Prof. Dr. Timm Maier

Chancellor, Andrew, Constantin, Daniel, Berloffa, Giuliano, Yang, Qinmei, Nosi, Vladimir, Loureiro, José Pedro, Colombo, Rodrigo, Jakob, Roman P., Joss, Daniel, Pfeffer, Michael, De Simone, Giulia, Morabito, Aurelia, Schaefer, Verena, Vacchini, Alessandro, Brunelli, Laura, Montagna, Daniela, Heim, Markus, Zippelius, Alfred, Davoli, Enrico, et al. (2024). The carbonyl nucleobase adduct M3Ade is a potent antigen for adaptive polyclonal MR1-restricted T cells [Journal-article]. Immunity, Online ahead of print. https://doi.org/10.1016/j.immuni.2024.11.019

Morita, Iori, Faraone, Adriana, Salvisberg, Elias, Zhang, Kailin, Jakob, Roman P., Maier, Timm, & Ward, Thomas R. (2024). Directed Evolution of an Artificial Hydroxylase Based on a Thermostable Human Carbonic Anhydrase Protein [Journal-article]. ACS Catalysis, 14, 17171–17179. https://doi.org/10.1021/acscatal.4c04163

Mukherjee, Manjistha, Waser, Valerie, Morris, Elinor F., Igareta, Nico V., Follmer, Alec H., Jakob, Roman P., Maier, Timm, Üzümcü, Dilbirin, & Ward, Thomas R. (2024). Artificial Peroxidase Based on the Biotin–Streptavidin Technology that Rivals the Efficiency of Natural Peroxidases. ACS Catalysis, 14(21), 16266–16276. https://doi.org/10.1021/acscatal.4c03208

Battaglioni, Stefania, Craigie, Louise-Marie, Filippini, Sofia, Maier, Timm, & Hall, Michael N. (2024). mTORC1 phosphorylates and stabilizes LST2 to negatively regulate EGFR [Journal-article]. Proceedings of the National Academy of Sciences, 121(34). https://doi.org/10.1073/pnas.2405959121

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

Chen, Dongping, Zhang, Xiang, Vorobieva, Anastassia Andreevna, Tachibana, Ryo, Stein, Alina, Jakob, Roman P., Zou, Zhi, Graf, Damian Alexander, Li, Ang, Maier, Timm, Correia, Bruno E., & Ward, Thomas R. (2024). An evolved artificial radical cyclase enables the construction of bicyclic terpenoid scaffolds via an H-atom transfer pathway [Journal-article]. Nature Chemistry, 16(10), 1656–1664. https://doi.org/10.1038/s41557-024-01562-5

Kaczmarczyk, Andreas, van Vliet, Simon, Jakob, Roman Peter, Dias Teixeira, Raphael, Scheidat, Inga, Reinders, Alberto, Klotz, Alexander, Maier, Timm, & Jenal, Urs. (2024). A genetically encoded biosensor to monitor dynamic changes of c-di-GMP with high temporal resolution. Nature Communications, 15. https://doi.org/10.1038/s41467-024-48295-0

Höing, Lars, Sowa, Sven T., Toplak, Marina, Reinhardt, Jakob K., Jakob, Roman, Maier, Timm, Lill, Markus A., & Teufel, Robin. (2024). Biosynthesis of the bacterial antibiotic 3,7-dihydroxytropolone through enzymatic salvaging of catabolic shunt products [Journal-article]. Chemical Science, 15(20), 7749–7756. https://doi.org/10.1039/d4sc01715c

Nemli, Dilara D., Jiang, Xiaohua, Jakob, Roman P., Gloder, Laura Muñoz, Schwardt, Oliver, Rabbani, Said, Maier, Timm, Ernst, Beat, & Cramer, Jonathan. (2024). Thermodynamics-Guided Design Reveals a Cooperative Hydrogen Bond in DC-SIGN-targeted Glycomimetics. Journal of Medicinal Chemistry, 67(16), 13813–13828. https://doi.org/10.1021/acs.jmedchem.4c00623

Wagner, Beatrice, Smieško, Martin, Jakob, Roman P., Mühlethaler, Tobias, Cramer, Jonathan, Maier, Tim, Rabbani, Said, Schwardt, Oliver, & Ernst, Beat. (2024). Analogues of the pan-selectin antagonist rivipansel (GMI-1070). European Journal of Medicinal Chemistry, 272. https://doi.org/10.1016/j.ejmech.2024.116455

