Sachse lab

Electron cryomicroscopy of autophagy complexes

All publications from the Sachse lab on Pubmed. For more details on citation statistics, follow us on Google Scholar, Researcher ID and ORCID.org.

2017

  • Jakobi, A. J., Wilmanns, M., and Sachse, C. (2017). Model-based local density sharpening of cryo-EM maps. eLife; 6:e27131.
  • Sadian, Y., Tafur, L., Kosinski, J., Jakobi, A. J., Wetzel, R., Buczak, K., Hagen, W. J., Beck, M., Sachse, C., and Müller, C. W., Structural insights into transcription initiation by yeast RNA polymerase I. EMBO J, 36, (18) 2698–2709.
  • Kolovou, A. , Schorb, M., Tarafder, A., Sachse, C., Schwab, Y., Santarella-Mellwig, R. (2017) A new method for cryo-sectioning cell monolayers using a correlative workflow. Methods Cell Biol., 140, 85–103.
  • Dauden, M. I., Kosinski, J., Kolaj-Robin, O., Desfosses, A., Ori, A., Faux, C., Hoffmann, N. A., Onuma, O. F., Breunig, K. D., Beck, M., Sachse, C., Seraphin, B., Glatt, S. & Müller, C. W. (2017). Architecture of the yeast Elongator complex. EMBO Rep,18(2) 264–279.

2016

  • Tafur, L., Sadian, Y., Hoffmann, N. A., Jakobi, A. J., Wetzel, R., Hagen, W. J. H., Sachse, C., & Müller, C. W. (2016). Molecular Structures of Transcribing RNA Polymerase I. Mol Cell, 64(6) 1135–1143.
  • Ohashi Y., Soler N., Garcia Ortegon M., Zhang L., Kirsten M. L., Perisic O., Masson G. R., Burke J. E., Jakobi A.J., Apostolakis A. A., Johnson C. M., Ohashi M., Ktistakis N. T., Sachse C., Williams R. L. (2016). Characterization of Atg38 and NRBF2, a fifth subunit of the autophagic Vps34 complex. Autophagy, 12(11), 2129–2144.
  • Schur, F.K.M., Obr, M., Hagen, W.J.H., Wan, W., Jakobi, A.J., Kirkpatrick, J.M., Sachse, C., Kräusslich, H.-G., Briggs J.A.G. (2016). An atomic model of HIV-1 capsid-SP1 reveals structures regulating assembly and maturation. (2016). An atomic model of HIV-1 capsid-SP1 reveals structures regulating assembly and maturation. Science, 353(6298), 506–508.
  • Fromm, S.A., Sachse, C. (2016). Cryo-EM structure determination using segmented helical image reconstruction. Methods in Enzymology, 579, 307–328.
  • Bertipaglia, C., Schneider, S., Tarafder, A. K., Jakobi, A. J., Bykov, Y. S., Picco, A., Kukulski W., Konsinski J., Hagen W.J.H., Wilmanns M., Briggs, J.A.G., Sachse, C. (2016). Higher-order assemblies of oligomeric cargo receptor complexes form the membrane scaffold of the Cvt vesicle. EMBO Rep, 17(7), 1044–1060.
  • Hoffmann, N. A., Jakobi, A. J., Vorländer, M. K., Sachse, C., & Müller, C. W. (2016). Transcribing RNA polymerase III observed by electron cryo-microscopy. FEBS J, 283(15), 2811–2819.
  • Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., … Sachse, C. … et al. (2016). Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). Autophagy, 12(1), 1–222.

