Weak protein–protein interactions in live cells are quantified by cell-volume modulation von Sukenik, Shahar, Ren, Pin, Gruebele, Martin

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Phase separation of YAP reorganizes genome topology for long-term YAP target gene expression von Cai, Danfeng, Feliciano, Daniel, Dong, Peng, Flores, Eduardo, Gruebele, Martin, Porat-Shliom, Natalie, Sukenik, Shahar, Liu, Zhe, Lippincott-Schwartz, Jennifer

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Intrinsically disordered protein biosensor tracks the physical-chemical effects of osmotic stress on cells von Cuevas-Velazquez, Cesar L., Vellosillo, Tamara, Guadalupe, Karina, Schmidt, Hermann Broder, Yu, Feng, Moses, David, Brophy, Jennifer A. N., Cosio-Acosta, Dante, Das, Alakananda, Wang, Lingxin, Jones, Alexander M., Covarrubias, Alejandra A., Sukenik, Shahar, Dinneny, José R.

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How does solvation in the cell affect protein folding and binding? von Davis, Caitlin M, Gruebele, Martin, Sukenik, Shahar

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Balance of enthalpy and entropy in depletion forces von Sukenik, Shahar, Sapir, Liel, Harries, Daniel

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In-Cell Titration of Small Solutes Controls Protein Stability and Aggregation von Sukenik, Shahar, Salam, Mohammed, Wang, Yuhan, Gruebele, Martin

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A prion-like protein regulator of seed germination undergoes hydration-dependent phase separation von Dorone, Yanniv, Boeynaems, Steven, Flores, Eduardo, Jin, Benjamin, Hateley, Shannon, Bossi, Flavia, Lazarus, Elena, Pennington, Janice G., Michiels, Emiel, De Decker, Mathias, Vints, Katlijn, Baatsen, Pieter, Bassel, George W., Otegui, Marisa S., Holehouse, Alex S., Exposito-Alonso, Moises, Sukenik, Shahar, Gitler, Aaron D., Rhee, Seung Y.

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Diversity in the mechanisms of cosolute action on biomolecular processes von Sukenik, Shahar, Sapir, Liel, Gilman-Politi, Regina, Harries, Daniel

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Disordered proteins interact with the chemical environment to tune their protective function during drying von Kc, Shraddha, Nguyen, Kenny H, Nicholson, Vincent, Walgren, Annie, Trent, Tony, Gollub, Edith, Romero-Perez, Paulette Sofia, Holehouse, Alex S, Sukenik, Shahar, Boothby, Thomas C

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Structural Preferences Shape the Entropic Force of Disordered Protein Ensembles von Yu, Feng, Sukenik, Shahar

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Can Local Probes Go Global? A Joint Experiment–Simulation Analysis of λ6–85 Folding von Sukenik, Shahar, Pogorelov, Taras V, Gruebele, Martin

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Crowding alone cannot account for cosolute effect on amyloid aggregation von Sukenik, Shahar, Politi, Regina, Ziserman, Lior, Danino, Dganit, Friedler, Assaf, Harries, Daniel

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Mapping fast protein folding with multiple-site fluorescent probes von Prigozhin, Maxim B, Shu-Han Chao, Shahar Sukenik, Taras V. Pogorelov, Martin Gruebele

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Structural preferences modulate the entropic force exerted by disordered proteins von Yu, Feng, Sukenik, Shahar

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Tuning protein condensate selectivity by changing solution composition von Flores, Eduardo, Sukenik, Shahar

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Linking disordered protein sequence and ensemble using interaction maps von Yu, Feng, Sukenik, Shahar

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Measuring the effects of infection on disordered viral proteins von Koenig, Patrick S., Sukenik, Shahar

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YAP condensates are highly organized hubs von Hao, Siyuan, Lee, Ye Jin, Benhamou Goldfajn, Nadav, Flores, Eduardo, Liang, Jindayi, Fuehrer, Hannah, Demmerle, Justin, Lippincott-Schwartz, Jennifer, Liu, Zhe, Sukenik, Shahar, Cai, Danfeng

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Insights into the disparate action of osmolytes and macromolecular crowders on amyloid formation von Sukenik, Shahar, Harries, Daniel

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Globular Protein Folding In Vitro and In Vivo von Gruebele, Martin, Dave, Kapil, Sukenik, Shahar

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