Research
Regulation of microtubule structure and dynamics
Proteins and their interaction networks are at the heart of life. Understanding how diverse proteins come together spatially and temporally and how their specific complexes translate into cellular functions is important to understand health and disease but represents a major challenge. Microtubules are filamentous structures fundamentally involved in diverse cellular processes ranging from cell division, motility and polarity to signaling and intracellular transport. They are also key to form centrioles of centrosomes and axonemes of cilia and flagella. Because of their important role for cell survival, the malfunctioning of the microtubule cytoskeleton is associated with several severe human pathologies including cancer and various forms of ciliopathies as well as cardiovascular, infectious and brain diseases. We use X-ray crystallography in combination with biochemical and biophysical methods to investigate how proteins and drugs regulate the structure, function and dynamics of the microtubule cytoskeleton.
Control of microtubule organization and dynamics: the two ends in the limelight.
Akhmanova, A., Steinmetz, M.O.
Nat. Rev. Mol. Cell Biol., 16, 711-726 (2015).
Molecular Mechanism of Action of Microtubule-Stabilizing Anticancer Agents.
Prota, A.E., Bargsten, K., Zurwerra, D., Field, J.J., Díaz, J.F. Altmann, K.-H., Steinmetz, M.O.
Science, 339, 587-590 (2013).
Structural basis of the nine-fold symmetry of centrioles.
Kitagawa, D., Vakonakis, I., Olieric, N., Hilbert, M., Keller, D., Olieric, V., Bortfeld, M., Erat, M.C., Flückiger, I., Gönczy, P., Steinmetz, M.O.
Cell 144, 1-12 (2011).
An EB1-binding motif acts as a microtubule tip localization signal.
Honnappa, S., Montenegro Gouveia, S., Weisbrich, A., Damberger, F.F., Bhavesh, N.S., Jawhari, H., Grigoriev, I., van Rijssel, F.J.A., Buey, R.M., Lawera, A., Jelesarov, I., Winkler, F.K., Wüthrich, K., Akhmanova, A. and Steinmetz, M.O.
Cell 138, 366-376 (2009).
Members
Head a.i. Division Biology and Chemistry
Events and Scientific Highlights
Tobias published a paper “Comprehensive Analysis of Binding Sites in Tubulin” in Angew Chem Int Ed Engl
Tobias defended his PhD with "summa cum laude"
September 2020: Two-day hike on the Creux_du_Van and visit to the asphalt mines of La Presta (Val-de-Travers NE)
Sung and Natacha published a paper “Structural basis of tubulin detyrosination by the vasohibin-SVBP enzyme complex” in Nat Struct Mol Biol. (2019)
June 2019: Three-days retreat in the Teamlodge in Lenk im Simmenthal (Canton Bern)
May 2019: Andrea was awarded the Horizon 2020 MSCA-ITN EJD Grant TubInTrain (www.tubintrain.eu).
The TubInTrain network has participants from six European countries and encompasses ten academic groups and ten companies committed to creating an outstanding training program for thirteen early stage researchers (ESRs) to elucidate the mechanisms of neurodegeneration associated to microtubules structure and dynamics.
January 2018: Natacha and Ashwani were awarded a FreeNovation grant (www.novartis.ch)
Development of lead molecules against apicomplex parasites
Apicomplexa are single-celled parasites responsible for diseases such as malaria, toxoplasmosis and cryptosporidiosis. Based on structural information on a protein, which plays an important role in the cell division of the Apicomplexa, lead molecules for this protein should be identified in this project. The results obtained will provide a basis for the development of novel drugs for the control of multidrug-resistant parasites.
Previous Events
Publications since 2002
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Gaillard N, Sharma A, Abbaali I, Liu T, Shilliday F, Cook AD, et al.
Inhibiting parasite proliferation using a rationally designed anti-tubulin agent
EMBO Molecular Medicine. 2021; 13(11): e13818 (12 pp.). https://doi.org/10.15252/emmm.202013818
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Gao L, Meiring JCM, Kraus Y, Wranik M, Weinert T, Pritzl SD, et al.
A robust, GFP-orthogonal photoswitchable inhibitor scaffold extends optical control over the microtubule cytoskeleton
Cell Chemical Biology. 2021; 28(2): 228-241. https://doi.org/10.1016/j.chembiol.2020.11.007
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Ijavi M, Style RW, Emmanouilidis L, Kumar A, Meier SM, Torzynski AL, et al.
Surface tensiometry of phase separated protein and polymer droplets by the sessile drop method
Soft Matter. 2021; 17(6): 1655-1662. https://doi.org/10.1039/d0sm01319f
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Jernigan F, Branstrom A, Baird JD, Cao L, Dali M, Furia B, et al.
Preclinical and early clinical development of PTC596, a novel small-molecule tubulin-binding agent
Molecular Cancer Therapeutics. 2021; 20(10): 1846-1857. https://doi.org/10.1158/1535-7163.MCT-20-0774
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Kumar A, Meier SM, Farcas A-M, Manatschal C, Barral Y, Steinmetz MO
Structure and regulation of the microtubule plus-end tracking protein Kar9
Structure. 2021; 29(11): 1266-1278.e4. https://doi.org/10.1016/j.str.2021.06.012
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Mühlethaler T, Gioia D, Prota AE, Sharpe ME, Cavalli A, Steinmetz MO
Comprehensive analysis of binding sites in tubulin
Angewandte Chemie International Edition. 2021; 60(24): 13331-13342. https://doi.org/10.1002/anie.202100273
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Sharma A, Olieric N, Steinmetz MO
Centriole length control
Current Opinion in Structural Biology. 2021; 66: 89-95. https://doi.org/10.1016/j.sbi.2020.10.011
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Yong C, Devine SM, Abel A-C, Tomlins SD, Muthiah D, Gao X, et al.
1,3-benzodioxole-modified noscapine analogues: synthesis, antiproliferative activity, and tubulin-bound structure
ChemMedChem. 2021; 16(18): 2882-2894. https://doi.org/10.1002/cmdc.202100363
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Atherton J, Hummel JJA, Olieric N, Locke J, Peña A, Rosenfeld SS, et al.
The mechanism of kinesin inhibition by kinesin binding protein
eLife. 2020; 9: e61481 (30 pp.). https://doi.org/10.7554/eLife.61481
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Estévez-Gallego J, Josa-Prado F, Ku S, Buey RM, Balaguer FA, Prota AE, et al.
