Author

J. M. Lotthammer

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· 6

Signature Assays, Organisms & Methods

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Approach:deep learning· 4 Research Focus:drug response / drug discovery· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:protein sequence· 2 Research Focus:sequence-to-function modeling· 2 Approach:statistical model· 2 Research Focus:cell signaling & trafficking· 1

Frequent Co-Authors

A. Meller· 3 shared G. R. Bowman· 3 shared A. S. Holehouse· 2 shared L. A. Leinwand· 2 shared L. Greenberg· 2 shared M. J. Greenberg· 2 shared R. J. Emenecker· 2 shared A. Ballesteros· 1 shared

Activity by Year

2021-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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3 shared papersBiophysics

A. Meller

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6 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

Divergent Molecular Phenotypes in Point Mutations at the Same Residue in Beta-Myosin Heavy Chain Lead to Distinct Cardiomyopathies

S. J. Lehman, A. Meller, S. O. Solieva, J. M. Lotthammer, L. Greenberg, S. J. Langer, M. J. Greenberg, J. C. Tardiff, G. R. Bowman, L. A. Leinwand

This study shows that two point mutations at the same residue in beta-myosin heavy chain cause distinct cardiomyopathies through different molecular mechanisms.

bioRxiv · Jul 3, 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

Drug specificity and affinity are encoded in the probability of cryptic pocket opening in myosin motor domains

A. Meller, J. M. Lotthammer, L. G. Smith, B. Novak, L. A. Lee, C. C. Kuhn, L. Greenberg, L. A. Leinwand, M. J. Greenberg, G. R. Bowman

This paper shows that the probability of cryptic pocket opening in myosin motor domains predicts drug specificity and affinity, using molecular dynamics simulations and Markov state models.

bioRxiv · Sep 5, 2022Biophysics

Predicting the locations of cryptic pockets from single protein structures using the PocketMiner graph neural network

A. Meller, M. Ward, J. Borowsky, J. M. Lotthammer, M. Kshirsagar, F. Oviedo, J. Lavista Ferres, G. R. Bowman

The paper introduces PocketMiner, a graph neural network that predicts cryptic pockets in proteins, identifying them accurately and rapidly, expanding the druggable proteome.

bioRxiv · Jun 28, 2022 · PreprintBiophysics

In Silico Electrophysiology of Inner-Ear Mechanotransduction Channel TMC1 Models

S. Walujkar, J. M. Lotthammer, C. R. Nisler, J. C. Sudar, A. Ballesteros, M. Sotomayor

The paper uses molecular dynamics simulations to study ion conduction in TMC1 models, revealing a peripheral permeation pathway and lipid-mediated gating mechanisms in inner-ear mechanotransduction channels.

bioRxiv · Sep 17, 2021 · PreprintBiophysics