Prof. Dr. Sebastian Hiller

Anna Leder, Guillaume Mas, Viktória Szentgyörgyi, Roman P. Jakob, Timm Maier, Anne Spang, & Sebastian Hiller. (2025). A multichaperone condensate enhances protein folding in the endoplasmic reticulum. Nature Cell Biology , 27(September), 1422–1430. https://doi.org/10.1038/s41556-025-01730-w

Stefańska, Marta, Müntener, Thomas, & Hiller, Sebastian. (2025). Photo-CIDNP for quantification of micromolar analytes in urine [Journal-article]. Communications Chemistry, 8(1). https://doi.org/10.1038/s42004-025-01626-8

Stefańska, Marta, Müntener, Thomas, & Hiller, Sebastian. (2025). Predictions of Steady-State Photo-CIDNP Enhancement by Machine Learning [Journal-article]. Journal of the American Chemical Society, 147(31), 27172–27178. https://doi.org/10.1021/jacs.5c07462

Wang, Guan, Yu, Bin, Chen, Yihao, Ding, Ruishen, Qi, Shixing, Zhao, Xiaoling, Gong, Zhou, Zhang, Xu, Hiller, Sebastian, Liu, Maili, & He, Lichun. (2025). An Unexpected Role of Molecular Chaperones in Regulating the Excited States and Activities of Folded Enzymes [Posted-content]. In bioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2025.07.15.664663

Leonte, Radu, Fischer, Patrick, Herguedas, Beatriz, García-Nafría, Javier, & Hiller, Sebastian. (2025). IVA Prime: Automated primer design for in vivo assembly cloning. Nucleic Acids Research, 53(W1), W330–W337. https://doi.org/10.1093/nar/gkaf386

Mas, Guillaume, & Hiller, Sebastian. (2025). Mechanism of ATP hydrolysis in the Hsp70 BiP nucleotide-binding domain [Journal-article]. Nature Communications, 16(1). https://doi.org/10.1038/s41467-025-60343-x

Sobkowiak, K., Kohzaki, M., Böhm, R., Mailler, J., Huber, F., Emamzadah, S., Tropia, L., Hiller, S., & Halazonetis, T. D. (2025). REV7 functions with REV3 as a checkpoint protein delaying mitotic entry until DNA replication is completed. Cell Reports, 44(4). https://doi.org/10.1016/j.celrep.2025.115431

Lehner,Philippe Alain, Degen, Morris, Jakob, Roman, Burmann, Björn M., Callon, Morgane, Modaresi, Seyed Majed, Maier, Timm, & Hiller, Sebastian. (2025). Architecture and conformational dynamics of the BAM-SurA holo insertase complex. Science Advances , 11(14). https://doi.org/10.1126/sciadv.ads6094

Träger, Lena, Degen, Morris, Pereira, Joana, Durairaj, Janini, Dias Teixeira, Raphael, Hiller, Sebastian, & Huguenin-Dezot, Nicolas. (2025). Structural basis for cooperative ssDNA binding by bacteriophage protein filament P12. Nucleic Acids Research, 53(5). https://doi.org/10.1093/nar/gkaf132

Modaresi, Seyed Majed, Sugiyama, Ryosuke, Tram, Nhan Dai Thien, Jakob, Roman P., Phan, Chin-Soon, Saei, Amir Ata, Morishita, Yohei, Mühlethaler, Tobias, Lim, Joel, Ritz, Danilo, Long, Preston Shi Yang, Lehner, Phillipe A, Lim, Zhen Heng, Degen, Morris, Yao, Ziwei, Maier, Timm, Hou, Yuxin, Lee, Jia Ying, Xu, Jian, et al. (2024). Antibiotics that Kill Gram-negative Bacteria by Restructuring the Outer Membrane Protein BamA [Posted-content]. In bioRxiv . Cold Spring Harbor Laboratory. https://doi.org/10.1101/2024.12.16.628070

Santi, Isabella, Dias Teixeira, Raphael, Manfredi, Pablo, Hernandez Gonzalez, Hector, Spiess, Daniel C, Mas, Guillaume, Klotz, Alexander, Kaczmarczyk, Andreas, Zamboni, Nicola, Hiller, Sebastian, & Jenal, Urs. (2024). Toxin-mediated depletion of NAD and NADP drives persister formation in a human pathogen [Journal-article]. The EMBO Journal, 43(21), 5211–5236. https://doi.org/10.1038/s44318-024-00248-5

Hiller, Sebastian, Szentgyörgyi, Viktória, Jakob, Roman, Maier, Timm, & Spang, Anne. (2024). A functional chaperone condensate in the endoplasmic reticulum. In Research Square. Research Square. https://doi.org/10.21203/rs.3.rs-4796355/v1

Lewis, Kim, Lee, Richard E., Brötz-Oesterhelt, Heike, Hiller, Sebastian, Rodnina, Marina V., Schneider, Tanja, Weingarth, Markus, & Wohlgemuth, Ingo. (2024). Sophisticated natural products as antibiotics [Journal-article]. Nature, 632(8023), 39–49. https://doi.org/10.1038/s41586-024-07530-w

