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Müntener, T., Joss, D., Häussinger, D. and Hiller, S. (2022) ‘Pseudocontact Shifts in Biomolecular NMR Spectroscopy’, Chemical Reviews, p. in press. 10.1021/acs.chemrev.1c00796.   edoc
Agustoni, E., Teixeira, R. D., Huber, M., Flister, S., Hiller, S. and Schirmer, T. (2022) ‘Acquisition of enzymatic progress curves in real time by quenching-free ion exchange chromatography’, Analytical biochemistry, 639, p. 114523. 10.1016/j.ab.2021.114523.   edoc
Shyp, V., Dubey, B. N., Böhm, R., Hartl, J., Nesper, J., Vorholt, J. A., Hiller, S., Schirmer, T. and Jenal, U. (2021) ‘Reciprocal growth control by competitive binding of nucleotide second messengers to a metabolic switch in Caulobacter crescentus’, Nature Microbiology, 6(1), pp. 59–72. 10.1038/s41564-020-00809-4.   edoc
Hiller, S. (2021) ‘Molecular chaperones and their denaturing effect on client proteins’, Journal of Biomolecular NMR, 75(1), pp. 1–8. 10.1007/s10858-020-00353-7.   edoc | Open Access
Ude, J., Tripathi, V., Buyck, J. M., Söderholm, S., Cunrath, O., Fanous, J., Claudi, B., Egli, A., Schleberger, C., Hiller, S. and Bumann, D. (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), p. e2107644118. 10.1073/pnas.2107644118.   edoc | Open Access
Ritzmann, N., Manioglu, S., Hiller, S. and Müller, D. J. (2021) ‘Monitoring the antibiotic darobactin modulating the β-barrel assembly factor BamA’, Structure, 30(March), pp. 1–10. 10.1016/j.str.2021.11.004.   edoc | Open Access
Ried, M. K., Wild, R., Zhu, J., Pipercevic, J., Sturm, K., Broger, L., Harmel, R. K., Abriata, L. A., Hothorn, L. A., Fiedler, D., Hiller, S. and Hothorn, M. (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), p. 384. 10.1038/s41467-020-20681-4.   edoc | Open Access
Hiller, S. and Broz, P. (2021) ‘Active membrane rupture spurs a range of cell deaths’, Nature, 591(7848), pp. 36–37. 10.1038/d41586-021-00297-4.   edoc
He, W., Yu, G., Li, T., Bai, L., Yang, Y., Xue, Z., Pang, Y., Reichmann, D., Hiller, S., He, L., Liu, M. and Quan, S. (2021) ‘Chaperone Spy Protects Outer Membrane Proteins from Folding Stress via Dynamic Complex Formation’, mBio, 12(5), p. e0213021. 10.1128/mBio.02130-21.   edoc | Open Access
Böhringer, N., Green, R., Liu, Y., Mettal, U., Marner, M., Modaresi, S. M., Jakob, R. P., Wuisan, Z. G., Maier, T., Iinishi, A., Hiller, S., Lewis, K. and Schäberle, T. F. (2021) ‘Mutasynthetic Production and Antimicrobial Characterization of Darobactin Analogs’, Microbiology spectrum, 9(3), p. e0153521. 10.1128/spectrum.01535-21.   edoc | Open Access
Macošek, J., Mas, G. and Hiller, S. (2021) ‘Redefining Molecular Chaperones as Chaotropes’, Frontiers in molecular biosciences, 8, p. 683132. 10.3389/fmolb.2021.683132.   edoc | Open Access
Vavassori, S., Chou, J., Faletti, L. E., Haunerdinger, V., Opitz, L., Joset, P., Fraser, C. J., Prader, S., Gao, X., Schuch, L. A., Wagner, M., Hoefele, J., Maccari, M. E., Zhu, Y., Elakis, G., Gabbett, M. T., Forstner, M., Omran, H., Kaiser, T., Kessler, C., Olbrich, H., Frosk, P., Almutairi, A., Platt, C. D., Elkins, M., Weeks, S., Rubin, T., Planas, R., Marchetti, T., Koovely, D., Klämbt, V., Soliman, N. A., von Hardenberg, S., Klemann, C., Baumann, U., Lenz, D., Klein-Franke, A., Schwemmle, M., Huber, M., Sturm, E., Hartleif, S., Häffner, K., Gimpel, C., Brotschi, B., Laube, G., Güngör, T., Buckley, M. F., Kottke, R., Staufner, C., Hildebrandt, F., Reu-Hofer, S., Moll, S., Weber, A., Kaur, H., Ehl, S., Hiller, S., Geha, R., Roscioli, T., Griese, M. and Pachlopnik Schmid, J. (2021) ‘Multisystem inflammation and susceptibility to viral infections in human ZNFX1 deficiency’, The Journal of Allergy & Clinical Immunology, 148(2), pp. 381–393. 10.1016/j.jaci.2021.03.045.   edoc | Open Access
