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  • Articles  (145)
  • Journal of Cellular Biochemistry  (5)
  • ACS Sustainable Chemistry & Engineering  (4)
  • Science  (4)
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  • Articles  (145)
  • 1
    Publication Date: 2016-03-29
    Description: It is a common complication to develop a secondary lymphedema after surgery or radiation, for example after axillary lymph node dissection due to breast cancer and current therapies are mainly symptomatic. Since these surgical procedures result in both, loss of adipose tissue and loss of lymphatic nodes and vessels, tissue engineering could be a new promising approach, to create an adipose tissue substitute comprised with a lymphatic network. We have conducted co-culture experiments to investigate the effects of human adipose-derived stem cells (ASCs) on human lymphatic endothelial cells (LECs) in terms of gene expression profile, proliferation, migration, and tube formation in vitro. In this respect, both cell types were co-cultured either indirectly or directly with or without the recombinant growth factor VEGF-C. Indirect co-cultures were performed with the aid of a transwell chamber. In case of direct co-culture, immunomagnetic separation by CD31 magnetic beads allowed examination of the LEC population. Direct and indirect co-culture of ASCs induced mRNA expression of lymphatic marker genes, proliferation and migration by LECs without affecting tube formation. Thus, we have shown that co-culture of ASCs with LECs might be a feasible approach that could be used in cell-based tissue engineering therapies to heal or improve a secondary lymphedema. This article is protected by copyright. All rights reserved
    Electronic ISSN: 0091-7419
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Published by Wiley
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  • 2
    Publication Date: 2016-01-12
    Description: Vascularization is important for bone development, fracture healing and engineering of artificial bone tissue. In the context of bone tissue engineering, it was shown that coimplantation of human primary umbilical vein endothelial cells (HUVECs) and human osteoblasts (hOBs) results in the formation of functional blood vessels and enhanced bone regeneration. Implanted endothelial cells do not only contribute to blood vessel formation, but also support proliferation, cell survival and osteogenic differentiation of coimplanted hOBs. These effects are partially mediated by direct heterotypic cell contacts. In a previous report we could show that cocultivated hOBs strongly increase the expression of genes involved in extracellular matrix (ECM) formation in HUVECs, suggesting that ECM may be involved in the intercellular communication between hOBs and HUVECs. The present study aimed at investigating whether comparable changes occur in hOBs. We therefore performed a microarray analysis of hOBs cultivated in direct contact with HUVECs, revealing 1004 differentially expressed genes. The differentially expressed genes could be assigned to the functional clusters ECM, proliferation, apoptosis and osteogenic differentiation. The microarray data could be confirmed by performing quantitative real time RT-PCR on selected genes. Furthermore, we could show that the ECM produced by HUVECs increased the expression of the osteogenic differentiation marker alkaline phosphatase (ALP) in hOBs. In summary, our data demonstrate that HUVECs provoke complex changes in gene expression patterns in cocultivated hOBs and that ECM plays and important role in this interaction. This article is protected by copyright. All rights reserved
    Electronic ISSN: 0091-7419
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Published by Wiley
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  • 3
    Publication Date: 1998-03-21
