1. Gemmer M, Förster F.
    A clearer picture of the ER translocon complex.
    Journal of cell science 133 (2020)
    PubMed, DOI:10.1242/jcs.231340, Open-access .
  2. Ferrari L, Stucchi R, Konstantoulea K, van de Kamp G, Kos R, Geerts WJC, van Bezouwen LS, Förster FG, Altelaar M, Hoogenraad CC, Rudiger SGD
    Arginine pi-stacking drives binding to fibrils of the Alzheimer protein Tau.
    Nature communications 11:571 (2020).
    PubMed, DOI:10.1038/s41467-019-13745-7
  3. Luo Y, Xiang S, Hooikaas PJ, van Bezouwen L, Jijumon AS, Janke C, Förster F, Akhmanova A, Baldus M,
    Direct observation of dynamic protein interactions involving human microtubules using solid-state NMR spectroscopy.
    Nature communications 11:18 (2020).
    PubMed, DOI:10.1038/s41467-019-13876-x.
  4. Klein MC, Lerner M, Nguyen D, Pfeffer S, Dudek J, Förster F, Helms V, Lang S, Zimmermann R.
    TRAM1 protein may support ER protein import by modulating the phospholipid bilayer near the lateral gate of the Sec61-channel.
    Channels 14:28-44 (2020).
    PubMed, DOI:10.1080/19336950.2020.1724759.
  5. Lang S, Nguyen D, Pfeffer S, Förster F, Helms V, Zimmermann R.
    Functions and Mechanisms of the Human Ribosome-Translocon Complex.
    Subcell Biochem 93:83-141 (2019).
  6. Gubins I, van der Schot G, Veltkamp RC, Förster F, Du X, Zeng X, Zhu Z, Chang L, Xu M, Moebel E et al.
    Classification in Cryo-Electron Tomograms. (2019). In: Eurographics Workshop on 3D Object Retrieval, (eds. S. Biasotti G. Lavoué B. Falcidieno and I. Pratikakis).
  7. Förster F.
    26S Proteasome: Structure and Function.
    In: Reference Module in Biomedical Research: Elsevier (2019).
  8. Nguyen D, Stutz R, Schorr S, Lang S, Pfeffer S, Freeze HH, Förster F, Helms V, Dudek J, Zimmermann R.
    Proteomics reveals signal peptide features determining the client specificity in human TRAP-dependent ER protein import.
    Nat. Commun. 9(1): 3765 (2018).
    PubMed, DOI:10.1038/s41467-018-06188-z.
  9. Oosterheert W, van Bezouwen LS, Rodenburg RNP, Granneman J, Forster F, Mattevi A, Gros P.
    Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction.
    Nat Commun 9(1): 4337 (2018).
    PubMed, DOI:10.1038/s41467-018-06817-7.
  10. Englmeier R, Forster F.
    Cryo-electron tomography for the structural study of mitochondrial translation.
    Tissue & cell (2018).
    PubMed, DOI:10.1016/j.tice.2018.08.009.
  11. Praest P, Liaci AM, Forster F, Wiertz E.
    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 (2018).
    PubMed, DOI:10.1016/j.molimm.2018.03.020, Open-access preprint
  12. Braunger K, Pfeffer S, Shrimal S, Gilmore R, Berninghausen O, Mandon EC, Becker T, Förster F, Beckmann R.
    Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum.
    Science (2018). PubMed, DOI:10.1126/science.aar7899, Open-access preprint
  13. Pfeffer S, Förster F.
    Structural Biology in Situ Using Cryo-Electron Subtomogram Analysis.
    in: Cellular Imaging, 237-259 (2018). DOI:10.1007/978-3-319-68997-5_9.
  14. Lang S, Pfeffer S, Lee PH, Cavalie A, Helms V, Förster F, Zimmermann R.
    An Update on Sec61 Channel Functions, Mechanisms, and Related Diseases.
    Frontiers in physiology 8:887 (2017). PubMed, DOI:10.3389/fphys.2017.00887.
  15. Freeman Rosenzweig ES, Xu B, Kuhn Cuellar L, Martinez-Sanchez A, Schaffer M, Strauss M, Cartwright HN, Ronceray P, Plitzko JM, Förster F, Wingreen NS, Engel BD, Mackinder LCM, Jonikas MC.
    The Eukaryotic CO2-Concentrating Organelle Is Liquid-like and Exhibits Dynamic Reorganization.
