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  • 1
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    Role of Yersinia murine toxin in survival of Yersinia pestis in the midgut of the flea vector (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-27
    Description: Transmission by flea bite is a relatively recent adaptation that distinguishes Yersinia pestis, the plague bacillus, from closely related enteric bacteria. Here, a plasmid-encoded phospholipase D (PLD), previously characterized as Yersinia murine toxin (Ymt), was shown to be required for survival of Y. pestis in the midgut of its principal vector, the rat flea Xenopsylla cheopis. Intracellular PLD activity appeared to protect Y. pestis from a cytotoxic digestion product of blood plasma in the flea gut. By enabling colonization of the flea midgut, acquisition of this PLD may have precipitated the transition of Y. pestis to obligate arthropod-borne transmission.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hinnebusch, B Joseph -- Rudolph, Amy E -- Cherepanov, Peter -- Dixon, Jack E -- Schwan, Tom G -- Forsberg, Ake -- New York, N.Y. -- Science. 2002 Apr 26;296(5568):733-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Human Bacterial Pathogenesis, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA. jhinnebusch@niaid.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11976454" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Toxins/genetics/*metabolism ; Digestive System/metabolism/microbiology ; Fluorescent Antibody Technique, Indirect ; Insect Vectors/metabolism/*microbiology ; Mutation ; Phospholipase D/genetics/*metabolism/toxicity ; Plague/transmission ; Plasmids ; Recombinant Fusion Proteins/metabolism/toxicity ; Siphonaptera/metabolism/*microbiology ; Spheroplasts/physiology ; Yersinia pestis/enzymology/genetics/pathogenicity/*physiology
    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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  • 2
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    Structural basis for retroviral integration into nucleosomes (2015)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2015-06-11
    Description: Retroviral integration is catalysed by a tetramer of integrase (IN) assembled on viral DNA ends in a stable complex, known as the intasome. How the intasome interfaces with chromosomal DNA, which exists in the form of nucleosomal arrays, is currently unknown. Here we show that the prototype foamy virus (PFV) intasome is proficient at stable capture of nucleosomes as targets for integration. Single-particle cryo-electron microscopy reveals a multivalent intasome-nucleosome interface involving both gyres of nucleosomal DNA and one H2A-H2B heterodimer. While the histone octamer remains intact, the DNA is lifted from the surface of the H2A-H2B heterodimer to allow integration at strongly preferred superhelix location +/-3.5 positions. Amino acid substitutions disrupting these contacts impinge on the ability of the intasome to engage nucleosomes in vitro and redistribute viral integration sites on the genomic scale. Our findings elucidate the molecular basis for nucleosome capture by the viral DNA recombination machinery and the underlying nucleosome plasticity that allows integration.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4530500/" 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/PMC4530500/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maskell, Daniel P -- Renault, Ludovic -- Serrao, Erik -- Lesbats, Paul -- Matadeen, Rishi -- Hare, Stephen -- Lindemann, Dirk -- Engelman, Alan N -- Costa, Alessandro -- Cherepanov, Peter -- P50 GM082251-06/GM/NIGMS NIH HHS/ -- R01 AI070042/AI/NIAID NIH HHS/ -- R01 AI070042-08/AI/NIAID NIH HHS/ -- England -- Nature. 2015 Jul 16;523(7560):366-9. doi: 10.1038/nature14495. Epub 2015 Jun 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chromatin Structure and Mobile DNA, The Francis Crick Institute, Blanche Lane, South Mimms EN6 3LD, UK. ; 1] Architecture and Dynamics of Macromolecular Machines, Clare Hall Laboratories, The Francis Crick Institute, Blanche Lane, South Mimms EN6 3LD, UK [2] National Institute for Biological Standards and Control, Microscopy and Imaging, Blanche Lane, South Mimms EN6 3QG, UK. ; Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, 450 Brookline Avenue, Boston, Massachusetts 02215, USA. ; NeCEN, Gorlaeus Laboratory, Einsteinweg 55, Leiden, 2333, the Netherlands. ; Division of Medicine, Imperial College London, St-Mary's Campus, Norfolk Place, London W2 1PG, UK. ; Institute of Virology, Technische Universitat Dresden, Fetscherstr. 74, Dresden 01307, Germany. ; Architecture and Dynamics of Macromolecular Machines, Clare Hall Laboratories, The Francis Crick Institute, Blanche Lane, South Mimms EN6 3LD, UK. ; 1] Chromatin Structure and Mobile DNA, The Francis Crick Institute, Blanche Lane, South Mimms EN6 3LD, UK [2] Division of Medicine, Imperial College London, St-Mary's Campus, Norfolk Place, London W2 1PG, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26061770" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Binding Sites/genetics ; Cryoelectron Microscopy ; DNA/genetics/metabolism/ultrastructure ; Genome/genetics ; Histones/chemistry/metabolism/ultrastructure ; Integrases/metabolism ; Models, Molecular ; Nucleosomes/*chemistry/genetics/ultrastructure/*virology ; Protein Multimerization ; Recombination, Genetic ; Spumavirus/chemistry/genetics/*metabolism/ultrastructure ; *Virus Integration