Pérez-Schindler, J., Kohl, B., Schneider-Heieck, K., Leuchtmann, A. B., Henríquez-Olguín, C., Adak, V., Maier, G., Delezie, J., Sakoparnig, T., Vargas-Fernández, E., Karrer-Cardel, B., Ritz, D., Schmidt, A., Hondele, M., Jensen, T. E., Hiller, S. and Handschin, C. (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), p. e2105951118. 10.1073/pnas.2105951118.   edoc | Open Access
Kaur, H., Jakob, R. P., Marzinek, J. K., Green, R., Imai, Y., Bolla, J. R., Agustoni, E., Robinson, C. V., Bond, P. J., Lewis, K., Maier, T. and Hiller, S. (2021) ‘The antibiotic darobactin mimics a β-strand to inhibit outer membrane insertase’, Nature, 593(7857), pp. 125–129. 10.1038/s41586-021-03455-w.   edoc
Pipercevic, J., Jakob, R. P., Righetto, R. D., Goldie, K. N., Stahlberg, H., Maier, T. and Hiller, S. (2021) ‘Identification of a Dps contamination in Mitomycin-C-induced expression of Colicin Ia’, Biochimica et Biophysica Acta (BBA) - Biomembranes, 1863(7), p. 183607. 10.1016/j.bbamem.2021.183607.   edoc
Gray, D. A., White, J. B. R., Oluwole, A. O., Rath, P., Glenwright, A. J., Mazur, A., Zahn, M., Baslé, A., Morland, C., Evans, S. L., Cartmell, A., Robinson, C. V., Hiller, S., Ranson, N. A., Bolam, D. N. and van den Berg, B. (2021) ‘Insights into SusCD-mediated glycan import by a prominent gut symbiont’, Nature Communications, 12(1), p. 44. 10.1038/s41467-020-20285-y.   edoc
Böhm, R., Imseng, S., Jakob, R. P., Hall, M. N., Maier, T. and Hiller, S. (2021) ‘The dynamic mechanism of 4E-BP1 recognition and phosphorylation by mTORC1’, Molecular Cell, 81(11), pp. 2403–2416.e5. 10.1016/j.molcel.2021.03.031.   edoc
Kaur, H., Grahl, A., Hartmann, J.-B. and Hiller, S. (2020) ‘Sample Preparation and Technical Setup for NMR Spectroscopy with Integral Membrane Proteins’, Methods in Molecular Biology, 2127, pp. 373–396. 10.1007/978-1-0716-0373-4_24.   edoc
Kohl, B., Brüderlin, M., Ritz, D., Schmidt, A. and Hiller, S. (2020) ‘Protocol for High-Yield Production of Photo-Leucine-Labeled Proteins in Escherichia coli’, Journal of Proteome Research, 19(8), pp. 3100–3108. 10.1021/acs.jproteome.0c00105.   edoc | Open Access
Bibow, S., Böhm, R., Modaresi, S. M. and Hiller, S. (2020) ‘Detergent Titration as an Efficient Method for NMR Resonance Assignments of Membrane Proteins in Lipid-Bilayer Nanodiscs’, Analytical Chemistry, 92(11), pp. 7786–7793. 10.1021/acs.analchem.0c00917.   edoc
Zhang, B., Liu, X., Lambert, E., Mas, G., Hiller, S., Veening, J.-W. and Perez, C. (2020) ‘Structure of a proton-dependent lipid transporter involved in lipoteichoic acids biosynthesis’, Nature Structural and Molecular Biology, 27, pp. 561–569. 10.1038/s41594-020-0425-5.   edoc
Müntener, T., Böhm, R., Atz, K., Häussinger, D. and Hiller, S. (2020) ‘NMR pseudocontact shifts in a symmetric protein homotrimer’, Journal of Biomolecular NMR, 74(8-9), pp. 413–419. 10.1007/s10858-020-00329-7.   edoc
Mas, G., Burmann, B. M., Sharpe, T., Claudi, B., Bumann, D. and Hiller, S. (2020) ‘Regulation of chaperone function by coupled folding and oligomerization’, Science advances, 6(43), p. eabc5822. 10.1126/sciadv.abc5822.   edoc | Open Access
Kaczmarczyk, A., Hempel, A. M., von Arx, C., Böhm, R., Dubey, B. N., Nesper, J., Schirmer, T., Hiller, S. and Jenal, U. (2020) ‘Precise Timing of Transcription by c-di-GMP Coordinates Cell Cycle and Morphogenesis in Caulobacter’, Nature Communications, 11(1), p. 816. 10.1038/s41467-020-14585-6.   edoc | Open Access
Böhm, R., Amodeo, G. F., Murlidaran, S., Chavali, S., Wagner, G., Winterhalter, M., Brannigan, G. and Hiller, S. (2020) ‘The Structural Basis for Low Conductance in the Membrane Protein VDAC upon β-NADH Binding and Voltage Gating’, Structure, 28(2), pp. 206–214.e4. 10.1016/j.str.2019.11.015.   edoc
Burmann, B. M., Gerez, J. A., Matečko-Burmann, I., Campioni, S., Kumari, P., Ghosh, D., Mazur, A., Aspholm, E. E., Šulskis, D., Wawrzyniuk, M., Bock, T., Schmidt, A., Rüdiger, S. G. D., Riek, R. and Hiller, S. (2020) ‘Regulation of α-synuclein by chaperones in mammalian cells’, Nature, 577, pp. 127–132. 10.1038/s41586-019-1808-9.   edoc