    Cell 171:148-162 e19 (2017). PubMed, DOI:10.1016/j.cell.2017.08.008.
  16. Englmeier R, Pfeffer S, Förster F.
    Structure of the human mitochondrial ribosome studied in situ by cryoelectron tomography.
    Structure 25:1574-81 (2017). PubMed, DOI:10.1016/j.str.2017.07.011, Open-access preprint .
  17. Snijder J, Schuller JM, Wiegard A, Lössl P, Schmelling N, Axmann IM, Plitzko JM, Förster F, Heck AJR.
    Structures of the cyanobacterial circadian oscillator frozen in a fully assembled state.
    Science 355:1181 (2017). DOI:10.1126/science.aag3218.
    Review in Nat. Rev. Microbiol.
  18. Pfeffer S, Dudek J, Schaffer M, Ng BG, Albert S, Plitzko JM, Baumeister W, Zimmermann R, Freeze HH, Engel BD, Förster F.
    Dissecting the molecular organization of the translocon-associated protein complex.
    Nat. Comm. 14516 (2017). DOI:10.1038/ncomms14516.
    News on C2W
  19. Wehmer M, Rudack T, Beck F, Aufderheide A, Pfeifer G, Plitzko JM, Förster F, Schulten K, Baumeister W, Sakata E.
    Structural insights into the functional cycle of the ATPase module of the 26S proteasome.
    Proc. Natl. Acad. Sci. USA (2017). PubMed: PubMed, DOI:10.1073/pnas.1621129114.
  20. Förster F, Koster AJ.
    Recent advances in electron tomography.
    J. Struct. Biol. (2016). PubMed: PubMed, DOI:10.1016/j.jsb.2016.11.005.
  21. Pfeffer S, Dudek J, Zimmermann R, Förster F.
    Organization of the native ribosome-translocon complex at the mammalian endoplasmic reticulum membrane.
    Biochim. Biophys. Acta (2016). PubMed, DOI:10.1016/j.bbagen.2016.06.024.
  22. Schweitzer A*, Aufderheide A*, Rudack T*, Beck F, Pfeifer G, Plitzko JM, Sakata E, Schulten K, Förster F, Baumeister W.
    Structure of the human 26S proteasome at a resolution of 3.9 Å.
    Proc. Natl. Acad. Sci. USA (2016). PubMed, DOI:10.1073/pnas.1608050113 (open access).
    * equal contribution
  23. Khoshouei M, Pfeffer S, Baumeister W, Förster F, Danev R.
    Subtomogram analysis using the Volta phase plate.
    J. Struct. Biol. (2016). PubMed, DOI:10.1016/j.jsb.2016.05.009.
  24. Mahamid J, Pfeffer S, Schaffer M, Villa E, Danev R, Kuhn Cuellar L, Förster F, Hyman AA, Plitzko JM, Baumeister W.
    Visualizing the molecular sociology at the HeLa cell nuclear periphery.
    Science 351:969-972 (2016). PubMed, DOI:10.1126/science.aad8857.
    Faculty of 1000
  25. Schuller JM, Beck F, Lossl P, Heck AJ, Förster F.
    Nucleotide-dependent conformational changes of the AAA+ ATPase p97 revisited.
    FEBS Lett. 590:595-604 (2016). PubMed, DOI:10.1002/1873-3468.12091.
  26. Pfeffer P, Förster F.
    Sec61: a static framework for membrane-protein insertion.
    Channels 10:1-3 (2016). PubMed, DOI:10.1080/19336950.2015.1125737
  27. Pfeffer S, Burbaum L, Unverdorben P, Pech M, Chen Y, Zimmermann R, Beckmann R, Förster F.
    Structure of the native Sec61 protein-conducting channel.
    Nat. Comm. 6:8403 (2015). DOI:10.1038/ncomms9403 (open access).
  28. Butryn A, Schuller JM, Stoehr G, Runge-Wollmann P, Förster F, Auble DT, Hopfner KP.
    Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1.
    eLife 4 (2015). PubMed, DOI:10.7554/eLife.07432. (open access)
  29. Aufderheide A, Unverdorben P, Baumeister W, Förster F.
    Structural Disorder and its Role in proteasomal Degradation.
    FEBS Lett. 589:2552–2560 (2015). PubMed, DOI:10.1016/j.febslet.2015.07.034.
  30. Burbaum L, Pfeffer S, Förster F.
    Eiskalt ausgetrickst.
