Stefan Raunser

Summary

Country: Germany

Publications

  1. doi request reprint Deciphering the tubulin code
    Stefan Raunser
    Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany Electronic address
    Cell 161:960-1. 2015
  2. doi request reprint Electron crystallography as a technique to study the structure on membrane proteins in a lipidic environment
    Stefan Raunser
    Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany
    Annu Rev Biophys 38:89-105. 2009
  3. doi request reprint Mechanism of Tc toxin action revealed in molecular detail
    Dominic Meusch
    1 Department of Physical Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany 2
    Nature 508:61-5. 2014
  4. pmc Insights from the reconstitution of the divergent outer kinetochore of Drosophila melanogaster
    Yahui Liu
    Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto Hahn Straße 11, 44227 Dortmund, Germany
    Open Biol 6:150236. 2016
  5. doi request reprint Membrane insertion of a Tc toxin in near-atomic detail
    Christos Gatsogiannis
    Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany
    Nat Struct Mol Biol 23:884-890. 2016
  6. doi request reprint A syringe-like injection mechanism in Photorhabdus luminescens toxins
    Christos Gatsogiannis
    Department of Physical Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany
    Nature 495:520-3. 2013
  7. pmc The role of Cdc42 and Gic1 in the regulation of septin filament formation and dissociation
    Yashar Sadian
    Department of Physical Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany
    elife 2:e01085. 2013
  8. doi request reprint Structure of mega-hemocyanin reveals protein origami in snails
    Christos Gatsogiannis
    Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Otto Hahn Strasse 11, 44227 Dortmund, Germany Institute of Chemistry and Biochemistry, Freie Universitat Berlin, Thielallee 63, 14195 Berlin, Germany Electronic address
    Structure 23:93-103. 2015
  9. doi request reprint Cryo-EM as a tool for structure-based drug development
    Felipe Merino
    Max Planck Institute of Molecular Physiology, Structural Biochemistry, Otto Hahn Str 11, 44227, Dortmund, Germany
    Angew Chem Int Ed Engl . 2016
  10. pmc The mother of all actins?
    Felipe Merino
    Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany
    elife 5:. 2016

Collaborators

  • Andrea Musacchio
  • Jürgen Markl
  • Alexander Leitner
  • Oliver T Fackler
  • Roland Benz
  • Matthias Geyer
  • Christof M Niemeyer
  • Hans Georg Mannherz
  • Thomas Walz
  • Alfred Wittinghofer
  • Christos Gatsogiannis
  • Felipe Merino
  • Arsen Petrovic
  • Dominic Meusch
  • Oliver Hofnagel
  • Rouslan G Efremov
  • Franz Herzog
  • Yahui Liu
  • Daniel Prumbaum
  • Alexandra Friese
  • Jenny Keller
  • Shyamal Mosalaganti
  • Michael Erkelenz
  • Alexander E Lang
  • Klaus Aktories
  • Elmar Behrmann
  • Yashar Sadian
  • Begona Sot
  • André Schönichen
  • Pascaline Rombaut
  • Alex C Faesen
  • Franziska Leidreiter
  • Daniel Roderer
  • Josef Fischböck
  • Pim J Huis In 't Veld
  • Ruedi Aebersold
  • Veronica Krenn
  • Valentina Cecatiello
  • Sabine Wohlgemuth
  • Ingrid R Vetter
  • Barbara Saccà
  • Anna De Antoni
  • Rebecca Meyer
  • Katharina Overlack
  • Sebastiano Pasqualato
  • Dennis M Bauer
  • Marta Mattiuzzo
  • Vanda Pfaumann
  • Cora Ann Schoenenberger
  • Antonina J Mazur
  • Roger S Goody
  • Csilla Patasi
  • Sonja Kuhn
  • Unai Silvan
  • Leif Dehmelt
  • Marian Farkasovsky

