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  • 1
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    Divergence of quaternary structures among bacterial flagellar filaments (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-04-19
    Description: It has been widely assumed that the atomic structure of the flagellar filament from Salmonella typhimurium serves as a model for all bacterial flagellar filaments given the sequence conservation in the coiled-coil regions responsible for polymerization. On the basis of electron microscopic images, we show that the flagellar filaments from Campylobacter jejuni have seven protofilaments rather than the 11 in S. typhimurium. The vertebrate Toll-like receptor 5 (TLR5) recognizes a region of bacterial flagellin that is involved in subunit-subunit assembly in Salmonella and many other pathogenic bacteria, and this short region has diverged in Campylobacter and related bacteria, such as Helicobacter pylori, which are not recognized by TLR5. The driving force in the change of quaternary structure between Salmonella and Campylobacter may have been the evasion of TLR5.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Galkin, Vitold E -- Yu, Xiong -- Bielnicki, Jakub -- Heuser, John -- Ewing, Cheryl P -- Guerry, Patricia -- Egelman, Edward H -- AI043559/AI/NIAID NIH HHS/ -- EB001567/EB/NIBIB NIH HHS/ -- New York, N.Y. -- Science. 2008 Apr 18;320(5874):382-5. doi: 10.1126/science.1155307.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Genetics, Box 800733, University of Virginia, Charlottesville, VA 22908-0733, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18420936" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Campylobacter jejuni/chemistry/genetics/*ultrastructure ; Cryoelectron Microscopy ; Evolution, Molecular ; Flagella/*chemistry/*ultrastructure ; Flagellin/*chemistry/genetics/immunology/metabolism ; Image Processing, Computer-Assisted ; Molecular Sequence Data ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Salmonella typhimurium/chemistry/*ultrastructure ; Toll-Like Receptor 5/immunology/metabolism
    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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    Sickle cell anemia research and a recombinant DNA technique (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stasiak, A -- West, S C -- Egelman, E H -- New York, N.Y. -- Science. 1997 Jul 25;277(5325):460-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9254412" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia, Sickle Cell/*genetics ; Artifacts ; Codon ; Cytosine ; DNA, Recombinant ; Gene Conversion ; Globins/genetics ; Hemoglobin A/genetics ; Hemoglobin, Sickle/*genetics ; Humans ; Mutation ; Oligodeoxyribonucleotides/*genetics ; Oligoribonucleotides/*genetics
    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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  • 3
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    Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-09-27
    Description: Like many bacterial pathogens, Salmonella spp. use a type III secretion system to inject virulence proteins into host cells. The Salmonella invasion protein A (SipA) binds host actin, enhances its polymerization near adherent extracellular bacteria, and contributes to cytoskeletal rearrangements that internalize the pathogen. By combining x-ray crystallography of SipA with electron microscopy and image analysis of SipA-actin filaments, we show that SipA functions as a "molecular staple," in which a globular domain and two nonglobular "arms" mechanically stabilize the filament by tethering actin subunits in opposing strands. Deletion analysis of the tethering arms provides strong support for this model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lilic, Mirjana -- Galkin, Vitold E -- Orlova, Albina -- VanLoock, Margaret S -- Egelman, Edward H -- Stebbins, C Erec -- New York, N.Y. -- Science. 2003 Sep 26;301(5641):1918-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Structural Microbiology, Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14512630" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/metabolism ; Actins/*metabolism ; Bacterial Proteins/*chemistry/genetics/*metabolism ; Binding Sites ; Crystallography, X-Ray ; Image Processing, Computer-Assisted ; Microfilament Proteins/*chemistry/genetics/*metabolism ; Microscopy, Electron ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/metabolism ; Salmonella typhimurium/chemistry/*metabolism ; Sequence Deletion ; Subtilisin/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Similarity of the yeast RAD51 filament to the bacterial RecA filament (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-26
    Description: The RAD51 protein functions in the processes of DNA repair and in mitotic and meiotic genetic recombination in the yeast Saccharomyces cerevisiae. The protein has adenosine triphosphate-dependent DNA binding activities similar to those of the Escherichia coli RecA protein, and the two proteins have 30 percent sequence homology. RAD51 polymerized on double-stranded DNA to form a helical filament nearly identical in low-resolution, three-dimensional structure to that formed by RecA. Like RecA, RAD51 also appears to force DNA into a conformation of approximately a 5.1-angstrom rise per base pair and 18.6 base pairs per turn. As in other protein families, its structural conservation appears to be stronger than its sequence conservation. Both the structure of the protein polymer formed by RecA and the DNA conformation induced by RecA appear to be general properties of a class of recombination proteins found in prokaryotes as well as eukaryotes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ogawa, T -- Yu, X -- Shinohara, A -- Egelman, E H -- GM35269/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Mar 26;259(5103):1896-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Osaka University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8456314" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/pharmacology ; Binding Sites ; DNA/chemistry/metabolism ; DNA Repair ; DNA, Single-Stranded/chemistry/metabolism ; DNA-Binding Proteins/*chemistry/metabolism ; Fourier Analysis ; Fungal Proteins/*chemistry/metabolism ; Meiosis ; Mitosis ; Molecular Structure ; Nucleic Acid Conformation ; Protein Structure, Secondary ; Rad51 Recombinase ; Rec A Recombinases/*chemistry/metabolism ; Recombinant Proteins/chemistry/metabolism ; Saccharomyces cerevisiae/*chemistry ; Saccharomyces cerevisiae Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    The location of DNA in RecA-DNA helical filaments (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-07-28