Rath, P., Sharpe, T. and Hiller, S. (2020) ‘The electrostatic core of the outer membrane protein X from E. coli’, Biochimica et Biophysica Acta (BBA) - Biomembranes, 1862(1), p. 183031. 10.1016/j.bbamem.2019.183031.   edoc
Orton, H. W., Stanek, J., Schubeis, T., Foucaudeau, D., Ollier, C., Draney, A. W., Le Marchand, T., Cala-De Paepe, D., Felli, I. C., Pierattelli, R., Hiller, S., Bermel, W. and Pintacuda, G. (2020) ‘Protein NMR resonance assignment without spectral analysis: 5D SOlid-State Automated Projection SpectroscopY (SO-APSY)’, Angewandte Chemie International Edition, 59(6), pp. 2380–2384. 10.1002/anie.201912211.   edoc
Dubey, B. N., Agustoni, E., Böhm, R., Kaczmarczyk, A., Mangia, F., von Arx, C., Jenal, U., Hiller, S., Plaza-Menacho, I. and Schirmer, T. (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), pp. 1000–1008. 10.1073/pnas.1911427117.   edoc | Open Access
Mas, G., Thoma, J. and Hiller, S. (2019) ‘The Periplasmic Chaperones Skp and SurA’, in Kuhn, A. (ed.) Bacterial Cell Walls and Membranes. Cham: Springer Nature (Subcellular Biochemistry), pp. 169–186. 10.1007/978-3-030-18768-2_6.   edoc
Mazur, A., Broz, P. and Hiller, S. (2019) ‘An integrative protocol for the structure determination of the mouse ASC-PYD filament’, in Sohn, J. (ed.) Methods in Enzymology. New York: Elsevier, pp. 205–222. 10.1016/bs.mie.2019.04.033.   edoc
He, L. and Hiller, S. (2019) ‘Frustrated Interfaces Facilitate Dynamic Interactions between Native Client Proteins and Holdase Chaperones’, Chembiochem : a European journal of chemical biology, 20(22), pp. 2803–2806. 10.1002/cbic.201900215.   edoc
Kaur, H., Hartmann, J.-B., Jakob, R. P., Zahn, M., Zimmermann, I., Maier, T., Seeger, M. A. and Hiller, S. (2019) ‘Identification of conformation-selective nanobodies against the membrane protein insertase BamA by an integrated structural biology approach’, Journal of Biomolecular NMR, 73, pp. 375–384. 10.1007/s10858-019-00250-8.   edoc
Luther, A., Urfer, M., Zahn, M., Müller, M., Wang, S.-Y., Mondal, M., Vitale, A., Hartmann, J.-B., Sharpe, T., Monte, F. L., Kocherla, H., Cline, E., Pessi, G., Rath, P., Modaresi, S. M., Chiquet, P., Stiegeler, S., Verbree, C., Remus, T., Schmitt, M., Kolopp, C., Westwood, M.-A., Desjonquères, N., Brabet, E., Hell, S., LePoupon, K., Vermeulen, A., Jaisson, R., Rithié, V., Upert, G., Lederer, A., Zbinden, P., Wach, A., Moehle, K., Zerbe, K., Locher, H. H., Bernardini, F., Dale, G. E., Eberl, L., Wollscheid, B., Hiller, S., Robinson, J. A. and Obrecht, D. (2019) ‘Chimeric peptidomimetic antibiotics against Gram-negative bacteria’, Nature, 576(7787), pp. 452–458. 10.1038/s41586-019-1665-6.   edoc
Imai, Y., Meyer, K. J., Iinishi, A., Favre-Godal, Q., Green, R., Manuse, S., Caboni, M., Mori, M., Niles, S., Ghiglieri, M., Honrao, C., Ma, X., Guo, J. J., Makriyannis, A., Linares-Otoya, L., Böhringer, N., Wuisan, Z. G., Kaur, H., Wu, R., Mateus, A., Typas, A., Savitski, M. M., Espinoza, J. L., O’Rourke, A., Nelson, K. E., Hiller, S., Noinaj, N., Schäberle, T. F., D’Onofrio, A. and Lewis, K. (2019) ‘A new antibiotic selectively kills Gram-negative pathogens’, Nature, 576(7787), pp. 459–464. 10.1038/s41586-019-1791-1.   edoc
Rath, P., Sharpe, T., Kohl, B. and Hiller, S. (2019) ‘Two-state folding of the outer membrane protein X into a lipid bilayer membrane’, Angewandte Chemie International Edition, 58(9), pp. 2665–2669. 10.1002/anie.201812321.   edoc | Open Access
Hiller, S. (2019) ‘Chaperone-Bound Clients: The Importance of Being Dynamic’, Trends in Biochemical Sciences, 44(6), pp. 517–527. 10.1016/j.tibs.2018.12.005.   edoc | Open Access
Sborgi, L., Ude, J., Dick, M. S., Vesin, J., Chambon, M., Turcatti, G., Broz, P. and Hiller, S. (2018) ‘Assay for high-throughput screening of inhibitors of the ASC-PYD inflammasome core filament’, Cell Stress, 2(4), pp. 82–90. 10.15698/cst2018.04.131.   edoc