Yu, K., Zhang, K., Jakob, R. P., Maier, T., & Ward, T. R. (2024). An artificial nickel chlorinase based on the biotin–streptavidin technology [Journal-article]. Chemical Communications, 60, 1944–1947. https://doi.org/10.1039/d3cc05847f

Mukherjee, Manjistha, Waser, Valerie, Igareta, Nico V., Follmer, Alec H., jakob, Roman P., Maier, Timm, Üzümcü, Dilbirin, & Ward, Thomas R. (2023). An Artificial Peroxidase based on the Biotin-Streptavidin Technology that Rivals the Efficiency of Natural Peroxidases [Posted-content]. In ChemRxiv. Cambridge University Press. https://doi.org/10.26434/chemrxiv-2023-s830k

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

Isaikina, Polina, Petrovic, Ivana, Jakob, Roman P., Sarma, Parishmita, Ranjan, Ashutosh, Baruah, Minakshi, Panwalkar, Vineet, Maier, Timm, Shukla, Arun K., & Grzesiek, Stephan. (2023). A key GPCR phosphorylation motif discovered in arrestin2⋅CCR5 phosphopeptide complexes. Molecular cell, 83(12), 2108–2121. https://doi.org/10.1016/j.molcel.2023.05.002

Shimobayashi, Mitsugu, Shetty, Sunil, Frei, Irina C., Wölnerhanssen, Bettina K., Weissenberger, Diana, Weissenberger, Diana, Dietz, Nikolaus, Thomas, Amandine, Ritz, Danilo, Meyer-Gerspach, Anne Christin, Maier, Timm, Hay, Nissim, Peterli, Ralph, Rohner, Nicolas, & Hall, Michael N. (2023). Diet-induced loss of adipose hexokinase 2 correlates with hyperglycemia. eLife, 12, e85103. https://doi.org/10.7554/elife.85103

Isaikina, Polina, Petrovic, Ivana, Jakob, Roman P., Sarma, Parishmita, Ranjan, Ashutosh, Baruah, Minakshi, Panwalkar, Vineet, Maier, Timm, Shukla, Arun K., & Grzesiek, Stephan. (2022). A key GPCR phosphorylation motif discovered in arrestin2•CCR5 phosphopeptide complexes [Posted-content]. bioRxiv. https://doi.org/10.1101/2022.10.10.511578

Kaczmarczyk, Andreas, van Vliet, Simon, Jakob, Roman Peter, Reinders, Alberto, Klotz, Alexander, Maier, Timm, & Jenal, Urs. (2022). A Novel Biosensor Reveals Dynamic Changes of C-di-GMP in Differentiating Cells with Ultra-High Temporal Resolution [Posted-content]. bioRxiv. https://doi.org/10.1101/2022.10.18.512705

Battaglioni, Stefania, Benjamin, Don, Wälchli, Matthias, Maier, Timm, & Hall, Michael N. (2022). mTOR substrate phosphorylation in growth control. Cell, 185(11), 1814–1836. https://doi.org/10.1016/j.cell.2022.04.013

Chaker-Margot, Malik, Werten, Sebastiaan, Dunzendorfer-Matt, Theresia, Lechner, Stefan, Ruepp, Angela, Scheffzek, Klaus, & Maier, Timm. (2022). Structural basis of activation of the tumor suppressor protein neurofibromin. Molecular Cell, 82(7), 1288–1296. https://doi.org/10.1016/j.molcel.2022.03.011

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

Mohammed, Inayathulla, Schmitz, Kai A., Schenck, Niko, Balasopoulos, Dimitrios, Topitsch, Annika, Maier, Timm, & Abrahams, Jan Pieter. (2022). Catalytic cycling of human mitochondrial Lon protease. Structure, 30(9), 1254–1268. https://doi.org/10.1016/j.str.2022.06.006

Tittes, Yves U., Herbst, Dominik A., Martin, Solène F. X., Munoz-Hernandez, Hugo, Jakob, Roman P., & Maier, Timm. (2022). The structure of a polyketide synthase bimodule core. Science Advances, 8(38), eabo6918. https://doi.org/10.1126/sciadv.abo6918

Zhang, Lei, Toplak, Marina, Saleem-Batcha, Raspudin, Höing, Lars Simon, Jakob, Roman, Jehmlich, Nico, von Bergen , Martin, Maier, Timm, & Teufel, Robin. (2022). Bacterial Dehydrogenases Facilitate Oxidative Inactivation and Bioremediation of Chloramphenicol. ChemBioChem, 24(2), e202200632. https://doi.org/10.1002/cbic.202200632

