Author

S. Wittmann

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

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:chromatin & epigenetic regulation· 3 Approach:statistical model· 3 Research Focus:cell signaling & trafficking· 2 Assay:proteomics· 2 Research Focus:cell type annotation· 1 Research Focus:drug response / drug discovery· 1 Organism:human· 1

Frequent Co-Authors

A. A. Hyman· 4 shared S. Alberti· 3 shared E. de Csillery· 2 shared G. Krainer· 2 shared T. M. Franzmann· 2 shared A. Klosin· 1 shared A. Sridhar· 1 shared A. Toth-Petroczy· 1 shared

Activity by Year

2020-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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4 shared papersBiophysics

A. A. Hyman

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Biomolecular condensates sustain pH gradients at equilibrium driven by charge neutralisation

H. Ausserwoeger, R. M. Scrutton, T. Sneideris, C. M. Fischer, D. Qian, E. de Csillery, I. Baronaite, K. L. Saar, A. Z. Bialek, M. M. Oeller, G. Krainer, T. M. Franzmann, S. Wittmann, J. M. Iglesias-Artola, G. Invernizzi, , T. P. J. Knowles

This study shows that biomolecular condensates can sustain pH gradients without energy input by neutralizing charges, revealing their role in creating pH microenvironments.

bioRxiv · May 23, 2024 · PreprintBiophysics

A conserved and tunable mechanism for the temperature-controlled condensation of the translation factor Ded1p

C. Jegers, T. M. Franzmann, J. Hübner, J. Schneider, C. Landerer, S. Wittmann, A. Toth-Petroczy, R. Sprangers, A. A. Hyman, S. Alberti

The paper investigates how Ded1p translation factors assemble into condensates in response to heat across fungi, identifying structural and amino acid determinants of temperature sensitivity.

bioRxiv · Oct 11, 2022 · PreprintBiochemistry

Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions

G. Krainer, T. J. Welsh, J. A. Joseph, J. R. Espinosa, S. Wittmann, E. de Csillery, A. Sridhar, Z. Toprakcioglu, G. Gudiskyte, M. A. Czekalska, W. E. Arter, P. St George-Hyslop, A. A. Hyman, R. Collepardo-Guevara, S. Alberti, T. P. Knowles

The paper shows that proteins forming liquid condensates can reenter a phase-separated state at high salt concentrations due to hydrophobic and non-ionic interactions, distinct from low-salt electrostatic-driven phase separation.

Nature Communications · Feb 17, 2021Peer-reviewedBiophysics

Surface condensation of a pioneer transcription factor on DNA

J. A. Morin, S. Wittmann, S. Choubey, A. Klosin, S. Golfier, A. A. Hyman, F. Julicher, S. W. Grill

This study uses optical tweezers to observe Klf4 condensation on DNA, showing surface-mediated microphases that reconcile phase separation with nuclear organization.

bioRxiv · Sep 24, 2020 · PreprintBiophysics