He, L. and Hiller, S. (2018) ‘Common Patterns in Chaperone Interactions with a Native Client Protein’, Angewandte Chemie International Edition, 57(20), pp. 5921–5924. 10.1002/anie.201713064.   edoc
Mas, G. and Hiller, S. (2018) ‘Conformational plasticity of molecular chaperones involved in periplasmic and outer membrane protein folding’, FEMS Microbiology Letters, 365(13), p. fny121. 10.1093/femsle/fny121.   edoc
Mulvihill, E., Sborgi, L., Mari, S. A., Pfreundschuh, M., Hiller, S. and Müller, D. J. (2018) ‘Mechanism of membrane pore formation by human gasdermin-D’, The EMBO journal, 37(14), p. e98321. 10.15252/embj.201798321.   edoc
Hartmann, J.-B., Zahn, M., Burmann, I. M., Bibow, S. and Hiller, S. (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), pp. 11252–11260. 10.1021/jacs.8b03220.   edoc
Bibow, S. and Hiller, S. (2018) ‘A guide to quantifying membrane protein dynamics in lipids and other native-like environments by solution-state NMR spectroscopy’, The FEBS journal, pp. 1–14. 10.1111/febs.14639.   edoc
Frey, L., Hiller, S., Riek, R. and Bibow, S. (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), pp. 15402–15411. 10.1021/jacs.8b09188.   edoc
Heilig, R., Dick, M. S., Sborgi, L., Meunier, E., Hiller, S. and Broz, P. (2018) ‘The Gasdermin-D pore acts as a conduit for IL-1β secretion in mice’, European journal of immunology, 48(4), pp. 584–592. 10.1002/eji.201747404.   edoc
Melo, E., Oertle, P., Trepp, C., Meistermann, H., Burgoyne, T., Sborgi, L., Cabrera, A. C., Chen, C.-Y., Hoflack, J.-C., Kam-Thong, T., Schmucki, R., Badi, L., Flint, N., Ghiani, Z. E., Delobel, F., Stucki, C., Gromo, G., Einhaus, A., Hornsperger, B., Golling, S., Siebourg-Polster, J., Gerber, F., Bohrmann, B., Futter, C., Dunkley, T., Hiller, S., Schilling, O., Enzmann, V., Fauser, S., Plodinec, M. and Iacone, R. (2018) ‘HtrA1 Mediated Intracellular Effects on Tubulin Using a Polarized RPE Disease Model’., EBioMedicine, 27, pp. 258–274. 10.1016/j.ebiom.2017.12.011.   edoc
Hiller, S. and Burmann, B. M. (2018) ‘Chaperone-client complexes: A dynamic liaison’, Journal of Magnetic Resonance, 289, pp. 142–155. 10.1016/j.jmr.2017.12.008.   edoc
Böhm, R., Wagner, G. and Hiller, S. (2017) ‘Solution Nuclear Magnetic Resonance Spectroscopy of Integral Membrane Proteins’, in Reference module in Life Sciences. New York: Elsevier, pp. 1–25. 10.1016/B978-0-12-809633-8.08077-8.   edoc
Thoma, J., Ritzmann, N., Wolf, D., Mulvihill, E., Hiller, S. and Müller, D. J. (2017) ‘Maltoporin LamB Unfolds β Hairpins along Mechanical Stress-Dependent Unfolding Pathways’, Structure, 25(7), pp. 1139–1144.e2. 10.1016/j.str.2017.05.010.   edoc
Holdbrook, D. A., Burmann, B. M., Huber, R. G., Petoukhov, M. V., Svergun, D. I., Hiller, S. and Bond, P. J. (2017) ‘A Spring-Loaded Mechanism Governs the Clamp-like Dynamics of the Skp Chaperone’, Structure, 25(7), pp. 1079–1088.e3. 10.1016/j.str.2017.05.018.   edoc
Morgado, L., Burmann, B. M., Sharpe, T., Mazur, A. and Hiller, S. (2017) ‘The dynamic dimer structure of the chaperone Trigger Factor’, Nature Communications, 8, p. 1992. 10.1038/s41467-017-02196-7.   edoc | Open Access
Sborgi, L., Rühl, S., Mulvihill, E., Pipercevic, J., Heilig, R., Stahlberg, H., Farady, C. J., Müller, D. J., Broz, P. and Hiller, S. (2016) ‘GSDMD membrane pore formation constitutes the mechanism of pyroptotic cell death’, The EMBO Journal, 35(16), pp. 1766–1778. 10.15252/embj.201694696.   edoc | Open Access
Raschle, T., Rios Flores, P., Opitz, C., Müller, D. J. and Hiller, S. (2016) ‘Monitoring Backbone Hydrogen-Bond Formation in β-Barrel Membrane Protein Folding’, Angewandte Chemie. International edition in English, 55(20), pp. 5952–5955. 10.1002/anie.201509910.   edoc | Open Access
He, L., Sharpe, T., Mazur, A. and Hiller, S. (2016) ‘A molecular mechanism of chaperone–client recognition’, Science Advances, 2(11), p. e1601625. 10.1126/sciadv.1601625.   edoc | Open Access
