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/s41467-023-39172-3Thärichen, 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/gkad015Gemmer, 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/10.1101/2022.10.05.510950Tirincsi, 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/cells11182925Fermie, 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 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-zZimmermann, 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/ijms222313028Liaci, 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/molecules26123591Fedry, 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 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.2005301117Schorr, 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.15274Ferrari, 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/10.1080/19336950.2020.1724759Luo, 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
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_4Gubins, 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 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.2018.03.0202018
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-zOosterheert, 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.aar7899https://dspace.library.uu.nl/bitstream/handle/1874/365216/BraungerEtAlScience2018PrePrint.pdf?sequence=32017
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.2017.00887Englmeier, 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.2017.08.008Pfeffer, 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/ncomms14516Wehmer, 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.1621129114Snijder, 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 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.1608050113Pfeffer, 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.2016.06.024Mahamid, 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.aad8857Schuller, 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/10.1002/1873-3468.120912015
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.1261197Aufderheide, 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.1510449112Butryn, 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.07432Dudek, 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.2014.06.011Pfeffer, 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/ncomms9403Pfeffer, 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/ncomms70192014
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.2014.7025418Byrne, 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.2014.10.035Chen, 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.2013.12.001Chen, 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.2014.08.007Förster, 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.1320298111Pathare, 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.1400546111Pfeffer, 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/ncomms4072Unverdorben, 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.14034091112013
Scholarly publications
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.2013.04.069Chen, 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.2013.03.002Śledź, 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.13057821102012
Scholarly publications
Förster, F. G., & Bohn, S. (2012). Chapter 850: 26S Proteasome. In Handbook of Proteolytic Enzymes (pp. 3691-3700). Elsevier.
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.2012.6235823Beck, 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.1213333109Hrabe, 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.2011.12.003Lasker, 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.1120559109Leitner, 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.M111.014126Pathare, 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.1117648108Pfeffer, 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.2012.06.010Sakata, 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.1119394109Schönegge, 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.2012.01.025Walzthoeni, 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.21032011
Scholarly publications
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.2010.10.003Sakata, 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.2011.04.0212010
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.1015530107Förster, 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 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.09050811062008
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.77.060407.135530Förster, 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.2008.01.021Tutus, 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.2008001282007
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/nature061702006
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.2005.09.010Ortiz, 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.2006.04.0142005
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.72.052103Förster, 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., 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.2005.02.005Nickell, 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.2004.10.0062004
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.1104808Frangakis, 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.2004.04.0032002
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.172520299Plitzko, 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