    Laborjournal (2015). (open access)
  31. Aufderheide A, Beck F, Stengel F, Hartwig M, Schweitzer A, Pfeifer G, Goldberg AL, Sakata E, Baumeister W, Förster F.
    Structural characterization of the interaction of Ubp6 with the 26S proteasome.
    Proc. Natl. Acad. Sci. USA 112:8626–8631 (2015). PubMed, DOI: 10.1073/pnas.1510449112 (open access)
    NSMB commentary
  32. Pfeffer S, Förster F.
    Proteintranslation und Prozessierung in physiologischer Umgebung abgebildet.
    Biospektrum 4:385-387 (2015). DOI:10.1007/s12268-015-0590-y
  33. Asano S*, Fukuda Y*, Beck F, Aufderheide A, Förster F, Danev R, Baumeister W.
    A molecular census of 26S proteasomes in intact neurons.
    Science 347:439-442 (2015). PubMed, DOI:10.1126/science.1261197.
    * equal contribution
    Faculty of 1000
  34. Pfeffer S*, Woellhaf MW*, Herrmann JM, Förster F.
    Organization of the mitochondrial translation machinery studied in situ by cryo-electron tomography.
    Nat. Commun. 6:6019 (2015). PubMed, DOI:10.1038/ncomms7019
    * equal contribution
    Laborjournal, VBio, Innovations-Report
  35. Byrne RT*, Schuller JM*, Unverdorben P, Förster F, Hopfner KP.
    Molecular architecture of the HerA–NurA DNA double-strand break resection complex.
    FEBS Lett. 24:4637-44 (2014). PubMed, DOI:10.1016/j.febslet.2014.10.035
    * equal contribution
  36. Chen Y, Pfeffer S, Fernandez JJ, Sorzano CO, Förster F.
    Autofocused 3D Classification of Cryoelectron Subtomograms.
    Structure 22:1528–1537 (2014). PubMed, DOI:10.1016/j.str.2014.08.007
  37. Förster F, Schuller JM, Unverdorben P, Aufderheide A.
    Emerging mechanistic insights into AAA complexes regulating proteasomal degradation degradation.
    Biomolecules 4:774-794 (2014). PubMed, DOI:10.3390/biom4030774 (open access)
  38. Dudek J, Pfeffer S, Lee PH, Jung M, Cavalie A, Helms V, Förster F, Zimmermann R.
    Protein Transport into the Human Endoplasmic Reticulum.
    J. Mol. Biol. (2014). PubMed, DOI: 10.1016/j.jmb.2014.06.011 (open access)
  39. Kuhn Cuellar L, Pfeffer S, Chen Y, Förster F.
    Automated detection of polysomes in cryoelectron tomography.
    in IEEE International Conference on Image Processing (ICIP) 2085-89 (IEEE Paris, 2014). DOI: 10.1109/ICIP.2014.7025418
  40. Leitner A, Joachimiak LA, Unverdorben P, Walzthoeni T, Frydman J, Förster F, Aebersold R.
    Chemical cross-linking/mass spectrometry targeting acidic residues in proteins and protein complexes.
    Proc. Natl. Acad. Sci. USA 111:9455-60 (2014). PubMed, DOI: 10.1073/pnas.1320298111 (open access)
  41. Unverdorben P*, Beck F*, Sledz P, Schweitzer A, Pfeifer G, Plitzko JM, Baumeister W, Förster F.
    Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome.
    Proc. Natl. Acad. Sci. USA 111:5544-9 (2014). PubMed, DOI: 10.1073/pnas.1403409111 (open access)
    * equal contribution
  42. Pathare GR, Nagy I, Sledz P, Anderson DJ, Zhou HJ, Pardon E, Steyaert J, Förster F, Bracher A, Baumeister W.
    Crystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11.
    Proc. Natl. Acad. Sci. USA 111:2984–89 (2014). PubMed, DOI: 10.1073/pnas.1400546111 (open access)
  43. Pfeffer S*, Dudek J*, Gogala M, Schorr S, Linxweiler J, Lang S, Becker T, Beckmann R, Zimmermann R, Förster F.
    Structure of the mammalian oligosaccharyl-transferase complex in the native ER protein translocon.
    Nat. Commun. 5:3072 (2014). PubMed, DOI: 10.1038/ncomms4072
    * equal contribution
  44. Chen X, Chen Y, Schuller JM, Navab N, Förster F.
    Automatic particle picking and multi-class classification in cryo-electron tomograms.