    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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    The mechanism of retroviral integration from X-ray structures of its key intermediates (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-11-12
    Description: To establish productive infection, a retrovirus must insert a DNA replica of its genome into host cell chromosomal DNA. This process is operated by the intasome, a nucleoprotein complex composed of an integrase tetramer (IN) assembled on the viral DNA ends. The intasome engages chromosomal DNA within a target capture complex to carry out strand transfer, irreversibly joining the viral and cellular DNA molecules. Although several intasome/transpososome structures from the DDE(D) recombinase superfamily have been reported, the mechanics of target DNA capture and strand transfer by these enzymes remained unclear. Here we report crystal structures of the intasome from prototype foamy virus in complex with target DNA, elucidating the pre-integration target DNA capture and post-catalytic strand transfer intermediates of the retroviral integration process. The cleft between IN dimers within the intasome accommodates chromosomal DNA in a severely bent conformation, allowing widely spaced IN active sites to access the scissile phosphodiester bonds. Our results resolve the structural basis for retroviral DNA integration and provide a framework for the design of INs with altered target sequences.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2999894/" 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/PMC2999894/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maertens, Goedele N -- Hare, Stephen -- Cherepanov, Peter -- G0900116/Medical Research Council/United Kingdom -- G0900116(90753)/Medical Research Council/United Kingdom -- G1000917/Medical Research Council/United Kingdom -- Medical Research Council/United Kingdom -- England -- Nature. 2010 Nov 11;468(7321):326-9. doi: 10.1038/nature09517.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Infectious Diseases, Imperial College London, St Mary's Campus, Norfolk Place, London W2 1PG, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21068843" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Catalytic Domain ; Crystallography, X-Ray ; DNA/chemistry/genetics/metabolism ; Integrases/genetics/metabolism ; Models, Molecular ; Molecular Conformation ; Spumavirus/*chemistry/enzymology/*physiology ; *Virus Integration
    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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  • 4
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    Retroviral intasome assembly and inhibition of DNA strand transfer (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-02-02
    Description: Integrase is an essential retroviral enzyme that binds both termini of linear viral DNA and inserts them into a host cell chromosome. The structure of full-length retroviral integrase, either separately or in complex with DNA, has been lacking. Furthermore, although clinically useful inhibitors of HIV integrase have been developed, their mechanism of action remains speculative. Here we present a crystal structure of full-length integrase from the prototype foamy virus in complex with its cognate DNA. The structure shows the organization of the retroviral intasome comprising an integrase tetramer tightly associated with a pair of viral DNA ends. All three canonical integrase structural domains are involved in extensive protein-DNA and protein-protein interactions. The binding of strand-transfer inhibitors displaces the reactive viral DNA end from the active site, disarming the viral nucleoprotein complex. Our findings define the structural basis of retroviral DNA integration, and will allow modelling of the HIV-1 intasome to aid in the development of antiretroviral drugs.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2837123/" 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/PMC2837123/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hare, Stephen -- Gupta, Saumya Shree -- Valkov, Eugene -- Engelman, Alan -- Cherepanov, Peter -- G0900116/Medical Research Council/United Kingdom -- P30 AI060354/AI/NIAID NIH HHS/ -- R01 AI070042/AI/NIAID NIH HHS/ -- R01 AI070042-04/AI/NIAID NIH HHS/ -- Medical Research Council/United Kingdom -- England -- Nature. 2010 Mar 11;464(7286):232-6. doi: 10.1038/nature08784. Epub 2010 Jan 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Medicine, Imperial College London, St-Mary's Campus, Norfolk Place, London W2 1PG, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20118915" target="_blank"〉PubMed〈/a〉
