Prof. dr. F.G. (Friedrich) Förster

David de Wiedgebouw
Universiteitsweg 99
Kamer 2.70
3584 CG Utrecht

Prof. dr. F.G. (Friedrich) Förster

Professor
Structural Biochemistry
+31 30 253 4318
f.g.forster@uu.nl

Highlighted publications

Gemmer, M., Chaillet, M. L., van Loenhout, J., Cuevas Arenas, R., Vismpas, D., Gröllers-Mulderij, M., Koh, F. A., Albanese, P., Scheltema, R. A., Howes, S. C., Kotecha, A., Fedry, J., & Förster, F. (2023). Visualization of translation and protein biogenesis at the ER membrane. Nature, 614(7946), 160-167. https://doi.org/10.1038/s41586-022-05638-5
Liaci, A. M., Steigenberger, B., Telles de Souza, P. C., Tamara, S., Gröllers-Mulderij, M., Ogrissek, P., Marrink, S. J., Scheltema, R. A., & Förster, F. (2021). Structure of the human signal peptidase complex reveals the determinants for signal peptide cleavage. Molecular Cell, 81(19), 3934-3948.e11. Advance online publication. https://doi.org/10.1016/j.molcel.2021.07.031
Braunger, K., Pfeffer, S., Shrimal, S., Gilmore, R., Berninghausen, O., Mandon, E. C., Becker, T., Förster, F., & Beckmann, R. (2018). Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum. Science, 360(6385), 215-219. https://doi.org/10.1126/science.aar7899
https://dspace.library.uu.nl/bitstream/handle/1874/365216/BraungerEtAlScience2018PrePrint.pdf?sequence=3
Unverdorben, P., Beck, F., Śledź, P., Schweitzer, A., Pfeifer, G., Plitzko, J. M., Baumeister, W., & Förster, F. (2014). Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome. Proceedings of the National Academy of Sciences of the United States of America, 111(15), 5544-9. https://doi.org/10.1073/pnas.1403409111
Beck, F., Unverdorben, P., Bohn, S., Schweitzer, A., Pfeifer, G., Sakata, E., Nickell, S., Plitzko, J. M., Villa, E., Baumeister, W., & Förster, F. (2012). Near-atomic resolution structural model of the yeast 26S proteasome. Proceedings of the National Academy of Sciences of the United States of America, 109(37), 14870-5. https://doi.org/10.1073/pnas.1213333109
Chen, Y., & Förster, F. (2014). Iterative reconstruction of cryo-electron tomograms using nonuniform fast Fourier transforms. Journal of Structural Biology, 185(3), 309-16. https://doi.org/10.1016/j.jsb.2013.12.001
Snijder, J., Schuller, J. M., Wiegard, A., Lössl, P., Schmelling, N., Axmann, I. M., Plitzko, J. M., Förster, F., & Heck, A. J. R. (2017). Structures of the cyanobacterial circadian oscillator frozen in a fully assembled state. Science, 355(6330), 1181-1184. https://doi.org/10.1126/science.aag3218
Pfeffer, S., Dudek, J., Schaffer, M., Ng, B. G., Albert, S., Plitzko, J. M., Baumeister, W., Zimmermann, R., Freeze, H. H., Engel, B. D., & Förster, F. (2017). Dissecting the molecular organization of the translocon-associated protein complex. Nature Communications, 8, Article 14516. https://doi.org/10.1038/ncomms14516
Pfeffer, S., Woellhaf, M. W., Herrmann, J. M., & Förster, F. (2015). Organization of the mitochondrial translation machinery studied in situ by cryoelectron tomography. Nature Communications [E], 6, Article 6019. https://doi.org/10.1038/ncomms7019
Pfeffer, S., Burbaum, L., Unverdorben, P., Pech, M., Chen, Y., Zimmermann, R., Beckmann, R., & Förster, F. (2015). Structure of the native Sec61 protein-conducting channel. Nature Communications [E], 6, Article 8403. https://doi.org/10.1038/ncomms9403

Publications

2023

Scholarly publications

Horst, S. V. D., Englmeier, R., Hanson, J., Smeekens, S., & Förster, F. (2023). Sucrose-mediated translational stalling involves a conserved ribosomal pocket. (pp. 1-19). bioRxiv. https://doi.org/10.1101/2023.08.27.554957
Chaillet, M. L., Schot, G. V. D., Gubins, I., Roet, S., Veltkamp, R. C., & Förster, F. (2023). Extensive Angular Sampling Enables the Sensitive Localization of Macromolecules in Electron Tomograms. International Journal of Molecular Sciences. https://doi.org/10.3390/ijms241713375
Homola, M., Büttner, C. R., Füzik, T., Křepelka, P., Holbová, R., Nováček, J., Chaillet, M., Förster, F., Wilson, W. H., Schroeder, D. C., & Plevka, P. (2023, Jun 30). Structure and replication cycle of a virus infecting climate-modulating algaEmiliania huxleyi. https://doi.org/10.1101/2023.06.30.547180
Kucińska, M. K., Fedry, J., Galli, C., Morone, D., Raimondi, A., Soldà, T., Förster, F., & Molinari, M. (2023). TMX4-driven LINC complex disassembly and asymmetric autophagy of the nuclear envelope upon acute ER stress. Nature Communications, 14(1), 3497. https://doi.org/10.1038/s41467-023-39172-3
Thärichen, L., Englmeier, R., & Förster, F. (2023). Sample Preparation of Isolated Mitochondria for Cryoelectron Tomography and In Situ Studies of Translation. Methods in Molecular Biology, 2661, 75-88. https://doi.org/10.1007/978-1-0716-3171-3_5
Fedry, J., Silva, J., Vanevic, M., Fronik, S., Mechulam, Y., Schmitt, E., des Georges, A., Faller, W., & Förster, F. (2023). Visualization of translation reorganization upon persistent collision stress in mammalian cells. bioRxiv. https://doi.org/10.1101/2023.03.23.533914
Bruekner, S. R., Pieters, W., Fish, A., Liaci, A. M., Scheffers, S., Rayner, E., Kaldenbach, D., Drost, L., Dekker, M., van Hees-Stuivenberg, S., Delzenne-Goette, E., de Konink, C., Houlleberghs, H., Dubbink, H. J., AlSaegh, A., de Wind, N., Förster, F., Te Riele, H., & Sixma, T. K. (2023). Unexpected moves: a conformational change in MutSα enables high-affinity DNA mismatch binding. Nucleic Acids Research. Advance online publication. https://doi.org/10.1093/nar/gkad015
Gemmer, M., Chaillet, M. L., van Loenhout, J., Cuevas Arenas, R., Vismpas, D., Gröllers-Mulderij, M., Koh, F. A., Albanese, P., Scheltema, R. A., Howes, S. C., Kotecha, A., Fedry, J., & Förster, F. (2023). Visualization of translation and protein biogenesis at the ER membrane. Nature, 614(7946), 160-167. https://doi.org/10.1038/s41586-022-05638-5

