Author

D. T. Murray

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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Biochemistry· 2 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 2 Assay:structural biology· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:development & morphogenesis· 1 Organism:Drosophila· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

K. M. Jami· 2 shared B. D. Fonda· 1 shared C. B. Stanley· 1 shared G. Nagy· 1 shared I. Hung· 1 shared K. Weiss· 1 shared L. Sutherland· 1 shared M. E. Stroupe· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 11 mutual co-author links

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2 shared papersBiophysics

K. M. Jami

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Author profile →

4 papers

Recent·Most cited

Liquid droplet aging and fibril formation of the stress granule protein TIA1 low complexity domain

Y. Wittmer, K. M. Jami, R. K. Stowell, T. Le, I. Hung, D. T. Murray

This study investigates how aging and mutations affect the fibril formation of the TIA1 low complexity domain, showing disease mutations do not favor specific fibril conformations.

bioRxiv · Mar 30, 2022 · PreprintBiophysics

Identification of the Rigid Core for Aged Liquid Droplets of the TDP-43 Low Complexity Domain

B. D. Fonda, K. M. Jami, N. R. Boulos, D. T. Murray

This study identifies a structured core in aged TDP-43 liquid droplets that resists fibril formation, revealing functional and pathological interactions within the low complexity domain.

bioRxiv · Mar 1, 2021Biophysics

Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase

D. T. Murray, K. Weiss, C. B. Stanley, G. Nagy, M. E. Stroupe

The paper reports the first solution structures of sulfite reductase heterodimers using small-angle neutron scattering, showing how subunit binding and oxidation state affect conformation and electron transfer.

bioRxiv · Dec 8, 2020Biochemistry

Dynamic structural order of a low complexity domain facilitates assembly of intermediate filaments

V. O. Sysoev, M. Kato, L. Sutherland, R. Hu, S. L. McKnight, D. T. Murray

The paper shows that low complexity domains in Drosophila Tm1 proteins form labile cross-β interactions, facilitating intermediate filament assembly through dynamic structural transitions.

bioRxiv · Apr 1, 2020Biochemistry