    2014 IEEE International Symposium on Biomedical Imaging Vol. in press (IEEE, Beijing, 2014). DOI: 10.1109/ISBI.2014.6868001
  45. Chen Y, Förster F.
    Iterative reconstruction of cryo-electron tomograms using nonuniform fast Fourier transforms.
    J. Struct. Biol. 185:309-316 (2014) PubMed, DOI: 10.1016/j.jsb.2013.12.001
    Faculty of 1000
  46. Förster F, Unverdorben P, Sledz P, Baumeister W.
    Unveiling the Long-Held Secrets of the 26S Proteasome.
    Structure 21:1551-1562 (2013). PubMed, DOI: 10.1016/j.str.2013.08.010
    Faculty of 1000
  47. Bohn S, Sakata E, Beck F, Pathare GR, Schnitger J, Nagy I, Baumeister W, Förster F.
    Localization of the regulatory particle subunit Sem1 in the 26S proteasome.
    Biochem. Biophys. Res. Commun. 435:250-4 (2013). PubMed, DOI: 10.1016/j.bbrc.2013.04.069
  48. Śledź P, Unverdorben P, Beck F, Pfeifer G, Schweitzer A, Förster F, Baumeister W.
    Structure of the 26S proteasome with ATP-γS bound provides insights into the mechanism of nucleotide-dependent substrate translocation.
    Proc. Natl. Acad. Sci. 110:7264-9 (2013). PubMed, DOI: 10.1073/pnas.1305782110 (open access)
  49. Chen Y, Pfeffer S, Hrabe T, Schuller J, Förster F.
    Fast and accurate reference-free Alignment of Subtomograms.
    J. Struct. Biol. 182:235-45 (2013) PubMed, DOI:10.1016/j.jsb.2013.03.002
  50. Sledz P, Förster F, Baumeister W.
    Allosteric Effects in the Regulation of 26S Proteasome Activities.
    J. Mol. Biol. 425:1415-23 (2013) PubMed, DOI:10.1016/j.jmb.2013.01.036
  51. Bohn S, Förster F.
    The 26S Proteasome.
    Handbook of Proteolytic Enzymes (Third Edition) (2013), Academic Press. DOI: 10.1016/B978-0-12-382219-2.00817-6, GoogleBooks
  52. Förster F, Sakata E.
    26S Proteasome structure and function.
    Encyclopedia of Biological Chemistry, Second Edition (2013). DOI: 10.1016/B978-0-12-378630-2.00466-7
  53. Beck F*, Unverdorben P*, Bohn S, Schweitzer A, Pfeifer G, Sakata E, Nickell S, Plitzko JM, Villa E, Baumeister W, Förster F.
    Near-atomic resolution structural model of the yeast 26S proteasome.
    Proc. Natl. Acad. Sci. 109:14870-5 (2012) PubMed, DOI: 10.1073/pnas.1213333109 (open access)
    * equal contribution
    Highlight on
    PDB Molecule of the Month
  54. Pfeffer S, Brandt F, Hrabe T, Lang S, Eibauer M, Zimmermann R, Förster F.
    Structure and 3D arrangement of ER membrane associated ribosomes.
    Structure 20:1508-18 (2012). PubMed, DOI: 10.1016/j.str.2012.06.010 (open access)
    Highlight by HFSP
    Best of Structure 2012
  55. Walzthoeni T, Claassen M, Leitner A, Herzog F, Bohn S, Förster F, Beck M, Aebersold R.
    False discovery rate estimation for cross-linked peptides identified by MS.
    Nat. Methods 9:901-3 (2012). PubMed, DOI: 10.1038/nmeth.2103
  56. Chen Y, Hrabe T, Pfeffer S, Pauly O, Mateus D, Navab N, Förster F.
    Detection and Identification of macromolecular complexes in cryo-electron tomograms using support vector machines.
    Biomedical Imaging (ISBI), 2012 9th IEEE International Symposium on, 1373-1376 (2012). DOI: 10.1109/ISBI.2012.6235823
  57. Schönegge AM, Villa E, Förster F, Hegerl R, Peters J, Baumeister W, Rockel B.
    The Structure of Human Tripeptidyl Peptidase II as Determined by a Hybrid Approach.