2022

Scholarly publications

Jager, L. D., Jansen, K. I., Kapitein, L. C., Förster, F., & Howes, S. C. (2022). Increased microtubule lattice spacing correlates with selective binding of kinesin-1 in cells. (pp. 1-24). bioRxiv. https://doi.org/10.1101/2022.05.25.493428
Kucińska, M. K., Fedry, J., Galli, C., Morone, D., Raimondi, A., Soldà, T., Förster, F., & Molinari, M. (2022, Oct 5). SEC62 and TMX4 control asymmetric autophagy of the nuclear envelope upon LINC complex disassembly. https://doi.org/10.1101/2022.10.05.510950
Tirincsi, A., O’Keefe, S., Nguyen, D., Sicking, M., Dudek, J., Förster, F., Jung, M., Hadzibeganovic, D., Helms, V., High, S., Zimmermann, R., & Lang, S. (2022). Proteomics Identifies Substrates and a Novel Component in hSnd2-Dependent ER Protein Targeting. Cells, 11(18), Article 2925. https://doi.org/10.3390/cells11182925
Fermie, J., de Jager, L., Foster, H. E., Veenendaal, T., de Heus, C., van Dijk, S., Ten Brink, C., Oorschot, V., Yang, L., Li, W., Müller, W. H., Howes, S., Carter, A. P., Förster, F., Posthuma, G., Gerritsen, H. C., Klumperman, J., & Liv, N. (2022). Bimodal endocytic probe for three-dimensional correlative light and electron microscopy. Cell Reports Methods, 2(5), Article 100220. https://doi.org/10.1016/j.crmeth.2022.100220
Förster, F. (2022). Subtomogram analysis: The sum of a tomogram's particles reveals molecular structure in situ. Journal of Structural Biology: X, 6, Article 100063. https://doi.org/10.1016/j.yjsbx.2022.100063
Hurdiss, D. L., El Kazzi, P., Bauer, L., Papageorgiou, N., Ferron, F. P., Donselaar, T., Van Vliet, A. L. W., Shamorkina, T. M., Snijder, J., Canard, B., Decroly, E., Brancale, A., Zeev-Ben-Mordehai, T., Förster, F., Van Kuppeveld, F. J. M., & Coutard, B. (2022). Fluoxetine targets an allosteric site in the enterovirus 2C AAA+ ATPase and stabilizes a ring-shaped hexameric complex. Science advances, 8(1), 1-12. Article abj7615. https://doi.org/10.1126/sciadv.abj7615