Mohammed, Inayathulla, Schmitz, Kai A., Schenck, Niko, Topitsch, Annika, Maier, Timm, & Abrahams, Jan Pieter. (2021). Catalytic cycling of human mitochondrial Lon protease [Posted-content]. bioRxiv. https://doi.org/10.1101/2021.07.28.454137

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

Cramer, Jonathan, Lakkaichi, Adem, Aliu, Butrint, Jakob, Roman P., Klein, Sebastian, Cattaneo, Ivan, Jiang, Xiaohua, Rabbani, Said, Schwardt, Oliver, Zimmer, Gert, Ciancaglini, Matias, Abreu Mota, Tiago, Maier, Timm, & Ernst, Beat. (2021). Sweet Drugs for Bad Bugs: A Glycomimetic Strategy against the DC-SIGN-Mediated Dissemination of SARS-CoV-2. Journal of the American Chemical Society, 143(42), 17465–17478. https://doi.org/10.1021/jacs.1c06778

Isaikina, Polina, Tsai, Ching-Ju, Dietz, Nikolaus, Pamula, Filip, Grahl, Anne, Goldie, Kenneth N., Guixà-González, Ramon, Branco, Camila, Paolini-Bertrand, Marianne, Calo, Nicolas, Cerini, Fabrice, Schertler, Gebhard F. X., Hartley, Oliver, Stahlberg, Henning, Maier, Timm, Deupi, Xavier, & Grzesiek, Stephan. (2021). Structural basis of the activation of the CC chemokine receptor 5 by a chemokine agonist. Science Advances, 7(25), eabg8685. https://doi.org/10.1126/sciadv.abg8685

Jia, Jian-Jun, Lahr, Roni M., Solgaard, Michael T., Moraes, Bruno J., Pointet, Roberta, Yang, An-Dao, Celucci, Giovanna, Graber, Tyson E., Hoang, Huy-Dung, Niklaus, Marius R., Pena, Izabella A., Hollensen, Anne K., Smith, Ewan M., Chaker-Margot, Malik, Anton, Leonie, Dajadian, Christopher, Livingstone, Mark, Hearnden, Jaclyn, Wang, Xu-Dong, et al. (2021). mTORC1 promotes TOP mRNA translation through site-specific phosphorylation of LARP1. Nucleic Acids Research, 49(6), 3461–3489. https://doi.org/10.1093/nar/gkaa1239

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

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

Tomašič, Tihomir, Rabbani, Said, Jakob, Roman P., Reisner, Andreas, Jakopin, Žiga, Maier, Timm, Ernst, Beat, & Anderluh, Marko. (2021). Does targeting Arg98 of FimH lead to high affinity antagonists? European Journal of Medicinal Chemistry, 211, 113093. https://doi.org/10.1016/j.ejmech.2020.113093

Wälchli, Matthias, Berneiser, Karolin, Mangia, Francesca, Imseng, Stefan, Craigie, Louise-Marie, Stuttfeld, Edward, Hall, Michael N., & Maier, Timm. (2021). Regulation of human mTOR complexes by DEPTOR. eLife, 10, e70871. https://doi.org/10.7554/elife.70871

Isaikina, Polina, Tsai, Ching-Ju, Dietz, Nikolaus, Pamula, Filip, Grahl, Anne, Goldie, Kenneth N., Guixà-González, Ramon, Schertler, Gebhard F.X., Hartley, Oliver, Stahlberg, Henning, Maier, Timm, Deupi, Xavier, & Grzesiek, Stephan. (2020). Structural basis of the activation of the CC chemokine receptor 5 by a chemokine agonist [Posted-content]. bioRxiv. https://doi.org/10.1101/2020.11.27.401117

Brunner, Janine D., Jakob, Roman P., Schulze, Tobias, Neldner, Yvonne, Moroni, Anna, Thiel, Gerhard, Maier, Timm, & Schenck, Stephan. (2020). Structural basis for ion selectivity in TMEM175 K+ channels. eLife, 9, 53683. https://doi.org/10.7554/elife.53683