Berhanu, Samuel, Majumder, Sagardip, Müntener, Thomas, Whitehouse, James, Berner, Carolin, Bera, Asim K., Kang, Alex, Liang, Binyong, Khan, Nasir, Sankaran, Banumathi, Tamm, Lukas K., Brockwell, David J., Hiller, Sebastian, Radford, Sheena E., Baker, David, & Vorobieva, Anastassia A. (2024). Sculpting conducting nanopore size and shape through de novo protein design. Science, 385(6706), 282–288. https://doi.org/10.1126/science.adn3796

Hiller, Sebastian, & Mas, Guillaume. (2024). Characterization of ATP hydrolysis in the Hsp70 BiP nucleotide binding domain [Posted-content]. In Research Square. Research Square Platform LLC. https://doi.org/10.21203/rs.3.rs-4017836/v1

Sollier, Julie, Basler, Marek, Broz, Petr, Dittrich, Petra S., Drescher, Knut, Egli, Adrian, Harms, Alexander, Hierlemann, Andreas, Hiller, Sebastian, King, Carolyn G., McKinney, John D., Moran-Gilad, Jacob, Neher, Richard A., Page, Malcolm G. P., Panke, Sven, Persat, Alexandre, Picotti, Paola, Rentsch, Katharina M., Rivera-Fuentes, Pablo, et al. (2024). Revitalizing antibiotic discovery and development through in vitro modelling of in-patient conditions. Nature Microbiology, 9(1), 1–3. https://doi.org/10.1038/s41564-023-01566-w

Hiller, Sebastian, Liu, Maili, & He, Lichun. (2023). Biophysics of Molecular Chaperones [Edited-book]. In Sebastian Hiller;Maili Liu;Lichun He (Ed.), Function, Mechanisms and Client Protein Interactions. Royal Society of Chemistry. https://doi.org/10.1039/9781839165986

Rath, P., Hermann, A., Schaefer, R., Agustoni, E., Vonach, J.-M., Siegrist, M., Miscenic, C., Tschumi, A., Roth, D., Bieniossek, C., & Hiller, S. (2023). High-throughput screening of BAM inhibitors in native membrane environment [Journal-article]. Nature Communications, 14(1). https://doi.org/10.1038/s41467-023-41445-w

Pipercevic, J., Kohl, B., Gerasimaite, R., Comte-Miserez, V., Hostachy, S., Müntener, T., Agustoni, E., Jessen, H. J., Fiedler, D., Mayer, A., & Hiller, S. (2023). Inositol pyrophosphates activate the vacuolar transport chaperone complex in yeast by disrupting a homotypic SPX domain interaction [Journal-article]. Nature Communications, 14(1). https://doi.org/10.1038/s41467-023-38315-w

Brüderlin, Mitchell, Böhm, Raphael, Fadel, Firas, Hiller, Sebastian, Schirmer, Tilman, & Dubey, Badri N. (2023). Structural features discriminating hybrid histidine kinase Rec domains from response regulator homologs. Nature communications, 14(1), 1002. https://doi.org/10.1038/s41467-023-36597-8

Degen, Morris, Santos, José Carlos, Pluhackova, Kristyna, Cebrero, Gonzalo, Ramos, Saray, Jankevicius, Gytis, Hartenian, Ella, Guillerm, Undina, Mari, Stefania A., Kohl, Bastian, Müller, Daniel J., Schanda, Paul, Maier, Timm, Perez, Camilo, Sieben, Christian, Broz, Petr, & Hiller, Sebastian. (2023). Structural basis of NINJ1-mediated plasma membrane rupture in cell death. Nature, 618(7967), 1065–1071. https://doi.org/10.1038/s41586-023-05991-z

Manner, Christina, Dias Teixeira, Raphael, Saha, Dibya, Kaczmarczyk, Andreas, Zemp, Raphaela, Wyss, Fabian, Jaeger, Tina, Laventie, Benoit-Joseph, Boyer, Sebastien, Malone, Jacob G., Qvortrup, Katrine, Andersen, Jens Bo, Givskov, Michael, Tolker-Nielsen, Tim, Hiller, Sebastian, Drescher, Knut, & Jenal, Urs. (2023). A genetic switch controls Pseudomonas aeruginosa surface colonization. Nature Microbiology, 8(8), 1520–1533. https://doi.org/10.1038/s41564-023-01403-0

Manioglu, S., Modaresi, S. M., Ritzmann, N., Thoma, J., Overall, S. A., Harms, A., Upert, G., Luther, A., Barnes, A. B., Obrecht, D., Müller, D. J., & Hiller, S. (2022). Antibiotic polymyxin arranges lipopolysaccharide into crystalline structures to solidify the bacterial membrane. Nature Communications, 13(1). https://doi.org/10.1038/s41467-022-33838-0

Hiller, Sebastian, & Burmann, Björn M. (2022). Describing dynamic chaperone-client complexes by solution NMR spectroscopy. In NMR Spectroscopy in probing Functional Dynamics at Biological Interfaces. Royal Society of Chemistry. https://doi.org/10.1039/9781839165702-00277

Mari, S. A., Pluhackova, K., Pipercevic, J., Leipner, M., Hiller, S., Engel, A., & Müller, D. J. (2022). Gasdermin-A3 pore formation propagates along variable pathways [Journal-article]. Nature Communications, 13(1). https://doi.org/10.1038/s41467-022-30232-8