2021

Scholarly publications

Gubins, I., Chaillet, M. L., van der Schot, G., Trueba, M. C., Veltkamp, R. C., Förster, F., Wang, X., Kihara, D., Moebel, E., Nguyen, N. P., White, T., Bunyak, F., Papoulias, G., Gerolymatos, S., Zacharaki, E. I., Moustakas, K., Zeng, X., Liu, S., Xu, M., ... Zhang, F. (2021). SHREC 2021: Classification in cryo-electron tomograms. In D. W. Fellner, W. Hansmann, W. Purgathofer, & F. Sillion (Eds.), EG 3DOR 2021 - Eurographics Workshop on 3D Object Retrieval Short Papers (pp. 5-17). (Eurographics Workshop on 3D Object Retrieval, EG 3DOR; Vol. 2021-September). Eurographics Association. https://doi.org/10.2312/3dor.20211307
Waltz, F., Salinas-Giegé, T., Englmeier, R., Meichel, H., Soufari, H., Kuhn, L., Pfeffer, S., Förster, F., Engel, B. D., Giegé, P., Drouard, L., & Hashem, Y. (2021). How to build a ribosome from RNA fragments in Chlamydomonas mitochondria. Nature Communications, 12(1), 1-15. Article 7176. https://doi.org/10.1038/s41467-021-27200-z
Zimmermann, R., Lang, S., Lerner, M., Förster, F., Nguyen, D., Helms, V., & Schrul, B. (2021). Quantitative proteomics and differential protein abundance analysis after the depletion of PEX3 from human cells identifies additional aspects of protein targeting to the ER. International Journal of Molecular Sciences, 22(23), 1-22. Article 13028. https://doi.org/10.3390/ijms222313028
Liaci, A. M., & Förster, F. (2021). Take me home, protein roads: Structural insights into signal peptide interactions during er translocation. International Journal of Molecular Sciences, 22(21), 1-19. Article 11871. https://doi.org/10.3390/ijms222111871
Liaci, A. M., Steigenberger, B., Telles de Souza, P. C., Tamara, S., Gröllers-Mulderij, M., Ogrissek, P., Marrink, S. J., Scheltema, R. A., & Förster, F. (2021). Structure of the human signal peptidase complex reveals the determinants for signal peptide cleavage. Molecular Cell, 81(19), 3934-3948.e11. Advance online publication. https://doi.org/10.1016/j.molcel.2021.07.031
Bhadra, P., Schorr, S., Lerner, M., Nguyen, D., Dudek, J., Förster, F., Helms, V., Lang, S., & Zimmermann, R. (2021). Quantitative proteomics and differential protein abundance analysis after depletion of putative mrna receptors in the er membrane of human cells identifies novel aspects of mrna targeting to the er. Molecules, 26(12), 1-36. Article 3591. https://doi.org/10.3390/molecules26123591
Fedry, J., Hurdiss, D. L., Wang, C., Li, W., Obal, G., Drulyte, I., Du, W., Howes, S. C., van Kuppeveld, F. J. M., Förster, F., & Bosch, B-J. (2021). Structural insights into the cross-neutralization of SARS-CoV and SARS-CoV-2 by the human monoclonal antibody 47D11. Science advances, 7(23), 1-11. Article eabf5632. Advance online publication. https://doi.org/10.1126/sciadv.abf5632
Englmeier, R., & Förster, F. (2021). In Situ Studies of Mitochondrial Translation by Cryo-Electron Tomography. Methods in Molecular Biology, 2192, 243-268. https://doi.org/10.1007/978-1-0716-0834-0_18

2020

Scholarly publications

Gubins, I., Chaillet, M. L., van der Schot, G., Veltkamp, R. C., Förster, F., Hao, Y., Wan, X., Cui, X., Zhang, F., Moebel, E., Wang, X., Kihara, D., Zeng, X., Xu, M., Nguyen, N. P., White, T., & Bunyak, F. (2020). SHREC’20 benchmark: Classification in cryo-electron tomograms. Computers and Graphics (Pergamon), 91, 279-289. https://doi.org/10.1016/j.cag.2020.07.010
Zhou, Y., Kastritis, P. L., Dougherty, S. E., Bouvette, J., Hsu, A. L., Burbaum, L., Mosalaganti, S., Pfeffer, S., Hagen, W. J. H., Förster, F., Borgnia, M. J., Vogel, C., Beck, M., Bartesaghi, A., & Silva, G. M. (2020). Structural impact of K63 ubiquitin on yeast translocating ribosomes under oxidative stress. Proceedings of the National Academy of Sciences of the United States of America, 117(36), 22157-22166. https://doi.org/10.1073/pnas.2005301117
Schorr, S., Nguyen, D., Haßdenteufel, S., Nagaraj, N., Cavalié, A., Greiner, M., Weissgerber, P., Loi, M., Paton, A. W., Paton, J. C., Molinari, M., Förster, F., Dudek, J., Lang, S., Helms, V., & Zimmermann, R. (2020). Identification of signal peptide features for substrate specificity in human Sec62/Sec63-dependent ER protein import. The FEBS journal, 287(21), 4612-4640. Advance online publication. https://doi.org/10.1111/febs.15274
Ferrari, L., Stucchi, R., Konstantoulea, K., van de Kamp, G., Kos, R., Geerts, W. J. C., van Bezouwen, L. S., Förster, F. G., Altelaar, M., Hoogenraad, C. C., & Rüdiger, S. G. D. (2020). Arginine π-stacking drives binding to fibrils of the Alzheimer protein Tau. Nature Communications, 11(1), 1-13. Article 571. https://doi.org/10.1038/s41467-019-13745-7
Klein, M-C., Lerner, M., Nguyen, D., Pfeffer, S., Dudek, J., Förster, F., Helms, V., Lang, S., & Zimmermann, R. (2020). TRAM1 protein may support ER protein import by modulating the phospholipid bilayer near the lateral gate of the Sec61-channel. Channels, 14(1), 28-44. https://doi.org/10.1080/19336950.2020.1724759
Gemmer, M., & Förster, F. (2020). A clearer picture of the ER translocon complex. Journal of Cell Science, 133(3). https://doi.org/10.1242/jcs.231340
Luo, Y., Xiang, S., Hooikaas, P. J., van Bezouwen, L., Jijumon, A. S., Janke, C., Förster, F., Akhmanova, A., & Baldus, M. (2020). Direct observation of dynamic protein interactions involving human microtubules using solid-state NMR spectroscopy. Nature Communications, 11(1), 18. https://doi.org/10.1038/s41467-019-13876-x

