Holger Stark

Summary

Country: Germany

Publications

  1. ncbi request reprint Arrangement of RNA and proteins in the spliceosomal U1 small nuclear ribonucleoprotein particle
    H Stark
    Institut fur Molekularbiologie und Tumorforschung, Marburg, Germany
    Nature 409:539-42. 2001
  2. ncbi request reprint Three-dimensional electron cryomicroscopy of ribosomes
    Holger Stark
    Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
    Curr Protein Pept Sci 3:79-91. 2002
  3. ncbi request reprint Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex
    Holger Stark
    Max Planck Institute for Biophysical Chemistry, 37077 Gottingen, Germany
    Nat Struct Biol 9:849-54. 2002
  4. ncbi request reprint Cryo-electron microscopy of spliceosomal components
    Holger Stark
    Max Planck Institute for Biophysical Chemistry, 37077 Gottingen, Germany
    Annu Rev Biophys Biomol Struct 35:435-57. 2006
  5. doi request reprint Localization of Prp8, Brr2, Snu114 and U4/U6 proteins in the yeast tri-snRNP by electron microscopy
    Irina Häcker
    Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D 37077 Gottingen, Germany
    Nat Struct Mol Biol 15:1206-12. 2008
  6. ncbi request reprint Major conformational change in the complex SF3b upon integration into the spliceosomal U11/U12 di-snRNP as revealed by electron cryomicroscopy
    Monika M Golas
    Department of Cellular Biochemistry and Research Group of 3D Electron Cryomicroscopy, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D 37077 Gottingen, Germany
    Mol Cell 17:869-83. 2005
  7. pmc Protein composition and electron microscopy structure of affinity-purified human spliceosomal B complexes isolated under physiological conditions
    Jochen Deckert
    Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
    Mol Cell Biol 26:5528-43. 2006
  8. ncbi request reprint Organization of core spliceosomal components U5 snRNA loop I and U4/U6 Di-snRNP within U4/U6.U5 Tri-snRNP as revealed by electron cryomicroscopy
    Bjoern Sander
    Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
    Mol Cell 24:267-78. 2006
  9. pmc Exon, intron and splice site locations in the spliceosomal B complex
    Elmar Wolf
    Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Gottingen, Germany
    EMBO J 28:2283-92. 2009
  10. doi request reprint Ribosome dynamics and tRNA movement by time-resolved electron cryomicroscopy
    Niels Fischer
    3D Electron Cryomicroscopy Group, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
    Nature 466:329-33. 2010

