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  • 1
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    Publisher Correction: Migrasome formation is mediated by assembly of micron-scale tetraspanin macrodomains (2019)
    Springer Nature
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    Publication Date: 2019
    Print ISSN: 1465-7392
    Electronic ISSN: 1476-4679
    Topics: Biology , Medicine
    Published by Springer Nature
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  • 2
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    Migrasome formation is mediated by assembly of micron-scale tetraspanin macrodomains (2019)
    Springer Nature
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    Publication Date: 2019
    Print ISSN: 1465-7392
    Electronic ISSN: 1476-4679
    Topics: Biology , Medicine
    Published by Springer Nature
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  • 3
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    Convergence of shock waves generated by underwater electrical explosion of cylindrical wire arrays between different boundary geometries (2015)
    American Institute of Physics (AIP)
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    Publication Date: 2015-10-21
    Description: The results of experiments and numerical simulations of a shock wave propagating between either conical or parabolic bounding walls are presented. The shock wave was generated by a microsecond timescale underwater electrical explosion of a cylindrical wire array supplied by a current pulse having an amplitude of ∼230 kA and a rise time of ∼1  μ s. It is shown that with the same energy density deposition into the exploding wire array, the shock wave converges faster between parabolic walls, and as a result, the pressure in the vicinity of convergence is ∼2.3 times higher than in the case of conical walls. The results obtained are compared to those of earlier experiments [Antonov et al ., Appl. Phys. Lett. 102 , 124104 (2013)] with explosions of spherical wire arrays. It is shown that at a distance of ∼400  μ m from the implosion origin the pressure obtained in the current experiments is higher than for the case of spherical wire arrays.
    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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    Counting electrons on supported nanoparticles (2016)
    Springer Nature
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    Publication Date: 2016-02-25
    Description: Nature Materials 15, 284 (2016). doi:10.1038/nmat4500 Authors: Yaroslava Lykhach, Sergey M. Kozlov, Tomáš Skála, Andrii Tovt, Vitalii Stetsovych, Nataliya Tsud, Filip Dvořák, Viktor Johánek, Armin Neitzel, Josef Mysliveček, Stefano Fabris, Vladimír Matolín, Konstantin M. Neyman & Jörg Libuda Electronic interactions between metal nanoparticles and oxide supports control the functionality of nanomaterials, for example, the stability, the activity and the selectivity of catalysts. Such interactions involve electron transfer across the metal/support interface. In this work we quantify this charge transfer on a well-defined platinum/ceria catalyst at particle sizes relevant for heterogeneous catalysis. Combining synchrotron-radiation photoelectron spectroscopy, scanning tunnelling microscopy and density functional calculations we show that the charge transfer per Pt atom is largest for Pt particles of around 50 atoms. Here, approximately one electron is transferred per ten Pt atoms from the nanoparticle to the support. For larger particles, the charge transfer reaches its intrinsic limit set by the support. For smaller particles, charge transfer is partially suppressed by nucleation at defects. These mechanistic and quantitative insights into charge transfer will help to make better use of particle size effects and electronic metal–support interactions in metal/oxide nanomaterials.