Zhong, F. L., Mamaï, O., Sborgi, L., Boussofara, L., Hopkins, R., Robinson, K., Szeverényi, I., Takeichi, T., Balaji, R., Lau, A., Tye, H., Roy, K., Bonnard, C., Ahl, P. J., Jones, L. A., Baker, P., Lacina, L., Otsuka, A., Fournie, P. R., Malecaze, F., Lane, E. B., Akiyama, M., Kabashima, K., Connolly, J. E., Masters, S. L., Soler, V. J., Omar, S. S., McGrath, J. A., Nedelcu, R., Gribaa, M., Denguezli, M., Saad, A., Hiller, S. and Reversade, B. (2016) ‘Germline NLRP1 Mutations Cause Skin Inflammatory and Cancer Susceptibility Syndromes via Inflammasome Activation’, Cell, 167(1), pp. 187–202.e17. 10.1016/j.cell.2016.09.001.   edoc
Ravotti, F., Sborgi, L., Cadalbert, R., Huber, M., Mazur, A., Broz, P., Hiller, S., Meier, B. H. and Böckmann, A. (2016) ‘Sequence-specific solid-state NMR assignments of the mouse ASC PYRIN domain in its filament form’, Biomolecular NMR Assignments, 10(1), pp. 107–115. 10.1007/s12104-015-9647-6.   edoc
Dick, M. S., Sborgi, L., Rühl, S., Hiller, S. and Broz, P. (2016) ‘ASC filament formation serves as a signal amplification mechanism for inflammasomes’, Nature Communications, 7, p. 11929. 10.1038/ncomms11929.   edoc | Open Access
Stanger, F. V., Burmann, B. M., Harms, A., Aragão, H., Mazur, A., Sharpe, T., Dehio, C., Hiller, S. and Schirmer, T. (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), pp. E529-E537. 10.1073/pnas.1516930113.   edoc | Open Access
Sborgi, L., Ravotti, F., Dandey, V. P., Dick, M. S., Mazur, A., Reckel, S., Chami, M., Scherer, S., Huber, M., Böckmann, A., Egelman, E. H., Stahlberg, H., Broz, P., Meier, B. H. and Hiller, S. (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), pp. 13237–13242. 10.1073/pnas.1507579112.   edoc | Open Access
Thoma, J., Burmann, B. M., Hiller, S. and Müller, D. J. (2015) ‘Impact of holdase chaperones Skp and SurA on the folding of β-barrel outer-membrane proteins’, Nature structural & molecular biology, 22(10), pp. 795–802. 10.1038/nsmb.3087.   edoc
Burmann, B. M. and Hiller, S. (2015) ‘Chaperones and chaperone-substrate complexes: dynamic playgrounds for NMR spectroscopists’, Progress in Nuclear Magnetic Resonance Spectroscopy, 86/87, pp. 41–64. 10.1016/j.pnmrs.2015.02.004.   edoc | Open Access
Gruss, F., Hiller, S. and Maier, T. (2015) ‘Purification and Bicelle Crystallization for Structure Determination of the E. coli Outer Membrane Protein TamA’, Methods in Molecular Biology, 1329, pp. 259–270. 10.1007/978-1-4939-2871-2_20.   edoc
Arquint, C., Gabryjonczyk, A.-M., Imseng, S., Böhm, R., Sauer, E., Hiller, S., Nigg, E. A. and Maier, T. (2015) ‘STIL binding to Polo-box 3 of PLK4 regulates centriole duplication’, eLife, 4, p. e07888. 10.7554/eLife.07888.   edoc | Open Access
Lori, C., Ozaki, S., Steiner, S., Böhm, R., Abel, S., Dubey, B. N., Schirmer, T., Hiller, S. and Jenal, U. (2015) ‘Cyclic di-GMP acts as a cell cycle oscillator to drive chromosome replication’, Nature, Vol. 523, H. 7559, pp. 236–239. 10.1038/nature14473.   edoc | Open Access
Brahimi-Horn, M. C., Lacas-Gervais, S., Adaixo, R., Ilc, K., Rouleau, M., Notte, A., Dieu, M., Michiels, C., Voeltzel, T., Maguer-Satta, V., Pelletier, J. ., Ilie, M., Hofman, P., Manoury, B., Schmidt, A., Hiller, S. ., Pouysségur, J. and Mazure, N. M. (2015) ‘Local mitochondrial-endolysosomal microfusion cleaves voltage-dependent anion channel 1 to promote survival in hypoxia’, Molecular and cellular biology, Vol. 35, H. 9, pp. 1491–1505. 10.1128/MCB.01402-14.   edoc
Burmann, B. M., Holdbrook, D. A., Callon, M., Bond, P. J. and Hiller, S. . (2015) ‘Revisiting the interaction between the chaperone Skp and lipopolysaccharide’, Biophysical journal, 108(6), pp. 1516–1526. 10.1016/j.bpj.2015.01.029.   edoc
Maier, T., Clantin, B., Gruss, F., Dewitte, F., Delattre, A.-S., Jacob-Dubuisson, F., Hiller, S. and Villeret, V. (2015) ‘Conserved Omp85 lid-lock structure and substrate recognition in FhaC’, Nature Communications, 6, p. 7452. 10.1038/ncomms8452.   edoc | Open Access