Ritzmann, Noah, Manioglu, Selen, Hiller, Sebastian, & Müller, Daniel J. (2022). Monitoring the antibiotic darobactin modulating the β-barrel assembly factor BamA. Structure, 30(3), 350–359. https://doi.org/10.1016/j.str.2021.11.004

Agustoni, Elia, Teixeira, Raphael Dias, Huber, Markus, Flister, Susanne, Hiller, Sebastian, & Schirmer, Tilman. (2022). Acquisition of enzymatic progress curves in real time by quenching-free ion exchange chromatography. Analytical Biochemistry, 639, 114523. https://doi.org/10.1016/j.ab.2021.114523

Kolloff, Christopher, Mazur, Adam, Marzinek, Jan K., Bond, Peter J., Olsson, Simon, & Hiller, Sebastian. (2022). Motional clustering in supra-τ; c; conformational exchange influences NOE cross-relaxation rate. Journal of Magnetic Resonance, 338, 107196. https://doi.org/10.1016/j.jmr.2022.107196

Miller, Ryan D., Iinishi, Akira, Modaresi, Seyed Majed, Yoo, Byung-Kuk, Curtis, Thomas D., Lariviere, Patrick J., Liang, Libang, Son, Sangkeun, Nicolau, Samantha, Bargabos, Rachel, Morrissette, Madeleine, Gates, Michael F., Pitt, Norman, Jakob, Roman P., Rath, Parthasarathi, Maier, Timm, Malyutin, Andrey G., Kaiser, Jens T., Niles, Samantha, et al. (2022). Computational identification of a systemic antibiotic for gram-negative bacteria. Nature Microbiology, 7(10), 1661–1672. https://doi.org/10.1038/s41564-022-01227-4

Müntener, Thomas, Joss, Daniel, Häussinger, Daniel, & Hiller, Sebastian. (2022). Pseudocontact Shifts in Biomolecular NMR Spectroscopy. Chemical Reviews, 122(10), 9422–9467. https://doi.org/10.1021/acs.chemrev.1c00796

Böhm, Raphael, Imseng, Stefan, Jakob, Roman P., Hall, Michael N., Maier, Timm, & Hiller, Sebastian. (2021). The dynamic mechanism of 4E-BP1 recognition and phosphorylation by mTORC1. Molecular Cell, 81(11), 2403–2416. https://doi.org/10.1016/j.molcel.2021.03.031

Böhringer, Nils, Green, Robert, Liu, Yang, Mettal, Ute, Marner, Michael, Modaresi, Seyed Majed, Jakob, Roman P., Wuisan, Zerlina G., Maier, Timm, Iinishi, Akira, Hiller, Sebastian, Lewis, Kim, & Schäberle, Till F. (2021). Mutasynthetic Production and Antimicrobial Characterization of Darobactin Analogs. Microbiology spectrum, 9(3), e0153521. https://doi.org/10.1128/spectrum.01535-21

Gray, Declan A., White, Joshua B. R., Oluwole, Abraham O., Rath, Parthasarathi, Glenwright, Amy J., Mazur, Adam, Zahn, Michael, Baslé, Arnaud, Morland, Carl, Evans, Sasha L., Cartmell, Alan, Robinson, Carol V., Hiller, Sebastian, Ranson, Neil A., Bolam, David N., & van den Berg, Bert. (2021). Insights into SusCD-mediated glycan import by a prominent gut symbiont. Nature Communications, 12(1), 44. https://doi.org/10.1038/s41467-020-20285-y

He, Wei, Yu, Gangjin, Li, Tianpeng, Bai, Ling, Yang, Yuanyuan, Xue, Zixiao, Pang, Yonghao, Reichmann, Dana, Hiller, Sebastian, He, Lichun, Liu, Maili, & Quan, Shu. (2021). Chaperone Spy Protects Outer Membrane Proteins from Folding Stress via Dynamic Complex Formation. mBio, 12(5), e0213021. https://doi.org/10.1128/mbio.02130-21

Hiller, Sebastian. (2021). Molecular chaperones and their denaturing effect on client proteins. Journal of Biomolecular NMR, 75(1), 1–8. https://doi.org/10.1007/s10858-020-00353-7

Hiller, Sebastian, & Broz, Petr. (2021). Active membrane rupture spurs a range of cell deaths. Nature, 591(7848), 36–37. https://doi.org/10.1038/d41586-021-00297-4

Kaur, Hundeep, Jakob, Roman P., Marzinek, Jan K., Green, Robert, Imai, Yu, Bolla, Jani Reddy, Agustoni, Elia, Robinson, Carol V., Bond, Peter J., Lewis, Kim, Maier, Timm, & Hiller, Sebastian. (2021). The antibiotic darobactin mimics a β-strand to inhibit outer membrane insertase. Nature, 593(7857), 125–129. https://doi.org/10.1038/s41586-021-03455-w

Macošek, Jakub, Mas, Guillaume, & Hiller, Sebastian. (2021). Redefining Molecular Chaperones as Chaotropes. Frontiers in Molecular Biosciences, 8, 683132. https://doi.org/10.3389/fmolb.2021.683132

