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  • 1
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    Existence of a return direction for plasma escaping from a pinched column in a plasma focus discharge (2015)
    American Institute of Physics (AIP)
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    Publication Date: 2015-05-16
    Description: The use of multi-frame interferometry used on the PF-1000 device with the deuterium filling showed the existence of a return motion of the top of several lobules of the pinched column formed at the pinched plasma column. This phenomenon was observed in the presence of an over-optimal mass in front of the anode, which depressed the intensity of the implosion and the smooth surface of the pinched plasma column. The observed evolution was explored through the use of closed poloidal currents transmitted outside the pinched plasma. This interpretation complements the scenario of the closed currents flowing within the structures inside the pinched column, which has been published recently on the basis of observations from interferometry, neutron, and magnetic probe diagnostics on this device.
    Print ISSN: 1070-664X
    Electronic ISSN: 1089-7674
    Topics: Physics
    Published by American Institute of Physics (AIP)
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  • 2
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    Filamentary structure of plasma produced by compression of puffing deuterium by deuterium or neon plasma sheath on plasma-focus discharge (2014)
    American Institute of Physics (AIP)
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    Publication Date: 2014-12-12
    Description: The present experiments were performed on the PF-1000 plasma focus device at a current of 2 MA with the deuterium injected from the gas-puff placed in the axis of the anode face. The XUV frames showed, in contrast with the interferograms, the fine structure: filaments and spots up to 1 mm diameter. In the deuterium filling, the short filaments are registered mainly in the region of the internal plasmoidal structures and their number correlates with the intensity of neutron production. The longer filamentary structure was recorded close to the anode after the constriction decay. The long curve-like filaments with spots were registered in the big bubble formed after the pinch phase in the head of the umbrella shape of the plasma sheath. Filaments can indicate the filamentary structure of the current in the pinch. Together with the filaments, small compact balls a few mm in diameter were registered by both interferometry and XUV frame pictures. They emerge out of the dense column and their life-time can be greater than hundreds of ns.
    Print ISSN: 1070-664X
    Electronic ISSN: 1089-7674
    Topics: Physics
    Published by American Institute of Physics (AIP)
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  • 3
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    Investigation of compression of puffing neon by deuterium current and plasma sheath in plasma focus discharge (2015)
    American Institute of Physics (AIP)
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    Publication Date: 2015-06-12
    Description: This paper presents the results of the research of the influence of compressed neon, injected by the gas-puff nozzle in front of the anode axis by the deuterium current and plasma sheath on the evolution of the pinch, and neutron production at the current of 2 MA. The intense soft X-ray emission shows the presence of neon in the central region of the pinch. During the implosion and stopping of the plasma sheath, the deuterium plasma penetrates into the internal neon layer. The total neutron yield of 10 10 –10 11 has a similar level as in the pure deuterium shots. The neutron and hard X-ray pulses from fusion D-D reaction are as well emitted both in the phase of the stopping implosion and during the evolution of instabilities at the transformation of plasmoidal structures and constrictions composed in this configuration from both gases. The fast deuterons can be accelerated at the decay of magnetic field of the current filaments in these structures.
    Print ISSN: 1070-664X
    Electronic ISSN: 1089-7674
    Topics: Physics
    Published by American Institute of Physics (AIP)
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  • 4
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    The influence of the nitrogen admixture on the evolution of a deuterium pinch column (2016)
    American Institute of Physics (AIP)
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    Publication Date: 2016-08-12
    Description: The application of a mixture of nitrogen and deuterium for the gas-puffing along the anode axis in deuterium plasma-focus discharges, as carried out at megaampere-level currents, enabled observations of the filamentary structure, and the decrease in the transformation velocity of the plasma column to be performed. It made possible to investigate the instability evolution during the production of hard X-rays and fast neutrons in more detail. The constriction of a plasma column transforms itself during the final phase of the compression into one or more small dense plasmoid-like structures which are separated by narrow necks. During the next phase, these structures start to decay by an expansion, in which a part of the plasma volume maintains its compactness. This evolution is explained by an increase and later decrease in the internal poloidal current component by reconnections of the associated magnetic lines, which are responsible for the acceleration of electron and ion beams.