Collaborators

Detail Information

Publications37

  1. ncbi request reprint Arrangement of RNA and proteins in the spliceosomal U1 small nuclear ribonucleoprotein particle
    H Stark
    Institut fur Molekularbiologie und Tumorforschung, Marburg, Germany
    Nature 409:539-42. 2001
    ....
  2. ncbi request reprint Three-dimensional electron cryomicroscopy of ribosomes
    Holger Stark
    Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
    Curr Protein Pept Sci 3:79-91. 2002
    ..In turn, the knowledge of the atomic structure of the ribosome makes detailed interpretations of cryo-EM maps possible at approximately 20 A resolution...
  3. ncbi request reprint Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex
    Holger Stark
    Max Planck Institute for Biophysical Chemistry, 37077 Gottingen, Germany
    Nat Struct Biol 9:849-54. 2002
    ..These results provide a detailed snapshot view of an important functional state of the ribosome and suggest mechanisms of decoding and GTPase activation...
  4. ncbi request reprint Cryo-electron microscopy of spliceosomal components
    Holger Stark
    Max Planck Institute for Biophysical Chemistry, 37077 Gottingen, Germany
    Annu Rev Biophys Biomol Struct 35:435-57. 2006
    ....
  5. doi request reprint Localization of Prp8, Brr2, Snu114 and U4/U6 proteins in the yeast tri-snRNP by electron microscopy
    Irina Häcker
    Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D 37077 Gottingen, Germany
    Nat Struct Mol Biol 15:1206-12. 2008
    ..The head and arm adopt variable relative positions. This molecular organization and dynamics suggest possible scenarios for structural events during catalytic activation...
  6. ncbi request reprint Major conformational change in the complex SF3b upon integration into the spliceosomal U11/U12 di-snRNP as revealed by electron cryomicroscopy
    Monika M Golas
    Department of Cellular Biochemistry and Research Group of 3D Electron Cryomicroscopy, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D 37077 Gottingen, Germany
    Mol Cell 17:869-83. 2005
    ..The manner in which SF3b is integrated in the U11/U12 di-snRNP has important implications for branch site recognition. Furthermore, a putative model of the pre-mRNA binding to the U11/U12 di-snRNP is proposed...
  7. pmc Protein composition and electron microscopy structure of affinity-purified human spliceosomal B complexes isolated under physiological conditions
    Jochen Deckert
    Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
    Mol Cell Biol 26:5528-43. 2006
    ..Furthermore, the spliceosomal complexes isolated here are well suited for complementation studies with purified proteins to dissect factor requirements for spliceosome activation and splicing catalysis...
  8. ncbi request reprint Organization of core spliceosomal components U5 snRNA loop I and U4/U6 Di-snRNP within U4/U6.U5 Tri-snRNP as revealed by electron cryomicroscopy
    Bjoern Sander
    Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
    Mol Cell 24:267-78. 2006
    ..We suggest that this central tri-snRNP region may be the site to which the prespliceosomal U2 snRNA has to approach closely during formation of the catalytic core of the spliceosome...
  9. pmc Exon, intron and splice site locations in the spliceosomal B complex
    Elmar Wolf
    Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Gottingen, Germany
    EMBO J 28:2283-92. 2009
    ..The gold-labelling method adopted here can be applied to other spliceosomal complexes and may thus contribute significantly to our overall understanding of the pre-mRNA splicing process...
  10. doi request reprint Ribosome dynamics and tRNA movement by time-resolved electron cryomicroscopy
    Niels Fischer
    3D Electron Cryomicroscopy Group, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
    Nature 466:329-33. 2010
    ..The ribosome functions as a Brownian machine that couples spontaneous conformational changes driven by thermal energy to directed movement...
  11. doi request reprint The evolutionarily conserved core design of the catalytic activation step of the yeast spliceosome
    Patrizia Fabrizio
    Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Gottingen, Germany
    Mol Cell 36:593-608. 2009
    ..Electron microscopy reveals high-quality images of yeast spliceosomes at defined functional stages, indicating that they are well-suited for three-dimensional structure analyses...
  12. ncbi request reprint Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation
    Mihaela Diaconu
    Röntgenkristallographie, Max Planck Institut fur biophysikalische Chemie, Am Fassberg 11, D 37077 Gottingen, Germany
    Cell 121:991-1004. 2005
    ..Highly mobile L7/12 C-terminal domains promote recruitment of translation factors to the ribosome and stimulate GTP hydrolysis by the ribosome bound factors through stabilization of their active GTPase conformation...
  13. doi request reprint 3D cryo-EM structure of an active step I spliceosome and localization of its catalytic core