Pérez-Schindler, Joaquín, Kohl, Bastian, Schneider-Heieck, Konstantin, Leuchtmann, Aurel B., Henríquez-Olguín, Carlos, Adak, Volkan, Maier, Geraldine, Delezie, Julien, Sakoparnig, Thomas, Vargas-Fernández, Elyzabeth, Karrer-Cardel, Bettina, Ritz, Danilo, Schmidt, Alexander, Hondele, Maria, Jensen, Thomas E., Hiller, Sebastian, & Handschin, Christoph. (2021). RNA-bound PGC-1α controls gene expression in liquid-like nuclear condensates. Proceedings of the National Academy of Sciences of the United States of America, 118(36), e2105951118. https://doi.org/10.1073/pnas.2105951118

Pipercevic, Joka, Jakob, Roman P., Righetto, Ricardo D., Goldie, Kenneth N., Stahlberg, Henning, Maier, Timm, & Hiller, Sebastian. (2021). Identification of a Dps contamination in Mitomycin-C-induced expression of Colicin Ia. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1863(7), 183607. https://doi.org/10.1016/j.bbamem.2021.183607

Ried, Martina K., Wild, Rebekka, Zhu, Jinsheng, Pipercevic, Joka, Sturm, Kristina, Broger, Larissa, Harmel, Robert K., Abriata, Luciano A., Hothorn, Ludwig A., Fiedler, Dorothea, Hiller, Sebastian, & Hothorn, Michael. (2021). Inositol pyrophosphates promote the interaction of SPX domains with the coiled-coil motif of PHR transcription factors to regulate plant phosphate homeostasis. Nature Communications, 12(1), 384. https://doi.org/10.1038/s41467-020-20681-4

Shyp, Viktoriya, Dubey, Badri Nath, Böhm, Raphael, Hartl, Johannes, Nesper, Jutta, Vorholt, Julia A., Hiller, Sebastian, Schirmer, Tilman, & Jenal, Urs. (2021). Reciprocal growth control by competitive binding of nucleotide second messengers to a metabolic switch in Caulobacter crescentus. Nature Microbiology, 6(1), 59–72. https://doi.org/10.1038/s41564-020-00809-4

Ude, Johanna, Tripathi, Vishwachi, Buyck, Julien M., Söderholm, Sandra, Cunrath, Olivier, Fanous, Joseph, Claudi, Beatrice, Egli, Adrian, Schleberger, Christian, Hiller, Sebastian, & Bumann, Dirk. (2021). Outer membrane permeability: Antimicrobials and diverse nutrients bypass porins in Pseudomonas aeruginosa. Proceedings of the National Academy of Sciences of the United States of America, 118(31), e2107644118. https://doi.org/10.1073/pnas.2107644118

Vavassori, Stefano, Chou, Janet, Faletti, Laura Eva, Haunerdinger, Veronika, Opitz, Lennart, Joset, Pascal, Fraser, Christopher J., Prader, Seraina, Gao, Xianfei, Schuch, Luise A., Wagner, Matias, Hoefele, Julia, Maccari, Maria Elena, Zhu, Ying, Elakis, George, Gabbett, Michael T., Forstner, Maria, Omran, Heymut, Kaiser, Thomas, et al. (2021). Multisystem inflammation and susceptibility to viral infections in human ZNFX1 deficiency. The Journal of Allergy & Clinical Immunology, 148(2), 381–393. https://doi.org/10.1016/j.jaci.2021.03.045

Bibow, Stefan, Böhm, Raphael, Modaresi, Seyed Majed, & Hiller, Sebastian. (2020). Detergent Titration as an Efficient Method for NMR Resonance Assignments of Membrane Proteins in Lipid-Bilayer Nanodiscs. Analytical Chemistry, 92(11), 7786–7793. https://doi.org/10.1021/acs.analchem.0c00917

Böhm, Raphael, Amodeo, Giuseppe Federico, Murlidaran, Sruthi, Chavali, Shashank, Wagner, Gerhard, Winterhalter, Mathias, Brannigan, Grace, & Hiller, Sebastian. (2020). The Structural Basis for Low Conductance in the Membrane Protein VDAC upon β-NADH Binding and Voltage Gating. Structure, 28(2), 206–214. https://doi.org/10.1016/j.str.2019.11.015

Burmann, Björn M., Gerez, Juan A., Matečko-Burmann, Irena, Campioni, Silvia, Kumari, Pratibha, Ghosh, Dhiman, Mazur, Adam, Aspholm, Emelie E., Šulskis, Darius, Wawrzyniuk, Magdalena, Bock, Thomas, Schmidt, Alexander, Rüdiger, Stefan G. D., Riek, Roland, & Hiller, Sebastian. (2020). Regulation of α-synuclein by chaperones in mammalian cells. Nature, 577(7788), 127–132. https://doi.org/10.1038/s41586-019-1808-9

Dubey, Badri N., Agustoni, Elia, Böhm, Raphael, Kaczmarczyk, Andreas, Mangia, Francesca, von Arx, Christoph, Jenal, Urs, Hiller, Sebastian, Plaza-Menacho, Iván, & Schirmer, Tilman. (2020). Hybrid histidine kinase activation by cyclic di-GMP-mediated domain liberation. Proceedings of the National Academy of Sciences of the United States of America, 117(2), 1000–1008. https://doi.org/10.1073/pnas.1911427117

