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  • 1
    Publication Date: 2006-12-16
    Description: The Stardust spacecraft collected thousands of particles from comet 81P/Wild 2 and returned them to Earth for laboratory study. The preliminary examination of these samples shows that the nonvolatile portion of the comet is an unequilibrated assortment of materials that have both presolar and solar system origin. The comet contains an abundance of silicate grains that are much larger than predictions of interstellar grain models, and many of these are high-temperature minerals that appear to have formed in the inner regions of the solar nebula. Their presence in a comet proves that the formation of the solar system included mixing on the grandest scales.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brownlee, Don -- Tsou, Peter -- Aleon, Jerome -- Alexander, Conel M O'd -- Araki, Tohru -- Bajt, Sasa -- Baratta, Giuseppe A -- Bastien, Ron -- Bland, Phil -- Bleuet, Pierre -- Borg, Janet -- Bradley, John P -- Brearley, Adrian -- Brenker, F -- Brennan, Sean -- Bridges, John C -- Browning, Nigel D -- Brucato, John R -- Bullock, E -- Burchell, Mark J -- Busemann, Henner -- Butterworth, Anna -- Chaussidon, Marc -- Cheuvront, Allan -- Chi, Miaofang -- Cintala, Mark J -- Clark, B C -- Clemett, Simon J -- Cody, George -- Colangeli, Luigi -- Cooper, George -- Cordier, Patrick -- Daghlian, C -- Dai, Zurong -- D'Hendecourt, Louis -- Djouadi, Zahia -- Dominguez, Gerardo -- Duxbury, Tom -- Dworkin, Jason P -- Ebel, Denton S -- Economou, Thanasis E -- Fakra, Sirine -- Fairey, Sam A J -- Fallon, Stewart -- Ferrini, Gianluca -- Ferroir, T -- Fleckenstein, Holger -- Floss, Christine -- Flynn, George -- Franchi, Ian A -- Fries, Marc -- Gainsforth, Z -- Gallien, J-P -- Genge, Matt -- Gilles, Mary K -- Gillet, Philipe -- Gilmour, Jamie -- Glavin, Daniel P -- Gounelle, Matthieu -- Grady, Monica M -- Graham, Giles A -- Grant, P G -- Green, Simon F -- Grossemy, Faustine -- Grossman, Lawrence -- Grossman, Jeffrey N -- Guan, Yunbin -- Hagiya, Kenji -- Harvey, Ralph -- Heck, Philipp -- Herzog, Gregory F -- Hoppe, Peter -- Horz, Friedrich -- Huth, Joachim -- Hutcheon, Ian D -- Ignatyev, Konstantin -- Ishii, Hope -- Ito, Motoo -- Jacob, Damien -- Jacobsen, Chris -- Jacobsen, Stein -- Jones, Steven -- Joswiak, David -- Jurewicz, Amy -- Kearsley, Anton T -- Keller, Lindsay P -- Khodja, H -- Kilcoyne, A L David -- Kissel, Jochen -- Krot, Alexander -- Langenhorst, Falko -- Lanzirotti, Antonio -- Le, Loan -- Leshin, Laurie A -- Leitner, J -- Lemelle, L -- Leroux, Hugues -- Liu, Ming-Chang -- Luening, K -- Lyon, Ian -- Macpherson, Glen -- Marcus, Matthew A -- Marhas, Kuljeet -- Marty, Bernard -- Matrajt, Graciela -- McKeegan, Kevin -- Meibom, Anders -- Mennella, Vito -- Messenger, Keiko -- Messenger, Scott -- Mikouchi, Takashi -- Mostefaoui, Smail -- Nakamura, Tomoki -- Nakano, T -- Newville, M -- Nittler, Larry R -- Ohnishi, Ichiro -- Ohsumi, Kazumasa -- Okudaira, Kyoko -- Papanastassiou, Dimitri A -- Palma, Russ -- Palumbo, Maria E -- Pepin, Robert O -- Perkins, David -- Perronnet, Murielle -- Pianetta, P -- Rao, William -- Rietmeijer, Frans J M -- Robert, Francois -- Rost, D -- Rotundi, Alessandra -- Ryan, Robert -- Sandford, Scott A -- Schwandt, Craig S -- See, Thomas H -- Schlutter, Dennis -- Sheffield-Parker, J -- Simionovici, Alexandre -- Simon, Steven -- Sitnitsky, I -- Snead, Christopher J -- Spencer, Maegan K -- Stadermann, Frank J -- Steele, Andrew -- Stephan, Thomas -- Stroud, Rhonda -- Susini, Jean -- Sutton, S R -- Suzuki, Y -- Taheri, Mitra -- Taylor, Susan -- Teslich, Nick -- Tomeoka, Kazu -- Tomioka, Naotaka -- Toppani, Alice -- Trigo-Rodriguez, Josep M -- Troadec, David -- Tsuchiyama, Akira -- Tuzzolino, Anthony J -- Tyliszczak, Tolek -- Uesugi, K -- Velbel, Michael -- Vellenga, Joe -- Vicenzi, E -- Vincze, L -- Warren, Jack -- Weber, Iris -- Weisberg, Mike -- Westphal, Andrew J -- Wirick, Sue -- Wooden, Diane -- Wopenka, Brigitte -- Wozniakiewicz, Penelope -- Wright, Ian -- Yabuta, Hikaru -- Yano, Hajime -- Young, Edward D -- Zare, Richard N -- Zega, Thomas -- Ziegler, Karen -- Zimmerman, Laurent -- Zinner, Ernst -- Zolensky, Michael -- New York, N.Y. -- Science. 2006 Dec 15;314(5806):1711-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Astronomy, University of Washington, Seattle, WA 98195, USA. brownlee@astro.washington.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17170289" target="_blank"〉PubMed〈/a〉