2019

Scholarly publications

Förster, F. G. (2019). 26S Proteasome: Structure and Function. In Reference Module in Biomedical Sciences https://doi.org/10.1016/b978-0-12-801238-3.11341-8
Ferrari, L., Stucci, R., Konstantoulea, A., van, D. K. G., Kos, R., Geerts, WJ., Forster, FG., Altelaar, M., Hoogenraad, C., & Rudiger, SG. (2019, Jan). Fibril formation rewires interactome of the Alzheimer protein Tau by π-stacking. https://doi.org/10.1101/522284
Lang, S., Nguyen, D., Pfeffer, S., Förster, F., Helms, V., & Zimmermann, R. (2019). Functions and Mechanisms of the Human Ribosome-Translocon Complex. In Subcellular Biochemistry (pp. 83-141). (Subcellular Biochemistry; Vol. 93). Springer. https://doi.org/10.1007/978-3-030-28151-9_4
Förster, F. G. (2019). 26S Proteasome: Structure and Function. In Reference Module in Biomedical Sciences (pp. 595-600) https://doi.org/10.1016/B978-0-12-801238-3.11341-8
Gubins, I., van der Schot, G., Veltkamp, R. C., Förster, F. G., Du, X., Zeng, X., Zhu, Z., Chang, L., Xu, M., Moebel, E., Martinez-Sanchez, A., Kervrann, C., Lai, T., Han, Terashi, Kihara, Himes, B. A., Wan, Zhang, ... Zhang (2019). Classification in cryo-electron tomograms. In SHREC’19 Track https://doi.org/10.2312/3dor.20191061
Englmeier, R., & Förster, F. (2019). Cryo-electron tomography for the structural study of mitochondrial translation. Tissue and Cell, 57, 129-138. https://doi.org/10.1016/j.tice.2018.08.009
https://dspace.library.uu.nl/bitstream/handle/1874/392076/Review_MiMB_revisedFinalWithFigures.pdf?sequence=3
Praest, P., Liaci, A. M., Förster, F., & Wiertz, E. J. H. J. (2019). New insights into the structure of the MHC class I peptide-loading complex and mechanisms of TAP inhibition by viral immune evasion proteins. Molecular Immunology, 113, 103-114. https://doi.org/10.1016/j.molimm.2018.03.020

2018

Scholarly publications

Ferrari, L., Geerts, WJ., van, W. M., Kos, R., Konstantoulea, A., van, B. LS., Forster, FG., & Rudiger, SG. (2018, Sept). Human chaperones untangle fibrils of the Alzheimer protein Tau. https://doi.org/10.1101/426650
Nguyen, D., Stutz, R., Schorr, S., Lang, S., Pfeffer, S., Freeze, H. H., Förster, F., Helms, V., Dudek, J., & Zimmermann, R. (2018). Proteomics reveals signal peptide features determining the client specificity in human TRAP-dependent ER protein import. Nature Communications, 9(1), Article 3765. https://doi.org/10.1038/s41467-018-06188-z
Oosterheert, W., van Bezouwen, L. S., Rodenburg, R. N. P., Granneman, J., Förster, F., Mattevi, A., & Gros, P. (2018). Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction. Nature Communications, 9(1), Article 4337. https://doi.org/10.1038/s41467-018-06817-7
Braunger, K., Pfeffer, S., Shrimal, S., Gilmore, R., Berninghausen, O., Mandon, E. C., Becker, T., Förster, F., & Beckmann, R. (2018). Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum. Science, 360(6385), 215-219. https://doi.org/10.1126/science.aar7899
https://dspace.library.uu.nl/bitstream/handle/1874/365216/BraungerEtAlScience2018PrePrint.pdf?sequence=3

2017

Scholarly publications

Lang, S., Pfeffer, S., Lee, P-H., Cavalié, A., Helms, V., Förster, F., & Zimmermann, R. (2017). An Update on Sec61 Channel Functions, Mechanisms, and Related Diseases. Frontiers in Physiology, 8. https://doi.org/10.3389/fphys.2017.00887
Englmeier, R., Pfeffer, S., & Förster, F. (2017). Structure of the Human Mitochondrial Ribosome Studied In Situ by Cryoelectron Tomography. Structure, 25(10), 1574-1581.e2. https://doi.org/10.1016/j.str.2017.07.011
Freeman Rosenzweig, E. S., Xu, B., Kuhn Cuellar, L., Martinez-Sanchez, A., Schaffer, M., Strauss, M., Cartwright, H. N., Ronceray, P., Plitzko, J. M., Förster, F., Wingreen, N. S., Engel, B. D., Mackinder, L. C. M., & Jonikas, M. C. (2017). The Eukaryotic CO2-Concentrating Organelle Is Liquid-like and Exhibits Dynamic Reorganization. Cell, 171(1), 148-162.e19. https://doi.org/10.1016/j.cell.2017.08.008
Pfeffer, S., Dudek, J., Schaffer, M., Ng, B. G., Albert, S., Plitzko, J. M., Baumeister, W., Zimmermann, R., Freeze, H. H., Engel, B. D., & Förster, F. (2017). Dissecting the molecular organization of the translocon-associated protein complex. Nature Communications, 8, Article 14516. https://doi.org/10.1038/ncomms14516
Wehmer, M., Rudack, T., Beck, F., Aufderheide, A., Pfeifer, G., Plitzko, J. M., Förster, F. G., Schulten, K., Baumeister, W., & Sakata, E. (2017). Structural insights into the functional cycle of the ATPase module of the 26S proteasome. Proceedings of the National Academy of Sciences of the United States of America, 114(6), 1305-1310. https://doi.org/10.1073/pnas.1621129114
Snijder, J., Schuller, J. M., Wiegard, A., Lössl, P., Schmelling, N., Axmann, I. M., Plitzko, J. M., Förster, F., & Heck, A. J. R. (2017). Structures of the cyanobacterial circadian oscillator frozen in a fully assembled state. Science, 355(6330), 1181-1184. https://doi.org/10.1126/science.aag3218
Förster, F., & Koster, A. J. (2017). Recent advances in electron tomography. Journal of Structural Biology, 197(2), 71-72. https://doi.org/10.1016/j.jsb.2016.11.005

