Research Topics
Genomes and Genes | Holger StarkSummaryCountry: Germany Publications
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Publications
Arrangement of RNA and proteins in the spliceosomal U1 small nuclear ribonucleoprotein particleH Stark
Institut fur Molekularbiologie und Tumorforschung, Marburg, Germany
Nature 409:539-42. 2001....- Cryo-electron microscopy of spliceosomal componentsHolger Stark
Max Planck Institute for Biophysical Chemistry, 37077 Gottingen, Germany
Annu Rev Biophys Biomol Struct 35:435-57. 2006.... - Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complexHolger 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... - Three-dimensional electron cryomicroscopy of ribosomesHolger 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... 
Localization of Prp8, Brr2, Snu114 and U4/U6 proteins in the yeast tri-snRNP by electron microscopyIrina 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...- Major conformational change in the complex SF3b upon integration into the spliceosomal U11/U12 di-snRNP as revealed by electron cryomicroscopyMonika M Golas
Department of Cellular Biochemistry and Research Group of 3D Electron Cryomicroscopy, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, , 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... 
Protein composition and electron microscopy structure of affinity-purified human spliceosomal B complexes isolated under physiological conditionsJochen Deckert
Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, , 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...- Exon, intron and splice site locations in the spliceosomal B complexElmar 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... - Organization of core spliceosomal components U5 snRNA loop I and U4/U6 Di-snRNP within U4/U6.U5 Tri-snRNP as revealed by electron cryomicroscopyBjoern Sander
Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, , 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... - The evolutionarily conserved core design of the catalytic activation step of the yeast spliceosomePatrizia 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... - Ribosome dynamics and tRNA movement by time-resolved electron cryomicroscopyNiels 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... - Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activationMihaela 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... - 3D cryo-EM structure of an active step I spliceosome and localization of its catalytic coreMonika 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... - Novel insights into the architecture and protein interaction network of yeast eIF3Sohail Khoshnevis
Department of Molecular Structural Biology, Institute of Microbiology and Genetics, Georg August University Gottingen, 37077 Gottingen, Germany
RNA 18:2306-19. 2012.... - GraFix: sample preparation for single-particle electron cryomicroscopyBerthold 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... - Structure of the hepatitis C virus IRES bound to the human 80S ribosome: remodeling of the HCV IRESDaniel Boehringer
Max Planck Institute for Biophysical Chemistry, 3D Electron Cryomicroscopy, Am Fassberg 11, , 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... - Molecular architecture of the multiprotein splicing factor SF3bMonika 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... - Merging molecular electron microscopy and mass spectrometry by carbon film-assisted endoproteinase digestionFlorian 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... - Structural mapping of spliceosomes by electron microscopyReinhard Luhrmann
Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
Curr Opin Struct Biol 19:96-102. 2009.... - Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a cryo-electron microscopy model of vertebrate APC/CPrakash 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... - Structure of yeast U6 snRNPs: arrangement of Prp24p and the LSm complex as revealed by electron microscopyRamazan 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... - Towards understanding selenocysteine incorporation into bacterial proteinsNiels 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... - Three-dimensional structure of a pre-catalytic human spliceosomal complex BDaniel 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... - Snapshots of the RNA editing machine in trypanosomes captured at different assembly stages in vivoMonika 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... - Parallel, distributed and GPU computing technologies in single-particle electron microscopyMartin Schmeisser
Max Planck Institute for Biophysical Chemistry, Germany
Acta Crystallogr D Biol Crystallogr 65:659-71. 2009.... - Automated correlation of single particle tilt pairs for Random Conical Tilt and Orthogonal Tilt ReconstructionsFlorian 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... - Chromatin affinity purification and quantitative mass spectrometry defining the interactome of histone modification patternsMiroslav 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... - Advantages of CCD detectors for de novo three-dimensional structure determination in single-particle electron microscopyB Sander
Research Group of 3D Electron Cryomicroscopy, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, , 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... - Corrim-based alignment for improved speed in single-particle image processingB Sander
Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Goettingen, Germany
J Struct Biol 143:219-28. 2003..quot;.. - Spontaneous reverse movement of mRNA-bound tRNA through the ribosomeAndrey 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... - Crystal structure of a core spliceosomal protein interfaceMatthew 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... - Quaternary structure of the European spiny lobster (Palinurus elephas) 1x6-mer hemocyanin from cryoEM and amino acid sequence dataUlrich 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... - The Three-dimensional Structure of an Ionotropic Glutamate Receptor Reveals a Dimer-of-dimers AssemblyWillem 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... - Structural insight into filament formation by mammalian septinsMinhajuddin 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... - Architecture of the human ndc80-hec1 complex, a critical constituent of the outer kinetochoreClaudio 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... - Composition and three-dimensional EM structure of double affinity-purified, human prespliceosomal A complexesNastaran 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...