    Print ISSN: 1070-664X
    Electronic ISSN: 1089-7674
    Topics: Physics
    Published by American Institute of Physics (AIP)
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  • 5
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    Influence of the Al wire placed in the anode axis on the transformation of the deuterium plasma column in the plasma focus discharge (2016)
    American Institute of Physics (AIP)
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    Publication Date: 2016-06-14
    Description: In this paper, we describe the influence of an Al wire of 270  μ m in diameter placed along the anode axis on the transformation of the deuterium pinch column in a megaampere (MA) plasma focus device. The evolution of the pinched column and of the wire corona was investigated by means of the multiframe interferometry, neutron and X-ray diagnostics. The wire corona did not influence considerably on the evolution of dense plasma structures and neutron production, but it increased the plasma density and consequently, the currents around its surface. The distribution of the closed internal currents (ranging hundreds of kA) and associated magnetic fields amounting to 5 T were also estimated in the dense plasma column and in plasmoidal structures at the near-equilibrium state. The description is based on the balance of the plasma pressure and the pressure of the internal poloidal and toroidal current components compressed by the external pinched column. The dominant number of fusion deuterium-deuterium (D-D) neutrons is produced during the evolution of instabilities, when the uninterrupted wire corona (containing deuterium) connects the dense structures of the pinch, and it did not allow the formation of a constriction of the sub-millimeter diameter.
    Print ISSN: 1070-664X
    Electronic ISSN: 1089-7674
    Topics: Physics
    Published by American Institute of Physics (AIP)
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  • 6
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    Research on anisotropy of fusion-produced protons and neutrons emission from high-current plasma-focus discharges (2015)
    American Institute of Physics (AIP)
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    Publication Date: 2015-01-13
    Description: The paper concerns fast protons and neutrons from D-D fusion reactions in a Plasma-Focus-1000U facility. Measurements were performed with nuclear-track detectors arranged in “sandwiches” of an Al-foil and two PM-355 detectors separated by a polyethylene-plate. The Al-foil eliminated all primary deuterons, but was penetrable for fast fusion protons. The foil and first PM-355 detector were penetrable for fast neutrons, which were converted into recoil-protons in the polyethylene and recorded in the second PM-355 detector. The “sandwiches” were irradiated by discharges of comparable neutron-yields. Analyses of etched tracks and computer simulations of the fusion-products behavior in the detectors were performed.
    Print ISSN: 0034-6748
    Electronic ISSN: 1089-7623
    Topics: Electrical Engineering, Measurement and Control Technology , Physics
    Published by American Institute of Physics (AIP)
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  • 7
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    Neutron production from puffing deuterium in plasma focus device (2014)
    American Institute of Physics (AIP)
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    Publication Date: 2014-08-08
    Description: The current research has continued on the PF-1000 plasma focus device at the current of 2 MA by comparison of the shots with and without injected deuterium. The increase of the total neutron yield at the level of 10 10 –10 11 per shot was achieved after the compression of about 10  μ g/cm of the deuterium from the gas-valve by about 46  μ g/cm of the neon or deuterium plasma sheath. It increases five times at the decrease of the puffing deuterium mass to one-half. In shots with neon in the chamber and with puffing deuterium, a considerable decrease was confirmed of the soft X-ray emission in comparison with shots without deuterium injection. This decrease can be explained by the absence of the neon in the region of the compressed and hot plasma. The deuterium plasma from the gas-puff should then be confined in the internal structures both in the phase of implosion as well as during their formation and transformation. In shots with puffing deuterium, the evolution of instabilities in the plasma column was suppressed. The deuterium plasma has a higher conductance and better ability to form expressive and dense plasmoids and to transport the internal current in comparison with neon plasma. Neutrons were produced both at the initial phase of stagnation, as well as at a later time at the evolution of the constrictions and dense plasmoids.