2015

  • Hoffmann, N. A., Jakobi, A. J., Moreno-Morcillo, M., Glatt, S., Kosinski, J., Hagen, W. J. H., Sachse, C., Müller C. W. (2015). Molecular structures of unbound and transcribing RNA polymerase III. Nature, 528(7581), 231–236.
  • Sachse, C. (2015). Single-particle based helical reconstruction—how to make the most of real and Fourier space. AIMS Biophysics, 2(2), 219–244.
  • Johansen, T., & Sachse, C. (2015). The higher-order molecular organization of p62/SQSTM1. Oncotarget, 6(19), 16796-16797.
  • Bharat, T.A.M., Murshudov, G.N., Sachse, C., and Löwe, J. (2015). Structures of actin-like ParM filaments show architecture of plasmid-segregating spindles. Nature, 523(7558), 106–110.
  • Ciuffa R., Lamark T., Tarafder A., Guesdon A., Rybina S., Hagen W.J.H., Johansen T., Sachse C. (2015). The selective autophagy receptor p62 forms a flexible filamentous helical scaffold. Cell reports, 11(5), 748–758.
  • Skruzny M., Desfosses A., Prinz S., Dodonova S.O., Gieras A., Uetrecht C., Jakobi A.J., Abella M., Hagen W.J.H., Schulz J., Meijers R., Rybin V., Briggs J.A.G., Sachse C., Kaksonen M., (2015). An organized co-assembly of clathrin adaptors is essential for endocytosis. Developmental cell, 33(2), 150–162.
  • Gutsche, I., Desfosses, A., Effantin, G., Ling, W.L., Haupt, M., Ruigrok, R.W.H., Sachse, C., and Schoehn, G. (2015). Near-atomic cryo-EM structure of the helical measles virus nucleocapsid. Science, 348(6235), 704–707.
  • Ehebauer, M.T., Zimmermann, M., Jakobi, A.J., Noens, E.E., Laubitz, D., Cichocki, B., Marrakchi, H., Lanéelle, M.-A., Daffé, M., Sachse, C., et al. (2015). Characterization of the Mycobacterial Acyl-CoA Carboxylase Holo Complexes Reveals Their Functional Expansion into Amino Acid Catabolism. PLoS Pathog 11, e1004623.
  • Fromm, S.A., Bharat, T.A.M., Jakobi, A.J., Hagen, W.J.H., and Sachse, C. (2015). Seeing tobacco mosaic virus through direct electron detectors. J Struct Biol 189, 87–97.
  • Elad, N., De Strooper, B., Lismont, S., Hagen, W., Veugelen, S., Arimon, M., Horre, K., Berezovska, O., Sachse, C., and Chavez-Gutierrez, L. (2015). The dynamic conformational landscape of  γ-secretase. J Cell Sci 128, 589–598.

2014

  • Vahokoski, J., Bhargav, S.P., Desfosses, A., Andreadaki, M., Kumpula, E.-P., Martinez, S.M., Ignatev, A., Lepper, S., Frischknecht, F., Sidén-Kiamos, I., Sachse, C. and Kursula, I. (2014). Structural differences explain diverse functions of Plasmodium actins. PLoS Pathog 10, e1004091.
  • Afonin, S., Glaser, R.W., Sachse, C., Salgado, J., Wadhwani, P., and Ulrich, A.S. (2014). (19)F NMR screening of unrelated antimicrobial peptides shows that membrane interactions are largely governed by lipids. Biochim Biophys Acta 1838, 2260–2268.
  • Desfosses, A., Ciuffa, R., Gutsche, I., and Sachse, C. (2014). SPRING - an image processing package for single-particle based helical reconstruction from electron cryomicrographs. J Struct Biol 185, 15–26.

2015

  • Hoffmann, N. A., Jakobi, A. J., Moreno-Morcillo, M., Glatt, S., Kosinski, J., Hagen, W. J. H., Sachse, C., Müller C. W. (2015). Molecular structures of unbound and transcribing RNA polymerase III. Nature, 528(7581), 231–236.
  • Sachse, C. (2015). Single-particle based helical reconstruction—how to make the most of real and Fourier space. AIMS Biophysics, 2(2), 219–244.
  • Johansen, T., & Sachse, C. (2015). The higher-order molecular organization of p62/SQSTM1. Oncotarget, 6(19), 16796-16797.
  • Bharat, T.A.M., Murshudov, G.N., Sachse, C., and Löwe, J. (2015). Structures of actin-like ParM filaments show architecture of plasmid-segregating spindles. Nature, 523(7558), 106–110.
  • Ciuffa R., Lamark T., Tarafder A., Guesdon A., Rybina S., Hagen W.J.H., Johansen T., Sachse C. (2015). The selective autophagy receptor p62 forms a flexible filamentous helical scaffold. Cell reports, 11(5), 748–758.
  • Skruzny M., Desfosses A., Prinz S., Dodonova S.O., Gieras A., Uetrecht C., Jakobi A.J., Abella M., Hagen W.J.H., Schulz J., Meijers R., Rybin V., Briggs J.A.G., Sachse C., Kaksonen M., (2015). An organized co-assembly of clathrin adaptors is essential for endocytosis. Developmental cell, 33(2), 150–162.
  • Gutsche, I., Desfosses, A., Effantin, G., Ling, W.L., Haupt, M., Ruigrok, R.W.H., Sachse, C., and Schoehn, G. (2015). Near-atomic cryo-EM structure of the helical measles virus nucleocapsid. Science, 348(6235), 704–707.
  • Ehebauer, M.T., Zimmermann, M., Jakobi, A.J., Noens, E.E., Laubitz, D., Cichocki, B., Marrakchi, H., Lanéelle, M.-A., Daffé, M., Sachse, C., et al. (2015). Characterization of the Mycobacterial Acyl-CoA Carboxylase Holo Complexes Reveals Their Functional Expansion into Amino Acid Catabolism. PLoS Pathog 11, e1004623.
  • Fromm, S.A., Bharat, T.A.M., Jakobi, A.J., Hagen, W.J.H., and Sachse, C. (2015). Seeing tobacco mosaic virus through direct electron detectors. J Struct Biol 189, 87–97.
  • Elad, N., De Strooper, B., Lismont, S., Hagen, W., Veugelen, S., Arimon, M., Horre, K., Berezovska, O., Sachse, C., and Chavez-Gutierrez, L. (2015). The dynamic conformational landscape of  γ-secretase. J Cell Sci 128, 589–598.

