Author

R. J. Emenecker

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· 3 Biochemistry· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Assay:protein sequence· 3 Approach:deep learning· 2 Research Focus:sequence-to-function modeling· 2 Approach:statistical model· 2 Research Focus:cell type annotation· 1 Research Focus:development & morphogenesis· 1 Organism:Drosophila· 1 Approach:experimental assay· 1

Frequent Co-Authors

A. S. Holehouse· 5 shared J. M. Lotthammer· 2 shared A. Martinez· 1 shared A. Schmid· 1 shared B. Nicholson· 1 shared D. Griffith· 1 shared D. Shabani· 1 shared F. Huth· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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5 shared papersBiophysics

A. S. Holehouse

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Author profile →

5 papers

Recent·Most cited

Rational design of disordered proteins for systematic sequence-to-function investigation

K. Hunter, T. Brandt, K. Guadalupe, K. C. Kolamunna, J. M. Lotthammer, N. M. Shamoon, B. Nicholson, L. Day, A. Martinez, A. S. Holehouse, S. Sukenik, R. J. Emenecker

This paper introduces GOOSE, a computational framework for designing intrinsically disordered proteins, and demonstrates its ability to create IDRs with specific functional responses.

bioRxiv · Oct 29, 2023 · PreprintBiophysics

Direct prediction of intrinsically disordered protein conformational properties from sequence

J. M. Lotthammer, G. M. Ginell, D. Griffith, R. J. Emenecker, A. S. Holehouse

This paper develops ALBATROSS, a deep learning model that predicts ensemble conformational properties of intrinsically disordered proteins from sequence, enabling proteome-wide analysis.

bioRxiv · May 8, 2023Biophysics

Sequence- and chemical specificity define the functional landscape of intrinsically disordered regions

I. Langstein-Skora, A. Schmid, F. Huth, D. Shabani, L. Spechtenhauser, M. Likhodeeva, F. Kunert, F. J. Metzner, R. J. Emenecker, M. O. G. Richardson, W. Aftab, M. J. Goetz, S. K. Payer, N. Pietrantoni, V. Sjenicic, , A. S. Holehouse

The paper investigates how sequence- and chemical specificity enable functional IDR diversity despite poor sequence conservation.

bioRxiv · Feb 10, 2022Biophysics

Sequence determinants of in cell condensate assembly morphology, dynamics, and oligomerization as measured by number and brightness analysis

R. J. Emenecker, A. S. Holehouse, L. Strader

This study uses number and brightness analysis to examine how IDR amino acid composition affects ARF19 condensate morphology and material properties, but not oligomeric state.

bioRxiv · Apr 18, 2021Biochemistry

The arrested state of processing bodies supports mRNA regulation in early development

M. Sankaranarayanan, R. J. Emenecker, M. Jahnel, I. R. E. A. Trussina, M. T. Wayland, S. Alberti, A. S. Holehouse, T. T. Weil

This study shows that arrested P body condensates in Drosophila oocytes prevent premature mRNA release, supporting mRNA regulation during early development.

bioRxiv · Mar 16, 2021 · PreprintCell Biology