    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
    Publication Date: 2006-12-16
    Description: We measured the elemental compositions of material from 23 particles in aerogel and from residue in seven craters in aluminum foil that was collected during passage of the Stardust spacecraft through the coma of comet 81P/Wild 2. These particles are chemically heterogeneous at the largest size scale analyzed ( approximately 180 ng). The mean elemental composition of this Wild 2 material is consistent with the CI meteorite composition, which is thought to represent the bulk composition of the solar system, for the elements Mg, Si, Mn, Fe, and Ni to 35%, and for Ca and Ti to 60%. The elements Cu, Zn, and Ga appear enriched in this Wild 2 material, which suggests that the CI meteorites may not represent the solar system composition for these moderately volatile minor elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flynn, George J -- Bleuet, Pierre -- Borg, Janet -- Bradley, John P -- Brenker, Frank E -- Brennan, Sean -- Bridges, John -- Brownlee, Don E -- Bullock, Emma S -- Burghammer, Manfred -- Clark, Benton C -- Dai, Zu Rong -- Daghlian, Charles P -- Djouadi, Zahia -- Fakra, Sirine -- Ferroir, Tristan -- Floss, Christine -- Franchi, Ian A -- Gainsforth, Zack -- Gallien, Jean-Paul -- Gillet, Philippe -- Grant, Patrick G -- Graham, Giles A -- Green, Simon F -- Grossemy, Faustine -- Heck, Philipp R -- Herzog, Gregory F -- Hoppe, Peter -- Horz, Friedrich -- Huth, Joachim -- Ignatyev, Konstantin -- Ishii, Hope A -- Janssens, Koen -- Joswiak, David -- Kearsley, Anton T -- Khodja, Hicham -- Lanzirotti, Antonio -- Leitner, Jan -- Lemelle, Laurence -- Leroux, Hugues -- Luening, Katharina -- Macpherson, Glenn J -- Marhas, Kuljeet K -- Marcus, Matthew A -- Matrajt, Graciela -- Nakamura, Tomoki -- Nakamura-Messenger, Keiko -- Nakano, Tsukasa -- Newville, Matthew -- Papanastassiou, Dimitri A -- Pianetta, Piero -- Rao, William -- Riekel, Christian -- Rietmeijer, Frans J M -- Rost, Detlef -- Schwandt, Craig S -- See, Thomas H -- Sheffield-Parker, Julie -- Simionovici, Alexandre -- Sitnitsky, Ilona -- Snead, Christopher J -- Stadermann, Frank J -- Stephan, Thomas -- Stroud, Rhonda M -- Susini, Jean -- Suzuki, Yoshio -- Sutton, Stephen R -- Taylor, Susan -- Teslich, Nick -- Troadec, D -- Tsou, Peter -- Tsuchiyama, Akira -- Uesugi, Kentaro -- Vekemans, Bart -- Vicenzi, Edward P -- Vincze, Laszlo -- Westphal, Andrew J -- Wozniakiewicz, Penelope -- Zinner, Ernst -- Zolensky, Michael E -- New York, N.Y. -- Science. 2006 Dec 15;314(5806):1731-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, State University of New York at Plattsburgh, 101 Broad Street, Plattsburgh, NY 12901, USA. george.flynn@plattsburgh.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17170294" target="_blank"〉PubMed〈/a〉
    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
    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
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 2012-09-18
    Description: The identification of proximate amino acids by chemical cross-linking and mass spectrometry (XL-MS) facilitates the structural analysis of homogeneous protein complexes. We gained distance restraints on a modular interaction network of protein complexes affinity-purified from human cells by applying an adapted XL-MS protocol. Systematic analysis of human protein phosphatase 2A (PP2A) complexes identified 176 interprotein and 570 intraprotein cross-links that link specific trimeric PP2A complexes to a multitude of adaptor proteins that control their cellular functions. Spatial restraints guided molecular modeling of the binding interface between immunoglobulin binding protein 1 (IGBP1) and PP2A and revealed the topology of TCP1 ring complex (TRiC) chaperonin interacting with the PP2A regulatory subunit 2ABG. This study establishes XL-MS as an integral part of hybrid structural biology approaches for the analysis of endogenous protein complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herzog, Franz -- Kahraman, Abdullah -- Boehringer, Daniel -- Mak, Raymond -- Bracher, Andreas -- Walzthoeni, Thomas -- Leitner, Alexander -- Beck, Martin -- Hartl, Franz-Ulrich -- Ban, Nenad -- Malmstrom, Lars -- Aebersold, Ruedi -- New York, N.Y. -- Science. 2012 Sep 14;337(6100):1348-52. doi: 10.1126/science.1221483.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Institute of Molecular Systems Biology, Eidgenossische Technische Hochschule Zurich, Wolfgang-Pauli Strasse 16, 8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22984071" target="_blank"〉PubMed〈/a〉
