ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    facet.materialart.
    Unknown
    Three-dimensional structure of herpes simplex virus from cryo-electron tomography (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-11-25
    Description: Herpes simplex virus, a DNA virus of high complexity, consists of a nucleocapsid surrounded by the tegument-a protein compartment-and the envelope. The latter components, essential for infectivity, are pleiomorphic. Visualized in cryo-electron tomograms of isolated virions, the tegument was seen to form an asymmetric cap: On one side, the capsid closely approached the envelope; on the other side, they were separated by approximately 35 nanometers of tegument. The tegument substructure was particulate, with some short actin-like filaments. The envelope contained 600 to 750 glycoprotein spikes that varied in length, spacing, and in the angles at which they emerge from the membrane. Their distribution was nonrandom, suggesting functional clustering.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grunewald, Kay -- Desai, Prashant -- Winkler, Dennis C -- Heymann, J Bernard -- Belnap, David M -- Baumeister, Wolfgang -- Steven, Alasdair C -- AI33077/AI/NIAID NIH HHS/ -- R01 AI033077/AI/NIAID NIH HHS/ -- R01 AI033077-10/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2003 Nov 21;302(5649):1396-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14631040" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Capsid/chemistry/ultrastructure ; Cercopithecus aethiops ; Cryoelectron Microscopy ; Herpesvirus 1, Human/*chemistry/physiology/*ultrastructure ; Humans ; Image Processing, Computer-Assisted ; Lipid Bilayers ; Nucleocapsid/ultrastructure ; Tomography ; Vero Cells ; Viral Envelope Proteins/analysis/ultrastructure ; Virion/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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 2
    facet.materialart.
    Unknown
    Cryo-electron tomography reveals the cytoskeletal structure of Spiroplasma melliferum (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-01-22
    Description: Evidence has accumulated recently that not only eukaryotes but also bacteria can have a cytoskeleton. We used cryo-electron tomography to study the three-dimensional structure of Spiroplasma melliferum cells in a close-to-native state at approximately 4-nanometer resolution. We showed that these cells possess two types of filaments arranged in three parallel ribbons underneath the cell membrane. These two filamentous structures are built of the fibril protein and possibly the actin-like protein MreB. On the basis of our structural data, we could model the motility modes of these cells and explain how helical Mollicutes can propel themselves by means of coordinated length changes of their cytoskeletal ribbons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kurner, Julia -- Frangakis, Achilleas S -- Baumeister, Wolfgang -- New York, N.Y. -- Science. 2005 Jan 21;307(5708):436-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15662018" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/analysis ; Blotting, Western ; Cell Membrane/ultrastructure ; Computer Simulation ; Cryoelectron Microscopy ; Cytoskeleton/chemistry/*ultrastructure ; Image Processing, Computer-Assisted ; Imaging, Three-Dimensional ; Models, Biological ; Movement ; Spiroplasma/chemistry/physiology/*ultrastructure ; Tomography
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 3
    facet.materialart.
    Unknown
    Nuclear pore complex structure and dynamics revealed by cryoelectron tomography (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-30
    Description: Nuclear pore complexes (NPCs) are gateways for nucleocytoplasmic exchange. To analyze their structure in a close-to-life state, we studied transport-active, intact nuclei from Dictyostelium discoideum by means of cryoelectron tomography. Subvolumes of the tomograms containing individual NPCs were extracted in silico and subjected to three-dimensional classification and averaging, whereby distinct structural states were observed. The central plug/transporter (CP/T) was variable in volume and could occupy different positions along the nucleocytoplasmic axis, which supports the notion that it essentially represents cargo in transit. Changes in the position of the CP/T were accompanied by structural rearrangements in the NPC scaffold.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beck, Martin -- Forster, Friedrich -- Ecke, Mary -- Plitzko, Jurgen M -- Melchior, Frauke -- Gerisch, Gunther -- Baumeister, Wolfgang -- Medalia, Ohad -- New York, N.Y. -- Science. 2004 Nov 19;306(5700):1387-90. Epub 2004 Oct 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15514115" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Animals ; Cell Nucleus/ultrastructure ; Cryoelectron Microscopy ; Cytoskeleton/ultrastructure ; Dictyostelium/chemistry/metabolism/*ultrastructure ; Image Processing, Computer-Assisted ; *Imaging, Three-Dimensional ; Nuclear Pore/chemistry/*ultrastructure ; Tomography/*methods
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 4
    facet.materialart.