2016

Scholarly publications

Schweitzer, A., Aufderheide, A., Rudack, T., Beck, F., Pfeifer, G., Plitzko, J. M., Sakata, E., Schulten, K., Foerster, F., & Baumeister, W. (2016). Structure of the human 26S proteasome at a resolution of 3.9 angstrom. Proceedings of the National Academy of Sciences of the United States of America, 113(28), 7816-7821. https://doi.org/10.1073/pnas.1608050113
Khoshouei, M., Pfeffer, S., Baumeister, W., Förster, F., & Danev, R. (2016). Subtomogram analysis using the Volta phase plate. Journal of Structural Biology. https://doi.org/10.1016/j.jsb.2016.05.009
Pfeffer, S., Dudek, J., Zimmermann, R., & Foerster, F. (2016). Organization of the native ribosome-translocon complex at the mammalian endoplasmic reticulum membrane. Biochimica et Biophysica Acta - General Subjects, 1860(10), 2122-2129. https://doi.org/10.1016/j.bbagen.2016.06.024
Mahamid, J., Pfeffer, S., Schaffer, M., Villa, E., Danev, R., Cuellar, L. K., Förster, F., Hyman, A. A., Plitzko, J. M., & Baumeister, W. (2016). Visualizing the molecular sociology at the HeLa cell nuclear periphery. Science, 351(6276), 969-72. https://doi.org/10.1126/science.aad8857
Pfeffer, S., & Förster, F. (2016). Sec61: A static framework for membrane-protein insertion. Channels, 10(2), 1-3. Advance online publication. https://doi.org/10.1080/19336950.2015.1125737
Schuller, J. M., Beck, F., Lössl, P., Heck, A. J. R., & Förster, F. (2016). Nucleotide-dependent conformational changes of the AAA+ ATPase p97 revisited. FEBS Letters, 590(5), 595-604. https://doi.org/10.1002/1873-3468.12091

2015

Scholarly publications

Pfeffer, S., & Förster, F. (2015). Proteintranslation und Prozessierung in physiologischer Umgebung abgebildet. BioSpektrum, 21(4), 385-387.
Asano, S., Fukuda, Y., Beck, F., Aufderheide, A., Förster, F., Danev, R., & Baumeister, W. (2015). Proteasomes. A molecular census of 26S proteasomes in intact neurons. Science, 347(6220), 439-42. https://doi.org/10.1126/science.1261197
Aufderheide, A., Beck, F., Stengel, F., Hartwig, M., Schweitzer, A., Pfeifer, G., Goldberg, A. L., Sakata, E., Baumeister, W., & Förster, F. (2015). Structural characterization of the interaction of Ubp6 with the 26S proteasome. Proceedings of the National Academy of Sciences of the United States of America, 112(28), 8626-31. https://doi.org/10.1073/pnas.1510449112
Aufderheide, A., Unverdorben, P., Baumeister, W., & Förster, F. (2015). Structural disorder and its role in proteasomal degradation. FEBS Letters, 589(19 Pt A), 2552-60. https://doi.org/10.1016/j.febslet.2015.07.034
Butryn, A., Schuller, J. M., Stoehr, G., Runge-Wollmann, P., Förster, F., Auble, D. T., & Hopfner, K-P. (2015). Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1. eLife, 4, Article e07432. https://doi.org/10.7554/eLife.07432
Dudek, J., Pfeffer, S., Lee, P-H., Jung, M., Cavalié, A., Helms, V., Förster, F., & Zimmermann, R. (2015). Protein transport into the human endoplasmic reticulum. Journal of Molecular Biology, 427(6 Pt A), 1159-75. https://doi.org/10.1016/j.jmb.2014.06.011
Pfeffer, S., Burbaum, L., Unverdorben, P., Pech, M., Chen, Y., Zimmermann, R., Beckmann, R., & Förster, F. (2015). Structure of the native Sec61 protein-conducting channel. Nature Communications [E], 6, Article 8403. https://doi.org/10.1038/ncomms9403
Pfeffer, S., Woellhaf, M. W., Herrmann, J. M., & Förster, F. (2015). Organization of the mitochondrial translation machinery studied in situ by cryoelectron tomography. Nature Communications [E], 6, Article 6019. https://doi.org/10.1038/ncomms7019

