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  • 1
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    Structure of the immature retroviral capsid at 8 A resolution by cryo-electron microscopy (2012)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2012-06-23
    Description: The assembly of retroviruses such as HIV-1 is driven by oligomerization of their major structural protein, Gag. Gag is a multidomain polyprotein including three conserved folded domains: MA (matrix), CA (capsid) and NC (nucleocapsid). Assembly of an infectious virion proceeds in two stages. In the first stage, Gag oligomerization into a hexameric protein lattice leads to the formation of an incomplete, roughly spherical protein shell that buds through the plasma membrane of the infected cell to release an enveloped immature virus particle. In the second stage, cleavage of Gag by the viral protease leads to rearrangement of the particle interior, converting the non-infectious immature virus particle into a mature infectious virion. The immature Gag shell acts as the pivotal intermediate in assembly and is a potential target for anti-retroviral drugs both in inhibiting virus assembly and in disrupting virus maturation. However, detailed structural information on the immature Gag shell has not previously been available. For this reason it is unclear what protein conformations and interfaces mediate the interactions between domains and therefore the assembly of retrovirus particles, and what structural transitions are associated with retrovirus maturation. Here we solve the structure of the immature retroviral Gag shell from Mason-Pfizer monkey virus by combining cryo-electron microscopy and tomography. The 8-A resolution structure permits the derivation of a pseudo-atomic model of CA in the immature retrovirus, which defines the protein interfaces mediating retrovirus assembly. We show that transition of an immature retrovirus into its mature infectious form involves marked rotations and translations of CA domains, that the roles of the amino-terminal and carboxy-terminal domains of CA in assembling the immature and mature hexameric lattices are exchanged, and that the CA interactions that stabilize the immature and mature viruses are almost completely distinct.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bharat, Tanmay A M -- Davey, Norman E -- Ulbrich, Pavel -- Riches, James D -- de Marco, Alex -- Rumlova, Michaela -- Sachse, Carsten -- Ruml, Tomas -- Briggs, John A G -- England -- Nature. 2012 Jul 19;487(7407):385-9. doi: 10.1038/nature11169.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Structural and Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22722831" target="_blank"〉PubMed〈/a〉
    Keywords: Capsid/metabolism/*ultrastructure ; *Cryoelectron Microscopy ; Mason-Pfizer monkey virus/*ultrastructure ; *Models, Molecular ; Protein Structure, Tertiary ; Virus Assembly
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    Molecular structures of unbound and transcribing RNA polymerase III (2015)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2015-11-26
    Description: Transcription of genes encoding small structured RNAs such as transfer RNAs, spliceosomal U6 small nuclear RNA and ribosomal 5S RNA is carried out by RNA polymerase III (Pol III), the largest yet structurally least characterized eukaryotic RNA polymerase. Here we present the cryo-electron microscopy structures of the Saccharomyces cerevisiae Pol III elongating complex at 3.9 A resolution and the apo Pol III enzyme in two different conformations at 4.6 and 4.7 A resolution, respectively, which allow the building of a 17-subunit atomic model of Pol III. The reconstructions reveal the precise orientation of the C82-C34-C31 heterotrimer in close proximity to the stalk. The C53-C37 heterodimer positions residues involved in transcription termination close to the non-template DNA strand. In the apo Pol III structures, the stalk adopts different orientations coupled with closed and open conformations of the clamp. Our results provide novel insights into Pol III-specific transcription and the adaptation of Pol III towards its small transcriptional targets.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4681132/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4681132/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffmann, Niklas A -- Jakobi, Arjen J -- Moreno-Morcillo, Maria -- Glatt, Sebastian -- Kosinski, Jan -- Hagen, Wim J H -- Sachse, Carsten -- Muller, Christoph W -- England -- Nature. 2015 Dec 10;528(7581):231-6. doi: 10.1038/nature16143. Epub 2015 Nov 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg, Germany. ; European Molecular Biology Laboratory (EMBL), Hamburg Unit, Notkestrasse 85, 22607 Hamburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26605533" target="_blank"〉PubMed〈/a〉
    Keywords: Cryoelectron Microscopy ; *Models, Molecular ; Protein Binding ; Protein Structure, Tertiary ; RNA Polymerase III/*chemistry ; Saccharomyces cerevisiae/*enzymology ; Saccharomyces cerevisiae Proteins/*chemistry
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