    Unknown
    Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-28
    Description: The three-dimensional structure of the proteasome from the archaebacterium Thermoplasma acidophilum has been elucidated by x-ray crystallographic analysis by means of isomorphous replacement and cyclic averaging. The atomic model was built and refined to a crystallographic R factor of 22.1 percent. The 673-kilodalton protease complex consists of 14 copies of two different subunits, alpha and beta, forming a barrel-shaped structure of four stacked rings. The two inner rings consist of seven beta subunits each, and the two outer rings consist of seven alpha subunits each. A narrow channel controls access to the three inner compartments. The alpha 7 beta 7 beta 7 alpha 7 subunit assembly has 72-point group symmetry. The structures of the alpha and beta subunits are similar, consisting of a core of two antiparallel beta sheets that is flanked by alpha helices on both sides. The binding of a peptide aldehyde inhibitor marks the active site in the central cavity at the amino termini of the beta subunits and suggests a novel proteolytic mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lowe, J -- Stock, D -- Jap, B -- Zwickl, P -- Baumeister, W -- Huber, R -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):533-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Biochemie, Abteilung fur Strukturforschung, Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7725097" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Archaeal Proteins ; Binding Sites ; Chaperonin 60/chemistry ; Computer Graphics ; Crystallography, X-Ray ; Cysteine Endopeptidases/*chemistry/metabolism ; Endopeptidases/*chemistry/metabolism ; Fourier Analysis ; Hydrogen Bonding ; Leupeptins/chemistry/metabolism ; *Models, Molecular ; Molecular Sequence Data ; Multienzyme Complexes/*chemistry/metabolism ; Protease Inhibitors/chemistry/metabolism ; Proteasome Endopeptidase Complex ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Proteins/metabolism ; Thermoplasma/*enzymology
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 5
    facet.materialart.
    Unknown
    Proteasome from Thermoplasma acidophilum: a threonine protease (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-28
    Description: The catalytic mechanism of the 20S proteasome from the archaebacterium Thermoplasma acidophilum has been analyzed by site-directed mutagenesis of the beta subunit and by inhibitor studies. Deletion of the amino-terminal threonine or its mutation to alanine led to inactivation of the enzyme. Mutation of the residue to serine led to a fully active enzyme, which was over ten times more sensitive to the serine protease inhibitor 3,4-dichloroisocoumarin. In combination with the crystal structure of a proteasome-inhibitor complex, the data show that the nucleophilic attack is mediated by the amino-terminal threonine of processed beta subunits. The conservation pattern of this residue in eukaryotic sequences suggests that at least three of the seven eukaryotic beta-type subunit branches should be proteolytically inactive.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seemuller, E -- Lupas, A -- Stock, D -- Lowe, J -- Huber, R -- Baumeister, W -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):579-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Abteilung fur Strukturbiologie Max-Planck Institut fur Biochemie, Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7725107" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Archaeal Proteins ; Binding Sites ; Coumarins/pharmacology ; Endopeptidases/*chemistry/metabolism ; Hydrogen-Ion Concentration ; Molecular Sequence Data ; Mutagenesis ; Protein Folding ; Sequence Alignment ; Serine Proteinase Inhibitors/pharmacology ; Thermoplasma/*enzymology
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 6
    Electronic Resource
    Electronic Resource
    Localization of subunits in proteasomes from Thermoplasma acidophilum by immunoelectron microscopy
    Amsterdam : Elsevier
    FEBS Letters 290 (1991), S. 186-190 
    Details
    ISSN: 0014-5793
    Keywords: Archaebacterium ; Immunoelectron microscopy ; Multicatalytic proteinase ; Proteasome
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(91)81256-8
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    The multicatalytic proteinase (prosome) is ubiquitous from eukaryotes to archaebacteria
    Amsterdam : Elsevier
    FEBS Letters 251 (1989), S. 125-131 
    Details
    ISSN: 0014-5793
    Keywords: Archaebacteria ; Electron microscopy ; Multicatalytic proteinase ; Prosome
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(89)81441-3
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Cloning and sequencing of the gene encoding the large (α-) subunit of the proteasome from Thermoplasma acidophilum
    Amsterdam : Elsevier
    FEBS Letters 278 (1991), S. 217-221 
    Details
    ISSN: 0014-5793
    Keywords: Archaebacterium ; Multicatalytic proteinase ; Prosome ; Proteasome ; Thermoplasma acidophilum
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(91)80120-R
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Electron microscopy and image analysis of the multicatalytic proteinase
    Amsterdam : Elsevier
    FEBS Letters 241 (1988), S. 239-245 
    Details
    ISSN: 0014-5793
    Keywords: Electron microscopy ; Image analysis ; Multicatalytic proteinase ; Negative staining
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(88)81069-X
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...