    Structure 20:593-603 (2012). PubMed, DOI: 10.1016/j.str.2012.01.025
  58. Leitner A, Reischl R, Walzthoeni T, Herzog F, Bohn S, Foerster F, Aebersold R.
    Expanding the chemical cross-linking toolbox by the use of multiple proteases and enrichment by size exclusion chromatography.
    Mol. Cell. Proteomics 11:M111.014126 (2012). PubMed, DOI: 10.1074/mcp.M111.014126 (open access)
  59. Lasker K*, Förster F*, Bohn S, Walzthoeni T, Villa E, Unverdorben P, Beck F, Aebersold R, Sali A, Baumeister W.
    Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach
    Proc. Natl. Acad. Sci. USA 109:1380-7 (2012). PubMed, DOI: 10.1073/pnas.1120559109 (open access)
    * equal contribution
  60. Hrabe T, Chen Y, Pfeffer S, Kuhn-Cuellar L, Mangold AV, Förster F.
    PyTom: a python-based toolbox for localization of macromolecules in cryo-electron tomograms and subtomogram analysis.
    J. Struct. Biol. 178:177-88 (2012). PubMed, DOI: 10.1016/j.jsb.2011.12.003.
  61. Sakata E, Bohn S, Mihalache O, Kiss P, Beck F, Nagy I, Nickell S, Tanaka K, Saeki Y, Förster F, Baumeister W.
    Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy.
    Proc. Natl. Acad. Sci. USA 109:1479-84 (2012). PubMed, DOI: 10.1073/pnas.1119394109 (open access)
  62. Pathare GR, 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.
    The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together.
    Proc. Natl. Acad. Sci. USA 109:149-54 (2012). PubMed, DOI: 10.1073/pnas.1119394109 (open access)
  63. Förster F, Villa E, Thomas D, Korinek A, Baumeister W.
    Structure determination of macromolecular complexes by cryo-electron microscopy in vitro and in situ.
    (Chap. 1.14), in Comprehensive Biophysics 1, Biophysical Techniques for Structural Characterization of Macromolecules, ed. Egelman, E. H., Dyson, H. J., Elsevier B. V. Academic Press, Oxford, pp. 245-276 (2012). Elsevier
  64. Lucic V, Baumeister W, Förster F.
    Studying the macromolecular machinery of cells in situ by cryo-electron tomography.
    (Chap. 2.5), in Comprehensive Biophysics 2, Biophysical Techniques for Characterization of Cells, ed. Egelman, E.H., Schwille, P., Elsevier B. V. Academic Press, Oxford, pp. 59-89 (2012). Elsevier
  65. Sakata E, Stengel F, Zhou M, Saeki Y, Förster F, Baumeister W, Tanaka K, Fukunaga K, Robinson CVR.
    The catalytic activity of Ubp6 enhances maturation of the proteasomal regulatory particle.
    Mol. Cell 42:637-49 (2011) PubMed, DOI: 10.1016/j.molcel.2011.04.021 (open access)
  66. Hrabe T, Förster F.
    Structure determination by Single Particle Cryo Electron Tomography.
    In: Encyclopedia of Life Sciences (2011). DOI: 10.1002/9780470015902.a0023175
  67. Bohn S, Beck F, Sakata E, Walzthoeni T, Beck M, Aebersold R, Förster F, Baumeister W, Nickell S.
    Structure of the 26S proteasome from Schizosaccharomyces pombe at sub-nanometer resolution.
    Proc. Natl. Acad. Sci. USA 107:20992-7 (2010) PubMed, DOI: 10.1073/pnas.1015530107 (open access)
    Faculty of 1000
  68. Abrahams et al.
    "4D biology for health and disease" workshop report
    N. Biotechnol. (2010) PubMed
  69. Förster F, Villa E.
    Integration of cryo-EM with atomic and protein-protein interaction data
    Meth. Enzymol. 483:47-72 (2010) PubMed, DOI: 10.1016/S0076-6879(10)83003-4
  70. Förster F, Han BG, Beck, M.
    Visual Proteomics
    Meth. Enzymol. 483:215-43 (2010) PubMed, DOI: 10.1016/S0076-6879(10)83011-3
  71. Förster F, Lasker K, Nickell S, Sali A, Baumeister W.
    Towards an integrated structural model of the 26S proteasome.
    Mol. Cell. Proteomics 9:1666-77 (2010). PubMed , DOI: 10.1074/mcp.R000002-MCP201
  72. Förster F, Lasker K, Beck F, Nickell S, Sali A, Baumeister W.
    An atomic model AAA-ATPase/20S core particle sub-complex of the 26S proteasome.