Kaczmarczyk, Andreas, Hempel, Antje M., von Arx, Christoph, Böhm, Raphael, Dubey, Badri N., Nesper, Jutta, Schirmer, Tilman, Hiller, Sebastian, & Jenal, Urs. (2020). Precise Timing of Transcription by c-di-GMP Coordinates Cell Cycle and Morphogenesis in Caulobacter. Nature Communications, 11(1), 816. https://doi.org/10.1038/s41467-020-14585-6

Kaur, Hundeep, Grahl, Anne, Hartmann, Jean-Baptiste, & Hiller, Sebastian. (2020). Sample Preparation and Technical Setup for NMR Spectroscopy with Integral Membrane Proteins. In Expression, Purification, and Structural Biology of Membrane Proteins (Vol. 2127, pp. 373–396). Humana Press. https://doi.org/10.1007/978-1-0716-0373-4_24

Kohl, Bastian, Brüderlin, Mitchell, Ritz, Danilo, Schmidt, Alexander, & Hiller, Sebastian. (2020). Protocol for High-Yield Production of Photo-Leucine-Labeled Proteins in Escherichia coli. Journal of Proteome Research, 19(8), 3100–3108. https://doi.org/10.1021/acs.jproteome.0c00105

Mas, Guillaume, Burmann, Björn M., Sharpe, Timothy, Claudi, Beatrice, Bumann, Dirk, & Hiller, Sebastian. (2020). Regulation of chaperone function by coupled folding and oligomerization. Science advances, 6(43), eabc5822. https://doi.org/10.1126/sciadv.abc5822

Müntener, Thomas, Böhm, Raphael, Atz, Kenneth, Häussinger, Daniel, & Hiller, Sebastian. (2020). NMR pseudocontact shifts in a symmetric protein homotrimer. Journal of Biomolecular NMR, 74(8-9), 413–419. https://doi.org/10.1007/s10858-020-00329-7

Orton, Henry W., Stanek, Jan, Schubeis, Tobias, Foucaudeau, Dylan, Ollier, Claire, Draney, Adrian W., Le Marchand, Tanguy, Cala-De Paepe, Diane, Felli, Isabella C., Pierattelli, Roberta, Hiller, Sebastian, Bermel, Wolfgang, & Pintacuda, Guido. (2020). Protein NMR resonance assignment without spectral analysis: 5D SOlid-State Automated Projection SpectroscopY (SO-APSY). Angewandte Chemie International Edition, 59(6), 2380–2384. https://doi.org/10.1002/anie.201912211

Rath, Parthasarathi, Sharpe, Timothy, & Hiller, Sebastian. (2020). The electrostatic core of the outer membrane protein X from E. coli. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1862(1), 183031. https://doi.org/10.1016/j.bbamem.2019.183031

Zhang, Bing, Liu, Xue, Lambert, Elisabeth, Mas, Guillaume, Hiller, Sebastian, Veening, Jan-Willem, & Perez, Camilo. (2020). Structure of a proton-dependent lipid transporter involved in lipoteichoic acids biosynthesis. Nature Structural and Molecular Biology, 27(6), 561–569. https://doi.org/10.1038/s41594-020-0425-5

Mas, Guillaume, Thoma, Johannes, & Hiller, Sebastian. (2019). The Periplasmic Chaperones Skp and SurA. In Kuhn, A. (Ed.), Bacterial Cell Walls and Membranes (Vol. 92, pp. 169–186). Springer Nature. https://doi.org/10.1007/978-3-030-18768-2_6

Mazur, Adam, Broz, Petr, & Hiller, Sebastian. (2019). An integrative protocol for the structure determination of the mouse ASC-PYD filament. In Sohn, Jungsan (Ed.), Methods in Enzymology (Vol. 625, pp. 205–222). Elsevier. https://doi.org/10.1016/bs.mie.2019.04.033

Bibow, Stefan, & Hiller, Sebastian. (2019). A guide to quantifying membrane protein dynamics in lipids and other native-like environments by solution-state NMR spectroscopy. FEBS Journal, 286(9), 1610–1623. https://doi.org/10.1111/febs.14639

He, Lichun, & Hiller, Sebastian. (2019). Frustrated Interfaces Facilitate Dynamic Interactions between Native Client Proteins and Holdase Chaperones. Chembiochem : A European Journal of Chemical Biology, 20(22), 2803–2806. https://doi.org/10.1002/cbic.201900215

Hiller, Sebastian. (2019). Chaperone-Bound Clients: The Importance of Being Dynamic. Trends in Biochemical Sciences, 44(6), 517–527. https://doi.org/10.1016/j.tibs.2018.12.005

Imai, Yu, Meyer, Kirsten J., Iinishi, Akira, Favre-Godal, Quentin, Green, Robert, Manuse, Sylvie, Caboni, Mariaelena, Mori, Miho, Niles, Samantha, Ghiglieri, Meghan, Honrao, Chandrashekhar, Ma, Xiaoyu, Guo, Jason J., Makriyannis, Alexandros, Linares-Otoya, Luis, Böhringer, Nils, Wuisan, Zerlina G., Kaur, Hundeep, Wu, Runrun, et al. (2019). A new antibiotic selectively kills Gram-negative pathogens. Nature, 576(7787), 459–+. https://doi.org/10.1038/s41586-019-1791-1