2014

Scholarly publications

Chen, X., Chen, Y., Schuller, J. M., Navab, N., & Förster, F. (2014). Automatic particle picking and multi-class classification in cryo-electron tomograms. In 2014 IEEE 11th International Symposium on Biomedical Imaging, ISBI 2014 (pp. 838-841). Article 6868001 Institute of Electrical and Electronics Engineers Inc..
Cuellar, L. K., Pfeffer, S., Chen, Y., & Förster, F. (2014). Automated detection of polysomes in cryoelectron tomography. In 2014 IEEE International Conference on Image Processing, ICIP 2014 (pp. 2085-2089). Article 7025418 Institute of Electrical and Electronics Engineers Inc.. https://doi.org/10.1109/ICIP.2014.7025418
Byrne, R. T., Schuller, J. M., Unverdorben, P., Förster, F., & Hopfner, K-P. (2014). Molecular architecture of the HerA-NurA DNA double-strand break resection complex. FEBS Letters, 588(24), 4637-44. https://doi.org/10.1016/j.febslet.2014.10.035
Chen, Y., & Förster, F. (2014). Iterative reconstruction of cryo-electron tomograms using nonuniform fast Fourier transforms. Journal of Structural Biology, 185(3), 309-16. https://doi.org/10.1016/j.jsb.2013.12.001
Chen, Y., Pfeffer, S., Fernández, J. J., Sorzano, C. O. S., & Förster, F. (2014). Autofocused 3D classification of cryoelectron subtomograms. Structure, 22(10), 1528-37. https://doi.org/10.1016/j.str.2014.08.007
Förster, F., Schuller, J. M., Unverdorben, P., & Aufderheide, A. (2014). Emerging mechanistic insights into AAA complexes regulating proteasomal degradation. Biomolecules, 4(3), 774-94. https://doi.org/10.3390/biom4030774
Leitner, A., Joachimiak, L. A., Unverdorben, P., Walzthoeni, T., Frydman, J., Förster, F., & Aebersold, R. (2014). Chemical cross-linking/mass spectrometry targeting acidic residues in proteins and protein complexes. Proceedings of the National Academy of Sciences of the United States of America, 111(26), 9455-60. https://doi.org/10.1073/pnas.1320298111
Pathare, G. R., Nagy, I., Śledź, P., Anderson, D. J., Zhou, H-J., Pardon, E., Steyaert, J., Förster, F., Bracher, A., & Baumeister, W. (2014). Crystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11. Proceedings of the National Academy of Sciences of the United States of America, 111(8), 2984-9. https://doi.org/10.1073/pnas.1400546111
Pfeffer, S., Dudek, J., Gogala, M., Schorr, S., Linxweiler, J., Lang, S., Becker, T., Beckmann, R., Zimmermann, R., & Förster, F. (2014). Structure of the mammalian oligosaccharyl-transferase complex in the native ER protein translocon. Nature Communications [E], 5, Article 3072. https://doi.org/10.1038/ncomms4072
Unverdorben, P., Beck, F., Śledź, P., Schweitzer, A., Pfeifer, G., Plitzko, J. M., Baumeister, W., & Förster, F. (2014). Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome. Proceedings of the National Academy of Sciences of the United States of America, 111(15), 5544-9. https://doi.org/10.1073/pnas.1403409111

2013

Scholarly publications

Bohn, S., & Förster, F. (2013). The 26S Proteasome. In Handbook of Proteolytic Enzymes (Vol. 3, pp. 3691-3700). Elsevier. https://doi.org/10.1016/B978-0-12-382219-2.00817-6
Förster, F. G., & Sakata, E. (2013). 26S Proteasome: Structure and Function. In Encyclopedia of Biological Chemistry (2 ed., pp. 595-600). Academic Press Inc.. https://doi.org/10.1016/B978-0-12-378630-2.00466-7
Bohn, S., Sakata, E., Beck, F., Pathare, G. R., Schnitger, J., Nágy, I., Baumeister, W., & Förster, F. (2013). Localization of the regulatory particle subunit Sem1 in the 26S proteasome. Biochemical and Biophysical Research Communications, 435(2), 250-4. https://doi.org/10.1016/j.bbrc.2013.04.069
Chen, Y., Pfeffer, S., Hrabe, T., Schuller, J. M., & Förster, F. (2013). Fast and accurate reference-free alignment of subtomograms. Journal of Structural Biology, 182(3), 235-45. https://doi.org/10.1016/j.jsb.2013.03.002
Förster, F., Unverdorben, P., Sledź, P., & Baumeister, W. (2013). Unveiling the long-held secrets of the 26S proteasome. Structure, 21(9), 1551-62. https://doi.org/10.1016/j.str.2013.08.010
Sledź, P., Förster, F., & Baumeister, W. (2013). Allosteric effects in the regulation of 26S proteasome activities. Journal of Molecular Biology, 425(9), 1415-23. https://doi.org/10.1016/j.jmb.2013.01.036
Śledź, P., Unverdorben, P., Beck, F., Pfeifer, G., Schweitzer, A., Förster, F., & Baumeister, W. (2013). Structure of the 26S proteasome with ATP-γS bound provides insights into the mechanism of nucleotide-dependent substrate translocation. Proceedings of the National Academy of Sciences of the United States of America, 110(18), 7264-7269. https://doi.org/10.1073/pnas.1305782110