    Print ISSN: 1476-1122
    Electronic ISSN: 1476-4660
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Natural Sciences in General , Physics
    Published by Springer Nature
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  • 5
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    Spatial organization of transcription elongation complex in Escherichia coli (1998)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1998-07-17
    Description: During RNA synthesis in the ternary elongation complex, RNA polymerase enzyme holds nucleic acids in three contiguous sites: the double-stranded DNA-binding site (DBS) ahead of the transcription bubble, the RNA-DNA heteroduplex-binding site (HBS), and the RNA-binding site (RBS) upstream of HBS. Photochemical cross-linking allowed mapping of the DNA and RNA contacts to specific positions on the amino acid sequence. Unexpectedly, the same protein regions were found to participate in both DBS and RBS. Thus, DNA entry and RNA exit occur close together in the RNA polymerase molecule, suggesting that the three sites constitute a single unit. The results explain how RNA in the integrated unit RBS-HBS-DBS may stabilize the ternary complex, whereas a hairpin in RNA result in its dissociation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nudler, E -- Gusarov, I -- Avetissova, E -- Kozlov, M -- Goldfarb, A -- GM49242/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jul 17;281(5375):424-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, New York University Medical Center, New York, NY 10016, USA. evgeny.nudler@med.nyu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9665887" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; DNA, Bacterial/chemistry/*metabolism ; DNA-Directed RNA Polymerases/chemistry/*metabolism ; Escherichia coli/*genetics/metabolism ; Idoxuridine/metabolism ; Models, Genetic ; Nucleic Acid Conformation ; Nucleic Acid Heteroduplexes/*metabolism ; Protein Binding ; RNA, Bacterial/chemistry/*metabolism ; Templates, Genetic ; *Transcription, Genetic ; Ultraviolet Rays
    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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  • 6
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    A structural model of transcription elongation (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-08-01
    Description: The path of the nucleic acids through a transcription elongation complex was tracked by mapping cross-links between bacterial RNA polymerase (RNAP) and transcript RNA or template DNA onto the x-ray crystal structure. In the resulting model, the downstream duplex DNA is nestled in a trough formed by the beta' subunit and enclosed on top by the beta subunit. In the RNAP channel, the RNA/DNA hybrid extends from the enzyme active site, along a region of the beta subunit harboring rifampicin resistance mutations, to the beta' subunit "rudder." The single-stranded RNA is then extruded through another channel formed by the beta-subunit flap domain. The model provides insight into the functional properties of the transcription complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Korzheva, N -- Mustaev, A -- Kozlov, M -- Malhotra, A -- Nikiforov, V -- Goldfarb, A -- Darst, S A -- GM30717/GM/NIGMS NIH HHS/ -- GM49242/GM/NIGMS NIH HHS/ -- GM53759/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Jul 28;289(5479):619-25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Public Health Research Institute, 455 First Avenue, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10915625" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cross-Linking Reagents ; Crystallography, X-Ray ; DNA/chemistry/genetics/*metabolism ; DNA Primers ; DNA-Directed RNA Polymerases/*chemistry/genetics/metabolism ; Models, Molecular ; Mutation ; Nucleic Acid Conformation ; Nucleic Acid Hybridization ; Oligodeoxyribonucleotides/chemistry/metabolism ; Oligoribonucleotides/chemistry/metabolism ; Protein Conformation ; Protein Structure, Tertiary ; RNA, Messenger/chemistry/genetics/*metabolism ; Templates, Genetic ; Thermus/enzymology ; *Transcription, Genetic
    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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  • 7
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    Biophysics: Joint effort bends membrane (2010)
    Nature Publishing Group (NPG)
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    Publication Date: 2010-01-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kozlov, Michael M -- England -- Nature. 2010 Jan 28;463(7280):439-40. doi: 10.1038/463439a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20110984" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Membrane/chemistry/*physiology ; Lipid Bilayers/*chemistry ; Lipids/chemistry ; Membrane Proteins/chemistry/metabolism ; Models, Chemical
    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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  • 8
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    Mapping of catalytic residues in the RNA polymerase active center (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-07-05