    Keywords: Catalytic Domain ; DNA, Viral/*metabolism ; HIV-1/enzymology/genetics ; Integrases/*chemistry/metabolism ; *Models, Molecular ; Protein Structure, Tertiary ; Retroviridae/*enzymology/*genetics
    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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  • 5
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    Centralspindlin links the mitotic spindle to the plasma membrane during cytokinesis (2012)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2012-12-14
    Description: At the end of cell division, cytokinesis splits the cytoplasm of nascent daughter cells and partitions segregated sister genomes. To coordinate cell division with chromosome segregation, the mitotic spindle controls cytokinetic events at the cell envelope. The spindle midzone stimulates the actomyosin-driven contraction of the cleavage furrow, which proceeds until the formation of a microtubule-rich intercellular bridge with the midbody at its centre. The midbody directs the final membrane abscission reaction and has been proposed to attach the cleavage furrow to the intercellular bridge. How the mitotic spindle is connected to the plasma membrane during cytokinesis is not understood. Here we identify a plasma membrane tethering activity in the centralspindlin protein complex, a conserved component of the spindle midzone and midbody. We demonstrate that the C1 domain of the centralspindlin subunit MgcRacGAP associates with the plasma membrane by interacting with polyanionic phosphoinositide lipids. Using X-ray crystallography we determine the structure of this atypical C1 domain. Mutations in the hydrophobic cap and in basic residues of the C1 domain of MgcRacGAP prevent association of the protein with the plasma membrane, and abrogate cytokinesis in human and chicken cells. Artificial membrane tethering of centralspindlin restores cell division in the absence of the C1 domain of MgcRacGAP. Although C1 domain function is dispensable for the formation of the midzone and midbody, it promotes contractility and is required for the attachment of the plasma membrane to the midbody, a long-postulated function of this organelle. Our analysis suggests that centralspindlin links the mitotic spindle to the plasma membrane to secure the final cut during cytokinesis in animal cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lekomtsev, Sergey -- Su, Kuan-Chung -- Pye, Valerie E -- Blight, Ken -- Sundaramoorthy, Sriramkumar -- Takaki, Tohru -- Collinson, Lucy M -- Cherepanov, Peter -- Divecha, Nullin -- Petronczki, Mark -- Cancer Research UK/United Kingdom -- England -- Nature. 2012 Dec 13;492(7428):276-9. doi: 10.1038/nature11773.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Division and Aneuploidy Laboratory, Cancer Research UK London Research Institute, Clare Hall Laboratories, Blanche Lane, South Mimms, Hertfordshire EN6 3LD, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23235882" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/*metabolism ; Cytokinesis/genetics/*radiation effects ; GTPase-Activating Proteins/chemistry/genetics/*metabolism ; HEK293 Cells ; HeLa Cells ; Humans ; Microtubule-Associated Proteins/chemistry/genetics/*metabolism ; Microtubules/chemistry/metabolism ; Models, Molecular ; Protein Binding ; Protein Kinase C-alpha/metabolism ; Protein Structure, Tertiary ; Protein Transport/drug effects ; Spindle Apparatus/*metabolism ; Tetradecanoylphorbol Acetate/analogs & derivatives/pharmacology
    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
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    Cryo-EM reveals a novel octameric integrase structure for betaretroviral intasome function (2016)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2016-02-19
    Description: Retroviral integrase catalyses the integration of viral DNA into host target DNA, which is an essential step in the life cycle of all retroviruses. Previous structural characterization of integrase-viral DNA complexes, or intasomes, from the spumavirus prototype foamy virus revealed a functional integrase tetramer, and it is generally believed that intasomes derived from other retroviral genera use tetrameric integrase. However, the intasomes of orthoretroviruses, which include all known pathogenic species, have not been characterized structurally. Here, using single-particle cryo-electron microscopy and X-ray crystallography, we determine an unexpected octameric integrase architecture for the intasome of the betaretrovirus mouse mammary tumour virus. The structure is composed of two core integrase dimers, which interact with the viral DNA ends and structurally mimic the integrase tetramer of prototype foamy virus, and two flanking integrase dimers that engage the core structure via their integrase carboxy-terminal domains. Contrary to the belief that tetrameric integrase components are sufficient to catalyse integration, the flanking integrase dimers were necessary for mouse mammary tumour virus integrase activity. The integrase octamer solves a conundrum for betaretroviruses as well as alpharetroviruses by providing critical carboxy-terminal domains to the intasome core that cannot be provided in cis because of evolutionarily restrictive catalytic core domain-carboxy-terminal domain linker regions. The octameric architecture of the intasome of mouse mammary tumour virus provides new insight into the structural basis of retroviral DNA integration.