    Print ISSN: 1070-664X
    Electronic ISSN: 1089-7674
    Topics: Physics
    Published by American Institute of Physics (AIP)
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  • 8
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    Structure of active beta-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide (2013)
    Nature Publishing Group (NPG)
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    Publication Date: 2013-04-23
    Description: The functions of G-protein-coupled receptors (GPCRs) are primarily mediated and modulated by three families of proteins: the heterotrimeric G proteins, the G-protein-coupled receptor kinases (GRKs) and the arrestins. G proteins mediate activation of second-messenger-generating enzymes and other effectors, GRKs phosphorylate activated receptors, and arrestins subsequently bind phosphorylated receptors and cause receptor desensitization. Arrestins activated by interaction with phosphorylated receptors can also mediate G-protein-independent signalling by serving as adaptors to link receptors to numerous signalling pathways. Despite their central role in regulation and signalling of GPCRs, a structural understanding of beta-arrestin activation and interaction with GPCRs is still lacking. Here we report the crystal structure of beta-arrestin-1 (also called arrestin-2) in complex with a fully phosphorylated 29-amino-acid carboxy-terminal peptide derived from the human V2 vasopressin receptor (V2Rpp). This peptide has previously been shown to functionally and conformationally activate beta-arrestin-1 (ref. 5). To capture this active conformation, we used a conformationally selective synthetic antibody fragment (Fab30) that recognizes the phosphopeptide-activated state of beta-arrestin-1. The structure of the beta-arrestin-1-V2Rpp-Fab30 complex shows marked conformational differences in beta-arrestin-1 compared to its inactive conformation. These include rotation of the amino- and carboxy-terminal domains relative to each other, and a major reorientation of the 'lariat loop' implicated in maintaining the inactive state of beta-arrestin-1. These results reveal, at high resolution, a receptor-interacting interface on beta-arrestin, and they indicate a potentially general molecular mechanism for activation of these multifunctional signalling and regulatory proteins.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3654799/" 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/PMC3654799/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shukla, Arun K -- Manglik, Aashish -- Kruse, Andrew C -- Xiao, Kunhong -- Reis, Rosana I -- Tseng, Wei-Chou -- Staus, Dean P -- Hilger, Daniel -- Uysal, Serdar -- Huang, Li-Yin -- Paduch, Marcin -- Tripathi-Shukla, Prachi -- Koide, Akiko -- Koide, Shohei -- Weis, William I -- Kossiakoff, Anthony A -- Kobilka, Brian K -- Lefkowitz, Robert J -- GM072688/GM/NIGMS NIH HHS/ -- GM087519/GM/NIGMS NIH HHS/ -- HL 075443/HL/NHLBI NIH HHS/ -- HL16037/HL/NHLBI NIH HHS/ -- HL70631/HL/NHLBI NIH HHS/ -- NS028471/NS/NINDS NIH HHS/ -- P41 RR011823/RR/NCRR NIH HHS/ -- R01 HL016037/HL/NHLBI NIH HHS/ -- R01 HL070631/HL/NHLBI NIH HHS/ -- R01 NS028471/NS/NINDS NIH HHS/ -- U01 GM094588/GM/NIGMS NIH HHS/ -- U54 GM074946/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2013 May 2;497(7447):137-41. doi: 10.1038/nature12120. Epub 2013 Apr 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23604254" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arrestins/*chemistry/immunology/*metabolism ; Crystallography, X-Ray ; Humans ; Immunoglobulin Fab Fragments/chemistry/immunology/metabolism ; Models, Molecular ; Phosphopeptides/*chemistry/*metabolism ; Phosphorylation ; Protein Binding ; Protein Conformation ; Protein Stability ; Rats ; Receptors, Vasopressin/*chemistry ; Rotation
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 9
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    Protein targeting. Structure of the Get3 targeting factor in complex with its membrane protein cargo (2015)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2015-03-07