    Biochem. Biophys. Res. Commun. 388:228-233 (2009). PubMed, DOI: 10.1016/j.bbrc.2009.07.145
  73. Nickell S, Beck F, Scheres S, Korinek A, Förster F, Lasker K, Mihalache O, Sun N, Nagy I, Sali A, Plitzko JM, Carazo JM, Mann M, Baumeister W,
    Insights into the molecular architecture of the 26S proteasome.
    Proc. Natl. Acad. Sci. USA 106:11943-7 (2009). PubMed, DOI: 10.1073/pnas.0905081106 (open access)
  74. Förster F, Webb B, Tsuruta H, Agard DA, Sali A,
    Integration of small angle X-ray scattering data and modeling for structure determination of multidomain proteins and complexes.
    J.Mol.Biol. 382:1089-1106 (2008). PubMed, DOI: 10.1016/j.jmb.2008.07.074
  75. Krukenberg KA, Förster F, Rice LM, Sali A, Agard DA,
    Novel conformation of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90.
    Structure, 16:755-65 (2008). PubMed, DOI: 10.1016/j.str.2008.01.021
    Faculty of 1000
  76. Alber F, Förster F, Korkin K, Topf M, Sali A,
    Integrating Diverse Data for Structure Determination of Macromolecular Assemblies.
    Annu. Rev. Biochem., 77:443-477 (2008). PubMed, DOI: 10.1146/annurev.biochem.77.060407.135530
  77. Förster F, Pruggnaller S, Seybert A, Frangakis AS,
    Classification of Cryo-Electron Sub-Tomograms using Constrained Correlation.
    J. Struct. Biol. 161:276-286 (2008). PubMed, DOI: 10.1016/j.jsb.2007.07.006
  78. Beck M, Lucic V, Förster F, Baumeister W, Medalia O,
    Snapshots of Nuclear Pore Complexes in Action Taken by Cryoelectron Tomography.
    Nature 449:611-615 (2007). PubMed, DOI: 10.1038/nature06170
  79. Förster F, Hegerl R,
    Structure determination in situ by averaging of tomograms.
    Methods Cell Biol. 79:741-67 (2007). PubMed, DOI: 10.1016/S0091-679X(06)79029-X
  80. Ortiz J, Förster F, Kürner J, Linaroudis A, Baumeister W,
    Mapping 70S ribosomes in intact cells by cryo-electron tomography and pattern recognition.
    J. Struct. Biol. 156:334-41 (2006). PubMed, DOI: 10.1016/j.jsb.2006.04.014
    Faculty of 1000
  81. Briggs JA, Grünewald K, Glass B, Förster F, Kräusslich HG, Fuller SD,
    The Mechanism of HIV-1 core assembly: insights from three-dimensional reconstructions of authentic virions.
    Structure 14:15-20 (2006). PubMed
    Faculty of 1000
  82. Lucic V, Förster F, Baumeister W,
    Structural studies by electron tomography: from cells to molecules.
    Annu. Rev. Biochem. 74:833-65 (2005). PubMed
  83. Förster F, Medalia O, Zauberman N, Baumeister W, Fass D,
    Retrovirus envelope protein complex structure in situ studied by cryo-electron tomography.
    Proc. Natl. Acad. Sci. USA 102:4729-34 (2005). PubMed, DOI: 10.1073/pnas.0409178102 (open access)
    Financial Times Deutschland
  84. Miao JW, Förster F, Levi O,
    Equally sloped tomography with oversampling reconstruction.
    Phys. Rev. B. 7205:2103-2106 (2005). DOI: 10.1103/PhysRevB.72.052103 (open access)
  85. Lucic V, Yang T, Schweikert G, Förster F, Baumeister W,
    Morphological characterization of molecular complexes present in the synaptic cleft.
    Structure. 13:423-34 (2005). PubMed
    Faculty of 1000
  86. Nickell S, Förster F, Linaroudis A, Net WD, Beck F, Hegerl R, Baumeister W, Plitzko JM,
    TOM software toolbox: acquisition and analysis for electron tomography.
    J. Struct. Biol. 149:227-34 (2005). PubMed
  87. Beck M, Förster F, Ecke M, Plitzko JM, Melchior F, Gerisch G, Baumeister W, Medalia O,
    Nuclear pore complex structure and dynamics revealed by cryoelectron tomography.