    Description: The helical filament that the RecA protein of Escherichia coli forms around DNA is the active apparatus in protein-catalyzed homologous genetic recombination. The actual position of DNA within this complex has been unknown. Image analysis has been performed on electron micrographs of filaments of RecA on double-stranded DNA and on single-stranded DNA to visualize a difference that is consistent with one strand of the double-stranded DNA. This localization of the DNA gives additional information about the unusual structure of DNA in the complex with RecA protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Egelman, E H -- Yu, X -- GM35269/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1989 Jul 28;245(4916):404-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2667137" target="_blank"〉PubMed〈/a〉
    Keywords: DNA, Bacterial/*analysis/ultrastructure ; DNA, Single-Stranded/*analysis/ultrastructure ; Escherichia coli/*genetics ; Fourier Analysis ; Image Processing, Computer-Assisted ; Macromolecular Substances ; Microscopy, Electron ; Rec A Recombinases/*analysis/ultrastructure ; *Recombination, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Virology. A virus that infects a hyperthermophile encapsidates A-form DNA (2015)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2015-05-23
    Description: Extremophiles, microorganisms thriving in extreme environmental conditions, must have proteins and nucleic acids that are stable at extremes of temperature and pH. The nonenveloped, rod-shaped virus SIRV2 (Sulfolobus islandicus rod-shaped virus 2) infects the hyperthermophilic acidophile Sulfolobus islandicus, which lives at 80 degrees C and pH 3. We have used cryo-electron microscopy to generate a three-dimensional reconstruction of the SIRV2 virion at ~4 angstrom resolution, which revealed a previously unknown form of virion organization. Although almost half of the capsid protein is unstructured in solution, this unstructured region folds in the virion into a single extended alpha helix that wraps around the DNA. The DNA is entirely in the A-form, which suggests a common mechanism with bacterial spores for protecting DNA in the most adverse environments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DiMaio, Frank -- Yu, Xiong -- Rensen, Elena -- Krupovic, Mart -- Prangishvili, David -- Egelman, Edward H -- GM035269/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2015 May 22;348(6237):914-7. doi: 10.1126/science.aaa4181.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Washington, Seattle, WA 98195, USA. ; Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22908, USA. ; Institut Pasteur, Department of Microbiology, 25 rue du Dr. Roux, Paris 75015, France. ; Institut Pasteur, Department of Microbiology, 25 rue du Dr. Roux, Paris 75015, France. egelman@virginia.edu david.prangishvili@pasteur.fr. ; Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22908, USA. egelman@virginia.edu david.prangishvili@pasteur.fr.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25999507" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cryoelectron Microscopy ; DNA, A-Form/*metabolism ; Molecular Sequence Data ; Protein Multimerization ; Protein Structure, Secondary ; Rudiviridae/*metabolism/ultrastructure ; Spores, Bacterial/genetics/virology ; Sulfolobus/*genetics/*virology ; Virion/*ultrastructure
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Electronic Resource
    Electronic Resource
    X-ray diffraction evidence that actin is a 100 Å filament (1984)
    [s.l.] : Nature Publishing Group
    Nature 307 (1984), S. 56-58 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The strongest feature in the muscle X-ray pattern arising from the thin filament is the 59 layer line (the measured amplitude distribution is shown in Fig. 1 A). Because of the different helical symmetries of actin and myosin in muscle, the 59 layer line arises only from the thin filament and is ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/307056a0
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  • 8
    Electronic Resource
    Electronic Resource
    F-actin is a helix with a random variable twist (1982)
    [s.l.] : Nature Publishing Group
    Nature 298 (1982), S. 131-135 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Image analysis of isolated F-actin filaments shows that the actin helix can be described by a constant rise per subunit but a considerably variable and randomized twist (number of units per turn). The ability of actin subunits to rotate through angles of the order of 10° from their helically ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/298131a0
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  • 9
    Electronic Resource
    Electronic Resource
    The Fourier transform of actin and other helical systems with cumulative random angular disorder (1982)
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 38 (1982), S. 796-799 
    Details
    ISSN: 1600-5724
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A general class of helical disorder exists which can be described by cumulative random angular motions of subunits. This disorder affects layer-line intensities and widths by a factor proportional to n2, the square of the order of the layer line. The result explains several features of actin and polytetrafluoroethylene (Teflon) transforms, and may be relevant to other helical systems.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0567739482001624
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  • 10
    Electronic Resource
    Electronic Resource
    Structure and function of RecA-DNA complexes (1994)
    Springer
    Cellular and molecular life sciences 50 (1994), S. 192-203 
    Details
    ISSN: 1420-9071
    Keywords: RecA ; RecA-DNA complexes ; homologous recombination ; Rad51 protein ; electron microscopy ; image analysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract While theE. coli RecA protein has been the most intensively studied enzyme of homologous recombination, the unusual RecA-DNA filament has stood alone until very recently. It now appears that this protein is part of a universal family that spans all of biology, and the filament that is formed by the protein on DNA is a universal structure. With RecA's role in recombination given new and greatly increased significance, we focus in this review on the energetics of the RecA-mediated strand exchange and the relation between the energetics and recombination spanning heterologous inserts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01924002
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