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    Cartwheel architecture of Trichonympha basal body (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-07-17
    Description: Centrioles and basal bodies are essential for the formation of cilia, flagella, and centrosomes. They exhibit a characteristic ninefold symmetry imparted by a cartwheel thought to contain rings of SAS-6 proteins. We used cryoelectron tomography to investigate the architecture of the exceptionally long cartwheel of the flagellate Trichonympha. We found that the cartwheel is a stack of central rings that exhibit a vertical periodicity of 8.5 nanometers and is able to accommodate nine SAS-6 homodimers. The spokes that emanate from two such rings associate into a layer, with a vertical periodicity of 17 nanometers on the cartwheel margin. Thus, by using the power of biodiversity, we unveiled the architecture of the cartwheel at the root of the ninefold symmetry of centrioles and basal bodies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guichard, Paul -- Desfosses, Ambroise -- Maheshwari, Aditi -- Hachet, Virginie -- Dietrich, Carsten -- Brune, Andreas -- Ishikawa, Takashi -- Sachse, Carsten -- Gonczy, Pierre -- New York, N.Y. -- Science. 2012 Aug 3;337(6094):553. doi: 10.1126/science.1222789. Epub 2012 Jul 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Swiss Institute for Experimental Cancer Research, School of Life Sciences, Swiss Federal Institute of Technology, Lausanne, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22798403" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Cycle Proteins/*ultrastructure ; Cryoelectron Microscopy ; Electron Microscope Tomography ; Hypermastigia/*ultrastructure ; Organelles/*ultrastructure
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Structural virology. Near-atomic cryo-EM structure of the helical measles virus nucleocapsid (2015)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2015-04-18
    Description: Measles is a highly contagious human disease. We used cryo-electron microscopy and single particle-based helical image analysis to determine the structure of the helical nucleocapsid formed by the folded domain of the measles virus nucleoprotein encapsidating an RNA at a resolution of 4.3 angstroms. The resulting pseudoatomic model of the measles virus nucleocapsid offers important insights into the mechanism of the helical polymerization of nucleocapsids of negative-strand RNA viruses, in particular via the exchange subdomains of the nucleoprotein. The structure reveals the mode of the nucleoprotein-RNA interaction and explains why each nucleoprotein of measles virus binds six nucleotides, whereas the respiratory syncytial virus nucleoprotein binds seven. It provides a rational basis for further analysis of measles virus replication and transcription, and reveals potential targets for drug design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gutsche, Irina -- Desfosses, Ambroise -- Effantin, Gregory -- Ling, Wai Li -- Haupt, Melina -- Ruigrok, Rob W H -- Sachse, Carsten -- Schoehn, Guy -- New York, N.Y. -- Science. 2015 May 8;348(6235):704-7. doi: 10.1126/science.aaa5137. Epub 2015 Apr 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CNRS, Unit for Virus Host-Cell Interactions, 38042 Grenoble, France. Universite Grenoble Alpes, Unit for Virus Host-Cell Interactions, 38042 Grenoble, France. gutsche@embl.fr. ; Structural and Computational Biology Unit, European Molecular Biology Laboratory, 69917 Heidelberg, Germany. ; CNRS, Unit for Virus Host-Cell Interactions, 38042 Grenoble, France. Universite Grenoble Alpes, Unit for Virus Host-Cell Interactions, 38042 Grenoble, France. ; Universite Grenoble Alpes, IBS, 38044 Grenoble, France. CNRS, IBS, 38044 Grenoble, France. CEA, IBS, 38044 Grenoble, France. ; Institut Laue-Langevin, 38000 Grenoble, France. ; CNRS, Unit for Virus Host-Cell Interactions, 38042 Grenoble, France. Universite Grenoble Alpes, Unit for Virus Host-Cell Interactions, 38042 Grenoble, France. Universite Grenoble Alpes, IBS, 38044 Grenoble, France. CNRS, IBS, 38044 Grenoble, France. CEA, IBS, 38044 Grenoble, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25883315" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cryoelectron Microscopy ; Humans ; Measles/*virology ; Measles virus/chemistry/*ultrastructure ; Molecular Sequence Data ; Nucleic Acid Conformation ; Nucleocapsid/chemistry/*ultrastructure ; Nucleoproteins/chemistry/ultrastructure ; Protein Structure, Secondary ; RNA, Viral/chemistry/ultrastructure ; Viral Proteins/chemistry/ultrastructure
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
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    Structures of actin-like ParM filaments show architecture of plasmid-segregating spindles (2015)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2015-04-29
