Sattler, Michael

FSP1 is a glutathione-independent ferroptosis suppressor

Doll, S., Freitas, F. P., Shah, R., Aldrovandi, M., da Silva, M. C., Ingold, I., Goya Grocin, A., Xavier da Silva, T. N., Panzilius, E., Scheel, C. H., et al. (2019) · Nature

Ferroptosis and cancer prognosisIron Metabolism and Disorders

Cited by 3,341

Structure of Bcl-x L -Bak Peptide Complex: Recognition Between Regulators of Apoptosis

Sattler, M., Liang, H., Nettesheim, D., Meadows, R. P., Harlan, J. E., Eberstadt, M., Yoon, H. S., Shuker, S. B., Chang, B. S., Minn, A. J., et al. (1997) · Science

Cell death mechanisms and regulationProtein Structure and Dynamics

Cited by 1,476

Active coacervate droplets as a model for membraneless organelles and protocells

Donau, C., Späth, F., Sosson, M., Kriebisch, B. A. K., Schnitter, F., Tena-Solsona, M., Kang, H.-S., Salibi, E., Sattler, M., Mutschler, H., et al. (2020) · Nature Communications

Origins and Evolution of LifeRNA and protein synthesis mechanisms

Cited by 309

Modulation of the Hsp90 Chaperone Cycle by a Stringent Client Protein

Lorenz, O. R., Freiburger, L., Rutz, D. A., Krause, M., Zierer, B. K., Alvira, S., Cuéllar, J., Valpuesta, J. M., Madl, T., Sattler, M., et al. (2014) · Molecular Cell

Heat shock proteins researchProtein Structure and Dynamics

Cited by 151

The structural analysis of shark IgNAR antibodies reveals evolutionary principles of immunoglobulins

Feige, M. J., Gräwert, M. A., Marcinowski, M., Hennig, J., Behnke, J., Ausländer, D., Herold, E. M., Peschek, J., Castro, C. D., Flajnik, M., et al. (2014) · Proceedings of the National Academy of Sciences

Monoclonal and Polyclonal Antibodies ResearchEnzyme Structure and Function

Cited by 91

MISATO: machine learning dataset of protein–ligand complexes for structure-based drug discovery

Siebenmorgen, T., Menezes, F., Benassou, S., Merdivan, E., Didi, K., Mourão, A. S. D., Kitel, R., Liò, P., Kesselheim, S., Piraud, M., et al. (2024) · Nature Computational Science

Computational Drug Discovery MethodsProtein Structure and Dynamics

Cited by 75

Structural and biochemical characterization of the yeast exosome component Rrp40

Oddone, A., Lorentzen, E., Basquin, J., Gasch, A., Rybin, V., Conti, E., & Sattler, M. (2007) · The EMBO Reports

RNA Research and SplicingEnzyme Structure and Function

Cited by 62

Client binding shifts the populations of dynamic Hsp90 conformations through an allosteric network

Lopez, A., Dahiya, V., Delhommel, F., Freiburger, L., Stehle, R., Asami, S., Rutz, D., Blair, L., Buchner, J., & Sattler, M. (2021) · Science Advances

Heat shock proteins researchProtein Structure and Dynamics

Cited by 59

Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle

Biebl, M. M., Lopez, A., Rehn, A., Freiburger, L., Lawatscheck, J., Blank, B., Sattler, M., & Buchner, J. (2021) · Nature Communications

Heat shock proteins researchProtein Structure and Dynamics

Cited by 58

The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs

Lingaraju, M., Johnsen, D., Schlundt, A., Langer, L. M., Basquin, J., Sattler, M., Heick Jensen, T., Falk, S., & Conti, E. (2019) · Nature Communications

RNA Research and SplicingRNA regulation and disease

Cited by 55

A switch point in the molecular chaperone Hsp90 responding to client interaction

Rutz, D. A., Luo, Q., Freiburger, L., Madl, T., Kaila, V. R. I., Sattler, M., & Buchner, J. (2018) · Nature Communications

Heat shock proteins researchProtein Structure and Dynamics

Cited by 37

Structural and Functional Analysis of the Signal-Transducing Linker in the pH-Responsive One-Component System CadC of Escherichia coli

Buchner, S., Schlundt, A., Lassak, J., Sattler, M., & Jung, K. (2015) · Journal of Molecular Biology

Bacterial Genetics and BiotechnologyProtein Structure and Dynamics

Cited by 32

The Charged Linker Modulates the Conformations and Molecular Interactions of Hsp90

López, A., Elimelech, A. R., Klimm, K., & Sattler, M. (2021) · ChemBioChem

Heat shock proteins researchProtein Structure and Dynamics

Cited by 30

Npl3 functions in mRNP assembly by recruitment of mRNP components to the transcription site and their transfer onto the mRNA

Keil, P., Wulf, A., Kachariya, N., Reuscher, S., Hühn, K., Silbern, I., Altmüller, J., Keller, M., Stehle, R., Zarnack, K., et al. (2023) · Nucleic Acids Research

RNA Research and SplicingGenomics and Chromatin Dynamics

Cited by 17

Allosteric activation of the SPRTN protease by ubiquitin maintains genome stability

Dürauer, S., Kang, H.-S., Wiebeler, C., Machida, Y., Schnapka, D. S., Yaneva, D., Renz, C., Götz, M. J., Weickert, P., Major, A. C., et al. (2025) · Nature Communications

Ubiquitin and proteasome pathwaysDNA Repair Mechanisms

Cited by 6

Allosteric activation of the SPRTN protease by ubiquitin maintains genome stability

Dürauer, S., Kang, H.-S., Wiebeler, C., Machida, Y., Schnapka, D. S., Yaneva, D., Renz, C., Götz, M. J., Weickert, P., Major, A. C., et al. (2024) · Nature Communications

Ubiquitin and proteasome pathwaysDNA Repair Mechanisms

Cited by 6

Npl3 functions in mRNP assembly by recruitment of mRNP components to the transcription site and their transfer onto the mRNA

Keil, P., Wulf, A., Kachariya, N., Reuscher, S., Hühn, K., Silbern, I., Altmüller, J., Stehle, R., Zarnack, K., Sattler, M., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory)

RNA Research and SplicingRNA and protein synthesis mechanisms

Cited by 0