Structural model for differential cap maturation at growing microtubule ends
eLife. 2020; 9: e50155 (26 pp.). https://doi.org/10.7554/eLife.50155
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Fiedler T, Fabrice TN, Studer V, Vinet A, Faltova L, Kammerer RA, et al.
Homodimerization of coronin A through the C-terminal coiled-coil domain is essential for multicellular differentiation of Dictyostelium discoideum
FEBS Letters. 2020; 594(13): 2116-2127. https://doi.org/10.1002/1873-3468.13787
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Guo B, Rodriguez-Gabin A, Prota AE, Mühlethaler T, Zhang N, Ye K, et al.
Structural refinement of the tubulin ligand (+)-discodermolide to attenuate chemotherapy-mediated senescence
Molecular Pharmacology. 2020; 98(2): 156-167. https://doi.org/10.1124/mol.119.117457
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Jost M, Chen Y, Gilbert LA, Horlbeck MA, Krenning L, Menchon G, et al.
Pharmaceutical-grade rigosertib is a microtubule-destabilizing agent
Molecular Cell. 2020; 79(1): 191-198.e3. https://doi.org/10.1016/j.molcel.2020.06.008
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Nass K, Cheng R, Vera L, Mozzanica A, Redford S, Ozerov D, et al.
Advances in long-wavelength native phasing at X-ray free-electron lasers
IUCrJ. 2020; 7: 965-975. https://doi.org/10.1107/S2052252520011379
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Oliva MA, Prota AE, Rodríguez-Salarichs J, Bennani YL, Jiménez-Barbero J, Bargsten K, et al.
Structural basis of noscapine activation for tubulin binding
Journal of Medicinal Chemistry. 2020; 63(15): 8495-8501. https://doi.org/10.1021/acs.jmedchem.0c00855
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Rodríguez-García R, Volkov VA, Chen C-Y, Katrukha EA, Olieric N, Aher A, et al.
Mechanisms of motor-independent membrane remodeling driven by dynamic microtubules
Current Biology. 2020; 30(6): 972-987. https://doi.org/10.1016/j.cub.2020.01.036
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Steib E, Laporte MH, Gambarotto D, Olieric N, Zheng C, Borgers S, et al.
WDR90 is a centriolar microtubule wall protein important for centriole architecture integrity
eLife. 2020; 9: e57205 (28 pp.). https://doi.org/10.7554/ELIFE.57205
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Akhmanova A, Steinmetz MO
Microtubule minus-end regulation at a glance
Journal of Cell Science. 2019; 132(11): jcs227850 (7 pp.). https://doi.org/10.1242/jcs.227850
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Atherton J, Luo Y, Xiang S, Yang C, Rai A, Jiang K, et al.
Structural determinants of microtubule minus end preference in CAMSAP CKK domains
Nature Communications. 2019; 10(1): 5236 (16 pp.). https://doi.org/10.1038/s41467-019-13247-6
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Brindisi M, Ulivieri C, Alfano G, Gemma S, de Asís Balaguer F, Khan T, et al.
Structure-activity relationships, biological evaluation and structural studies of novel pyrrolonaphthoxazepines as antitumor agents
European Journal of Medicinal Chemistry. 2019; 162: 290-320. https://doi.org/10.1016/j.ejmech.2018.11.004
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Chen X, Widmer LA, Stangier MM, Steinmetz MO, Stelling J, Barral Y
Remote control of microtubule plus-end dynamics and function from the minus-end
eLife. 2019; 8: e48627 (32 pp.). https://doi.org/10.7554/eLife.48627
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Cury NM, Mühlethaler T, Laranjeira ABA, Canevarolo RR, Zenatti PP, Lucena-Agell D, et al.
Structural basis of colchicine-site targeting acylhydrazones active against multidrug-resistant acute lymphoblastic leukemia
iScience. 2019; 21: 95-109. https://doi.org/10.1016/j.isci.2019.10.003
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Dohle W, Prota AE, Menchon G, Hamel E, Steinmetz MO, Potter BVL
Tetrahydroisoquinoline sulfamates as potent microtubule disruptors: synthesis, antiproliferative and antitubulin activity of dichlorobenzyl-based derivatives, and a Tubulin cocrystal structure.
ACS Omega. 2019; 4: 755-764. https://doi.org/10.1021/acsomega.8b02879
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Dolenc J, van Gunsteren WF, Prota AE, Steinmetz MO, Missimer JH
Conformational properties of the chemotherapeutic drug analogue Epothilone A: how to model a flexible protein ligand using scarcely available experimental data
Journal of Chemical Information and Modeling. 2019; 59(5): 2218-2230. https://doi.org/10.1021/acs.jcim.9b00171
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Faltova L, Jiang K, Frey D, Wu Y, Capitani G, Prota AE, et al.
Crystal structure of a heterotetrameric katanin p60:p80 complex
Structure. 2019; 27(9): 1375-1383.e3. https://doi.org/10.1016/j.str.2019.07.002
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Hooikaas PJ, Martin M, Mühlethaler T, Kuijntjes G-J, Peeters CAE, Katrukha EA, et al.
MAP7 family proteins regulate kinesin-1 recruitment and activation
Journal of Cell Biology. 2019; 218(4): 1298-1318. https://doi.org/10.1083/jcb.201808065
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Kashyap AS, Fernandez-Rodriguez L, Zhao Y, Monaco G, Trefny MP, Yoshida N, et al.
GEF-H1 signaling upon microtubule destabilization is required for dendritic cell activation and specific anti-tumor responses
Cell Reports. 2019; 28(13): 3367-3380.e1. https://doi.org/10.1016/j.celrep.2019.08.057
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La Sala G, Olieric N, Sharma A, Viti F, de Asis Balaguer Perez F, Huang L, et al.
Structure, thermodynamics, and kinetics of plinabulin binding to two tubulin isotypes
Chem. 2019; 5(11): 2969-2986. https://doi.org/10.1016/j.chempr.2019.08.022
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Patterson JC, Joughin BA, Prota AE, Mühlethaler T, Jonas OH, Whitman MA, et al.
VISAGE reveals a targetable mitotic spindle vulnerability in cancer cells
Cell Systems. 2019; 9(1): 74-92.e8. https://doi.org/10.1016/j.cels.2019.05.009
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Rai A, Liu T, Glauser S, Katrukha EA, Estévez-Gallego J, Rodríguez-García R, et al.
Taxanes convert regions of perturbed microtubule growth into rescue sites
Nature Materials. 2019; 19: 355-365. https://doi.org/10.1038/s41563-019-0546-6
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Wang N, Bosc C, Ryul Choi S, Boulan B, Peris L, Olieric N, et al.
