Author

S. Dobler

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

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Evolutionary Biology· 4 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Approach:biophysical modeling· 1 Organism:chicken / avian· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:DNA methylation· 1 Organism:fungi (other)· 1

Frequent Co-Authors

S. Mohammadi· 4 shared A. J. Crawford· 3 shared P. Andolfatto· 3 shared J. F. Storz· 2 shared K. Zhang· 2 shared L. Yang· 2 shared M. d. P. Rodriguez-Ordonez· 2 shared S. Herrera-Alvarez· 2 shared

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2020-2024 · peak 2/yr

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10 top collaborators · 40 mutual co-author links

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4 shared papersEvolutionary Biology

S. Mohammadi

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5 papers

Recent·Most cited

Evaluating the efficacy of protein quantification methods on membrane proteins

J. Loeptien, S. Vesting, S. Dobler, S. Mohammadi

This study evaluates common protein quantification methods for membrane proteins and finds that they underestimate concentrations compared to a newly developed ELISA, which provides reliable results.

bioRxiv · Apr 2, 2024Biochemistry

Epistatic effects between amino acid insertions and substitutions mediate toxin-resistance of vertebrate Na+,K+-ATPases

S. Mohammadi, H. I. Özdemir, P. Ozbek, F. Sumbul, J. Stiller, Y. Deng, A. J. Crawford, H. M. Rowland, J. F. Storz, P. Andolfatto, S. Dobler

The paper shows how amino acid insertions and substitutions in Na+,K+-ATPase affect toxin resistance in different vertebrate lineages through epistatic interactions.

bioRxiv · Sep 1, 2022Evolutionary Biology

Constraints on the evolution of toxin-resistant Na,K-ATPases have limited dependence on sequence divergence

S. Mohammadi, S. Herrera-Alvarez, L. Yang, M. d. P. Rodriguez-Ordonez, K. Zhang, J. Storz, S. Dobler, A. J. Crawford, P. Andolfatto

The paper investigates how intramolecular epistasis affects the evolution of CTS-resistant Na,K-ATPases, finding that resistance substitutions have pleiotropic effects independent of sequence divergence.

bioRxiv · Nov 29, 2021Evolutionary Biology

Different combinations of insect Na,K-ATPase α- and β-subunit paralogs enable fine tuning of toxin resistance and enzyme kinetics

M. Herbertz, S. Dalla, V. Wagschal, R. Turjalei, M. Heiser, S. Dobler

This study examines how different combinations of Na,K-ATPase α- and β-subunit paralogs in milkweed bugs affect toxin resistance and enzyme kinetics.

bioRxiv · Aug 28, 2020Evolutionary Biology

Concerted evolution reveals co-adapted amino acid substitutions in Na+K+-ATPase of frogs that prey on toxic toads

S. Mohammadi, L. Yang, A. Harpak, S. Herrera-Alvarez, M. d. P. Rodriguez-Ordonez, J. Peng, K. Zhang, J. F. Storz, S. Dobler, A. J. Crawford, P. Andolfatto

The paper shows that selection maintains adaptive division-of-labor between tandem duplicates of ATP1A1 in frogs, countering gene conversion to confer toxin resistance.

bioRxiv · Aug 4, 2020Evolutionary Biology