2013

  • Gombos, L., Neuner, A., Berynskyy, M., Fava, L.L., Wade, R.C., Sachse, C., and Schiebel, E. (2013). GTP regulates the microtubule nucleation activity of γ-tubulin. Nat Cell Biol 15, 1317–1327.

2012

  • Bharat, T.A.M., Davey, N.E., Ulbrich, P., Riches, J.D., de Marco, A., Rumlova, M., Sachse, C., Ruml, T., and Briggs, J.A.G. (2012). Structure of the immature retroviral capsid at 8 Å resolution by cryo-electron microscopy. Nature 487, 385–389.
  • Guichard, P., Desfosses, A., Maheshwari, A., Hachet, V., Dietrich, C., Brune, A., Ishikawa, T., Sachse, C., and Gönczy, P. (2012). Cartwheel architecture of Trichonympha basal body. Science 337, 553.

2010

  • Korkhov, V.M., Sachse, C., Short, J.M., and Tate, C.G. (2010). Three-dimensional structure of TspO by electron cryomicroscopy of helical crystals. Structure 18, 677–687.
  • Sachse, C., Grigorieff, N., and Fändrich, M. (2010). Nanoscale flexibility parameters of Alzheimer amyloid fibrils determined by electron cryo-microscopy. Angew Chem Int Ed Engl 49, 1321–1323.

2009

  • Low, H.H., Sachse, C., Amos, L.A., and Löwe, J. (2009). Structure of a bacterial dynamin-like protein lipid tube provides a mechanism for assembly and membrane curving. Cell 139, 1342–1352.
  • Meinhardt, J., Sachse, C., Hortschansky, P., Grigorieff, N., and Fändrich, M. (2009). Abeta(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils. J Mol Biol 386, 869–877.
  • Schmidt, M., Sachse, C., Richter, W., Xu, C., Fändrich, M., and Grigorieff, N. (2009). Comparison of Alzheimer Abeta(1-40) and Abeta(1-42) amyloid fibrils reveals similar protofilament structures. Proc Natl Acad Sci USA 106, 19813–19818.

2008

  • Chen, J.Z., Sachse, C., Xu, C., Mielke, T., Spahn, C.M.T., and Grigorieff, N. (2008). A dose-rate effect in single-particle electron microscopy. J Struct Biol 161, 92–100.
  • Sachse, C., Fändrich, M., and Grigorieff, N. (2008). Paired beta-sheet structure of an Abeta(1-40) amyloid fibril revealed by electron microscopy. Proc Natl Acad Sci USA 105, 7462–7466.

2007

  • Habicht, G., Haupt, C., Friedrich, R.P., Hortschansky, P., Sachse, C., Meinhardt, J., Wieligmann, K., Gellermann, G.P., Brodhun, M., Götz, J., et al. (2007). Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Abeta protofibrils. Proc Natl Acad Sci USA 104, 19232–19237.
  • Sachse, C., Chen, J.Z., Coureux, P.-D., Stroupe, M.E., Fändrich, M., and Grigorieff, N. (2007). High-resolution electron microscopy of helical specimens: a fresh look at tobacco mosaic virus. J Mol Biol 371, 812–835.

2006

  • Sachse, C., Xu, C., Wieligmann, K., Diekmann, S., Grigorieff, N., and Fändrich, M. (2006). Quaternary structure of a mature amyloid fibril from Alzheimer's Abeta(1-40) peptide. J Mol Biol 362, 347–354.

2005

  • Glaser, R.W., Sachse, C., Dürr, U.H.N., Wadhwani, P., Afonin, S., Strandberg, E., and Ulrich, A.S. (2005). Concentration-dependent realignment of the antimicrobial peptide PGLa in lipid membranes observed by solid-state 19F-NMR. Biophys. J. 88, 3392–3397.

2004

  • Glaser, R.W., Sachse, C., Dürr, U.H.N., Wadhwani, P., and Ulrich, A.S. (2004). Orientation of the antimicrobial peptide PGLa in lipid membranes determined from 19F-NMR dipolar couplings of 4-CF3-phenylglycine labels. J. Magn. Reson. 168, 153–163.