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ballandras-Colas, Allison -- Brown, Monica -- Cook, Nicola J -- Dewdney, Tamaria G -- Demeler, Borries -- Cherepanov, Peter -- Lyumkis, Dmitry -- Engelman, Alan N -- 9 P41 GM103310/GM/NIGMS NIH HHS/ -- P30 AI060354/AI/NIAID NIH HHS/ -- P41 GM103331/GM/NIGMS NIH HHS/ -- P50 GM082251/GM/NIGMS NIH HHS/ -- P50 GM103368/GM/NIGMS NIH HHS/ -- R01 AI070042/AI/NIAID NIH HHS/ -- England -- Nature. 2016 Feb 18;530(7590):358-61. doi: 10.1038/nature16955.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Immunology and Virology, Dana-Farber Cancer Institute and Department of Medicine, Harvard Medical School, 450 Brookline Avenue, Boston, Massachusetts 02215, USA. ; Laboratory of Genetics and Helmsley Center for Genomic Medicine, The Salk Institute for Biological Studies, 10010 N Torrey Pines Road, La Jolla, California 92037, USA. ; Clare Hall Laboratories, The Francis Crick Institute, Blanche Lane, South Mimms, Potters Bar, Hertfordshire EN6 3LD, UK. ; Department of Biochemistry, The University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, Texas 78229, USA. ; Division of Medicine, Imperial College London, St. Mary's Campus, Norfolk Place, London W2 1PG, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26887496" target="_blank"〉PubMed〈/a〉
    Keywords: Catalytic Domain ; *Cryoelectron Microscopy ; Crystallography, X-Ray ; DNA, Viral/chemistry/*metabolism/*ultrastructure ; Integrases/*chemistry/metabolism/*ultrastructure ; Mammary Tumor Virus, Mouse/chemistry/*enzymology/genetics/ultrastructure ; Models, Molecular ; *Protein Multimerization ; Protein Structure, Quaternary ; Spumavirus/chemistry/enzymology ; Virus Integration
    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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  • 7
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    Forecasting Resource as a Method of Increasing the Security of Technical Devices (2017)
    Institute of Physics (IOP)
    Details
    Publication Date: 2017-10-24
    Description: The article shows a method of increasing the safe operation of technical devices at various stages of the life cycle according to the proposed classification parameters of the resource by applying the model of resource prediction. The model takes into account the presence of defects, the rate of corrosion and corrosion resistance of the material, the volume of technical diagnosis, the degree of risk in case of failure or damage of technical devices. The article shows the application of the model resource of the technical device from the manufacture to the end of its service life.
    Print ISSN: 1757-8981
    Electronic ISSN: 1757-899X
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Published by Institute of Physics (IOP)
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  • 8
    Electronic Resource
    Electronic Resource
    Analysis of model relations for turbulent heat diffusion as applied to the calculation of wake flows (1986)
    Springer
    Journal of engineering physics and thermophysics 51 (1986), S. 1378-1382 
    Details
    ISSN: 1573-871X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract An experimental test of the known approximations is made and a new relation is proposed for turbulent diffusion of heat or of a passive admixture.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00870346
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  • 9
    Electronic Resource
    Electronic Resource
    Experimental verification of models of triple mixed correlation between velocity and temperature as applied to the calculation of jet flows (1987)
    Springer
    Journal of engineering physics and thermophysics 52 (1987), S. 259-264 
    Details
    ISSN: 1573-871X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract The optimum values of the constants in the well-known approximation of the moment u 2 2 θ are determined from the results of experimental investigations of nonisothermal wakes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00872501
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  • 10
    Electronic Resource
    Electronic Resource
    Plane turbulent wake with zero excess momentum (1987)
    Springer
    Journal of engineering physics and thermophysics 52 (1987), S. 536-542 
    Details
    ISSN: 1573-871X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract A plane momentumless wake is investigated on the basis of numerical computations by the uiuj—ɛ model of turbulence and an aerodynamic experiment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00873306
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