    Description: Entry into anaphase and exit from mitosis depend on a ubiquitin-protein ligase complex called the anaphase-promoting complex (APC) or cyclosome. At least 12 different subunits were detected in the purified particle from budding yeast, including the previously identified proteins Apc1p, Cdc16p, Cdc23p, Cdc26p, and Cdc27p. Five additional subunits purified in low nanogram amounts were identified by tandem mass spectrometric sequencing. Apc2p, Apc5p, and the RING-finger protein Apc11p are conserved from yeast to humans. Apc2p is similar to the cullin Cdc53p, which is a subunit of the ubiquitin-protein ligase complex SCFCdc4 required for the initiation of DNA replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zachariae, W -- Shevchenko, A -- Andrews, P D -- Ciosk, R -- Galova, M -- Stark, M J -- Mann, M -- Nasmyth, K -- New York, N.Y. -- Science. 1998 Feb 20;279(5354):1216-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, A-1030 Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9469814" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Anaphase ; Anaphase-Promoting Complex-Cyclosome ; Animals ; Cell Cycle Proteins/chemistry/metabolism ; *Cullin Proteins ; Cyclins/metabolism ; DNA Replication ; Fungal Proteins/*chemistry/genetics/isolation & purification ; Genes, Fungal ; Humans ; Ligases/*chemistry/genetics/isolation & purification ; Mass Spectrometry ; Molecular Sequence Data ; Saccharomyces cerevisiae/*chemistry/*cytology/genetics ; *Saccharomyces cerevisiae Proteins ; Sequence Alignment ; Spindle Apparatus/metabolism ; *Ubiquitin-Protein Ligase Complexes ; Ubiquitin-Protein Ligases ; Ubiquitins/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 1999-08-14
    Description: Intracellular membrane fusion is crucial for the biogenesis and maintenance of cellular compartments, for vesicular traffic between them, and for exo- and endocytosis. Parts of the molecular machinery underlying this process have been identified, but most of these components operate in mutual recognition of the membranes. Here it is shown that protein phosphatase 1 (PP1) is essential for bilayer mixing, the last step of membrane fusion. PP1 was also identified in a complex that contained calmodulin, the second known factor implicated in the regulation of bilayer mixing. The PP1-calmodulin complex was required at multiple sites of intracellular trafficking; hence, PP1 may be a general factor controlling membrane bilayer mixing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peters, C -- Andrews, P D -- Stark, M J -- Cesaro-Tadic, S -- Glatz, A -- Podtelejnikov, A -- Mann, M -- Mayer, A -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1999 Aug 13;285(5430):1084-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Friedrich-Miescher-Laboratorium, Spemannstrasse 37-39, 72076 Tubingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10446058" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Transport ; Calcium/metabolism ; Calmodulin/analysis/metabolism ; Carboxypeptidases/metabolism ; Cathepsin A ; Cell Membrane/metabolism ; Endocytosis ; Endoplasmic Reticulum/metabolism ; Enzyme Inhibitors/pharmacology ; Fluorescent Dyes ; Golgi Apparatus/metabolism ; Intracellular Membranes/*metabolism ; *Membrane Fusion ; Microcystins ; Mutation ; Peptides, Cyclic/pharmacology ; Phosphoprotein Phosphatases/antagonists & inhibitors/genetics/*metabolism ; Protein Phosphatase 1 ; Pyridinium Compounds ; Quaternary Ammonium Compounds ; Saccharomyces cerevisiae/genetics/*metabolism ; Temperature ; Vacuoles/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 2018-11-23
    Description: Measurement of the mass of particles in the mega- to gigadalton range is challenging with conventional mass spectrometry. Although this mass range appears optimal for nanomechanical resonators, nanomechanical mass spectrometers often suffer from prohibitive sample loss, extended analysis time, or inadequate resolution. We report on a system architecture combining nebulization of the analytes from solution, their efficient transfer and focusing without relying on electromagnetic fields, and the mass measurements of individual particles using nanomechanical resonator arrays. This system determined the mass distribution of ~30-megadalton polystyrene nanoparticles with high detection efficiency and effectively performed molecular mass measurements of empty or DNA-filled bacteriophage T5 capsids with masses up to 105 megadaltons using less than 1 picomole of sample and with an instrument resolution above 100.
    Keywords: Physics, Applied, Chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Geosciences , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 1991-05-31