2012

Scholarly publications

Förster, F. G., & Bohn, S. (2012). Chapter 850: 26S Proteasome. In Handbook of Proteolytic Enzymes (pp. 3691-3700). Elsevier.
Lučić, V., Baumeister, W., & Förster, F. (2012). Studying the macromolecular machinery of cells in situ by cryo-electron tomography. In Comprehensive Biophysics (Vol. 2, pp. 59-89). Elsevier. https://doi.org/10.1016/B978-0-12-374920-8.00211-3
Förster, F., Villa, E., Thomas, D., Korinek, A., & Baumeister, W. (2012). Structure determination of macromolecular complexes by cryo-electron microscopy in vitro and in situ. In Comprehensive Biophysics (Vol. 1, pp. 245-276). Elsevier. https://doi.org/10.1016/B978-0-12-374920-8.00118-1
Chen, Y., Hrabe, T., Pfeffer, S., Pauly, O., Mateus, D., Navab, N., & Förster, F. (2012). Detection and identification of macromolecular complexes in cryo-electron tomograms using support vector machines. In Proceedings - International Symposium on Biomedical Imaging (pp. 1373-1376). Article 6235823 https://doi.org/10.1109/ISBI.2012.6235823
Beck, F., Unverdorben, P., Bohn, S., Schweitzer, A., Pfeifer, G., Sakata, E., Nickell, S., Plitzko, J. M., Villa, E., Baumeister, W., & Förster, F. (2012). Near-atomic resolution structural model of the yeast 26S proteasome. Proceedings of the National Academy of Sciences of the United States of America, 109(37), 14870-5. https://doi.org/10.1073/pnas.1213333109
Hrabe, T., Chen, Y., Pfeffer, S., Cuellar, L. K., Mangold, A-V., & Förster, F. (2012). PyTom: a python-based toolbox for localization of macromolecules in cryo-electron tomograms and subtomogram analysis. Journal of Structural Biology, 178(2), 177-88. https://doi.org/10.1016/j.jsb.2011.12.003
Lasker, K., Förster, F., Bohn, S., Walzthoeni, T., Villa, E., Unverdorben, P., Beck, F., Aebersold, R., Sali, A., & Baumeister, W. (2012). Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach. Proceedings of the National Academy of Sciences of the United States of America, 109(5), 1380-7. https://doi.org/10.1073/pnas.1120559109
Leitner, A., Reischl, R., Walzthoeni, T., Herzog, F., Bohn, S., Förster, F., & Aebersold, R. (2012). Expanding the chemical cross-linking toolbox by the use of multiple proteases and enrichment by size exclusion chromatography. Molecular & Cellular Proteomics, 11(3), M111.014126. https://doi.org/10.1074/mcp.M111.014126
Pathare, G. R., Nagy, I., Bohn, S., Unverdorben, P., Hubert, A., Körner, R., Nickell, S., Lasker, K., Sali, A., Tamura, T., Nishioka, T., Förster, F., Baumeister, W., & Bracher, A. (2012). The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together. Proceedings of the National Academy of Sciences of the United States of America, 109(1), 149-54. https://doi.org/10.1073/pnas.1117648108
Pfeffer, S., Brandt, F., Hrabe, T., Lang, S., Eibauer, M., Zimmermann, R., & Förster, F. (2012). Structure and 3D arrangement of endoplasmic reticulum membrane-associated ribosomes. Structure, 20(9), 1508-18. https://doi.org/10.1016/j.str.2012.06.010
Sakata, E., Bohn, S., Mihalache, O., Kiss, P., Beck, F., Nagy, I., Nickell, S., Tanaka, K., Saeki, Y., Förster, F., & Baumeister, W. (2012). Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy. Proceedings of the National Academy of Sciences of the United States of America, 109(5), 1479-84. https://doi.org/10.1073/pnas.1119394109
Schönegge, A-M., Villa, E., Förster, F., Hegerl, R., Peters, J., Baumeister, W., & Rockel, B. (2012). The structure of human tripeptidyl peptidase II as determined by a hybrid approach. Structure, 20(4), 593-603. https://doi.org/10.1016/j.str.2012.01.025
Walzthoeni, T., Claassen, M., Leitner, A., Herzog, F., Bohn, S., Förster, F., Beck, M., & Aebersold, R. (2012). False discovery rate estimation for cross-linked peptides identified by mass spectrometry. Nature Methods, 9(9), 901-3. https://doi.org/10.1038/nmeth.2103

2011

Scholarly publications

Hrabe, T., & Förster, F. (2011). Structure determination by Single Particle Cryo Electron Tomography. https://doi.org/10.1002/9780470015902.a0023175
Abrahams, J-P., Apweiler, R., Balling, R., Bertero, M. G., Bujnicki, J. M., Chayen, N. E., Chène, P., Corthals, G. L., Dyląg, T., Förster, F., Heck, A. J. R., Henderson, P. J. F., Herwig, R., Jehenson, P., Kokalj, S. J., Laue, E., Legrain, P., Martens, L., Migliorini, C., ... Taussig, M. J. (2011). "4D Biology for health and disease" workshop report. Biotechnology Journal, 28(4), 291-3. https://doi.org/10.1016/j.nbt.2010.10.003
Sakata, E., Stengel, F., Fukunaga, K., Zhou, M., Saeki, Y., Förster, F., Baumeister, W., Tanaka, K., & Robinson, C. V. (2011). The catalytic activity of Ubp6 enhances maturation of the proteasomal regulatory particle. Molecular Cell, 42(5), 637-49. https://doi.org/10.1016/j.molcel.2011.04.021

2010

Scholarly publications

Bohn, S., Beck, F., Sakata, E., Walzthoeni, T., Beck, M., Aebersold, R., Förster, F., Baumeister, W., & Nickell, S. (2010). Structure of the 26S proteasome from Schizosaccharomyces pombe at subnanometer resolution. Proceedings of the National Academy of Sciences of the United States of America, 107(49), 20992-7. https://doi.org/10.1073/pnas.1015530107
Förster, F., Han, B-G., & Beck, M. (2010). Visual proteomics. Methods in Enzymology, 483, 215-43. https://doi.org/10.1016/S0076-6879(10)83011-3
Förster, F., Lasker, K., Nickell, S., Sali, A., & Baumeister, W. (2010). Toward an integrated structural model of the 26S proteasome. Molecular & Cellular Proteomics, 9(8), 1666-77. https://doi.org/10.1074/mcp.R000002-MCP201
Förster, F., & Villa, E. (2010). Integration of cryo-EM with atomic and protein-protein interaction data. Methods in Enzymology, 483, 47-72. https://doi.org/10.1016/S0076-6879(10)83003-4

2009

Scholarly publications

Förster, F., Lasker, K., Beck, F., Nickell, S., Sali, A., & Baumeister, W. (2009). An atomic model AAA-ATPase/20S core particle sub-complex of the 26S proteasome. Biochemical and Biophysical Research Communications, 388(2), 228-33. https://doi.org/10.1016/j.bbrc.2009.07.145
Nickell, S., Beck, F., Scheres, S. H. W., Korinek, A., Förster, F., Lasker, K., Mihalache, O., Sun, N., Nagy, I., Sali, A., Plitzko, J. M., Carazo, J-M., Mann, M., & Baumeister, W. (2009). Insights into the molecular architecture of the 26S proteasome. Proceedings of the National Academy of Sciences of the United States of America, 106(29), 11943-7. https://doi.org/10.1073/pnas.0905081106