Structural basis of tubulin detyrosination by the vasohibin–SVBP enzyme complex
Nature Structural and Molecular Biology. 2019; 26(7): 571-582. https://doi.org/10.1038/s41594-019-0241-y
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de Asís Balaguer F, Mühlethaler T, Estévez-Gallego J, Calvo E, Giménez-Abián J, Risinger AL, et al.
Crystal structure of the cyclostreptin-tubulin adduct: implications for tubulin activation by taxane-site ligands
International Journal of Molecular Sciences. 2019; 20(6): 1392 (17 pp.). https://doi.org/10.3390/ijms20061392
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Aher A, Kok M, Sharma A, Rai A, Olieric N, Rodriguez-Garcia R, et al.
CLASP suppresses microtubule catastrophes through a single TOG domain
Developmental Cell. 2018; 46(1): 40-58.e8. https://doi.org/10.1016/j.devcel.2018.05.032
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Bianchi S, Rogala KB, Dynes NJ, Hilbert M, Leidel SA, Steinmetz MO, et al.
Interaction between the Caenorhabditis elegans centriolar protein SAS-5 and microtubules facilitates organelle assembly
Molecular Biology of the Cell. 2018; 29(6): 722-735. https://doi.org/10.1091/mbc.E17-06-0412
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Bueno O, Estévez Gallego J, Martins S, Prota AE, Gago F, Gómez-SanJuan A, et al.
High-affinity ligands of the colchicine domain in tubulin based on a structure-guided design
Scientific Reports. 2018; 8(1): 4242 (17 pp.). https://doi.org/10.1038/s41598-018-22382-x
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Dohle W, Jourdan FL, Menchon G, Prota AE, Foster PA, Mannion P, et al.
Quinazolinone-based anticancer agents: synthesis, antiproliferative SAR, antitubulin activity, and tubulin Co-crystal structure
Journal of Medicinal Chemistry. 2018; 61(3): 1031-1044. https://doi.org/10.1021/acs.jmedchem.7b01474
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Jiang K, Faltova L, Hua S, Capitani G, Prota AE, Landgraf C, et al.
Structural basis of formation of the microtubule minus-end-regulating CAMSAP-katanin complex
Structure. 2018; 26(3): 375-382. https://doi.org/10.1016/j.str.2017.12.017
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Kraatz SHW, Bianchi S, Steinmetz MO
Combinatorial use of disulfide bridges and native sulfur-SAD phasing for rapid structure determination of coiled-coils
Bioscience Reports. 2018; 38(5): BSR20181073 (11 pp.). https://doi.org/10.1042/BSR20181073
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Menchon G, Prota AE, Lucena-Agell D, Bucher P, Jansen R, Irschik H, et al.
A fluorescence anisotropy assay to discover and characterize ligands targeting the maytansine site of tubulin
Nature Communications. 2018; 9(1): 2106 (9 pp.). https://doi.org/10.1038/s41467-018-04535-8
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Sharma A, Gerard SF, Olieric N, Steinmetz MO
Cep120 promotes microtubule formation through a unique tubulin binding C2 domain
Journal of Structural Biology. 2018; 203(1): 62-70. https://doi.org/10.1016/j.jsb.2018.01.009
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Smedley CJ, Stanley PA, Qazzaz ME, Prota AE, Olieric N, Collins H, et al.
Sustainable syntheses of (-)-jerantinines A & E and structural characterisation of the jerantinine-tubulin complex at the colchicine binding site
Scientific Reports. 2018; 8(1): 10617 (7 pp.). https://doi.org/10.1038/s41598-018-28880-2
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Stangier MM, Kumar A, Chen X, Farcas A-M, Barral Y, Steinmetz MO
Structure-function relationship of the Bik1-Bim1 complex
Structure. 2018; 26(4): 607-618.e4. https://doi.org/10.1016/j.str.2018.03.003
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Steinmetz MO, Prota AE
Microtubule-targeting agents: strategies to hijack the cytoskeleton
Trends in Cell Biology. 2018; 28(10): 776-792. https://doi.org/10.1016/j.tcb.2018.05.001
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Atherton J, Jiang K, Stangier MM, Luo Y, Hua S, Houben K, et al.
A structural model for microtubule minus-end recognition and protection by CAMSAP proteins
Nature Structural and Molecular Biology. 2017; 24(11): 931-943. https://doi.org/10.1038/nsmb.3483
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Bohnacker T, Prota AE, Beaufils F, Burke JE, Melone A, Inglis AJ, et al.
Deconvolution of buparlisib's mechanism of action defines specific PI3K and tubulin inhibitors for therapeutic intervention
Nature Communications. 2017; 8: 14683 (13 pp.). https://doi.org/10.1038/ncomms14683
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Canela M-D, Noppen S, Bueno O, Prota AE, Bargsten K, Sáez-Calvo G, et al.
Antivascular and antitumor properties of the tubulin-binding chalcone TUB091
Oncotarget. 2017; 8(9): 14325-14342. https://doi.org/10.18632/oncotarget.9527
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Gaspari R, Prota AE, Bargsten K, Cavalli A, Steinmetz MO
Structural basis of cis- and trans-combretastatin binding to tubulin
Chem. 2017; 2(1): 102-113. https://doi.org/10.1016/j.chempr.2016.12.005
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Hamel V, Steib E, Hamelin R, Armand F, Borgers S, Flückiger I, et al.
Identification of Chlamydomonas central core centriolar proteins reveals a role for human WDR90 in ciliogenesis
Current Biology. 2017; 27(16): 2486-2498. https://doi.org/10.1016/j.cub.2017.07.011
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Jiang K, Rezabkova L, Hua S, Liu Q, Capitani G, Altelaar AFM, et al.
Microtubule minus-end regulation at spindle poles by an ASPM-katanin complex
Nature Cell Biology. 2017; 19(5): 480-492. https://doi.org/10.1038/ncb3511
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Jost M, Chen Y, Gilbert LA, Horlbeck MA, Krenning L, Menchon G, et al.
Combined CRISPRi/a-based chemical genetic screens reveal that rigosertib is a microtubule-destabilizing agent
Molecular Cell. 2017; 68(1): 210-223. https://doi.org/10.1016/j.molcel.2017.09.012
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Kumar A, Manatschal C, Rai A, Grigoriev I, Steiner Degen M, Jaussi R, et al.