Cramer, Jonathan, Jiang, Xiaohua, Schönemann, Wojciech, Silbermann, Marleen, Zihlmann, Pascal, Siegrist, Stefan, Fiege, Brigitte, Jakob, Roman Peter, Rabbani, Said, Maier, Timm, & Ernst, Beat. (2020). Enhancing the enthalpic contribution of hydrogen bonds by solvent shielding. RSC Chemical Biology, 1(4), 281–287. https://doi.org/10.1039/d0cb00108b

Künzli, Marco, Schreiner, David, Pereboom, Tamara C., Swarnalekha, Nivedya, Litzler, Ludivine C., Lötscher, Jonas, Ertuna, Yusuf I., Roux, Julien, Geier, Florian, Jakob, Roman P., Maier, Timm, Hess, Christoph, Taylor, Justin J., & King, Carolyn G. (2020). Long-lived T follicular helper cells retain plasticity and help sustain humoral immunity. Science Immunology, 5(45), eaay5552. https://doi.org/10.1126/sciimmunol.aay5552

Perez, Camilo, & Maier, Timm. (2020). Expression, Purification, and Structural Biology of Membrane Proteins. In Methods in Molecular Biology (1 ed., Vol. 2127). Humana Press. https://doi.org/10.1007/978-1-0716-0373-4

Righetto, Ricardo D., Anton, Leonie, Adaixo, Ricardo, Jakob, Roman P., Zivanov, Jasenko, Mahi, Mohamed-Ali, Ringler, Philippe, Schwede, Torsten, Maier, Timm, & Stahlberg, Henning. (2020). High-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica. Nature Communications, 11(1), 5101. https://doi.org/10.1038/s41467-020-18870-2

Righetto, Ricardo D., Anton, Leonie, Adaixo, Ricardo, Jakob, Roman P., Zivanov, Jasenko, Mahi, Mohamed-Ali, Ringler, Philippe, Schwede, Torsten, Maier, Timm, & Stahlberg, Henning. (2020). Author Correction: High-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica. Nature Communications, 11(1), 5873. https://doi.org/10.1038/s41467-020-19845-z

Scaiola, Alain, Mangia, Francesca, Imseng, Stefan, Boehringer, Daniel, Berneiser, Karolin, Shimobayashi, Mitsugu, Stuttfeld, Edward, Hall, Michael N., Ban, Nenad, & Maier, Timm. (2020). The 3.2-Å resolution structure of human mTORC2. Science advances, 6(45), eabc1251. https://doi.org/10.1126/sciadv.abc1251

Shimobayashi, Mitsugu, Shetty, Sunil, Frei, Irina C., Wölnerhanssen, Bettina K., Weissenberger, Diana, Dietz, Nikolaus, Thomas, Amandine, Ritz, Danilo, Meyer-Gerspach, Anne Christin, Maier, Timm, Hay, Nissim, Peterli, Ralph, Rohner, Nicolas, & Hall, Michael N. (2020). Diet-induced loss of adipose Hexokinase 2 triggers hyperglycemia. bioRxiv. https://doi.org/10.1101/2019.12.28.887794

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

Sauer, Maximilian M., Jakob, Roman P., Luber, Thomas, Canonica, Fabia, Navarra, Giulio, Ernst, Beat, Unverzagt, Carlo, Maier, Timm, & Glockshuber, Rudi. (2019). Binding of the bacterial adhesin FimH to its natural, multivalent high-mannose type glycan targets. Journal of the American Chemical Society, 141(2), 936–944. https://doi.org/10.1021/jacs.8b10736

Schönemann, Wojciech, Cramer, Jonathan, Mühlethaler, Tobias, Fiege, Brigitte, Silbermann, Marleen, Rabbani, Said, Dätwyler, Philipp, Zihlmann, Pascal, Jakob, Roman P., Sager, Christoph P., Smiesko, Martin, Schwardt, Oliver, Maier, Timm, & Ernst, Beat. (2019). Improvement of Aglycone π-Stacking Yields Nano- to Subnanomolar FimH Antagonists. ChemMedChem, 14(7), 749–757. https://doi.org/10.1002/cmdc.201900051

Brunner, Janine D., Jakob, Roman P., Schulze, Tobias, Neldner, Yvonne, Moroni, Anna, Thiel, Gerhard, Maier, Timm, & Schenck, Stephan. (2018). Structural basis for ion selectivity in TMEM175 K+ channels [Posted-content]. bioRxiv. https://doi.org/10.1101/480863