    Monika M Golas
    Research Group of 3D Electron Cryomicroscopy, Max Planck Institute for Biophysical Chemistry, D 37077 Gottingen, Germany
    Mol Cell 40:927-38. 2010
    ..As C complex domains could be recognized in these structures, their position in the C complex could be determined, thereby allowing the region harboring the spliceosome's catalytic core to be localized...
  14. pmc Novel insights into the architecture and protein interaction network of yeast eIF3
    Sohail Khoshnevis
    Department of Molecular Structural Biology, Institute of Microbiology and Genetics, Georg August University Gottingen, 37077 Gottingen, Germany
    RNA 18:2306-19. 2012
    ....
  15. ncbi request reprint Structure of the hepatitis C virus IRES bound to the human 80S ribosome: remodeling of the HCV IRES
    Daniel Boehringer
    Max Planck Institute for Biophysical Chemistry, 3D Electron Cryomicroscopy, Am Fassberg 11, 37077 Gottingen, Germany
    Structure 13:1695-706. 2005
    ..The comparison with the previously published binary 40S-HCV IRES complex reveals structural rearrangements in the two pseudoknot structures of the HCV IRES in translation initiation...
  16. ncbi request reprint Molecular architecture of the multiprotein splicing factor SF3b
    Monika M Golas
    Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
    Science 300:980-4. 2003
    ..The 22 tandem helical repeats of the protein SF3b155 are located in the outer shell of the complex enclosing p14...
  17. ncbi request reprint GraFix: sample preparation for single-particle electron cryomicroscopy
    Berthold Kastner
    Department of Cellular Biochemsitry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
    Nat Methods 5:53-5. 2008
    ..The method can be used to prepare samples for negative-stain, cryo-negative-stain and, particularly, unstained cryo-EM...
  18. pmc Merging molecular electron microscopy and mass spectrometry by carbon film-assisted endoproteinase digestion
    Florian M Richter
    Max Planck Institute for Biophysical Chemistry, Gottingen, Germany
    Mol Cell Proteomics 9:1729-41. 2010
    ..We suggest our approach to be an optimization technique for the compositional analysis of macromolecules by mass spectrometry in general...
  19. ncbi request reprint Structural mapping of spliceosomes by electron microscopy
    Reinhard Luhrmann
    Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
    Curr Opin Struct Biol 19:96-102. 2009
    ....
  20. ncbi request reprint Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a cryo-electron microscopy model of vertebrate APC/C
    Prakash Dube
    Max Planck Institute for Biophysical Chemistry, Goettingen, Germany
    Mol Cell 20:867-79. 2005
    ..We have further identified a large flexible domain in APC/C that adopts a different orientation upon Cdh1 binding. Cdh1 may thus activate APC/C both by recruiting substrates and by inducing conformational changes...
  21. ncbi request reprint Three-dimensional structure of a pre-catalytic human spliceosomal complex B
    Daniel Boehringer
    Max Planck Institute for Biophysical Chemistry, Department of Cellular Biochemistry, Am Fassberg 11, 37077 Goettingen, Germany
    Nat Struct Mol Biol 11:463-8. 2004
    ..The body is very similar in size and shape to the isolated U4/U6.U5 tri-snRNP. This provides initial insight into the structural organization of complex B...
  22. pmc Structure of yeast U6 snRNPs: arrangement of Prp24p and the LSm complex as revealed by electron microscopy
    Ramazan Karaduman
    Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, D 37077 Gottingen, Germany
    RNA 14:2528-37. 2008
    ..Further, LSmp-Prp24p interactions may be restricted to the closed form, which appears to represent the solution structure of the U6 snRNP particle...
  23. ncbi request reprint Towards understanding selenocysteine incorporation into bacterial proteins
    Niels Fischer
    3D Electron Cryomicroscopy Group, Max Planck Institute for Biophysical Chemistry, D 37077 Gottingen, Germany
    Biol Chem 388:1061-7. 2007
    ..The results indicate that mthSelA forms a homodecamer that has a ring-like structure with five bilobed wings, similar to the structure of the E. coli complex determined previously...
  24. doi request reprint Structural determinants and mechanism of mammalian CRM1 allostery
    Nicole Dölker
    Abteilung für theoretische und computergestützte Biophysik, Max Planck Institut fur biophysikalische Chemie, Am Faßberg 11, 37077 Gottingen, Germany
    Structure 21:1350-60. 2013
    ..Cooperative CRM1 export complex assembly thus constitutes a highly dynamic process, encompassing an intricate interplay of global and local structural changes. ..
  25. pmc Snapshots of the RNA editing machine in trypanosomes captured at different assembly stages in vivo
    Monika M Golas
    Research Group of 3D Electron Cryomicroscopy, Max Planck Institute for Biophysical Chemistry, Gottingen, Germany
    EMBO J 28:766-78. 2009