Short linear sequence motif LxxPTPh targets diverse proteins to growing microtubule ends
Structure. 2017; 25(6): 924-932. https://doi.org/10.1016/j.str.2017.04.010
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Prota AE, Bargsten K, Redondo-Horcajo M, Smith AB, Yang C-PH, McDaid HM, et al.
Structural basis of microtubule stabilization by discodermolide
ChemBioChem. 2017; 18(10): 905-909. https://doi.org/10.1002/cbic.201600696
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Rezabkova L, Jiang K, Capitani G, Prota AE, Akhmanova A, Steinmetz MO, et al.
Structural basis of katanin p60:p80 complex formation
Scientific Reports. 2017; 7: 14893 (8 pp.). https://doi.org/10.1038/s41598-017-14194-2
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Sharma A, Sáez-Calvo G, Olieric N, de Asís Balaguer F, Barasoain I, Lamberth C, et al.
Quinolin-6-yloxyacetamides are microtubule destabilizing agents that bind to the colchicine site of tubulin
International Journal of Molecular Sciences. 2017; 18(7): 1336 (11 pp.). https://doi.org/10.3390/ijms18071336
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Sáez-Calvo G, Sharma A, de Asís Balaguer F, Barasoain I, Rodríguez-Salarichs J, Olieric N, et al.
Triazolopyrimidines are microtubule-stabilizing agents that bind the vinca inhibitor site of tubulin
Cell Chemical Biology. 2017; 24(6): 737-750. https://doi.org/10.1016/j.chembiol.2017.05.016
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Weinert T, Olieric N, Cheng R, Brünle S, James D, Ozerov D, et al.
Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons
Nature Communications. 2017; 8(1): 542 (11 pp.). https://doi.org/10.1038/s41467-017-00630-4
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van Riel WE, Rai A, Bianchi S, Katrukha EA, Liu Q, Heck AJR, et al.
Kinesin-4 KIF21B is a potent microtubule pausing factor
eLife. 2017; 6: e24746 (30 pp.). https://doi.org/10.7554/eLife.24746
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Bianchi S, van Riel WE, Kraatz SHW, Olieric N, Frey D, Katrukha EA, et al.
Structural basis for misregulation of kinesin KIF21A autoinhibition by CFEOM1 disease mutations
Scientific Reports. 2016; 6: 30668 (16 pp.). https://doi.org/10.1038/srep30668
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Burger D, Stihle M, Sharma A, Di Lello P, Benz J, D'Arcy B, et al.
Crystal structures of the human doublecortin C- and N-terminal domains in complex with specific antibodies
Journal of Biological Chemistry. 2016; 291(31): 16292-16306. https://doi.org/10.1074/jbc.M116.726547
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Doodhi H, Prota AE, Rodríguez-García R, Xiao H, Custar DW, Bargsten K, et al.
Termination of protofilament elongation by eribulin induces lattice defects that promote microtubule catastrophes
Current Biology. 2016; 26(13): 1713-1721. https://doi.org/10.1016/j.cub.2016.04.053
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Guesdon A, Bazile F, Buey RM, Mohan R, Monier S, García RR, et al.
EB1 interacts with outwardly curved and straight regions of the microtubule lattice
Nature Cell Biology. 2016; 18(10): 1102-1108. https://doi.org/10.1038/ncb3412
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Hilbert M, Noga A, Frey D, Hamel V, Guichard P, Kraatz SHW, et al.
SAS-6 engineering reveals interdependence between cartwheel and microtubules in determining centriole architecture
Nature Cell Biology. 2016; 18(4): 393-403. https://doi.org/10.1038/ncb3329
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Kevenaar JT, Bianchi S, van Spronsen M, Olieric N, Lipka J, Frias CP, et al.
Kinesin-binding protein controls microtubule dynamics and cargo trafficking by regulating kinesin motor activity
Current Biology. 2016; 26(7): 849-861. https://doi.org/10.1016/j.cub.2016.01.048
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Kraatz S, Guichard P, Obbineni JM, Olieric N, Hatzopoulos GN, Hilbert M, et al.
The human centriolar protein CEP135 contains a two-stranded coiled-coil domain critical for microtubule binding
Structure. 2016; 24(8): 1358-1371. https://doi.org/10.1016/j.str.2016.06.011
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Manatschal C, Farcas A-M, Degen MS, Bayer M, Kumar A, Landgraf C, et al.
Molecular basis of Kar9-Bim1 complex function during mating and spindle positioning
Molecular Biology of the Cell. 2016; 27(23): 3729-3745. https://doi.org/10.1091/mbc.E16-07-0552
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Olieric V, Weinert T, Finke AD, Anders C, Li D, Olieric N, et al.
Data-collection strategy for challenging native SAD phasing
Acta Crystallographica Section D: Structural Biology. 2016; 72(3): 421-429. https://doi.org/10.1107/S2059798315024110
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Prota AE, Setter J, Waight AB, Bargsten K, Murga J, Diaz JF, et al.
Pironetin binds covalently to αCys316 and perturbs a major loop and helix of α-tubulin to inhibit microtubule formation
Journal of Molecular Biology. 2016; 428(15): 2981-2988. https://doi.org/10.1016/j.jmb.2016.06.023
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Rezabkova L, Kraatz SHW, Akhmanova A, Steinmetz MO, Kammerer RA
Biophysical and structural characterization of the centriolar protein CEP104 interaction network
Journal of Biological Chemistry. 2016; 291(35): 18496-18504. https://doi.org/10.1074/jbc.M116.739771
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Sharma A, Aher A, Dynes NJ, Frey D, Katrukha EA, Jaussi R, et al.
Centriolar CPAP/SAS-4 imparts slow processive microtubule growth
Developmental Cell. 2016; 37(4): 362-376. https://doi.org/10.1016/j.devcel.2016.04.024
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Trigili C, Barasoain I, Sánchez-Murcia PA, Bargsten K, Redondo-Horcajo M, Nogales A, et al.
Structural determinants of the dictyostatin chemotype for tubulin binding affinity and antitumor activity against taxane- and epothilone-resistant cancer cells
ACS Omega. 2016; 1(6): 1192-1204. https://doi.org/10.1021/acsomega.6b00317
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Waight AB, Bargsten K, Doronina S, Steinmetz MO, Sussman D, Prota AE
Structural basis of microtubule destabilization by potent auristatin anti-mitotics
PLoS One. 2016; 11(8): e0160890 (14 pp.). https://doi.org/10.1371/journal.pone.0160890
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Wieczorek M, Tcherkezian J, Bernier C, Prota AE, Chaaban S, Rolland Y, et al.