Morgado, L., Zeth, K., Burmann, B. M., Maier, T. and Hiller, S. . (2015) ‘Characterization of the insertase BamA in three different membrane mimetics by solution NMR spectroscopy’, Journal of biomolecular NMR, Vol. 61, H. 3-4, pp. 333–345. 10.1007/s10858-015-9906-y.   edoc
Jakob, R. P., Koch, J. R., Burmann, B. M., Schmidpeter, P. A. M., Hunkeler, M., Hiller, S., Schmid, F. X. and Maier, T. (2015) ‘Dimeric structure of the bacterial extracellular foldase PrsA’, Journal of Biological Chemistry, 290(6), pp. 3278–3292. 10.1074/jbc.M114.622910.   edoc | Open Access
Etzkorn, M., Zoonens, M., Catoire, L. J., Popot, J.-L. and Hiller, S. . (2014) ‘How amphipols embed membrane proteins : global solvent accessibility and interaction with a flexible protein terminus’, The journal of membrane biology, Vol. 247, H. 9-10, pp. 965–970.   edoc
Kentner, D., Martano, G., Callon, M., Chiquet, P., Brodmann, M., Burton, O., Wahlander, A., Nanni, P., Delmotte, N., Grossmann, J., Limenitakis, J., Schlapbach, R., Kiefer, P., Vorholt, J. A., Hiller, S. and Bumann, D. (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), pp. 9929–9934. 10.1073/pnas.1406694111.   edoc
Callon, M., Burmann, B. M. and Hiller, S. . (2014) ‘Structural mapping of a chaperone-substrate interaction surface’, Angewandte Chemie. International edition in English, Vol. 53, H. 20, pp. 5069–5072.   edoc
Schnarwiler, F., Niemann, M., Doiron, N., Harsman, A., Käser, S., Mani, J., Chanfon, A., Dewar, C. E., Oeljeklaus, S., Jackson, C. B., Pusnik, M., Schmidt, O., Meisinger, C., Hiller, S. ., Warscheid, B., Schnaufer, A. C., Ochsenreiter, T. and Schneider, A. (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, Vol. 111, H. 21, pp. 7624–7629. 10.1073/pnas.1404854111.   edoc
Gruss, F., Zähringer, F., Jakob, R. P., Burmann, B. M., Hiller, S. . and Maier, T. (2013) ‘The structural basis of autotransporter translocation by TamA’, Nature structural & molecular biology, Vol. 20, no. 11, pp. 1318–1320. 10.1038/nsmb.2689.   edoc
Burmann, B. M., Wang, C. and Hiller, S. (2013) ‘Conformation and dynamics of the periplasmic membrane-protein–chaperone complexes OmpX–Skp and tOmpA–Skp’, Nature structural & molecular biology, 20(11), pp. 1265–1272. 10.1038/nsmb.2677.   edoc
Hiller, S. . (2013) ‘The functional heart of the M2 channel’, Biophysical journal, Vol. 104, H. 8, pp. 1639–1640. 10.1016/j.bpj.2013.03.020.   edoc
Reckel, S. and Hiller, S. (2013) ‘Perspectives of Solution NMR Spectroscopy for Structural and Functional Studies of Integral Membrane Proteins’, Molecular physics, Vol. 111, H. 7, pp. 843–849. 10.1080/00268976.2013.783639.   edoc
Bühler, M. and Hiller, S. . (2012) ‘Dynamic nature of heterochromatin highlighted by a HP1(Swi6)-dependent gene silencing mechanism’, Cell cycle. Landes Bioscience, pp. 3907–3908. 10.4161/cc.22234.   edoc
Hiller, S. . and Wagner, G. (2012) ‘Solution NMR Spectroscopy of Integral Membrane Proteins’, in Comprehensive Biophysics. Burlington: Elsevier, pp. 120–138. 10.1016/B978-0-12-374920-8.00508-7.   edoc
Burmann, B. M. and Hiller, S. (2012) ‘Solution NMR studies of membrane-protein-chaperone complexes’, Chimia, 66(10), pp. 759–763. 10.2533/chimia.2012.759.   edoc | Open Access
Markley, J. L., Akutsu, H., Asakura, T., Baldus, M., Boelens, R., Bonvin, A., Kaptein, R., Bax, A., Bezsonova, I., Gryk, M. R., Hoch, J. C., Korzhnev, D. M., Maciejewski, M. W., Case, D., Chazin, W. J., Cross, T. A., Dames, S., Kessler, H., Lange, O., Madl, T., Reif, B., Sattler, M., Eliezer, D., Fersht, A., Forman-Kay, J., Kay, L. E., Fraser, J., Gross, J., Kortemme, T., Sali, A., Fujiwara, T., Gardner, K., Luo, X., Rizo-Rey, J., Rosen, M., Gil, R. R., Ho, C., Rule, G., Gronenborn, A. M., Ishima, R., Klein-Seetharaman, J., Tang, P., van der Wel, P., Xu, Y., Grzesiek, S., Hiller, S., Seelig, J., Laue, E. D., Mott, H., Nietlispach, D., Barsukov, I., Lian, L.-Y., Middleton, D., Blumenschein, T., Moore, G., Campbell, I., Schnell, J., Vakonakis, I. J., Watts, A., Conte, M. R., Mason, J., Pfuhl, M., Sanderson, M. R., Craven, J., Williamson, M., Dominguez, C., Roberts, G., Günther, U., Overduin, M., Werner, J., Williamson, P., Blindauer, C., Crump, M., Driscoll, P., Frenkiel, T., Golovanov, A., Matthews, S., Parkinson, J., Uhrin, D., Williams, M., Neuhaus, D., Oschkinat, H., Ramos, A., Shaw, D. E., Steinbeck, C., Vendruscolo, M., Vuister, G. W., Walters, K. J., Weinstein, H., Wüthrich, K. and Yokoyama, S. (2012) ‘In support of the BMRB’, Nature Structural and Molecular Biology, 19(9), pp. 854–860. 10.1038/nsmb.2371.   edoc