    Description: Tail-anchored (TA) proteins are a physiologically important class of membrane proteins targeted to the endoplasmic reticulum by the conserved guided-entry of TA proteins (GET) pathway. During transit, their hydrophobic transmembrane domains (TMDs) are chaperoned by the cytosolic targeting factor Get3, but the molecular nature of the functional Get3-TA protein targeting complex remains unknown. We reconstituted the physiologic assembly pathway for a functional targeting complex and showed that it comprises a TA protein bound to a Get3 homodimer. Crystal structures of Get3 bound to different TA proteins showed an alpha-helical TMD occupying a hydrophobic groove that spans the Get3 homodimer. Our data elucidate the mechanism of TA protein recognition and shielding by Get3 and suggest general principles of hydrophobic domain chaperoning by cellular targeting factors.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4413028/" 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/PMC4413028/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mateja, Agnieszka -- Paduch, Marcin -- Chang, Hsin-Yang -- Szydlowska, Anna -- Kossiakoff, Anthony A -- Hegde, Ramanujan S -- Keenan, Robert J -- MC_UP_A022_1007/Medical Research Council/United Kingdom -- P41 GM103403/GM/NIGMS NIH HHS/ -- R01 GM086487/GM/NIGMS NIH HHS/ -- U01 GM094588/GM/NIGMS NIH HHS/ -- U54 GM087519/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2015 Mar 6;347(6226):1152-5. doi: 10.1126/science.1261671.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, The University of Chicago, 929 East 57th Street, Chicago, IL 60637, USA. ; MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK. rhegde@mrc-lmb.cam.ac.uk bkeenan@uchicago.edu. ; Department of Biochemistry and Molecular Biology, The University of Chicago, 929 East 57th Street, Chicago, IL 60637, USA. rhegde@mrc-lmb.cam.ac.uk bkeenan@uchicago.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25745174" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/*chemistry/metabolism ; Crystallography, X-Ray ; Cytosol/enzymology ; Guanine Nucleotide Exchange Factors/*chemistry/metabolism ; Hydrophobic and Hydrophilic Interactions ; Membrane Proteins/*chemistry/metabolism ; Molecular Chaperones/chemistry/metabolism ; Multiprotein Complexes/chemistry/metabolism ; Protein Multimerization ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Transport ; Saccharomyces cerevisiae Proteins/*chemistry/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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  • 10
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    Architecture of the fungal nuclear pore inner ring complex (2015)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2015-09-01
    Description: The nuclear pore complex (NPC) constitutes the sole gateway for bidirectional nucleocytoplasmic transport. We present the reconstitution and interdisciplinary analyses of the ~425-kilodalton inner ring complex (IRC), which forms the central transport channel and diffusion barrier of the NPC, revealing its interaction network and equimolar stoichiometry. The Nsp1*Nup49*Nup57 channel nucleoporin heterotrimer (CNT) attaches to the IRC solely through the adaptor nucleoporin Nic96. The CNT*Nic96 structure reveals that Nic96 functions as an assembly sensor that recognizes the three-dimensional architecture of the CNT, thereby mediating the incorporation of a defined CNT state into the NPC. We propose that the IRC adopts a relatively rigid scaffold that recruits the CNT to primarily form the diffusion barrier of the NPC, rather than enabling channel dilation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stuwe, Tobias -- Bley, Christopher J -- Thierbach, Karsten -- Petrovic, Stefan -- Schilbach, Sandra -- Mayo, Daniel J -- Perriches, Thibaud -- Rundlet, Emily J -- Jeon, Young E -- Collins, Leslie N -- Huber, Ferdinand M -- Lin, Daniel H -- Paduch, Marcin -- Koide, Akiko -- Lu, Vincent -- Fischer, Jessica -- Hurt, Ed -- Koide, Shohei -- Kossiakoff, Anthony A -- Hoelz, Andre -- ACB-12002/PHS HHS/ -- AGM-12006/PHS HHS/ -- P30-CA014599/CA/NCI NIH HHS/ -- R01-GM090324/GM/NIGMS NIH HHS/ -- R01-GM111461/GM/NIGMS NIH HHS/ -- U01-GM094588/GM/NIGMS NIH HHS/ -- U54-GM087519/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2015 Oct 2;350(6256):56-64. doi: 10.1126/science.aac9176. Epub 2015 Aug 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉California Institute of Technology, Division of Chemistry and Chemical Engineering, 1200 East California Boulevard, Pasadena, CA 91125, USA. ; Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA. ; Biochemistry Center of Heidelberg University, 69120 Heidelberg, Germany. ; California Institute of Technology, Division of Chemistry and Chemical Engineering, 1200 East California Boulevard, Pasadena, CA 91125, USA. hoelz@caltech.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26316600" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chaetomium/metabolism/*ultrastructure ; Fungal Proteins/chemistry/*ultrastructure ; Molecular Sequence Data ; Nuclear Pore/metabolism/*ultrastructure ; Nuclear Pore Complex Proteins/chemistry/*ultrastructure ; Nuclear Proteins/chemistry/*ultrastructure ; Protein Binding ; Protein Multimerization ; Protein Structure, Secondary ; Protein Structure, Tertiary
    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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