    ..Variability analysis indicates that subsets of complexes lack or possess additional domains, suggesting binding sites for components. Together, a picture of the RNA editing machinery is provided...
  26. doi request reprint Automated correlation of single particle tilt pairs for Random Conical Tilt and Orthogonal Tilt Reconstructions
    Florian Hauer
    Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
    J Struct Biol 181:149-54. 2013
    ..The algorithm reliably correlates correct pairs even from noisy micrographs. We further demonstrate the applicability of the algorithm by using it to obtain initial references both from negative stain and unstained cryo datasets...
  27. pmc Parallel, distributed and GPU computing technologies in single-particle electron microscopy
    Martin Schmeisser
    Max Planck Institute for Biophysical Chemistry, Germany
    Acta Crystallogr D Biol Crystallogr 65:659-71. 2009
    ....
  28. pmc Chromatin affinity purification and quantitative mass spectrometry defining the interactome of histone modification patterns
    Miroslav Nikolov
    Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, 37077 Gottingen, Germany
    Mol Cell Proteomics 10:M110.005371. 2011
    ..Our proof-of-principle studies show that chromatin templates with defined modification patterns can be used to decipher how the histone code is read and translated...
  29. ncbi request reprint Advantages of CCD detectors for de novo three-dimensional structure determination in single-particle electron microscopy
    B Sander
    Research Group of 3D Electron Cryomicroscopy, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
    J Struct Biol 151:92-105. 2005
    ..With 4-fold binning of the CCD camera and at very high magnification (> 300 kx) film is still superior beyond 7 A resolution...
  30. ncbi request reprint Corrim-based alignment for improved speed in single-particle image processing
    B Sander
    Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Goettingen, Germany
    J Struct Biol 143:219-28. 2003
    ..quot;..
  31. pmc Crystal structure of a core spliceosomal protein interface
    Matthew J Schellenberg
    Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada T6G 2H7
    Proc Natl Acad Sci U S A 103:1266-71. 2006
    ..SF3b155 presents a noncanonical surface for RNA recognition at the heart of the mammalian spliceosome...
  32. ncbi request reprint Spontaneous reverse movement of mRNA-bound tRNA through the ribosome
    Andrey L Konevega
    Institute of Physical Biochemistry, University of Witten Herdecke, 58448 Witten, Germany
    Nat Struct Mol Biol 14:318-24. 2007
    ..These results lend support to the diffusion model of tRNA movement during translocation. In the cell, tRNA movement is biased in the forward direction by EF-G, which acts as a Brownian ratchet and prevents backward movement...
  33. ncbi request reprint Quaternary structure of the European spiny lobster (Palinurus elephas) 1x6-mer hemocyanin from cryoEM and amino acid sequence data
    Ulrich Meissner
    Institute of Zoology, University of Mainz, Muellerweg 6, D 55099 Mainz, Germany
    J Mol Biol 325:99-109. 2003
    ..By molecular modelling, we have found the putative locations for the amino acid sequence (597-605) and the C-terminal end (654-657), which are absent in the available P.interruptus X-ray data...
  34. ncbi request reprint The Three-dimensional Structure of an Ionotropic Glutamate Receptor Reveals a Dimer-of-dimers Assembly
    Willem Tichelaar
    Ion Channel Structure Group, Max Planck Institute for Medical Research, Jahnstr 29, D 69120 Heidelberg, Germany
    J Mol Biol 344:435-42. 2004
    ..Internal cavities located along the longitudinal axis may represent components of the ion conduction pathway...
  35. ncbi request reprint Structural insight into filament formation by mammalian septins
    Minhajuddin Sirajuddin
    Abteilung Strukturelle Biologie, Max Planck Institut fur molekulare Physiologie, Otto Hahn Strasse 11, 44227 Dortmund, Germany
    Nature 449:311-5. 2007
    ..The architecture of septin filaments differs fundamentally from that of other cytoskeletal structures...
  36. ncbi request reprint Architecture of the human ndc80-hec1 complex, a critical constituent of the outer kinetochore
    Claudio Ciferri
    Department of Experimental Oncology, European Institute of Oncology, Via Ripamonti 435, 20141 Milan, Italy
    J Biol Chem 280:29088-95. 2005
    ..The recombinant complex displays normal kinetochore localization upon injection in HeLa cells and is therefore a faithful copy of the endogenous Ndc80 complex...
  37. pmc Composition and three-dimensional EM structure of double affinity-purified, human prespliceosomal A complexes
    Nastaran Behzadnia
    Department of Cellular Biochemistry, MPI of Biophysical Chemistry, Gottingen, Germany
    EMBO J 26:1737-48. 2007
    ..Complexes isolated here are well suited for in vitro assembly studies to determine factor requirements for the A to B complex transition...