Personal profile
Research interests
A large fraction of proteins and protein regions are classified as "intrinsically disordered". These regions have historically been hard to study, but play key roles in a wide variety of cellular functions. Furthermore, these regions are strongly implicated in many diseases. In the Holehouse lab, we integrate a range of computational approaches (simulations, bioinformatics, systems biology) with experimental data to uncover how intrinsically disordered regions mediate cellular function, with a particular interest in biological phase separation.
Mentoring
A major goal of our group is to create an environment that is safe and supportive for lab members from all communities and backgrounds. Diversity in experience, perspective, and culture is a major asset and one that can only be realized through an inclusive environment that promotes and supports the success of scientists from groups that are traditionally underrepresented in science, technology, engineering, and mathematics (STEM). This support extends beyond our physical lab space to all members of the broader scientific community, and trainees from groups underrepresented in STEM should feel welcome to contact Alex or another member of the lab for support and advice.
Available to Mentor:
- PhD Students
- Postdocs
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Collaborations and top research areas from the last five years
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Accurate predictions of disordered protein ensembles with STARLING
Novak, B., Lotthammer, J. M., Emenecker, R. J. & Holehouse, A. S., 2026, (Accepted/In press) In: Nature.Research output: Contribution to journal › Article › peer-review
Open Access -
Sequence and chemical specificity define the functional landscape of intrinsically disordered regions
Langstein-Skora, I., Schmid, A., Huth, F., Shabani, D., Spechtenhauser, L., Likhodeeva, M., Kunert, F., Metzner, F. J., Emenecker, R. J., Richardson, M. O., Aftab, W., Götz, M. J., Payer, S. K., Pietrantoni, N., Valka, V., Ravichandran, S. K., Bartke, T., Hopfner, K. P., Gerland, U. & Korber, P. & 1 others, , Feb 2026, In: Nature Cell Biology. 28, 2, p. 323-337 15 p.Research output: Contribution to journal › Article › peer-review
Open Access1 Link opens in a new tab Scopus citations -
The filamentous ultrastructure of the PopZ condensate is required for its cellular function
Scholl, D., Boyd, T., Latham, A. P., Salazar, A., Khan, A. M. A. M., Boeynaems, S., Holehouse, A. S., Lander, G. C., Sali, A., Park, D., Deniz, A. A. & Lasker, K., Mar 2026, In: Nature Structural and Molecular Biology. 33, 3, p. 420-432 13 p.Research output: Contribution to journal › Article › peer-review
Open Access -
A phase transition modulates the protective function of a tardigrade disordered protein during desiccation
Nguyen, K., Biswas, S., Shraddha, K. C., Walgren, A., Nicholson, V., Childs, C., Medina-Rodriguez, B. X., Alvarado, V., Sukenik, S., Holehouse, A. & Boothby, T. C., Oct 2025, In: Protein Science. 34, 10, e70300.Research output: Contribution to journal › Article › peer-review
Open Access1 Link opens in a new tab Scopus citations -
Disentangling Folding from Energetic Traps in Simulations of Disordered Proteins
Lotthammer, J. M. & Holehouse, A. S., Mar 24 2025, In: Journal of Chemical Information and Modeling. 65, 6, p. 2897-2910 14 p.Research output: Contribution to journal › Article › peer-review
2 Link opens in a new tab Scopus citations