    Description: When the Mg2+ ion in the catalytic center of Escherichia coli RNA polymerase (RNAP) is replaced with Fe2+, hydroxyl radicals are generated. In the promoter complex, such radicals cleave template DNA near the transcription start site, whereas the beta' subunit is cleaved at a conserved motif NADFDGD (Asn-Ala-Asp-Phe-Asp-Gly-Asp). Substitution of the three aspartate residues with alanine creates a dominant lethal mutation. The mutant RNAP is catalytically inactive but can bind promoters and form an open complex. The mutant fails to support Fe2+-induced cleavage of DNA or protein. Thus, the NAD-FDGD motif is involved in chelation of the active center Mg2+.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zaychikov, E -- Martin, E -- Denissova, L -- Kozlov, M -- Markovtsov, V -- Kashlev, M -- Heumann, H -- Nikiforov, V -- Goldfarb, A -- Mustaev, A -- New York, N.Y. -- Science. 1996 Jul 5;273(5271):107-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Limnological Institute, Russian Academy of Sciences, Irkutsk, Russia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658176" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aspartic Acid/metabolism ; Binding Sites ; DNA/metabolism ; DNA-Directed RNA Polymerases/*chemistry/genetics/*metabolism ; Dithiothreitol/pharmacology ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli/*enzymology ; Ferrous Compounds/metabolism ; Hydroxyl Radical ; Magnesium/metabolism ; Molecular Sequence Data ; Mutagenesis ; Promoter Regions, Genetic
    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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  • 9
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    How synaptotagmin promotes membrane fusion (2007)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2007-05-05
    Description: Synaptic vesicles loaded with neurotransmitters are exocytosed in a soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE)-dependent manner after presynaptic depolarization induces calcium ion (Ca2+) influx. The Ca2+ sensor required for fast fusion is synaptotagmin-1. The activation energy of bilayer-bilayer fusion is very high (approximately 40 k(B)T). We found that, in response to Ca2+ binding, synaptotagmin-1 could promote SNARE-mediated fusion by lowering this activation barrier by inducing high positive curvature in target membranes on C2-domain membrane insertion. Thus, synaptotagmin-1 triggers the fusion of docked vesicles by local Ca2+-dependent buckling of the plasma membrane together with the zippering of SNAREs. This mechanism may be widely used in membrane fusion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martens, Sascha -- Kozlov, Michael M -- McMahon, Harvey T -- MC_U105178795/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2007 May 25;316(5828):1205-8. Epub 2007 May 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council-Laboratory of Molecular Biology, Hills Road, CB2 0QH Cambridge, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17478680" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*physiology ; Cell Membrane/*physiology/ultrastructure ; Exocytosis/physiology ; Humans ; Liposomes ; Membrane Fusion ; Models, Biological ; Rats ; SNARE Proteins/*physiology ; Synaptic Vesicles/*physiology/ultrastructure ; Synaptotagmin I/*physiology
    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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    Membrane proteins of the endoplasmic reticulum induce high-curvature tubules (2008)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2008-03-01
    Description: The tubular structure of the endoplasmic reticulum (ER) appears to be generated by integral membrane proteins, the reticulons and a protein family consisting of DP1 in mammals and Yop1p in yeast. Here, individual members of these families were found to be sufficient to generate membrane tubules. When we purified yeast Yop1p and incorporated it into proteoliposomes, narrow tubules (approximately 15 to 17 nanometers in diameter) were generated. Tubule formation occurred with different lipids; required essentially only the central portion of the protein, including its two long hydrophobic segments; and was prevented by mutations that affected tubule formation in vivo. Tubules were also formed by reconstituted purified yeast Rtn1p. Tubules made in vitro were narrower than normal ER tubules, due to a higher concentration of tubule-inducing proteins. The shape and oligomerization of the "morphogenic" proteins could explain the formation of the tubular ER.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hu, Junjie -- Shibata, Yoko -- Voss, Christiane -- Shemesh, Tom -- Li, Zongli -- Coughlin, Margaret -- Kozlov, Michael M -- Rapoport, Tom A -- Prinz, William A -- Howard Hughes Medical Institute/ -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2008 Feb 29;319(5867):1247-50. doi: 10.1126/science.1153634.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18309084" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biopolymers/chemistry/metabolism ; COS Cells ; Cercopithecus aethiops ; Endoplasmic Reticulum/*chemistry/metabolism/*ultrastructure ; Hydrophobic and Hydrophilic Interactions ; Intracellular Membranes/chemistry/ultrastructure ; Lipid Bilayers ; Membrane Lipids/chemistry ; Membrane Proteins/*chemistry/*metabolism ; Membrane Transport Proteins/*chemistry/*metabolism ; Microscopy, Electron ; Models, Biological ; Molecular Sequence Data ; Mutant Proteins/chemistry/metabolism ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Proteolipids/chemistry ; Saccharomyces cerevisiae Proteins/*chemistry/genetics/*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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