Keller, C., Adaixo, R., Stunnenberg, R., Woolcock, K. J., Hiller, S. . and Bühler, M. (2012) ‘HP1(Swi6) mediates the recognition and destruction of heterochromatic RNA transcripts’, Molecular cell, 47(2), pp. 215–227.   edoc
Harsman, A., Niemann, M., Pusnik, M., Schmidt, O., Burmann, B. M., Hiller, S. ., Meisinger, C., Schneider, A. and Wagner, R. (2012) ‘Bacterial origin of a mitochondrial outer membrane protein translocase : new perspectives from comparative single channel electrophysiology’, Journal of biological chemistry, Vol. 287, H. 37, pp. 31437–31445.   edoc
Hiller, S. . and Wider, G. (2012) ‘Automated projection spectroscopy and its applications’, Topics in current chemistry, Vol. 316, pp. 21–47.   edoc
Yu, T.-Y., Raschle, T., Hiller, S. . and Wagner, G. (2012) ‘Solution NMR spectroscopic characterization of human VDAC-2 in detergent micelles and lipid bilayer nanodiscs’, Biochimica et biophysica acta. BBA. Biomembranes, Vol. 1818, H. 6, pp. 1562–1569.   edoc
Huber, M., Böckmann, A., Hiller, S. . and Meier, B. H. (2012) ‘4D solid-state NMR for protein structure determination’, Physical Chemistry, Chemical Physics, 14(15), pp. 5239–5246. 10.1039/c2cp23872a.   edoc
Huber, M., Hiller, S., Schanda, P., Ernst, M., Böckmann, A., Verel, R. and Meier, B. H. (2011) ‘A proton-detected 4D solid-state NMR experiment for protein structure determination ’, ChemPhysChem, 12(5), pp. 915–918. 10.1002/cphc.201100062.   edoc
Krähenbühl, B., Hiller, S. . and Wider, G. (2011) ‘4D APSY-HBCB(CG)CDHD experiment for automated assignment of aromatic amino acid side chains in proteins’, Journal of biomolecular NMR, Vol. 51, pp. 313–318. 10.1007/s10858-011-9572-7.   edoc
Gossert, A. D., Hiller, S. . and Fernández, C. (2011) ‘Automated NMR resonance assignment of large proteins for protein-ligand interaction studies’, Journal of the American Chemical Society, Vol. 133, pp. 210–213. 10.1021/ja108383x.   edoc
Kräutler, V., Hiller, S. and Hünenberger, P. H. (2010) ‘Residual structure in a peptide fragment of the outer membrane protein X under denaturing conditions: a molecular dynamics study ’, European biophysics journal, 39(10), pp. 1421–1432. 10.1007/s00249-010-0596-9.   edoc
Takeuchi, K., Frueh, D. P., Sun, Z.-Y. J., Hiller, S. and Wagner, G. (2010) ‘CACA-TOCSY with alternate 13C-12C labeling: a 13Calpha direct detection experiment for mainchain resonance assignment, dihedral angle information, and amino acid type identification’, Journal of biomolecular NMR, 47(1), pp. 55–63. 10.1007/s10858-010-9410-3.   edoc
Hiller, S., Malia, T. J., Garces, R. G., Orekhov, V. Y. and Wagner, G. (2010) ‘Backbone and ILV side chain methyl group assignments of the integral human membrane protein VDAC-1’, Biomolecular NMR Assignments, 4(1), pp. 29–32. 10.1007/s12104-009-9194-0.   edoc
Hiller, S. ., Abramson, J. ., Mannella, C., Wagner, G. and Zeth, K. (2010) ‘The 3D structures of VDAC represent a native conformation’, Trends in biochemical sciences, Vol. 35, pp. 514–521. 10.1016/j.tibs.2010.03.005.   edoc
Raschle, T., Hiller, S. ., Etzkorn, M. and Wagner, G. (2010) ‘Nonmicellar systems for solution NMR spectroscopy of membrane proteins’, Current Opinion in Structural Biology, Vol. 20, pp. 471–479. 10.1016/   edoc
Raschle, T., Hiller, S., Yu, T.-Y., Rice, A. J., Walz, T. and Wagner, G. (2009) ‘Structural and functional characterization of the integral membrane protein VDAC-1 in lipid bilayer nanodiscs’, The journal of the American Chemical Society, 131(49), pp. 17777–17779. 10.1021/ja907918r.   edoc
