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  • 1
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    Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-09
    Description: Electron tomography of vitrified cells is a noninvasive three-dimensional imaging technique that opens up new vistas for exploring the supramolecular organization of the cytoplasm. We applied this technique to Dictyostelium cells, focusing on the actin cytoskeleton. In actin networks reconstructed without prior removal of membranes or extraction of soluble proteins, the cross-linking of individual microfilaments, their branching angles, and membrane attachment sites can be analyzed. At a resolution of 5 to 6 nanometers, single macromolecules with distinct shapes, such as the 26S proteasome, can be identified in an unperturbed cellular environment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Medalia, Ohad -- Weber, Igor -- Frangakis, Achilleas S -- Nicastro, Daniela -- Gerisch, Gunther -- Baumeister, Wolfgang -- New York, N.Y. -- Science. 2002 Nov 8;298(5596):1209-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute for Biochemistry, D-82152 Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12424373" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/chemistry/metabolism/*ultrastructure ; Actins/ultrastructure ; Animals ; Binding Sites ; Cell Membrane/metabolism/ultrastructure ; Cell Movement ; Dictyostelium/chemistry/physiology/*ultrastructure ; Endoplasmic Reticulum, Rough/ultrastructure ; Freezing ; *Image Processing, Computer-Assisted ; Macromolecular Substances ; Microfilament Proteins/*ultrastructure ; Organelles/*ultrastructure ; Peptide Hydrolases/ultrastructure ; *Proteasome Endopeptidase Complex ; Proteome ; Protozoan Proteins/ultrastructure ; Ribosomes/ultrastructure ; Tomography/*methods
    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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  • 2
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    A giant protease with potential to substitute for some functions of the proteasome (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-02-12
    Description: An alanyl-alanyl-phenylalanyl-7-amino-4-methylcoumarin-hydrolyzing protease particle copurifying with 26S proteasomes was isolated and identified as tripeptidyl peptidase II (TPPII), a cytosolic subtilisin-like peptidase of unknown function. The particle is larger than the 26S proteasome and has a rod-shaped, dynamic supramolecular structure. TPPII exhibits enhanced activity in proteasome inhibitor-adapted cells and degrades polypeptides by exo- as well as predominantly trypsin-like endoproteolytic cleavage. TPPII may thus participate in extralysosomal polypeptide degradation and may in part account for nonproteasomal epitope generation as postulated for certain major histocompatibility complex class I alleles. In addition, TPPII may be able to substitute for some metabolic functions of the proteasome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geier, E -- Pfeifer, G -- Wilm, M -- Lucchiari-Hartz, M -- Baumeister, W -- Eichmann, K -- Niedermann, G -- New York, N.Y. -- Science. 1999 Feb 12;283(5404):978-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck Institute of Immunobiology, Stubeweg 51, D-79108 Freiburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9974389" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcysteine/analogs & derivatives/pharmacology ; Alleles ; Amino Acid Chloromethyl Ketones/pharmacology ; Aminopeptidases ; Animals ; Cell Survival ; Coumarins/metabolism ; Cysteine Endopeptidases/*metabolism ; Cytosol/enzymology ; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases ; Epitopes/metabolism ; Genes, MHC Class I ; Hydrolysis ; Mice ; Molecular Weight ; Multienzyme Complexes/*metabolism ; Oligopeptides/metabolism ; Proteasome Endopeptidase Complex ; Serine Endopeptidases/chemistry/isolation & purification/*metabolism ; Serine Proteinase Inhibitors/pharmacology ; Substrate Specificity ; Tumor Cells, Cultured
    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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  • 3
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    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
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  • 4
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    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
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  • 5
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    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
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  • 6
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    Neuroscience. Monte Carlo places strong odds on ectopic release (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lucic, Vladan -- Baumeister, Wolfgang -- New York, N.Y. -- Science. 2005 Jul 15;309(5733):387-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, 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/16020717" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/metabolism ; Acetylcholinesterase/metabolism ; Animals ; Chick Embryo ; *Computer Simulation ; Diffusion ; Ganglia, Parasympathetic/*physiology ; Mathematics ; *Models, Neurological ; *Monte Carlo Method ; Receptors, Nicotinic/*metabolism ; Stochastic Processes ; *Synaptic Transmission ; Synaptic Vesicles/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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  • 7