Detail Information

Publications16

  1. doi request reprint Deciphering the tubulin code
    Stefan Raunser
    Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany Electronic address
    Cell 161:960-1. 2015
    ..Garnham et al. report the first structure of a TTLL protein alone and in complex with microtubules, elucidating their mechanism of action...
  2. doi request reprint Electron crystallography as a technique to study the structure on membrane proteins in a lipidic environment
    Stefan Raunser
    Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany
    Annu Rev Biophys 38:89-105. 2009
    ....
  3. doi request reprint Mechanism of Tc toxin action revealed in molecular detail
    Dominic Meusch
    1 Department of Physical Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany 2
    Nature 508:61-5. 2014
    ..Our results allow us to understand key steps of infections involving Tc toxins at the molecular level. ..
  4. pmc Insights from the reconstitution of the divergent outer kinetochore of Drosophila melanogaster
    Yahui Liu
    Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto Hahn Straße 11, 44227 Dortmund, Germany
    Open Biol 6:150236. 2016
    ..Our studies shed light on the structural and functional organization of a highly divergent kinetochore particle. ..
  5. doi request reprint Membrane insertion of a Tc toxin in near-atomic detail
    Christos Gatsogiannis
    Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany
    Nat Struct Mol Biol 23:884-890. 2016
    ..The linker domain is folded and packed into a pocket formed by the other domains of the toxin, thereby considerably contributing to stabilization of the pore state...
  6. doi request reprint A syringe-like injection mechanism in Photorhabdus luminescens toxins
    Christos Gatsogiannis
    Department of Physical Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany
    Nature 495:520-3. 2013
    ..luminescens and other pathogens, including human pathogenic bacteria, and serves as a strong foundation for the development of biopesticides...
  7. pmc The role of Cdc42 and Gic1 in the regulation of septin filament formation and dissociation
    Yashar Sadian
    Department of Physical Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany
    elife 2:e01085. 2013
    ..Based on our results we propose a novel regulatory mechanism for septin filament formation and dissociation. DOI: http://dx.doi.org/10.7554/eLife.01085.001. ..
  8. doi request reprint Structure of mega-hemocyanin reveals protein origami in snails
    Christos Gatsogiannis
    Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Otto Hahn Strasse 11, 44227 Dortmund, Germany Institute of Chemistry and Biochemistry, Freie Universitat Berlin, Thielallee 63, 14195 Berlin, Germany Electronic address
    Structure 23:93-103. 2015
    ..A comparison between the two structures suggests a surprisingly simple evolutionary mechanism leading to these large oxygen transporters. ..
  9. doi request reprint Cryo-EM as a tool for structure-based drug development
    Felipe Merino
    Max Planck Institute of Molecular Physiology, Structural Biochemistry, Otto Hahn Str 11, 44227, Dortmund, Germany
    Angew Chem Int Ed Engl . 2016
    ..Finally, we stress the current limits of cryo-EM, and methodological issues related to its usage as drug development tool...
  10. pmc The mother of all actins?
    Felipe Merino
    Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany
    elife 5:. 2016
    ..New insights into the structure of filaments made of crenactin, a homolog of actin found in archaea, shed light on how the cytoskeleton might have evolved...
  11. pmc Molecular requirements for the inter-subunit interaction and kinetochore recruitment of SKAP and Astrin
    Alexandra Friese
    Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto Hahn Straße 11, 44227 Dortmund, Germany
    Nat Commun 7:11407. 2016
    ..Collectively, our studies represent the first thorough mechanistic analysis of SKAP and Astrin, and significantly advance our functional understanding of these important mitotic proteins. ..
  12. doi request reprint Architecture and conformational switch mechanism of the ryanodine receptor
    Rouslan G Efremov
    1 Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany 2 Structural Biology Research Center, Vlaams Instituut voor Biotechnologie VIB, 1050 Brussels, Belgium 3 Structural Biology Brussels, Vrije Universiteit Brussel VUB, 1050 Brussels, Belgium
    Nature 517:39-43. 2015
    ..We identify the calcium-binding EF-hand domain and show that it functions as a conformational switch allosterically gating the channel. ..
  13. doi request reprint Modular assembly of RWD domains on the Mis12 complex underlies outer kinetochore organization
    Arsen Petrovic
    Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto Hahn Straße 11, 44227 Dortmund, Germany
    Mol Cell 53:591-605. 2014
    ..Our observations unveil a regular pattern in the construction of the outer kinetochore. ..
  14. doi request reprint A facile method for preparation of tailored scaffolds for DNA-origami
    Michael Erkelenz
    Technische Universitat Dortmund, Fakultat Chemie, Biologisch Chemische Mikrostrukturtechnik, Otto Hahn Str 6, 44227 Dortmund, Germany
    Small 10:73-7. 2014
    ....
  15. doi request reprint FHOD1 is a combined actin filament capping and bundling factor that selectively associates with actin arcs and stress fibers
    André Schönichen
    Department of Physical Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany
    J Cell Sci 126:1891-901. 2013
    ....
  16. pmc Ras GTPase activating (RasGAP) activity of the dual specificity GAP protein Rasal requires colocalization and C2 domain binding to lipid membranes
    Begona Sot
    Department of Structural Biology, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany
    Proc Natl Acad Sci U S A 110:111-6. 2013
    ..Finally we show, that similar to the C2 domains of synaptotagmins, the Rasal tandem C2 domains are able to sense and induce membrane curvature by the insertion of hydrophobic loops into the membrane...