Hiller, S., Ibraghimov, I., Wagner, G. and Orekhov, V. Y. (2009) ‘Coupled decomposition of four-dimensional NOESY spectra’, The journal of the American Chemical Society, 131(36), pp. 12970–12978. 10.1021/ja902012x.   edoc
Hiller, S. and Wagner, G. (2009) ‘The role of solution NMR in the structure determinations of VDAC-1 and other membrane proteins’, Current opinion in structural biology, 19(4), pp. 396–401. 10.1016/   edoc
Hiller, S., Arthanari, H. and Wagner, G. (2009) ‘The T-lock: automated compensation of radio-frequency induced sample heating’, Journal of biomolecular NMR, 44(2), pp. 69–76. 10.1007/s10858-009-9319-x.   edoc
Hiller, S., Wider, G. and Wüthrich, K. (2008) ‘APSY-NMR with proteins: practical aspects and backbone assignment’, Journal of biomolecular NMR, 42(3), pp. 179–195. 10.1007/s10858-008-9266-y.   edoc
Hiller, S., Joss, R. and Wider, G. (2008) ‘Automated NMR assignment of protein side chain resonances using automated projection spectroscopy (APSY)’, The journal of the American Chemical Society, 130(36), pp. 12073–12079. 10.1021/ja803161d.   edoc
Hiller, S., Garces, R. G., Malia, T. J., Orekhov, V. Y., Colombini, M. and Wagner, G. (2008) ‘Solution structure of the integral human membrane protein VDAC-1 in detergent micelles’, Science, 321(5893), pp. 1206–1210. 10.1126/science.1161302.   edoc
Suzuki, C., Garces, R. G., Edmonds, K. A., Hiller, S., Hyberts, S. G., Marintchev, A. and Wagner, G. (2008) ‘PDCD4 inhibits translation initiation by binding to eIF4A using both its MA3 domains’, Proceedings of the National Academy of Sciences of the United States of America, 105(9), pp. 3274–3279. 10.1073/pnas.0712235105.   edoc
Hiller, S., Wider, G., Imbach, L. L. and Wüthrich, K. (2008) ‘Interactions with hydrophobic clusters in the urea-unfolded membrane protein OmpX’, Angewandte Chemie. International edition in English, 47(5), pp. 977–981. 10.1002/anie.200703367.   edoc
Etezady-Esfarjani, T., Hiller, S., Villalba, C. and Wüthrich, K. (2007) ‘Cell-free protein synthesis of perdeuterated proteins for NMR studies ’, Journal of biomolecular NMR, 39(3), pp. 229–238. 10.1007/s10858-007-9188-0.   edoc
Hiller, S., Wasmer, C., Wider, G. and Wüthrich, K. (2007) ‘Sequence-specific resonance assignment of soluble nonglobular proteins by 7D APSY-NMR spectroscopy’, The journal of the American Chemical Society, 129(35), pp. 10823–10828. 10.1021/ja072564+.   edoc
Gossert, A. D., Hiller, S., Fiorito, F. and Wüthrich, K. (2007) ‘NMR assignment of the E. coli type 1 pilus protein FimF’, Journal of biomolecular NMR, 38(2), pp. 195–195. 10.1007/s10858-006-9123-9.   edoc
Fiorito, F., Hiller, S., Wider, G. and Wüthrich, K. (2006) ‘Automated resonance assignment of proteins: 6D APSY-NMR’, Journal of biomolecular NMR, 35(1), pp. 27–37. 10.1007/s10858-006-0030-x.   edoc | Open Access
Hiller, S., Fiorito, F., Wüthrich, K. and Wider, G. (2005) ‘Automated projection spectroscopy (APSY)’, Proceedings of the National Academy of Sciences of the United States of America, 102(31), pp. 10876–10881. 10.1073/pnas.0504818102.   edoc
Hiller, S., Wider, G., Etezady-Esfarjani, T., Horst, R. and Wüthrich, K. (2005) ‘Managing the solvent water polarization to obtain improved NMR spectra of large molecular structures’, Journal of biomolecular NMR, 32(1), pp. 61–70. 10.1007/s10858-005-3070-8.   edoc | Open Access
Tafer, H., Hiller, S., Hilty, C., Fernández, C. and Wüthrich, K. (2004) ‘Nonrandom structure in the urea-unfolded Escherichia coli outer membrane protein X (OmpX)’, Biochemistry, 43(4), pp. 860–869. 10.1021/bi0356606.   edoc | Open Access
Hiller, S., Kohl, A., Fiorito, F., Herrmann, T., Wider, G., Tschopp, J., Grütter, M. G. and Wüthrich, K. (2003) ‘NMR structure of the apoptosis- and inflammation-related NALP1 pyrin domain ’, Structure, 11(10), pp. 1199–1205. 10.1016/j.str.2003.08.009.   edoc | Open Access