The synthetic diazonamide DZ-2384 has distinct effects on microtubule curvature and dynamics without neurotoxicity
Science Translational Medicine. 2016; 8(365): 365ra159 (14 pp.). https://doi.org/10.1126/scitranslmed.aag1093
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Akhmanova A, Steinmetz MO
Control of microtubule organization and dynamics: two ends in the limelight
Nature Reviews Molecular Cell Biology. 2015; 16(12): 711-726. https://doi.org/10.1038/nrm4084
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Janke C, Steinmetz MO
Optochemistry to control the microtubule cytoskeleton
EMBO Journal. 2015; 34(16): 2114-2116. https://doi.org/10.15252/embj.201592415
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Weinert T, Olieric V, Waltersperger S, Panepucci E, Chen L, Zhang H, et al.
Fast native-SAD phasing for routine macromolecular structure determination
Nature Methods. 2015; 12(2): 131-133. https://doi.org/10.1038/nmeth.3211
DORA PSI -
Benoit RM, Frey D, Hilbert M, Kevenaar JT, Wieser MM, Stirnimann CU, et al.
Structural basis for recognition of synaptic vesicle protein 2C by botulinum neurotoxin A
Nature. 2014; 505(7481): 108-111. https://doi.org/10.1038/nature12732
DORA PSI -
Duellberg C, Trokter M, Jha R, Sen I, Steinmetz MO, Surrey T
Reconstitution of a hierarchical +TIP interaction network controlling microtubule end tracking of dynein
Nature Cell Biology. 2014; 16(8): 804-811. https://doi.org/10.1038/ncb2999
DORA PSI -
Khan MA, Rupp VM, Orpinell M, Hussain MS, Altmüller J, Steinmetz MO, et al.
A missense mutation in the PISA domain of HsSAS-6 causes autosomal recessive primary microcephaly in a large consanguineous Pakistani family
Human Molecular Genetics. 2014; 23(22): 5940-5949. https://doi.org/10.1093/hmg/ddu318
DORA PSI -
López MP, Huber F, Grigoriev I, Steinmetz MO, Akhmanova A, Koenderink GH, et al.
Actin-microtubule coordination at growing microtubule ends
Nature Communications. 2014; 5: 4778 (9 pp.). https://doi.org/10.1038/ncomms5778
DORA PSI -
Pfreundschuh M, Alsteens D, Hilbert M, Steinmetz MO, Müller DJ
Localizing chemical groups while imaging single native proteins by high-resolution atomic force microscopy
Nano Letters. 2014; 14(5): 2957-2964. https://doi.org/10.1021/nl5012905
DORA PSI -
Preciado López M, Huber F, Grigoriev I, Steinmetz MO, Akhmanova A, Dogterom M, et al.
In vitro reconstitution of dynamic microtubules interacting with actin filament networks
In: Vale RD, ed. Reconstituting the cytoskeleton. Methods in enzymology. Amsterdam: Elsevier; 2014:301-320. https://doi.org/10.1016/B978-0-12-397924-7.00017-0
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Prota AE, Bargsten K, Diaz JF, Marsh M, Cuevas C, Liniger M, et al.
A new tubulin-binding site and pharmacophore for microtubule-destabilizing anticancer drugs
Proceedings of the National Academy of Sciences of the United States of America PNAS. 2014; 111(38): 13817-13821. https://doi.org/10.1073/pnas.1408124111
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Prota AE, Bargsten K, Northcote PT, Marsh M, Altmann K-H, Miller JH, et al.
Structural basis of microtubule stabilization by laulimalide and peloruside A
Angewandte Chemie International Edition. 2014; 53(6): 1621-1625. https://doi.org/10.1002/anie.201307749
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Prota AE, Danel F, Bachmann F, Bargsten K, Buey RM, Pohlmann J, et al.
The novel microtubule-destabilizing drug BAL27862 binds to the colchicine site of tubulin with distinct effects on microtubule organization
Journal of Molecular Biology. 2014; 426(8): 1848-1860. https://doi.org/10.1016/j.jmb.2014.02.005
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Bjelić S, Wieser M, Frey D, Stirnimann CU, Chance MR, Jaussi R, et al.
Structural basis for the oligomerization-state switch from a dimer to a trimer of an engineered cortexillin-1 coiled-coil variant
PLoS One. 2013; 8(5): e63370 (7 pp.). https://doi.org/10.1371/journal.pone.0063370
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Guichard P, Hachet V, Majubu N, Neves A, Demurtas D, Olieric N, et al.
Native architecture of the centriole proximal region reveals features underlying its 9-fold radial symmetry
Current Biology. 2013; 23(17): 1620-1628. https://doi.org/10.1016/j.cub.2013.06.061
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Hilbert M, Erat MC, Hachet V, Guichard P, Blank ID, Flückiger I, et al.
Caenorhabditis elegans centriolar protein SAS-6 forms a spiral that is consistent with imparting a ninefold symmetry
Proceedings of the National Academy of Sciences of the United States of America PNAS. 2013; 110(28): 11373-11378. https://doi.org/10.1073/pnas.1302721110
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Mohan R, Katrukha EA, Doodhi H, Smal I, Meijering E, Kapitein LC, et al.
End-binding proteins sensitize microtubules to the action of microtubule-targeting agents
Proceedings of the National Academy of Sciences of the United States of America PNAS. 2013; 110(22): 8900-8905. https://doi.org/10.1073/pnas.1300395110
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Prota AE, Bargsten K, Zurwerra D, Field JJ, Díaz JF, Altmann K-H, et al.
Molecular mechanism of action of microtubule-stabilizing anticancer agents
Science. 2013; 339(6119): 587-590. https://doi.org/10.1126/science.1230582
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Prota AE, Magiera MM, Kuijpers M, Bargsten K, Frey D, Wieser M, et al.
Structural basis of tubulin tyrosination by tubulin tyrosine ligase
Journal of Cell Biology. 2013; 200(3): 259-270. https://doi.org/10.1083/jcb.201211017
DORA PSI -
Sen I, Veprintsev D, Akhmanova A, Steinmetz MO
End binding proteins are obligatory dimers
PLoS One. 2013; 8(9): e74448 (7 pp.). https://doi.org/10.1371/journal.pone.0074448
DORA PSI -
Allison JR, Hertig S, Missimer JH, Smith LJ, Steinmetz MO, Dolenc J
Probing the structure and dynamics of proteins by combining molecular dynamics simulations and experimental NMR data
Journal of Chemical Theory and Computation. 2012; 8(10): 3430-3444. https://doi.org/10.1021/ct300393b
DORA PSI -
Bjelić S, De Groot CO, Schärer MA, Jaussi R, Bargsten K, Salzmann M, et al.