Vigano, M. Alessandra, Bieli, Dimitri, Schaefer, Jonas V., Peter Jakob, Roman, Matsuda, Shinya, Maier, Timm, Plückthun, Andreas, & Affolter, Markus. (2018). DARPins recognizing mTFP1 as novel reagents for in vitro and in vivo protein manipulations [Posted-content]. bioRxiv. https://doi.org/10.1101/354134

Bauer, Daniela, Meinhold, Sarah, Jakob, Roman P., Stigler, Johannes, Merkel, Ulrich, Maier, Timm, Rief, Matthias, & Žoldák, Gabriel. (2018). A folding nucleus and minimal ATP binding domain of Hsp70 identified by single-molecule force spectroscopy. Proceedings of the National Academy of Sciences of the United States of America, 115(18), 4666–4671. https://doi.org/10.1073/pnas.1716899115

Herbst, Dominik A., Huitt-Roehl, Callie R., Jakob, Roman P., Kravetz, Jacob M., Storm, Philip A., Alley, Jamie R., Townsend, Craig A., & Maier, Timm. (2018). The structural organization of substrate loading in iterative polyketide synthases. Nature Chemical Biology, 14(5), 474–479. https://doi.org/10.1038/s41589-018-0026-3

Herbst, Dominik A., Townsend, Craig A., & Maier, Timm. (2018). The architectures of iterative type I PKS and FAS. Natural Product Reports, 35(10), 1046–1069. https://doi.org/10.1039/c8np00039e

Hunkeler, Moritz, Hagmann, Anna, Stuttfeld, Edward, Chami, Mohamed, Guri, Yakir, Stahlberg, Henning, & Maier, Timm. (2018). Structural basis for regulation of human acetyl-CoA carboxylase. Nature, 558(7710), 470–474. https://doi.org/10.1038/s41586-018-0201-4

Imseng, Stefan, Aylett, Christopher Hs, & Maier, Timm. (2018). Architecture and activation of phosphatidylinositol 3-kinase related kinases. Current Opinion in Structural Biology, 49, 177–189. https://doi.org/10.1016/j.sbi.2018.03.010

Maier, Timm, & Weissman, Kira J. (2018). Macromolecular assemblies: Assembly, dynamics and control of activity. Current Opinion in Structural Biology, 49, vi–vii. https://doi.org/10.1016/j.sbi.2018.04.001

Rabbani, Said, Fiege, Brigitte, Eris, Deniz, Silbermann, Marleen, Jakob, Roman Peter, Navarra, Giulio, Maier, Timm, & Ernst, Beat. (2018). Conformational Switch of the Bacterial Adhesin FimH in the Absence of the Regulatory Domain: Engineering a Minimalistic Allosteric System. Journal of Biological Chemistry, 293(5), 1835–1849. https://doi.org/10.1074/jbc.m117.802942

Sager, Christoph P., Fiege, Brigitte, Zihlmann, Pascal, Vannam, Raghu, Rabbani, Said, Jakob, Roman P., Preston, Roland C., Zalewski, Adam, Maier, Timm, Peczuh, Mark W., & Ernst, Beat. (2018). The price of flexibility - a case study on septanoses as pyranose mimetics. Chemical Science, 9(3), 646–654. https://doi.org/10.1039/c7sc04289b

Stuttfeld, E., Aylett, C. H. S., Imseng, S., Boehringer, D., Scaiola, A., Sauer, E., Hall, M. N., Maier, T., & Ban, N. (2018). Architecture of the human mTORC2 core complex. eLife, 7, e33101. https://doi.org/10.7554/elife.33101

Vigano, M. Alessandra, Bieli, Dimitri, Schaefer, Jonas V., Jakob, Roman Peter, Matsuda, Shinya, Maier, Timm, Plückthun, Andreas, & Affolter, Markus. (2018). DARPins recognizing mTFP1 as novel reagents for in vitro and in vivo protein manipulations. Biology Open, 7(11), bio036749. https://doi.org/10.1242/bio.036749

Vigano, M. Alessandra, Bieli, Dimitri, Schaefer, Jonas V., Jakob, Roman P., Matsuda, Shinya, Maier, Timm, Plückthun, Andreas, & Affolter, Markus. (2018). Correction:DARPins recognizing mTFP1 as novel reagents for in vitro; and in vivo protein manipulations. Biology Open, 7(12), bio036749. https://doi.org/10.1242/bio.040832