2008

Scholarly publications

Alber, F., Förster, F., Korkin, D., Topf, M., & Sali, A. (2008). Integrating diverse data for structure determination of macromolecular assemblies. Annual Review of Biochemistry, 77, 443-77. https://doi.org/10.1146/annurev.biochem.77.060407.135530
Förster, F., Pruggnaller, S., Seybert, A., & Frangakis, A. S. (2008). Classification of cryo-electron sub-tomograms using constrained correlation. Journal of Structural Biology, 161(3), 276-86. https://doi.org/10.1016/j.jsb.2007.07.006
Förster, F., Webb, B., Krukenberg, K. A., Tsuruta, H., Agard, D. A., & Sali, A. (2008). Integration of small-angle X-ray scattering data into structural modeling of proteins and their assemblies. Journal of Molecular Biology, 382(4), 1089-106. https://doi.org/10.1016/j.jmb.2008.07.074
Krukenberg, K. A., Förster, F., Rice, L. M., Sali, A., & Agard, D. A. (2008). Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90. Structure, 16(5), 755-65. https://doi.org/10.1016/j.str.2008.01.021
Tutus, M., Rossetti, F. F., Schneck, E., Fragneto, G., Förster, F., Richter, R., Nawroth, T., & Tanaka, M. (2008). Orientation-selective incorporation of transmembrane F0F1 ATP synthase complex from micrococcus luteus in polymer-supported membranes. Macromolecular Bioscience, 8(11), 1034-43. https://doi.org/10.1002/mabi.200800128

2007

Scholarly publications

Beck, M., Lucić, V., Förster, F., Baumeister, W., & Medalia, O. (2007). Snapshots of nuclear pore complexes in action captured by cryo-electron tomography. Nature, 449(7162), 611-5. https://doi.org/10.1038/nature06170
Förster, F., & Hegerl, R. (2007). Structure determination in situ by averaging of tomograms. Methods in Cell Biology, 79, 741-67. https://doi.org/10.1016/S0091-679X(06)79029-X

2006

Scholarly publications

Briggs, J. A. G., Grünewald, K., Glass, B., Förster, F., Kräusslich, H-G., & Fuller, S. D. (2006). The mechanism of HIV-1 core assembly: insights from three-dimensional reconstructions of authentic virions. Structure, 14(1), 15-20. https://doi.org/10.1016/j.str.2005.09.010
Ortiz, J. O., Förster, F., Kürner, J., Linaroudis, A. A., & Baumeister, W. (2006). Mapping 70S ribosomes in intact cells by cryoelectron tomography and pattern recognition. Journal of Structural Biology, 156(2), 334-41. https://doi.org/10.1016/j.jsb.2006.04.014

2005

Scholarly publications

Miao, J., Förster, F., & Levi, O. (2005). Equally sloped tomography with oversampling reconstruction. Physical review. B, Condensed matter and materials physics, 72(5), Article 052103. https://doi.org/10.1103/PhysRevB.72.052103
Förster, F., Medalia, O., Zauberman, N., Baumeister, W., & Fass, D. (2005). Retrovirus envelope protein complex structure in situ studied by cryo-electron tomography. Proceedings of the National Academy of Sciences of the United States of America, 102(13), 4729-34. https://doi.org/10.1073/pnas.0409178102
Lucić, V., Förster, F., & Baumeister, W. (2005). Structural studies by electron tomography: from cells to molecules. Annual Review of Biochemistry, 74, 833-65. https://doi.org/10.1146/annurev.biochem.73.011303.074112
Lucić, V., Yang, T., Schweikert, G., Förster, F., & Baumeister, W. (2005). Morphological characterization of molecular complexes present in the synaptic cleft. Structure, 13(3), 423-34. https://doi.org/10.1016/j.str.2005.02.005
Nickell, S., Förster, F., Linaroudis, A., Net, W. D., Beck, F., Hegerl, R., Baumeister, W., & Plitzko, J. M. (2005). TOM software toolbox: acquisition and analysis for electron tomography. Journal of Structural Biology, 149(3), 227-34. https://doi.org/10.1016/j.jsb.2004.10.006

2004

Scholarly publications

Kurz, P., Förster, F., Nordström, L., Bihlmayer, G., & Blügel, S. (2004). Ab initio treatment of noncollinear magnets with the full-potential linearized augmented plane wave method. Physical review. B, condensed matter, 69(2), 244151-2441515. Article 024415.
Beck, M., Förster, F., Ecke, M., Plitzko, J. M., Melchior, F., Gerisch, G., Baumeister, W., & Medalia, O. (2004). Nuclear pore complex structure and dynamics revealed by cryoelectron tomography. Science, 306(5700), 1387-90. https://doi.org/10.1126/science.1104808
Frangakis, A. S., & Förster, F. (2004). Computational exploration of structural information from cryo-electron tomograms. Current Opinion in Structural Biology, 14(3), 325-31. https://doi.org/10.1016/j.sbi.2004.04.003

2002

Scholarly publications

Frangakis, A. S., Böhm, J., Förster, F., Nickell, S., Nicastro, D., Typke, D., Hegerl, R., & Baumeister, W. (2002). Identification of macromolecular complexes in cryoelectron tomograms of phantom cells. Proceedings of the National Academy of Sciences of the United States of America, 99(22), 14153-14158. https://doi.org/10.1073/pnas.172520299
Plitzko, J. M., Frangakis, A. S., Nickell, S., Förster, F., Gross, A., & Baumeister, W. (2002). In vivo veritas: Electron cryotomography of cells. Trends in Biotechnology, 20(8). https://doi.org/10.1016/S0167-7799(02)02017-6