Interaction of mammalian end binding proteins with CAP-Gly domains of CLIP-170 and p150glued
Journal of Structural Biology. 2012; 177(1): 160-167. https://doi.org/10.1016/j.jsb.2011.11.010
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Buey RM, Sen I, Kortt O, Mohan R, Gfeller D, Veprintsev D, et al.
Sequence determinants of a microtubule tip localization signal (MtLS)
Journal of Biological Chemistry. 2012; 287(34): 28227-28242. https://doi.org/10.1074/jbc.M112.373928
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Calligaris D, Manatschal C, Marcellin M, Villard C, Monsarrat B, Burlet-Schiltz O, et al.
Tyrosine-dependent capture of CAP-Gly domain-containing proteins in complex mixture by EB1 C-terminal peptidic probes
Journal of Proteomics. 2012; 75(12): 3605-3616. https://doi.org/10.1016/j.jprot.2012.04.006
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Dinkel H, Michael S, Weatheritt RJ, Davey NE, Van Roey K, Altenberg B, et al.
ELM - the database of eukaryotic linear motifs
Nucleic Acids Research. 2012; 40(D1): D242-D251. https://doi.org/10.1093/nar/gkr1064
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Jiang K, Toedt G, Montenegro Gouveia S, Davey NE, Hua S, van der Vaart B, et al.
A proteome-wide screen for mammalian SxIP motif-containing microtubule plus-end tracking proteins
Current Biology. 2012; 22(19): 1800-1807. https://doi.org/10.1016/j.cub.2012.07.047
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Lopus M, Manatschal C, Buey RM, Bjelić S, Miller HP, Steinmetz MO, et al.
Cooperative stabilization of microtubule dynamics by EB1 and CLIP-170 involves displacement of stably bound Pi at microtubule ends
Biochemistry. 2012; 51(14): 3021-3030. https://doi.org/10.1021/bi300038t
DORA PSI -
Missimer JH, Steinmetz MO, van Gunsteren WF, Dolenc J
Influence of 63Ser phosphorylation and dephosphorylation on the structure of the stathmin helical nucleation sequence: a molecular dynamics study
Biochemistry. 2012; 51(42): 8455-8463. https://doi.org/10.1021/bi300885y
DORA PSI -
Akhmanova A, Steinmetz MO
Microtubule end binding: EBs sense the guanine nucleotide state
Current Biology. 2011; 21(8): R283-R285. https://doi.org/10.1016/j.cub.2011.03.023
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Buey RM, Mohan R, Leslie K, Walzthoeni T, Missimer JH, Menzel A, et al.
Insights into EB1 structure and the role of its c-terminal domain for discriminating microtubule tips from the lattice
Molecular Biology of the Cell. 2011; 22(16): 2912-2923. https://doi.org/10.1091/mbc.E11-01-0017
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Kitagawa D, Vakonakis I, Olieric N, Hilbert M, Keller D, Olieric V, et al.
Structural basis of the 9-fold symmetry of centrioles
Cell. 2011; 144(3): 364 (12 pp.)-375. https://doi.org/10.1016/j.cell.2011.01.008
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van der Vaart B, Manatschal C, Grigoriev I, Olieric V, Gouveia SM, Bjelić S, et al.
SLAIN2 links microtubule plus end-tracking proteins and controls microtubule growth in interphase
Journal of Cell Biology. 2011; 193(6): 1083-1099. https://doi.org/10.1083/jcb.201012179
DORA PSI -
Akhmanova A, Steinmetz MO
Microtubule +TIPs at a glance
Journal of Cell Science. 2010; 123(20): 3415-3419. https://doi.org/10.1242/jcs.062414
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Ciani B, Bjelić S, Honnappa S, Jawhari H, Jaussi R, Payapilly A, et al.
Molecular basis of coiled-coil oligomerization-state specificity
Proceedings of the National Academy of Sciences of the United States of America PNAS. 2010; 107(46): 19850-19855. https://doi.org/10.1073/pnas.1008502107
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De Groot CO, Jelesarov I, Damberger FF, Bjelić S, Schärer MA, Bhavesh NS, et al.
Molecular insights into mammalian end-binding protein heterodimerization
Journal of Biological Chemistry. 2010; 285(8): 5802-5814. https://doi.org/10.1074/jbc.M109.068130
DORA PSI -
Dolenc J, Missimer JH, Steinmetz MO, van Gunsteren WF
Methods of NMR structure refinement: molecular dynamics simulations improve the agreement with measured NMR data of a C-terminal peptide of GCN4-p1
Journal of Biomolecular NMR. 2010; 47(3): 221-235. https://doi.org/10.1007/s10858-010-9425-9
DORA PSI -
Lachkar S, Lebois M, Steinmetz MO, Guichet A, Lal N, Curmi PA, et al.
Drosophila stathmins bind tubulin heterodimers with high and variable stoichiometries
Journal of Biological Chemistry. 2010; 285(15): 11667-11680. https://doi.org/10.1074/jbc.M109.096727
DORA PSI -
Macdonald PR, Lustig A, Steinmetz MO, Kammerer RA
Laminin chain assembly is regulated by specific coiled-coil interactions
Journal of Structural Biology. 2010; 170(2): 398-405. https://doi.org/10.1016/j.jsb.2010.02.004
DORA PSI -
Missimer JH, Dolenc J, Steinmetz MO, Van Gunsteren WF
Exploring the trigger sequence of the GCN4 coiled-coil: biased molecular dynamics resolves apparent inconsistencies in NMR measurements
Protein Science. 2010; 19(12): 2462-2474. https://doi.org/10.1002/pro.528
DORA PSI -
Montenegro Gouveia S, Leslie K, Kapitein LC, Buey RM, Grigoriev I, Wagenbach M, et al.
In vitro reconstitution of the functional interplay between MCAK and EB3 at microtubule plus ends
Current Biology. 2010; 20(19): 1717-1722. https://doi.org/10.1016/j.cub.2010.08.020
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Olieric N, Kuchen M, Wagen S, Sauter M, Crone S, Edmondson S, et al.
Automated seamless DNA co-transformation cloning with direct expression vectors applying positive or negative insert selection
BMC Biotechnology. 2010; 10: 56 (10 pp.). https://doi.org/10.1186/1472-6750-10-56
DORA PSI -
Schmidt F, Treiber N, Zocher G, Bjelic S, Steinmetz MO, Kalbacher H, et al.