    Keywords: Chaperonins/chemistry ; Cross-Linking Reagents/chemistry ; Crystallography, X-Ray ; Humans ; Mass Spectrometry/*methods ; *Metabolic Networks and Pathways ; Protein Conformation ; Protein Interaction Mapping/*methods ; Protein Phosphatase 2/*chemistry
    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
    Publication Date: 2014-11-22
    Description: Chromosome segregation depends on sister chromatid cohesion mediated by cohesin. The cohesin subunits Smc1, Smc3, and Scc1 form tripartite rings that are thought to open at distinct sites to allow entry and exit of DNA. However, direct evidence for the existence of open forms of cohesin is lacking. We found that cohesin's proposed DNA exit gate is formed by interactions between Scc1 and the coiled-coil region of Smc3. Mutation of this interface abolished cohesin's ability to stably associate with chromatin and to mediate cohesion. Electron microscopy revealed that weakening of the Smc3-Scc1 interface resulted in opening of cohesin rings, as did proteolytic cleavage of Scc1. These open forms may resemble intermediate states of cohesin normally generated by the release factor Wapl and the protease separase, respectively.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huis in 't Veld, Pim J -- Herzog, Franz -- Ladurner, Rene -- Davidson, Iain F -- Piric, Sabina -- Kreidl, Emanuel -- Bhaskara, Venugopal -- Aebersold, Ruedi -- Peters, Jan-Michael -- New York, N.Y. -- Science. 2014 Nov 21;346(6212):968-72. doi: 10.1126/science.1256904.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research Institute of Molecular Pathology (IMP), Vienna Biocenter (VBC), 1030 Vienna, Austria. ; Department of Biology, Institute of Molecular Systems Biology, Eidgenossische Technische Hochschule (ETH) Zurich, 8093 Zurich, Switzerland. Department of Biochemistry, Gene Center, Ludwig-Maximilian University, 81377 Munich, Germany. ; Department of Biology, Institute of Molecular Systems Biology, Eidgenossische Technische Hochschule (ETH) Zurich, 8093 Zurich, Switzerland. ; Research Institute of Molecular Pathology (IMP), Vienna Biocenter (VBC), 1030 Vienna, Austria. peters@imp.ac.at.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25414306" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/genetics/metabolism ; Cell Cycle Proteins/chemistry/genetics/*metabolism ; Chondroitin Sulfate Proteoglycans/chemistry/genetics/*metabolism ; Chromatin/metabolism ; Chromosomal Proteins, Non-Histone/chemistry/genetics/*metabolism ; *Chromosome Segregation ; DNA/*metabolism ; DNA Replication ; Humans ; Mass Spectrometry ; Microscopy, Electron ; Molecular Sequence Data ; Nuclear Proteins/chemistry/genetics/*metabolism ; Phosphoproteins/chemistry/genetics/*metabolism ; Protein Multimerization ; Protein Structure, Tertiary ; Proto-Oncogene Proteins/genetics/metabolism ; Separase/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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  • 6
    Publication Date: 2022-05-30
    Language: English
    Type: info:eu-repo/semantics/other
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  • 7
    Publication Date: 2013-09-16
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 8
    Publication Date: 2012-11-06
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 9
    Publication Date: 2013-10-02
    Description: MicroRNAs (miRNAs) guide Argonaute (Ago) proteins to target mRNAs, leading to gene silencing. However, Ago proteins are not the actual mediators of gene silencing but interact with a member of the GW182 protein family (also known as GW proteins), which coordinates all downstream steps in gene silencing. GW proteins contain...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 10
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