    Description: Filamentous bacteriophage Pf1 assembles by a membrane-mediated process during which the viral DNA is secreted through the membrane while being encapsulated by the major coat protein. Neutron diffraction studies showed that in the virus most of the coat protein consists of two alpha-helical segments arranged end-to-end with an intervening mobile surface loop. Nuclear magnetic resonance studies of the coat protein in the membrane-bound form have shown that the secondary structure is essentially identical to that in the intact virus. A comparison indicates that during membrane-mediated viral assembly, while the secondary structure of the coat protein is largely conserved, its tertiary structure changes substantially.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nambudripad, R -- Stark, W -- Opella, S J -- Makowski, L -- New York, N.Y. -- Science. 1991 May 31;252(5010):1305-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, Boston University, MA 02215.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925543" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophages/chemistry ; Capsid/*chemistry/metabolism ; *Capsid Proteins ; Cell Membrane/*metabolism ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Structure ; Neutrons ; Protein Conformation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 1992-11-06
    Description: A 9.5-kilobase plasmid of Yersinia pestis, the causative agent of plague, is required for high virulence when mice are inoculated with the bacterium by subcutaneous injection. Inactivation of the plasmid gene pla, which encodes a surface protease, increased the median lethal dose of the bacteria for mice by a millionfold. Moreover, cloned pla was sufficient to restore segregants lacking the entire pla-bearing plasmid to full virulence. Both pla+ strains injected subcutaneously and pla- mutants injected intravenously reached high titers in liver and spleen of infected mice, whereas pla- mutants injected subcutaneously failed to do so even though they establish a sustained local infection at the injection site. More inflammatory cells accumulated in lesions caused by the pla- mutants than in lesions produced by the pla+ parent. The Pla protease was shown to be a plasminogen activator with unusual kinetic properties. It can also cleave complement C3 at a specific site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sodeinde, O A -- Subrahmanyam, Y V -- Stark, K -- Quan, T -- Bao, Y -- Goguen, J D -- AI22176/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Nov 6;258(5084):1004-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester 01655.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1439793" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Bacterial Proteins ; Colony Count, Microbial ; Escherichia coli/enzymology ; Fibrinolysin/chemistry/metabolism ; Injections, Intravenous ; Kinetics ; Liver/microbiology ; Mice ; Molecular Sequence Data ; Mutation ; Plague/microbiology ; Plasmids ; Plasminogen Activators/genetics/*physiology ; Recombinant Proteins/metabolism ; Spleen/microbiology ; Tissue Plasminogen Activator/metabolism ; Urokinase-Type Plasminogen Activator/metabolism ; Yersinia pestis/*enzymology/isolation & purification/*pathogenicity
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
    Publication Date: 1992-10-09
    Description: Starch, a major storage metabolite in plants, positively affects the agricultural yield of a number of crops. Its biosynthetic reactions use adenosine diphosphate glucose (ADPGlc) as a substrate; ADPGlc pyrophosphorylase, the enzyme involved in ADPGlc formation, is regulated by allosteric effectors. Evidence that this plastidial enzyme catalyzes a rate-limiting reaction in starch biosynthesis was derived by expression in plants of a gene that encodes a regulatory variant of this enzyme. Allosteric regulation was demonstrated to be the major physiological mechanism that controls starch biosynthesis. Thus, plant and bacterial systems for starch and glycogen biosynthesis are similar and distinct from yeast and mammalian systems, wherein glycogen synthase has been demonstrated to be the rate-limiting regulatory step.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stark, D M -- Timmerman, K P -- Barry, G F -- Preiss, J -- Kishore, G M -- New York, N.Y. -- Science. 1992 Oct 9;258(5080):287-92.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17835129" target="_blank"〉PubMed〈/a〉
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
    Publication Date: 2009-03-17
