1. de Jager L, Jansen KI, Kapitein LC, Förster F, Howes SC.
    Increased microtubule lattice spacing correlates with selective binding of kinesin-1 in cells.
    bioRxiv:2022.05.25.493428 (2022).
  2. Förster F.
    Subtomogram analysis: The sum of a tomogram’s particles reveals molecular structure in situ.
    Journal of Structural Biology: X 2022, 6:100063.
  3. Fermie J, de Jager L, Foster H, Veenendaal T, de Heus C, van Dijk S, ten Brink C, Oorschot V, Yang L, Li W, Müller W, Howes S, Carter A, Förster F, Posthuma G, Gerritsen H, Klumperman J, Liv N.
    Bimodal Endocytic Probe for Three-Dimensional Correlative Light and Electron Microscopy.
    Cell Rep. Methods 2022, 2:100220.
  4. Hurdiss DL, El Kazzi P, Bauer L, Papageorgiou N, Ferron FP, Donselaar T, van Vliet ALW, Canard B, Decroly E, Brancale A, Zeev-Ben-Mordehai T, Förster F, van Kuppeveld FJM, Coutard B.
    Fluoxetine targets an allosteric site in the enterovirus 2C AAA+ ATPase and stabilizes a ring-shaped hexameric complex.
    Sci Adv 2022 8:eabj7615.
  5. Gubins I, Chaillet ML, van der Schot G, Trueba MC, Veltkamp RC, Förster F, Wang X, Kihara D, Moebel E, Nguyen NP, White T, Bunyak F, Papoulias G, Gerolymatos S, Zacharaki EI, Moustakas K, Zeng X, Liu S, Xu M, Wang Y, Chen C, Cui X, Zhang F.
    SHREC 2021: Classification in Cryo-electron Tomograms.
    In: Eurographics Workshop on 3D Object Retrieval (Biasotti, S, Dyke, R M, Lai, Y, Rosin, P L & Veltkamp, R C, eds.), pp. 5-17. The Eurographics Association.
  6. Liaci AM, Förster F.
    Take Me Home, Protein Roads: Structural Insights into Signal Peptide Interactions during ER Translocation.
    Int J Mol Sci 2021, 22.
  7. Englmeier R, Förster F.
    In Situ Studies of Mitochondrial Translation by Cryo-Electron Tomography.
    Methods Mol. Biol. 2021, 2192:243-268.
  8. Zimmermann R, Lang S, Lerner M, Forster F, Nguyen D, Helms V, Schrul B.
    Quantitative Proteomics and Differential Protein Abundance Analysis after the Depletion of PEX3 from Human Cells Identifies Additional Aspects of Protein Targeting to the ER.
    Int J Mol Sci 22 (2021).
  9. Waltz F, Salinas-Giegé T, Englmeier R, Meichel H, Soufari H, Kuhn L, Pfeffer S, Förster F, Engel BD, Giegé P, Drouard L, Hashem Y.
    How to build a ribosome from RNA fragments in Chlamydomonas mitochondria.
    Nature Communications 2021, 12:7176 (2021).
  10. Liaci AM, Steigenberger B, Tamara S, de Souza PCT, Gröllers-Mulderij M, Ogrissek P, Marrink SJ, Scheltema RA, Förster F.
    Structure of the Human Signal Peptidase Complex Reveals the Determinants for Signal Peptide Cleavage.
    Molecular Cell 2021, 81:3934-3948.
    PubMed, DOI:10.1016/j.molcel.2021.07.031, Open-access preprint ,
    bioRxiv:2020.11.11.378711 (2020).
  11. Fedry J, Hurdiss DL, Wang C, Li W, Obal G, Drulyte I, Du W, Howes SC, van Kuppeveld FJM, Förster F, Bosch BJ.
    Structural insights into the cross-neutralization of SARS-CoV and SARS-CoV-2 by the human monoclonal antibody 47D11.
    Science Adv. 2021, 7.
  12. Bhadra P, Schorr S, Lerner M, Nguyen D, Dudek J, Förster F, Helms V, Lang S, Zimmermann R.
    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 2021, 26:3591.