Insights into peroxisome function from the structure of PEX3 in complex with a soluble fragment of PEX19
Journal of Biological Chemistry. 2010; 285(33): 25410-25417. https://doi.org/10.1074/jbc.M110.138503
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Bieniossek C, Nie Y, Frey D, Olieric N, Schaffitzel C, Collinson I, et al.
Automated unrestricted multigene recombineering for multiprotein complex production
Nature Methods. 2009; 6(6): 447-450. https://doi.org/10.1038/nmeth.1326
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Honnappa S, Gouveia SM, Weisbrich A, Damberger FF, Bhavesh NS, Jawhari H, et al.
An EB1-binding motif acts as a microtubule tip localization signal
Cell. 2009; 138(2): 366-376. https://doi.org/10.1016/j.cell.2009.04.065
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Komarova Y, De Groot CO, Grigoriev I, Gouveia SM, Munteanu EL, Schober JM, et al.
Mammalian end binding proteins control persistent microtubule growth
Journal of Cell Biology. 2009; 184(5): 691-706. https://doi.org/10.1083/jcb.200807179
DORA PSI -
Manna T, Thrower DA, Honnappa S, Steinmetz MO, Wilson L
Regulation of microtubule dynamic instability in vitro by differentially phosphorylated stathmin
Journal of Biological Chemistry. 2009; 284(23): 15640-15649. https://doi.org/10.1074/jbc.M900343200
DORA PSI -
Wasmer C, Benkemoun L, Sabaté R, Steinmetz MO, Coulary-Salin B, Wang L, et al.
Solid-state NMR spectroscopy reveals that E. coli inclusion bodies of HET-s(218-289) are amyloids
Angewandte Chemie International Edition. 2009; 48(26): 4858-4860. https://doi.org/10.1002/anie.200806100
DORA PSI -
Akhmanova A, Steinmetz MO
Tracking the ends: a dynamic protein network controls the fate of microtubule tips
Nature Reviews Molecular Cell Biology. 2008; 9(4): 309-322. https://doi.org/10.1038/nrm2369
DORA PSI -
Dolenc J, Baron R, Missimer JH, Steinmetz MO, van Gunsteren WF
Exploring the conserved water site and hydration of a coiled-coil trimerisation motif: a MD simulation study
ChemBioChem. 2008; 9(11): 1749-1756. https://doi.org/10.1002/cbic.200800096
DORA PSI -
Grigoriev I, Gouveia SM, van der Vaart B, Demmers J, Smyth JT, Honnappa S, et al.
STIM1 is a MT-plus-end-tracking protein involved in remodeling of the ER
Current Biology. 2008; 18(3): 177-182. https://doi.org/10.1016/j.cub.2007.12.050
DORA PSI -
Hwang S-J, Kim SH, Kim H-Z, Steinmetz MO, Koh GY, Lee GM
High-level expression and purification of a designed angiopoietin-1 chimeric protein, COMP-Ang1, produced in Chinese hamster ovary cells
Protein Journal. 2008; 27(5): 319-326. https://doi.org/10.1007/s10930-008-9140-5
DORA PSI -
Manna T, Honnappa S, Steinmetz MO, Wilson L
Suppression of microtubule dynamic instability by the +TIP protein EB1 and its modulation by the CAP-Gly domain of p150Glued
Biochemistry. 2008; 47(2): 779-786. https://doi.org/10.1021/bi701912g
DORA PSI -
Steinmetz MO, Gattin Z, Verel R, Ciani B, Stromer T, Green JM, et al.
Atomic models of de novo designed ccβ-Met amyloid-like fibrils
Journal of Molecular Biology. 2008; 376(3): 898-912. https://doi.org/10.1016/j.jmb.2007.11.100
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Steinmetz MO, Akhmanova A
Capturing protein tails by CAP-Gly domains
Trends in Biochemical Sciences. 2008; 33(11): 535-545. https://doi.org/10.1016/j.tibs.2008.08.006
DORA PSI -
Verel R, Tomka IT, Bertozzi C, Cadalbert R, Kammerer RA, Steinmetz MO, et al.
Polymorphism in an amyloid-like fibril-forming model peptide
Angewandte Chemie International Edition. 2008; 47(31): 5842-5845. https://doi.org/10.1002/anie.200800021
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Frey D, Kambach C, Steinmetz MO, Jaussi R
Production of in vitro amplified DNA pseudolibraries and high-throughput cDNA target amplification
BMC Biotechnology. 2007; 7: 31 (5 pp.). https://doi.org/10.1186/1472-6750-7-31
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John CM, Hite RK, Weirich CS, Fitzgerald DJ, Jawhari H, Faty M, et al.
The Caenorhabditis elegans septin complex is nonpolar
EMBO Journal. 2007; 26(14): 3296-3307. https://doi.org/10.1038/sj.emboj.7601775
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Missimer JH, Steinmetz MO, Baron R, Winkler FK, Kammerer RA, Daura X, et al.
Configurational entropy elucidates the role of salt-bridge networks in protein thermostability
Protein Science. 2007; 16(7): 1349-1359. https://doi.org/10.1110/ps.062542907
DORA PSI -
Ruch C, Skiniotis G, Steinmetz MO, Walz T, Ballmer-Hofer K
Structure of a VEGF–VEGF receptor complex determined by electron microscopy
Nature Structural and Molecular Biology. 2007; 14(3): 249-250. https://doi.org/10.1038/nsmb1202
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Scherr N, Honnappa S, Kunz G, Mueller P, Jayachandran R, Winkler F, et al.
Structural basis for the specific inhibition of protein kinase G, a virulence factor of Mycobacterium tuberculosis
Proceedings of the National Academy of Sciences of the United States of America PNAS. 2007; 104(29): 12151-12156. https://doi.org/10.1073/pnas.0702842104
DORA PSI -
Steinmetz MO, Jelesarov I, Matousek WM, Honnappa S, Jahnke W, Missimer JH, et al.
Molecular basis of coiled-coil formation
Proceedings of the National Academy of Sciences of the United States of America PNAS. 2007; 104(17): 7062-7067. https://doi.org/10.1073/pnas.0700321104
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Steinmetz MO
Structure and thermodynamics of the tubulin–stathmin interaction
Journal of Structural Biology. 2007; 158(2): 137-147. https://doi.org/10.1016/j.jsb.2006.07.018
DORA PSI -
Teuling E, Ahmed S, Haasdijk E, Demmers J, Steinmetz MO, Akhmanova A, et al.