Kaur, Hundeep, Hartmann, Jean-Baptiste, Jakob, Roman P., Zahn, Michael, Zimmermann, Iwan, Maier, Timm, Seeger, Markus A., & Hiller, Sebastian. (2019). Identification of conformation-selective nanobodies against the membrane protein insertase BamA by an integrated structural biology approach. Journal of Biomolecular NMR, 73(6-7), 375–384. https://doi.org/10.1007/s10858-019-00250-8

Luther, Anatol, Urfer, Matthias, Zahn, Michael, Müller, Maik, Wang, Shuang-Yan, Mondal, Milon, Vitale, Alessandra, Hartmann, Jean-Baptiste, Sharpe, Timothy, Monte, Fabio Lo, Kocherla, Harsha, Cline, Elizabeth, Pessi, Gabriella, Rath, Parthasarathi, Modaresi, Seyed Majed, Chiquet, Petra, Stiegeler, Sarah, Verbree, Carolin, Remus, Tobias, et al. (2019). Chimeric peptidomimetic antibiotics against Gram-negative bacteria. Nature, 576(7787), 452–458. https://doi.org/10.1038/s41586-019-1665-6

Rath, Parthasarathi, Sharpe, Timothy, Kohl, Bastian, & Hiller, Sebastian. (2019). Two-state folding of the outer membrane protein X into a lipid bilayer membrane. Angewandte Chemie International Edition, 58(9), 2665–2669. https://doi.org/10.1002/anie.201812321

Frey, Lukas, Hiller, Sebastian, Riek, Roland, & Bibow, Stefan. (2018). Lipid- and Cholesterol-Mediated Time-Scale-Specific Modulation of the Outer Membrane Protein X Dynamics in Lipid Bilayers. Journal of the American Chemical Society, 140(45), 15402–15411. https://doi.org/10.1021/jacs.8b09188

Hartmann, Jean-Baptiste, Zahn, Michael, Burmann, Irena Matecko, Bibow, Stefan, & Hiller, Sebastian. (2018). Sequence-Specific Solution NMR Assignments of the beta-Barrel Insertase BamA to Monitor Its Conformational Ensemble at the Atomic Level. Journal of the American Chemical Society, 140(36), 11252–11260. https://doi.org/10.1021/jacs.8b03220

Heilig, Rosalie, Dick, Mathias S., Sborgi, Lorenzo, Meunier, Etienne, Hiller, Sebastian, & Broz, Petr. (2018). The Gasdermin-D pore acts as a conduit for IL-1β secretion in mice. European Journal of Immunology, 48(4), 584–592. https://doi.org/10.1002/eji.201747404

He, Lichun, & Hiller, Sebastian. (2018). Common Patterns in Chaperone Interactions with a Native Client Protein. Angewandte Chemie International Edition, 57(20), 5921–5924. https://doi.org/10.1002/anie.201713064

Hiller, Sebastian, & Burmann, Björn M. (2018). Chaperone-client complexes: A dynamic liaison. Journal of Magnetic Resonance, 289, 142–155. https://doi.org/10.1016/j.jmr.2017.12.008

Mas, Guillaume, & Hiller, Sebastian. (2018). Conformational plasticity of molecular chaperones involved in periplasmic and outer membrane protein folding. FEMS Microbiology Letters, 365(13), fny121. https://doi.org/10.1093/femsle/fny121

Melo, Esther, Oertle, Philipp, Trepp, Carolyn, Meistermann, Hélène, Burgoyne, Thomas, Sborgi, Lorenzo, Cabrera, Alvaro Cortes, Chen, Chia-Yi, Hoflack, Jean-Christophe, Kam-Thong, Tony, Schmucki, Roland, Badi, Laura, Flint, Nicholas, Ghiani, Zeynep Eren, Delobel, Fréderic, Stucki, Corinne, Gromo, Giulia, Einhaus, Alfred, Hornsperger, Benoit, et al. (2018). HtrA1 Mediated Intracellular Effects on Tubulin Using a Polarized RPE Disease Model. EBioMedicine, 27, 258–274. https://doi.org/10.1016/j.ebiom.2017.12.011

Mulvihill, Estefania, Sborgi, Lorenzo, Mari, Stefania A., Pfreundschuh, Moritz, Hiller, Sebastian, & Müller, Daniel J. (2018). Mechanism of membrane pore formation by human gasdermin-D. The EMBO Journal, 37(14), e98321. https://doi.org/10.15252/embj.201798321

Sborgi, Lorenzo, Ude, Johanna, Dick, Mathias S., Vesin, Johnathan, Chambon, Marc, Turcatti, Gerardo, Broz, Petr, & Hiller, Sebastian. (2018). Assay for high-throughput screening of inhibitors of the ASC-PYD inflammasome core filament. Cell Stress, 2(4), 82–90. https://doi.org/10.15698/cst2018.04.131

Böhm, Raphael, Wagner, Gerhard, & Hiller, Sebastian. (2017). Solution Nuclear Magnetic Resonance Spectroscopy of Integral Membrane Proteins. In Reference module in Life Sciences (pp. 1–25). Elsevier. https://doi.org/10.1016/b978-0-12-809633-8.08077-8