  13. Gubins I, Chaillet ML, van der Schot G, Veltkamp RC, Förster F, Hao Y, Wan X, Cui X, Zhang F, Moebel E, Wang X, Kihara D, Zeng X, Xu M, Nguyen NP, White T, Bunyak F.
    SHREC 2020: Classification in cryo-electron tomograms.
    Computers & Graphics 2021, 91:279-289
  14. Zhou Y, Kastritis PL, Dougherty SE, Bouvette J, Hsu AL, Burbaum L, Mosalaganti S, Pfeffer S, Hagen WJH, Förster F, Borgnia MJ, Vogel C, Beck M, Bartesaghi A, Silva GM.
    Structural impact of K63 ubiquitin on yeast translocating ribosomes under oxidative stress.
    Proc. Natl. Acad. Sci. USA 2020, 117:22157-22166. 
  15. Schorr S, Nguyen D, Hassdenteufel S, Nagaraj N, Cavalie A, Greiner M, Weissgerber P, Loi M, Paton AW, Paton JC, Molinari M, Förster F, Dudek J, Lang S, Helms V, Zimmermann R.
    Identification of signal peptide features for substrate specificity in human Sec62/Sec63-dependent ER protein import.
    FEBS J. 2020.
  16. 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 .
  17. 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
  18. 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.
  19. 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.
  20. 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).
  21. 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).
  22. Förster F.
    26S Proteasome: Structure and Function.
    In: Reference Module in Biomedical Research: Elsevier (2019).
  23. 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.
  24. 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.
  25. 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.
  26. 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
  27. 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
  28. 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.
  29. 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.
  30. 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.
  31. 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 .
  32. 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.
  33. 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
  34. 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.
  35. Förster F, Koster AJ.
    Recent advances in electron tomography.
    J. Struct. Biol. (2016). PubMed: PubMed, DOI:10.1016/j.jsb.2016.11.005.
  36. 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.
  37. 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
  38. 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.
  39. 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
  40. 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.
  41. Pfeffer P, Förster F.
    Sec61: a static framework for membrane-protein insertion.
    Channels 10:1-3 (2016). PubMed, DOI:10.1080/19336950.2015.1125737
  42. 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).
  43. 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)
  44. 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.
  45. Burbaum L, Pfeffer S, Förster F.
    Eiskalt ausgetrickst.
    Laborjournal (2015). (open access)
  46. 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
  47. Pfeffer S, Förster F.
    Proteintranslation und Prozessierung in physiologischer Umgebung abgebildet.
    Biospektrum 4:385-387 (2015). DOI:10.1007/s12268-015-0590-y
  48. 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
  49. 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
  50. 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
  51. 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
  52. 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)
  53. 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)
  54. 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
  55. 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)
  56. 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
  57. 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)
  58. 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
  59. 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
  60. 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
  61. 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
  62. 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
  63. 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)
  64. 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
  65. 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
  66. 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
  67. 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
  68. 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
  69. 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
  70. 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
  71. 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
  72. 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
  73. 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)
  74. 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
  75. 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.
  76. 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)
  77. 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)
  78. 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
  79. 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
  80. 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)
  81. Hrabe T, Förster F.
    Structure determination by Single Particle Cryo Electron Tomography.
    In: Encyclopedia of Life Sciences (2011). DOI: 10.1002/9780470015902.a0023175
  82. 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
  83. Abrahams et al.
    "4D biology for health and disease" workshop report
    N. Biotechnol. (2010) PubMed
  84. 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
  85. Förster F, Han BG, Beck, M.
    Visual Proteomics
    Meth. Enzymol. 483:215-43 (2010) PubMed, DOI: 10.1016/S0076-6879(10)83011-3
  86. 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
  87. 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
  88. 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)
  89. 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
  90. 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
  91. 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
  92. 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
  93. 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
  94. 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
  95. 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
  96. 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
  97. Lucic V, Förster F, Baumeister W,
    Structural studies by electron tomography: from cells to molecules.
    Annu. Rev. Biochem. 74:833-65 (2005). PubMed
  98. 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
  99. 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)
  100. 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
  101. 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
  102. 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
  103. 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/
  104. 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)
  105. 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)
  106. 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.