    Description: Active segregation of Escherichia coli low-copy-number plasmid R1 involves formation of a bipolar spindle made of left-handed double-helical actin-like ParM filaments. ParR links the filaments with centromeric parC plasmid DNA, while facilitating the addition of subunits to ParM filaments. Growing ParMRC spindles push sister plasmids to the cell poles. Here, using modern electron cryomicroscopy methods, we investigate the structures and arrangements of ParM filaments in vitro and in cells, revealing at near-atomic resolution how subunits and filaments come together to produce the simplest known mitotic machinery. To understand the mechanism of dynamic instability, we determine structures of ParM filaments in different nucleotide states. The structure of filaments bound to the ATP analogue AMPPNP is determined at 4.3 A resolution and refined. The ParM filament structure shows strong longitudinal interfaces and weaker lateral interactions. Also using electron cryomicroscopy, we reconstruct ParM doublets forming antiparallel spindles. Finally, with whole-cell electron cryotomography, we show that doublets are abundant in bacterial cells containing low-copy-number plasmids with the ParMRC locus, leading to an asynchronous model of R1 plasmid segregation.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4493928/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4493928/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bharat, Tanmay A M -- Murshudov, Garib N -- Sachse, Carsten -- Lowe, Jan -- 095514/Wellcome Trust/United Kingdom -- 095514/Z/11/Z/Wellcome Trust/United Kingdom -- MC-UP-A025-1012/Medical Research Council/United Kingdom -- MC_U105184326/Medical Research Council/United Kingdom -- U105184326/Medical Research Council/United Kingdom -- England -- Nature. 2015 Jul 2;523(7558):106-10. doi: 10.1038/nature14356. Epub 2015 Apr 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Structural Studies Division, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK. ; Structural and Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, Heidelberg 69117, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25915019" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*chemistry/metabolism/*ultrastructure ; Adenylyl Imidodiphosphate/metabolism ; Cryoelectron Microscopy ; Crystallography, X-Ray ; Escherichia coli/*chemistry/genetics/ultrastructure ; Escherichia coli Proteins/*chemistry/metabolism/*ultrastructure ; *Models, Molecular ; Plasmids/*metabolism ; Protein Binding ; Protein Structure, Quaternary ; *Spindle Apparatus/chemistry/metabolism/ultrastructure
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 6
    Electronic Resource
    Electronic Resource
    Ornithologische Notizen vom Westerwalde (1875)
    Springer
    Journal of ornithology 23 (1875), S. 417-428 
    Details
    ISSN: 1439-0361
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02023160
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  • 7
    Electronic Resource
    Electronic Resource
    Ornithologische Beobachtungen vom Westerwalde (1876)
    Springer
    Journal of ornithology 24 (1876), S. 279-283 
    Details
    ISSN: 1439-0361
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02004127
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  • 8
    Electronic Resource
    Electronic Resource
    Interference of Higgs boson resonances in $\mu^ + \mu^- \to\tilde{\chi}^0_i\tilde{\chi}^0_j$ with longitudinal beam polarization (2004)
    Springer
    The European physical journal 37 (2004), S. 495-505 
    Details
    ISSN: 1434-6052
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract. We study the interference of resonant Higgs boson exchange in neutralino production in $\mu^ + \mu^-$ annihilation with longitudinally polarized beams. We use the energy distribution of the decay lepton in the process $\tilde{\chi}^0_j \to \ell^{\pm} \tilde{\ell}^\mp$ to determine the polarization of the neutralinos. In the CP-conserving minimal supersymmetric standard model a non-vanishing asymmetry in the lepton energy spectrum is caused by the interference of Higgs boson exchange channels with different CP-eigenvalues. The contribution of this interference is large if the heavy neutral bosons H and A are nearly degenerate. We show that the asymmetry can be used to determine the couplings of the neutral Higgs bosons to the neutralinos. In particular, the asymmetry allows one to determine the relative phase of the couplings. We find large asymmetries and cross sections for a set of reference scenarios with nearly degenerate neutral Higgs bosons.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1140/epjc/s2004-02014-1
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  • 9
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    Comparison of Alzheimer A (1-40) and A (1-42) amyloid fibrils reveals similar protofilament structures (2009)
    National Academy of Sciences
    Details
    Publication Date: 2009-10-20
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 10
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    Paired  -sheet structure of an A (1-40) amyloid fibril revealed by electron microscopy (2008)
    National Academy of Sciences
    Details
    Publication Date: 2008-05-15
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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