Holdbrook, Daniel A., Burmann, Björn M., Huber, Roland G., Petoukhov, Maxim V., Svergun, Dmitri I., Hiller, Sebastian, & Bond, Peter J. (2017). A Spring-Loaded Mechanism Governs the Clamp-like Dynamics of the Skp Chaperone. Structure, 25(7), 1079–+. https://doi.org/10.1016/j.str.2017.05.018

Morgado, Leonor, Burmann, Björn M., Sharpe, Timothy, Mazur, Adam, & Hiller, Sebastian. (2017). The dynamic dimer structure of the chaperone Trigger Factor. Nature Communications, 8(1), 1992. https://doi.org/10.1038/s41467-017-02196-7

Thoma, Johannes, Ritzmann, Noah, Wolf, Dominik, Mulvihill, Estefania, Hiller, Sebastian, & Müller, Daniel J. (2017). Maltoporin LamB Unfolds β Hairpins along Mechanical Stress-Dependent Unfolding Pathways. Structure, 25(7), 1139–1144. https://doi.org/10.1016/j.str.2017.05.010

Dick, Mathias S., Sborgi, Lorenzo, Rühl, Sebastian, Hiller, Sebastian, & Broz, Petr. (2016). ASC filament formation serves as a signal amplification mechanism for inflammasomes. Nature Communications, 7, 11929. https://doi.org/10.1038/ncomms11929

He, Lichun, Sharpe, Timothy, Mazur, Adam, & Hiller, Sebastian. (2016). A molecular mechanism of chaperone-client recognition. Science Advances, 2(11), e1601625. https://doi.org/10.1126/sciadv.1601625

Raschle, Thomas, Rios Flores, Perla, Opitz, Christian, Müller, Daniel J., & Hiller, Sebastian. (2016). Monitoring Backbone Hydrogen-Bond Formation in β-Barrel Membrane Protein Folding. Angewandte Chemie. International edition in English, 55(20), 5–5952. https://doi.org/10.1002/anie.201509910

Ravotti, Francesco, Sborgi, Lorenzo, Cadalbert, Riccardo, Huber, Matthias, Mazur, Adam, Broz, Petr, Hiller, Sebastian, Meier, Beat H., & Böckmann, Anja. (2016). Sequence-specific solid-state NMR assignments of the mouse ASC PYRIN domain in its filament form. Biomolecular NMR Assignments, 10(1), 15–107. https://doi.org/10.1007/s12104-015-9647-6

Sborgi, Lorenzo, Rühl, Sebastian, Mulvihill, Estefania, Pipercevic, Joka, Heilig, Rosalie, Stahlberg, Henning, Farady, Christopher J., Müller, Daniel J., Broz, Petr, & Hiller, Sebastian. (2016). GSDMD membrane pore formation constitutes the mechanism of pyroptotic cell death. The EMBO Journal, 35(16), 78–1766. https://doi.org/10.15252/embj.201694696

Stanger, Frédéric V., Burmann, Björn M., Harms, Alexander, Aragão, Hugo, Mazur, Adam, Sharpe, Timothy, Dehio, Christoph, Hiller, Sebastian, & Schirmer, Tilman. (2016). Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification. Proceedings of the National Academy of Sciences of the United States of America, 113(5), E529–37. https://doi.org/10.1073/pnas.1516930113

Zhong, Franklin L., Mamaï, Ons, Sborgi, Lorenzo, Boussofara, Lobna, Hopkins, Richard, Robinson, Kim, Szeverényi, Ildikó, Takeichi, Takuya, Balaji, Reshmaa, Lau, Aristotle, Tye, Hazel, Roy, Keya, Bonnard, Carine, Ahl, Patricia J., Jones, Leigh Ann, Baker, Paul, Lacina, Lukas, Otsuka, Atsushi, Fournie, Pierre R., et al. (2016). Germline NLRP1 Mutations Cause Skin Inflammatory and Cancer Susceptibility Syndromes via Inflammasome Activation. Cell, 167(1), 187–202. https://doi.org/10.1016/j.cell.2016.09.001

Arquint, Christian, Gabryjonczyk, Anna-Maria, Imseng, Stefan, Böhm, Raphael, Sauer, Evelyn, Hiller, Sebastian, Nigg, Erich A., & Maier, Timm. (2015). STIL binding to Polo-box 3 of PLK4 regulates centriole duplication. eLife, 4, e07888. https://doi.org/10.7554/elife.07888

Brahimi-Horn, M. Christiane, Lacas-Gervais, Sandra, Adaixo, Ricardo, Ilc, Karine, Rouleau, Matthieu, Notte, Annick, Dieu, Marc, Michiels, Carine, Voeltzel, Thibault, Maguer-Satta, Véronique, Pelletier, Joffrey, Ilie, Marius, Hofman, Paul, Manoury, Bénédicte, Schmidt, Alexander, Hiller, Sebastian, Pouysségur, Jacques, & Mazure, Natalie M. (2015). Local mitochondrial-endolysosomal microfusion cleaves voltage-dependent anion channel 1 to promote survival in hypoxia. Molecular and Cellular Biology, 35(9), 505–1491. https://doi.org/10.1128/mcb.01402-14

Burmann, Björn M., & Hiller, Sebastian. (2015). Chaperones and chaperone-substrate complexes: dynamic playgrounds for NMR spectroscopists. Progress in Nuclear Magnetic Resonance Spectroscopy, 86-87, 41–64. https://doi.org/10.1016/j.pnmrs.2015.02.004