Zihlmann, Pascal, Silbermann, Marleen, Sharpe, Timothy, Jiang, Xiaohua, Mühlethaler, Tobias, Jakob, Roman P., Rabbani, Said, Sager, Christoph P., Frei, Priska, Pang, Lijuan, Maier, Timm, & Ernst, Beat. (2018). KinITC-One Method Supports both Thermodynamic and Kinetic SARs as Exemplified on FimH Antagonists. Chemistry (Weinheim an Der Bergstrasse, Germany), 24(49), 13049–13057. https://doi.org/10.1002/chem.201802599

Anton, Leonie, Sborgi, Lorenzo, Hiller, Sebastian, Broz, Petr, & Maier, Timm. (2017). Insights into Gasdermin D activation from the crystal structure of its C-terminal domain [Posted-content]. bioRxiv. https://doi.org/10.1101/187211

Benning, Friederike M. C., Sakiyama, Yusuke, Mazur, Adam, Bukhari, Habib S. T., Lim, Roderick Y. H., & Maier, Timm. (2017). High-Speed Atomic Force Microscopy Visualization of the Dynamics of the Multienzyme Fatty Acid Synthase. ACS Nano, 11(11), 10852–10859. https://doi.org/10.1021/acsnano.7b04216

Maier, Timm. (2017). Fatty acid synthases: Re-engineering biofactories. Nature Chemical Biology, 13(4), 344–345. https://doi.org/10.1038/nchembio.2338

Navarra, Giulio, Zihlmann, Pascal, Jakob, Roman P., Stangier, Katia, Preston, Roland C., Rabbani, Said, Smiesko, Martin, Wagner, Bea, Maier, Timm, & Ernst, Beat. (2017). Carbohydrate-Lectin Interactions - An Unexpected Contribution to Affinity. ChemBioChem, 18(6), 539–544. https://doi.org/10.1002/cbic.201600615

Roth, Christian, Weizenmann, Nicole, Bexten, Nicola, Saenger, Wolfram, Zimmermann, Wolfgang, Maier, Timm, & Sträter, Norbert. (2017). Amylose recognition and ring-size determination of amylomaltase. Science Advances, 3(1), e1601386. https://doi.org/10.1126/sciadv.1601386

Storm, Philip A., Herbst, Dominik A., Maier, Timm, & Townsend, Craig A. (2017). Functional and Structural Analysis of Programmed C-Methylation in the Biosynthesis of the Fungal Polyketide Citrinin. Cell Chemical Biology, 24(3), 316–325. https://doi.org/10.1016/j.chembiol.2017.01.008

Stuttfeld, Edward, Imseng, Stefan, & Maier, Timm. (2017). A central role for a region in the middle. eLife, 6, e25700. https://doi.org/10.7554/elife.25700

Wang, Jing, Brackmann, Maximilian, Castaño-Díez, Daniel, Kudryashev, Mikhail, Goldie, Kenneth N., Maier, Timm, Stahlberg, Henning, & Basler, Marek. (2017). Cryo-EM structure of the extended type VI secretion system sheath-tube complex. Nature Microbiology, 2(11), 1507–1512. https://doi.org/10.1038/s41564-017-0020-7

Herbst, Dominik A., Jakob, Roman P., Zähringer, Franziska, & Maier, Timm. (2016). Erratum: Mycocerosic acid synthase exemplifies the architecture of reducing polyketide synthases (Nature (2016) 531 (533-537) DOI:10.1038/nature16993). Nature, 536(7616), 360. https://doi.org/10.1038/nature18281

Aylett, Christopher H. S., Sauer, Evelyn, Imseng, Stefan, Boehringer, Daniel, Hall, Michael N., Ban, Nenad, & Maier, Timm. (2016). Architecture of human mTOR complex 1. Science, 351(6268), 48–52. https://doi.org/10.1126/science.aaa3870

Hagmann, Anna, Hunkeler, Moritz, Stuttfeld, Edward, & Maier, Timm. (2016). Hybrid Structure of a Dynamic Single-Chain Carboxylase from Deinococcus radiodurans. Structure, 24(8), 1227–1236. https://doi.org/10.1016/j.str.2016.06.001

Herbst, Dominik A., Jakob, Roman P., Zähringer, Franziska, & Maier, Timm. (2016). Mycocerosic acid synthase exemplifies the architecture of reducing polyketide synthases. Nature, 531(7595), 533–537. https://doi.org/10.1038/nature16993