Motor neuron disease-associated mutant vesicle-associated membrane protein-associated protein (VAP) B recruits wild-type VAPs into endoplasmic reticulum-derived tubular aggregates
Journal of Neuroscience. 2007; 27(36): 9801-9815. https://doi.org/10.1523/JNEUROSCI.2661-07.2007
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Weisbrich A, Honnappa S, Jaussi R, Okhrimenko O, Frey D, Jelesarov I, et al.
Structure-function relationship of CAP-Gly domains
Nature Structural and Molecular Biology. 2007; 14(10): 959-967. https://doi.org/10.1038/nsmb1291
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Honnappa S, Jahnke W, Seelig J, Steinmetz MO
Control of intrinsically disordered stathmin by multisite phosphorylation
Journal of Biological Chemistry. 2006; 281(23): 16078-16083. https://doi.org/10.1074/jbc.M513524200
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Honnappa S, Okhrimenko O, Jaussi R, Jawhari H, Jelesarov I, Winkler FK, et al.
Key interaction modes of dynamic +TIP networks
Molecular Cell. 2006; 23(5): 663-671. https://doi.org/10.1016/j.molcel.2006.07.013
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Kammerer RA, Steinmetz MO
De novo design of a two-stranded coiled-coil switch peptide
Journal of Structural Biology. 2006; 155(2): 146-153. https://doi.org/10.1016/j.jsb.2006.01.017
DORA PSI -
Macdonald PR, Progias P, Ciani B, Patel S, Mayer U, Steinmetz MO, et al.
Structure of the extracellular domain of tie receptor tyrosine kinases and localization of the angiopoietin-binding epitope
Journal of Biological Chemistry. 2006; 281(38): 28408-28414. https://doi.org/10.1074/jbc.M605219200
DORA PSI -
Siemer AB, Ritter C, Steinmetz MO, Ernst M, Riek R, Meier BH
13C, 15N resonance assignment of parts of the HET-s prion protein in its amyloid form
Journal of Biomolecular NMR. 2006; 34(2): 75-87. https://doi.org/10.1007/s10858-005-5582-7
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Gatfield J, Albrecht I, Zanolari B, Steinmetz MO, Pieters J
Association of the leukocyte plasma membrane with the actin cytoskeleton through coiled coil-mediated trimeric coronin 1 molecules
Molecular Biology of the Cell. 2005; 16(6): 2786-2798. https://doi.org/10.1091/mbc.E05-01-0042
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Gigant B, Wang C, Ravelli RBG, Roussi F, Steinmetz MO, Curmi PA, et al.
Structural basis for the regulation of tubulin by vinblastine
Nature. 2005; 435(7041): 519-522. https://doi.org/10.1038/nature03566
DORA PSI -
Honnappa S, John CM, Kostrewa D, Winkler FK, Steinmetz MO
Structural insights into the EB1-APC interaction
EMBO Journal. 2005; 24(2): 261-269. https://doi.org/10.1038/sj.emboj.7600529
DORA PSI -
Kim K-T, Choi H-H, Steinmetz MO, Maco B, Kammerer RA, Ahn SY, et al.
Oligomerization and multimerization are critical for angiopoietin-1 to bind and phosphorylate Tie2
Journal of Biological Chemistry. 2005; 280(20): 20126-20131. https://doi.org/10.1074/jbc.M500292200
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Kostrewa D, Kammerer RA, Progias P, Honnappa S, Avila D, Lustig A, et al.
A conserved trimerization motif controls the topology of short coiled coils
Proceedings of the National Academy of Sciences of the United States of America PNAS. 2005; 102(39): 13891-13896. https://doi.org/10.1073/pnas.0502390102
DORA PSI -
Missimer JH, Steinmetz MO, Jahnke W, Winkler FK, van Gunsteren WF, Daura X
Molecular-dynamics simulations of C- and N-terminal peptide derivatives of GCN4-p1 in aqueous solution
Chemistry and Biodiversity. 2005; 2(8): 1086-1104. https://doi.org/10.1002/cbdv.200590078
DORA PSI -
Steinmetz MO, García-Echeverría C, Kammerer RA
Design of a coiled-coil-based model peptide system to explore the fundamentals of amyloid fibril formation
International Journal of Peptide Research and Therapeutics. 2005; 11(1): 43-52. https://doi.org/10.1007/s10989-004-1720-4
DORA PSI -
Cho C-H, Kammerer RA, Lee HJ, Steinmetz MO, Ryu YS, Lee SH, et al.
COMP-Ang1: a designed angiopoietin-1 variant with nonleaky angiogenic activity
Proceedings of the National Academy of Sciences of the United States of America PNAS. 2004; 101(15): 5547-5552. https://doi.org/10.1073/pnas.0307574101
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Kammerer RA, Kostrewa D, Zurdo J, Detken A, García-Echeverría C, Green JD, et al.
Exploring amyloid formation by a de novo design
Proceedings of the National Academy of Sciences of the United States of America PNAS. 2004; 101(13): 4435-4440. https://doi.org/10.1073/pnas.0306786101
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Honnappa S, Cutting B, Jahnke W, Seelig J, Steinmetz MO
Thermodynamics of the Op18/stathmin-tubulin interaction
Journal of Biological Chemistry. 2003; 278(40): 38926-38934. https://doi.org/10.1074/jbc.M305546200
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EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY 162, 290 (2018).
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MOLECULAR CELL Oct 5;68(1), 210 (2017).DOI: 10.1016/j.molcel.2017.09.012
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NATURE COMMUNICATIONS 8, 14683 (2017).DOI: 10.1038/ncomms14683
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Former Members
Bargsten, Katja
Technician
Bianchi, Sarah
Ph.D. student
Bjelic, Sasa
Postdoc
Brunner, Janine
Postdoc
Bortfeld, Miriam
Technician
De Groot, Christian
Ph.D. student
Hilbert, Manuel
Postdoc
Honnappa, Srinivas
Ph.D. student, Postdoc
Jawhari, Hatim
Postdoc
John, Corinne
Ph.D. student
Kambach, Christian
Senior scientist
Kraatz, Sebastian
Ph.D. student
Kumar, Anil
Postdoc
Manatschal, Cristina
Ph.D. student
Martinez, Ruben
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Menchon, Grégory
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Rezabkova, Lenka
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Sejwal, Kushal
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Sen, Indrani
Ph.D. student
Stangier, Marcel
Ph.D student
Steiner-Degen, Miriam
Postdoc
Vakonakis, John
Postdoc
Weisbrich, Anke
Ph.D student