    Description: Once all chromosomes are connected to the mitotic spindle (bioriented), anaphase is initiated by the protein ubiquitylation activity of the anaphase-promoting complex/cyclosome (APC/C) and its coactivator Cdc20 (APC/C(Cdc20)). Before chromosome biorientation, anaphase is delayed by a mitotic checkpoint complex (MCC) that inhibits APC/C(Cdc20). We used single-particle electron microscopy to obtain three-dimensional models of human APC/C in various functional states: bound to MCC, to Cdc20, or to neither (apo-APC/C). These experiments revealed that MCC associates with the Cdc20 binding site on APC/C, locks the otherwise flexible APC/C in a "closed" state, and prevents binding and ubiquitylation of a wide range of different APC/C substrates. These observations clarify the structural basis for the inhibition of APC/C by spindle checkpoint proteins.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2989460/" 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/PMC2989460/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herzog, Franz -- Primorac, Ivana -- Dube, Prakash -- Lenart, Peter -- Sander, Bjorn -- Mechtler, Karl -- Stark, Holger -- Peters, Jan-Michael -- F 3407/Austrian Science Fund FWF/Austria -- New York, N.Y. -- Science. 2009 Mar 13;323(5920):1477-81. doi: 10.1126/science.1163300.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, 1030 Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19286556" target="_blank"〉PubMed〈/a〉
    Keywords: Anaphase ; Anaphase-Promoting Complex-Cyclosome ; Cdc20 Proteins ; Cell Cycle Proteins/chemistry/metabolism ; HeLa Cells ; Humans ; Image Processing, Computer-Assisted ; Imaging, Three-Dimensional ; Microscopy, Electron ; *Mitosis ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Spindle Apparatus/*metabolism ; Ubiquitin-Conjugating Enzymes/chemistry/metabolism ; Ubiquitin-Protein Ligase Complexes/*chemistry/*metabolism ; Ubiquitination
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
    Publication Date: 2009-07-04
    Description: The accretion of matter onto a massive black hole is believed to feed the relativistic plasma jets found in many active galactic nuclei (AGN). Although some AGN accelerate particles to energies exceeding 10(12) electron volts and are bright sources of very-high-energy (VHE) gamma-ray emission, it is not yet known where the VHE emission originates. Here we report on radio and VHE observations of the radio galaxy Messier 87, revealing a period of extremely strong VHE gamma-ray flares accompanied by a strong increase of the radio flux from its nucleus. These results imply that charged particles are accelerated to very high energies in the immediate vicinity of the black hole.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉VERITAS Collaboration -- VLBA 43 GHz M87 Monitoring Team -- H.E.S.S. Collaboration -- MAGIC Collaboration -- Acciari, V A -- Aliu, E -- Arlen, T -- Bautista, M -- Beilicke, M -- Benbow, W -- Bradbury, S M -- Buckley, J H -- Bugaev, V -- Butt, Y -- Byrum, K -- Cannon, A -- Celik, O -- Cesarini, A -- Chow, Y C -- Ciupik, L -- Cogan, P -- Cui, W -- Dickherber, R -- Fegan, S J -- Finley, J P -- Fortin, P -- Fortson, L -- Furniss, A -- Gall, D -- Gillanders, G H -- Grube, J -- Guenette, R -- Gyuk, G -- Hanna, D -- Holder, J -- Horan, D -- Hui, C M -- Humensky, T B -- Imran, A -- Kaaret, P -- Karlsson, N -- Kieda, D -- Kildea, J -- Konopelko, A -- Krawczynski, H -- Krennrich, F -- Lang, M J -- LeBohec, S -- Maier, G -- McCann, A -- McCutcheon, M -- Millis, J -- Moriarty, P -- Ong, R A -- Otte, A N -- Pandel, D -- Perkins, J S -- Petry, D -- Pohl, M -- Quinn, J -- Ragan, K -- Reyes, L C -- Reynolds, P T -- Roache, E -- Rose, H J -- Schroedter, M -- Sembroski, G H -- Smith, A W -- Swordy, S P -- Theiling, M -- Toner, J A -- Varlotta, A -- Vincent, S -- Wakely, S P -- Ward, J E -- Weekes, T C -- Weinstein, A -- Williams, D A -- Wissel, S -- Wood, M -- Walker, R C -- Davies, F -- Hardee, P E -- Junor, W -- Ly, C -- Aharonian, F -- Akhperjanian, A G -- Anton, G -- Barres de Almeida, U -- Bazer-Bachi, A R -- Becherini, Y -- Behera, B -- Bernlohr, K -- Bochow, A -- Boisson, C -- Bolmont, J -- Borrel, V -- Brucker, J -- Brun, F -- Brun, P -- Buhler, R -- Bulik, T -- Busching, I -- Boutelier, T -- Chadwick, P M -- Charbonnier, A -- Chaves, R C G -- Cheesebrough, A -- Chounet, L-M -- Clapson, A C -- Coignet, G -- Dalton, M -- Daniel, M K -- Davids, I D -- Degrange, B -- Deil, C -- Dickinson, H J -- Djannati-Atai, A -- Domainko, W -- Drury, L O'C -- Dubois, F -- Dubus, G -- Dyks, J -- Dyrda, M -- Egberts, K -- Emmanoulopoulos, D -- Espigat, P -- Farnier, C -- Feinstein, F -- Fiasson, A -- Forster, A -- Fontaine, G -- Fussling, M -- Gabici, S -- Gallant, Y A -- Gerard, L -- Gerbig, D -- Giebels, B -- Glicenstein, J F -- Gluck, B -- Goret, P -- Gohring, D -- Hauser, D -- Hauser, M -- Heinz, S -- Heinzelmann, G -- Henri, G -- Hermann, G -- Hinton, J A -- Hoffmann, A -- Hofmann, W -- Holleran, M -- Hoppe, S -- Horns, D -- Jacholkowska, A -- de Jager, O C -- Jahn, C -- Jung, I -- Katarzynski, K -- Katz, U -- Kaufmann, S -- Kendziorra, E -- Kerschhaggl, M -- Khangulyan, D -- Khelifi, B -- Keogh, D -- Kluzniak, W -- Kneiske, T -- Komin, Nu -- Kosack, K -- Lamanna, G -- Lenain, J-P -- Lohse, T -- Marandon, V -- Martin, J M -- Martineau-Huynh, O -- Marcowith, A -- Maurin, D -- McComb, T J L -- Medina, M C -- Moderski, R -- Moulin, E -- Naumann-Godo, M -- de Naurois, M -- Nedbal, D -- Nekrassov, D -- Nicholas, B -- Niemiec, J -- Nolan, S J -- Ohm, S -- Olive, J-F -- de Ona Wilhelmi, E -- Orford, K J -- Ostrowski, M -- Panter, M -- Paz Arribas, M -- Pedaletti, G -- Pelletier, G -- Petrucci, P-O -- Pita, S -- Puhlhofer, G -- Punch, M -- Quirrenbach, A -- Raubenheimer, B C -- Raue, M -- Rayner, S M -- Renaud, M -- Rieger, F -- Ripken, J -- Rob, L -- Rosier-Lees, S -- Rowell, G -- Rudak, B -- Rulten, C B -- Ruppel, J -- Sahakian, V -- Santangelo, A -- Schlickeiser, R -- Schock, F M -- Schroder, R -- Schwanke, U -- Schwarzburg, S -- Schwemmer, S -- Shalchi, A -- Sikora, M -- Skilton, J L -- Sol, H -- Spangler, D -- Stawarz, L -- Steenkamp, R -- Stegmann, C -- Stinzing, F -- Superina, G -- Szostek, A -- Tam, P H -- Tavernet, J-P -- Terrier, R -- Tibolla, O -- Tluczykont, M -- van Eldik, C -- Vasileiadis, G -- Venter, C -- Venter, L -- Vialle, J P -- Vincent, P -- Vivier, M -- Volk, H J -- Volpe, F -- Wagner, S J -- Ward, M -- Zdziarski, A A -- Zech, A -- Anderhub, H -- Antonelli, L A -- Antoranz, P -- Backes, M -- Baixeras, C -- Balestra, S -- Barrio, J A -- Bastieri, D -- Becerra Gonzalez, J -- Becker, J K -- Bednarek, W -- Berger, K -- Bernardini, E -- Biland, A -- Bock, R K -- Bonnoli, G -- Bordas, P -- Borla Tridon, D -- Bosch-Ramon, V -- Bose, D -- Braun, I -- Bretz, T -- Britvitch, I -- Camara, M -- Carmona, E -- Commichau, S -- Contreras, J L -- Cortina, J -- Costado, M T -- Covino, S -- Curtef, V -- Dazzi, F -- De Angelis, A -- De Cea del Pozo, E -- Delgado Mendez, C -- De los Reyes, R -- De Lotto, B -- De Maria, M -- De Sabata, F -- Dominguez, A -- Dorner, D -- Doro, M -- Elsaesser, D -- Errando, M -- Ferenc, D -- Fernandez, E -- Firpo, R -- Fonseca, M V -- Font, L -- Galante, N -- Garcia Lopez, R J -- Garczarczyk, M -- Gaug, M -- Goebel, F -- Hadasch, D -- Hayashida, M -- Herrero, A -- Hildebrand, D -- Hohne-Monch, D -- Hose, J -- Hsu, C C -- Jogler, T -- Kranich, D -- La Barbera, A -- Laille, A -- Leonardo, E -- Lindfors, E -- Lombardi, S -- Longo, F -- Lopez, M -- Lorenz, E -- Majumdar, P -- Maneva, G -- Mankuzhiyil, N -- Mannheim, K -- Maraschi, L -- Mariotti, M -- Martinez, M -- Mazin, D -- Meucci, M -- Miranda, J M -- Mirzoyan, R -- Miyamoto, H -- Moldon, J -- Moles, M -- Moralejo, A -- Nieto, D -- Nilsson, K -- Ninkovic, J -- Oya, I -- Paoletti, R -- Paredes, J M -- Pasanen, M -- Pascoli, D -- Pauss, F -- Pegna, R G -- Perez-Torres, M A -- Persic, M -- Peruzzo, L -- Prada, F -- Prandini, E -- Puchades, N -- Reichardt, I -- Rhode, W -- Ribo, M -- Rico, J -- Rissi, M -- Robert, A -- Rugamer, S -- Saggion, A -- Saito, T Y -- Salvati, M -- Sanchez-Conde, M -- Satalecka, K -- Scalzotto, V -- Scapin, V -- Schweizer, T -- Shayduk, M -- Shore, S N -- Sidro, N -- Sierpowska-Bartosik, A -- Sillanpaa, A -- Sitarek, J -- Sobczynska, D -- Spanier, F -- Stamerra, A -- Stark, L S -- Takalo, L -- Tavecchio, F -- Temnikov, P -- Tescaro, D -- Teshima, M -- Torres, D F -- Turini, N -- Vankov, H -- Wagner, R M -- Zabalza, V -- Zandanel, F -- Zanin, R -- Zapatero, J -- New York, N.Y. -- Science. 2009 Jul 24;325(5939):444-8. doi: 10.1126/science.1175406. Epub 2009 Jul 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fred Lawrence Whipple Observatory, Harvard-Smithsonian Center for Astrophysics, Amado, AZ 85645, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19574351" target="_blank"〉PubMed〈/a〉
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