    Science. 306:1387-90 (2004). PubMed
    Faculty of 1000
  88. Frangakis AS, Förster F,
    Computational exploration of structural information from cryo-electron tomograms.
    Curr. Opin. Struct. Biol. 14:325-31 (2004). PubMed, DOI:10.1016/
  89. Kurz P, Förster F, Nordstrom L, Bihlmayer G, Blugel S,
    Ab initio treatment of noncollinear magnets with the full-potential linearized augmented plane wave method.
    Phys. Rev. B. 69 085317 (2004). DOI:10.1103/PhysRevB.69.024415 (open access)
  90. Frangakis AS, Böhm J, Förster F, Nickell S, Nicastro D, Typke D, Hegerl R, Baumeister W,
    Identification of macromolecular complexes in cryoelectron tomograms of phantom cells.
    Proc. Natl. Acad. Sci. USA. 99:14153-8 (2002). PubMed, DOI:10.1073/pnas.172520299 (open access)
  91. Plitzko JM, Frangakis AS, Nickell S, Förster F, Gross A, Baumeister W,
    In vivo veritas: electron cryotomography of cells.
    Trends Biotech. 20 (8 Suppl.) S40-S44 (2002). DOI:10.1016/S0167-7799(02)02017-6


  1. Luis Kuhn Cuellar (2016): Geometric analysis of macromolecule organization within cryo-electron tomograms. PhD Thesis TU Muenchen.
  2. Antje Aufderheide (2016): Structural studies of the 26S proteasome and its interaction with Ubp6 by cryo-electron microscopy. PhD Thesis TU Muenchen.
  3. Jan M. Schuller (2016): Cryo-EM single particle analysis of ASCE-ATPases. PhD Thesis TU Muenchen.
  4. Robert Englmeier (2016): Structural investigation of mitochondrial translation systems using Cryoelectron Tomography. Master Thesis LMU Muenchen.
  5. Laura Burbaum (2015): Strukturanalyse von Hefe-Polysomen mittels Kryo-Elektronentomographie. Master Thesis Westfälische Wilhelms-Universität Münster.
  6. Stefan Pfeffer (2015): Structural analysis of co-translational protein transport at native membranes. PhD Thesis TU Muenchen.
  7. Yuxiang Chen (2014): 3D Image Processing for Structural Analysis of Macromolecules Using Cryo-Electron Tomography. PhD Thesis TU Muenchen.
  8. Corinna Brockhaus (2014): Structural studies of the protein complexes p97-p47 and p97-Npl4-Ufd1. Bachelor Thesis LMU Muenchen.
  9. Pia Unverdorben (2014): Pseudo-atomare Interpretation von Konformationsaenderungen des 26S Proteasoms nach Klassifizierung von Kryo-Elektronenmikroskopie-Daten. PhD Thesis TU Muenchen.
  10. Michaela Hartwig (2014): Strukturelle Untersuchung der AAA-ATPase Cdc48 mit ihren Kofaktoren. Bachelor Thesis Hochschule Muenchen
  11. Robin Stocklauser (2012): Kryoelektronentomographische Analyse makromolekularer Komplexe in Mitochondrien. Bachelor Thesis Univ. Ulm.
  12. Thomas Hrabe (2012): Entwicklung rechnergestuetzter Methoden fuer die Strukturanalyse von Makromolekülen durch die Kryoelektronentomographie. PhD Thesis TU Muenchen.
  13. Yuxiang Chen (2010): Identification of Macromolecular Complexes in Cryo-electron Tomograms using Support Vector Machine and Combined Correlation Functions. Master Thesis TU Muenchen.
  14. Stefan Pfeffer (2010): Kryoelektronentomographische Analyse membrangebundener eukaryotischer Polyribosomen. Diploma Thesis Univ. Tuebingen.
  15. Ann-Victoria Mangold (2010): Kryoelektronentomographische Untersuchungen an mikrosomalen Fraktionen aus Saccharomyces cerevisiae. Diploma Thesis Univ. Stuttgart.
  16. Friedrich Förster (2005): Quantitative Analyse von Kryoelektronentomogrammen mittels Korrelationsmethoden. PhD Thesis TU Muenchen.
  17. Friedrich Förster (2000): Untersuchung von nichtkollinearem Magnetismus in ultraduennen Filmen. Diploma Thesis RWTH Aachen.