Hunkeler, Moritz, Stuttfeld, Edward, Hagmann, Anna, Imseng, Stefan, & Maier, Timm. (2016). The dynamic organization of fungal acetyl-CoA carboxylase. Nature Communications, 7, 11196. https://doi.org/10.1038/ncomms11196

Jakob, Roman P., Schmidpeter, Philipp A. M., Koch, Johanna R., Schmid, Franz X., & Maier, Timm. (2016). Structural and Functional Characterization of a Novel Family of Cyclophilins, the AquaCyps. PLoS ONE, 11(6), e0157070. https://doi.org/10.1371/journal.pone.0157070

Preston, Roland C., Jakob, Roman P., Binder, Florian P. C., Sager, Christoph P., Ernst, Beat, & Maier, Timm. (2016). E-selectin ligand complexes adopt an extended high-affinity conformation. Journal of Molecular Cell Biology, 8(1), 62–72. https://doi.org/10.1093/jmcb/mjv046

Sauer, Maximilian M, Jakob, Roman P, Eras, Jonathan, Baday, Sefer, Eriş, Deniz, Navarra, Giulio, Bernèche, Simon, Ernst, Beat, Maier, Timm, & Glockshuber, Rudi. (2016). Catch-bond mechanism of the bacterial adhesin FimH. Nature Communications, 7, 10738. https://doi.org/10.1038/ncomms10738

Silván, Unai, Hyotyla, Janne, Mannherz, Hans-Georg, Ringler, Philippe, Müller, Shirley A., Aebi, Ueli, Maier, Timm, & Schoenenberger, Cora-Ann. (2016). Contributions of the lower dimer to supramolecular actin patterning revealed by TIRF microscopy. Journal of Structural Biology, 195(2), 159–166. https://doi.org/10.1016/j.jsb.2016.05.008

Studer, G., Jakob, R. P., Mahi, M. A., Wiesand, U., Schwede, T., & Maier, T. (2016). Crystal structure of urease from Yersinia enterocolitica (Studer, Gabriel, Ed.) [Data set]. Worldwide Protein Data Bank. https://doi.org/10.2210/pdb4z42/pdb

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

Blatter, Markus, Dunin-Horkawicz, Stanislaw, Grishina, Irma, Maris, Christophe, Thore, Stephane, Maier, Timm, Bindereif, Albrecht, Bujnicki, Janusz M., & Allain, Frederic H. -T. (2015). The signature of the five-stranded vRRM fold defined by functional, structural and computational analysis of the hnRNP L protein. Journal of Molecular Biology, 427(19), 3001–3022. https://doi.org/10.1016/j.jmb.2015.05.020

Fiege, Brigitte, Rabbani, Said, Preston, Roland C., Jakob, Roman P., Zihlmann, Pascal, Schwardt, Oliver, Jiang, Xiaohua, Maier, Timm, & Ernst, Beat. (2015). The Tyrosine Gate of the Bacterial Lectin FimH : a Conformational Analysis by NMR Spectroscopy and X-ray Crystallography. ChemBioChem, 16(8), 1235–1246. https://doi.org/10.1002/cbic.201402714

Fujieda, Nobutaka, Schaetti, Jonas, Stuttfeld, Edward, Ohkubo, Kei, Maier, Timm, Fukuzumi, Shunichi, & Ward, Thomas R. (2015). Enzyme repurposing of a hydrolase as an emergent peroxidase upon metal binding. Chemical Science, 6(7), 4060–4065. https://doi.org/10.1039/c5sc01065a

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, 259–270. 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

Kleeb, Simon, Pang, Lijuan, Mayer, Katharina, Eris, Deniz, Sigl, Anja, Preston, Roland C., Zihlmann, Pascal, Sharpe, Timothy, Jakob, Roman P., Abgottspon, Daniela, Hutter, Aline S., Scharenberg, Meike, Jiang, Xiaohua, Navarra, Giulio, Rabbani, Said, Smiesko, Martin, Lüdin, Nathalie, Bezençon, Jacqueline, Schwardt, Oliver, et al. (2015). FimH Antagonists: Bioisosteres To Improve the in Vitro and in Vivo PK/PD Profile. Journal of Medicinal Chemistry, 58(5), 2221–2239. https://doi.org/10.1021/jm501524q

Kudryashev, Mikhail, Wang, Ray Yu-Ruei, Brackmann, Maximilian, Scherer, Sebastian, Maier, Timm, Baker, David, DiMaio, Frank, Stahlberg, Henning, Egelman, Edward H, & Basler, Marek. (2015). Structure of the Type VI Secretion System Contractile Sheath. Cell, 160(5), 952–962. https://doi.org/10.1016/j.cell.2015.01.037

