in the cell

D. Moses, K. Guadalupe, F. Yu, E. Flores, A. Perez, R. L. McAnelly, N. M. Shamoon, E. Cuevas-Zepeda, A. Merg, E. W. Martin, A. S. Holehouse, S. Sukenik

The paper shows that structural biases in intrinsically disordered proteins persist in human cells and can respond to intracellular changes.

bioRxiv · Nov 24, 2021Biophysics

Intrinsically disordered protein biosensor tracks the physical-chemical effects of osmotic stress on cells

C. L. Cuevas-Velazquez, T. Vellosillo, K. Guadalupe, H. B. Schmidt, F. Yu, D. Moses, J. A. Brophy, D. Cosio-Acosta, A. Das, L. Wang, A. M. Jones, A. A. Covarrubias, S. Sukenik, J. R. Dinneny

The paper develops a FRET biosensor using intrinsically disordered proteins to monitor osmotic stress effects across multiple organisms.

bioRxiv · Feb 17, 2021Cell Biology

Probing the Hidden Sensitivity of Intrinsically Disordered Proteins to their Chemical Environment

D. Moses, F. Yu, G. Ginell, N. M. Shamoon, P. S. Koenig, A. S. Holehouse, S. Sukenik

This study develops a framework to characterize how intrinsically disordered proteins (IDRs) respond to their chemical environment, finding sequence-dependent sensitivity and potential regulatory roles.

bioRxiv · Aug 17, 2020Biophysics