Burmann, Björn M., Holdbrook, Daniel A., Callon, Morgane, Bond, Peter J., & Hiller, Sebastian. (2015). Revisiting the interaction between the chaperone Skp and lipopolysaccharide. Biophysical Journal, 108(6), 26–1516. https://doi.org/10.1016/j.bpj.2015.01.029

Gruss, Fabian, Hiller, Sebastian, & Maier, Timm. (2015). Purification and Bicelle Crystallization for Structure Determination of the E. coli Outer Membrane Protein TamA. Methods in Molecular Biology, 1329, 70–259. https://doi.org/10.1007/978-1-4939-2871-2_20

Jakob, Roman P., Koch, Johanna R., Burmann, Björn M., Schmidpeter, Philipp A. M., Hunkeler, Moritz, Hiller, Sebastian, Schmid, Franz X., & Maier, Timm. (2015). Dimeric structure of the bacterial extracellular foldase PrsA. Journal of Biological Chemistry, 290(6), 3278–3292. https://doi.org/10.1074/jbc.m114.622910

Lori, Christian, Ozaki, Shogo, Steiner, Samuel, Böhm, Raphael, Abel, Sören, Dubey, Badri N., Schirmer, Tilman, Hiller, Sebastian, & Jenal, Urs. (2015). Cyclic di-GMP acts as a cell cycle oscillator to drive chromosome replication. Nature, 523(7559), 9–236. https://doi.org/10.1038/nature14473

Maier, Timm, Clantin, Bernard, Gruss, Fabian, Dewitte, Frédérique, Delattre, Anne-Sophie, Jacob-Dubuisson, Françoise, Hiller, Sebastian, & Villeret, Vincent. (2015). Conserved Omp85 lid-lock structure and substrate recognition in FhaC. Nature Communications, 6, 7452. https://doi.org/10.1038/ncomms8452

Morgado, Leonor, Zeth, Kornelius, Burmann, Björn M., Maier, Timm, & Hiller, Sebastian. (2015). Characterization of the insertase BamA in three different membrane mimetics by solution NMR spectroscopy. Journal of Biomolecular NMR, 61(3-4), 45–333. https://doi.org/10.1007/s10858-015-9906-y

Sborgi, Lorenzo, Ravotti, Francesco, Dandey, Venkata Prasad, Dick, Mathias S., Mazur, Adam, Reckel, Sina, Chami, Mohamed, Scherer, Sebastian, Huber, Matthias, Böckmann, Anja, Egelman, Edward H., Stahlberg, Henning, Broz, Petr, Meier, Beat H., & Hiller, Sebastian. (2015). Structure and assembly of the mouse ASC inflammasome by combined NMR spectroscopy and cryo-electron microscopy. Proceedings of the National Academy of Sciences of the United States of America, 112(43), 42–13237. https://doi.org/10.1073/pnas.1507579112

Thoma, Johannes, Burmann, Björn M., Hiller, Sebastian, & Müller, Daniel J. (2015). Impact of holdase chaperones Skp and SurA on the folding of β-barrel outer-membrane proteins. Nature Structural & Molecular Biology, 22(10), 795–802. https://doi.org/10.1038/nsmb.3087

Callon, Morgane, Burmann, Björn M., & Hiller, Sebastian. (2014). Structural mapping of a chaperone-substrate interaction surface. Angewandte Chemie. International Edition in English, 53(20), 72–5069. https://doi.org/10.1002/anie.201310963

Etzkorn, Manuela, Zoonens, Manuel, Catoire, Laurent J., Popot, Jean-Luc, & Hiller, Sebastian. (2014). How amphipols embed membrane proteins : global solvent accessibility and interaction with a flexible protein terminus. The Journal of Membrane Biology, 247(9-10), 965–970. https://doi.org/10.1007/s00232-014-9657-9

Kentner, David, Martano, Giuseppe, Callon, Morgane, Chiquet, Petra, Brodmann, Maj, Burton, Olga, Wahlander, Asa, Nanni, Paolo, Delmotte, Nathanaël, Grossmann, Jonas, Limenitakis, Julien, Schlapbach, Ralph, Kiefer, Patrick, Vorholt, Julia A., Hiller, Sebastian, & Bumann, Dirk. (2014). Shigella reroutes host cell central metabolism to obtain high-flux nutrient supply for vigorous intracellular growth. Proceedings of the National Academy of Sciences of the United States of America, 111(27), 34–9929. https://doi.org/10.1073/pnas.1406694111

Schnarwiler, Felix, Niemann, Moritz, Doiron, Nicholas, Harsman, Anke, Käser, Sandro, Mani, Jan, Chanfon, Astrid, Dewar, Caroline E., Oeljeklaus, Silke, Jackson, Christopher B., Pusnik, Mascha, Schmidt, Oliver, Meisinger, Chris, Hiller, Sebastian, Warscheid, Bettina, Schnaufer, Achim C., Ochsenreiter, Torsten, & Schneider, André. (2014). Trypanosomal TAC40 constitutes a novel subclass of mitochondrial β-barrel proteins specialized in mitochondrial genome inheritance. Proceedings of the National Academy of Sciences of the United States of America, 111(21), 9–7624. https://doi.org/10.1073/pnas.1404854111