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), 333–345. https://doi.org/10.1007/s10858-015-9906-y

Bukhari, Habib S. T., Jakob, Roman P., & Maier, Timm. (2014). Evolutionary origins of the multienzyme architecture of giant fungal Fatty Acid synthase. Structure, 22(12), 1775–1785. https://doi.org/10.1016/j.str.2014.09.016

Gruss, Fabian, Zähringer, Franziska, Jakob, Roman P., Burmann, Björn M., Hiller, Sebastian, & Maier, Timm. (2013). The structural basis of autotransporter translocation by TamA. Nature Structural & Molecular Biology, 20(11), 1318–U247. https://doi.org/10.1038/nsmb.2689

Sauer, Evelyn, Imseng, Stefan, Maier, Timm, & Hall, Michael N. (2013). Conserved sequence motifs and the structure of the mTOR kinase domain. Biochemical Society Transactions, 41(4), 889–895. https://doi.org/10.1042/bst20130113

Maier, T., Leibundgut, M., Boehringer, D., & Ban, N. (2010). Structure and function of eukaryotic fatty acid synthases. Quarterly Reviews of Biophysics, 43(3), 373–422. https://doi.org/10.1017/s0033583510000156

Mocibob, Marko, Ivic, Nives, Bilokapic, Silvija, Maier, Timm, Luic, Marija, Ban, Nenad, & Weygand-Durasevic, Ivana. (2010). Homologs of aminoacyl-tRNA synthetases acylate carrier proteins and provide a link between ribosomal and nonribosomal peptide synthesis. Proceedings of the National Academy of Sciences of the United States of America, 107(33), 14585–14590. https://doi.org/10.1073/pnas.1007470107

Mocibob, M., Ivic, N., Bilokapic, S., Maier, T., Luic, M., Ban, N., & Weygand-Durasevic, I. (2010). New links between protein biosynthesis and nonribosomal peptide synthesis. The FEBS Journal, 277, 260–261.

Müller, M., Grauschopf, U., Maier, T., Glockshuber, R., & Ban, N. (2009). The structure of a cytolytic alpha-helical toxin pore reveals its assembly mechanism. Nature, 459(7247), 726–U135. https://doi.org/10.1038/nature08026

Bingel-Erlenmeyer, R., Kohler, R., Kramer, G., Sandikci, A., Antolic, S., Maier, T., Schaffitzel, C., Wiedmann, B., Bukau, B., & Ban, N. (2008). A peptide deformylase-ribosome complex reveals mechanism of nascent chain processing. Nature, 452(7183), 108–U13. https://doi.org/10.1038/nature06683

Leibundgut, M., Maier, T., Jenni, S., & Ban, N. (2008). The multienzyme architecture of eukaryotic fatty acid synthases. Current Opinion in Structural Biology, 18(6), 714–725. https://doi.org/10.1016/j.sbi.2008.09.008

Maier, T., Leibundgut, M., & Ban, N. (2008). The crystal structure of a mammalian fatty acid synthase. Science, 321(5894), 1315–1322. https://doi.org/10.1126/science.1161269

Merz, F., Boehringer, D., Schaffitzel, C., Preissler, S., Hoffmann, A., Maier, T., Rutkowska, A., Lozza, J., Ban, N., Bukau, B., & Deuerling, E. (2008). Molecular mechanism and structure of Trigger Factor bound to the translating ribosome. The EMBO Journal, 27(11), 1622–1632. https://doi.org/10.1038/emboj.2008.89

Rossmann, M., Schultz-Heienbrok, R., Behlke, J., Remmel, N., Alings, C., Sandhoff, K., Saenger, W., & Maier, T. (2008). Crystal structures of human saposins C and D: Implications for lipid recognition and membrane interactions. Structure, 16(5), 809–817. https://doi.org/10.1016/j.str.2008.02.016

Bilokapic, S., Maier, T., Ahel, D., Gruic-Sovulj, I., Soll, D., Weygand-Durasevic, I., & Ban, N. (2006). Structure of the unusual seryl-tRNA synthetase reveals a distinct zinc-dependent mode of substrate recognition. The EMBO Journal, 25(11), 2498–2509. https://doi.org/10.1038/sj.emboj.7601129