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    Varshavsky's contributions (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baumeister, Wolfgang -- Bachmair, Andreas -- Chau, Vincent -- Cohen, Robert -- Coffino, Phil -- Demartino, George -- Deshaies, Raymond -- Dohmen, Juergen -- Emr, Scott -- Finley, Daniel -- Hampton, Randy -- Hill, Christopher -- Hochstrasser, Mark -- Huber, Robert -- Jackson, Peter -- Jentsch, Stefan -- Johnson, Erica -- Kwon, Yong Tae -- Pagano, Michele -- Pickart, Cecile -- Rechsteiner, Martin -- Scheffner, Martin -- Sommer, Thomas -- Tansey, William -- Tyers, Mike -- Vierstra, Richard -- Weissman, Allan -- Wilkinson, Keith D -- Wolf, Dieter -- New York, N.Y. -- Science. 2004 Nov 19;306(5700):1290-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15550643" target="_blank"〉PubMed〈/a〉
    Keywords: History, 20th Century ; History, 21st Century ; Nobel Prize ; Proteasome Endopeptidase Complex/*metabolism ; Proteins/metabolism ; Ubiquitin/*metabolism ; Ubiquitin-Protein Ligase Complexes/genetics/*metabolism ; United States
    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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  • 8
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    Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-11
    Description: The Escherichia coli chaperonin GroEL and its regulator GroES are thought to mediate adenosine triphosphate-dependent protein folding as an asymmetrical complex, with substrate protein bound within the GroEL cylinder. In contrast, a symmetrical complex formed between one GroEL and two GroES oligomers, with substrate protein binding to the outer surface of GroEL, was recently proposed to be the functional chaperonin unit. Electron microscopic and biochemical analyses have now shown that unphysiologically high magnesium concentrations and increased pH are required to assemble symmetrical complexes, the formation of which precludes the association of unfolded polypeptide. Thus, the functional significance of GroEL:(GroES)2 particles remains to be demonstrated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Engel, A -- Hayer-Hartl, M K -- Goldie, K N -- Pfeifer, G -- Hegerl, R -- Muller, S -- da Silva, A C -- Baumeister, W -- Hartl, F U -- GM 50908/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):832-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Maurice E. Muller Institute, Biozentrum, University of Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638600" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/pharmacology ; Adenylyl Imidodiphosphate/pharmacology ; Chaperonin 10/chemistry/*metabolism/ultrastructure ; Chaperonin 60/chemistry/*metabolism/ultrastructure ; Hydrogen-Ion Concentration ; Magnesium/pharmacology ; Microscopy, Electron, Scanning Transmission ; Protein Folding
    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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  • 9
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    Tricorn protease--the core of a modular proteolytic system (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-22
    Description: Large macromolecular assemblies have evolved as a means of compartmentalizing reactions in organisms lacking membrane-bounded compartments. A tricorn-shaped protease was isolated from the archaeon Thermoplasma and was shown to form a multisubunit proteolytic complex. The 120-kilodalton monomer assembled to form a hexameric toroid that could assemble further into a capsid structure. Tricorn protease appeared to act as the core of a proteolytic system; when it interacted with several smaller proteins, it displayed multicatalytic activities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tamura, T -- Tamura, N -- Cejka, Z -- Hegerl, R -- Lottspeich, F -- Baumeister, W -- New York, N.Y. -- Science. 1996 Nov 22;274(5291):1385-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institute for Biochemistry, D-82152 Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8910281" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cloning, Molecular ; Cysteine Endopeptidases/metabolism ; Endopeptidases/*chemistry/genetics/isolation & purification/*metabolism ; Genes, Bacterial ; Microscopy, Electron ; Models, Molecular ; Molecular Sequence Data ; Molecular Weight ; Multienzyme Complexes/metabolism ; Peptides/metabolism ; Proteasome Endopeptidase Complex ; *Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/metabolism ; Substrate Specificity ; Thermoplasma/*enzymology
    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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  • 10
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    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
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