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  • 1
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    Architecture of RNA polymerase II and implications for the transcription mechanism (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-04-28
    Description: A backbone model of a 10-subunit yeast RNA polymerase II has been derived from x-ray diffraction data extending to 3 angstroms resolution. All 10 subunits exhibit a high degree of identity with the corresponding human proteins, and 9 of the 10 subunits are conserved among the three eukaryotic RNA polymerases I, II, and III. Notable features of the model include a pair of jaws, formed by subunits Rpb1, Rpb5, and Rpb9, that appear to grip DNA downstream of the active center. A clamp on the DNA nearer the active center, formed by Rpb1, Rpb2, and Rpb6, may be locked in the closed position by RNA, accounting for the great stability of transcribing complexes. A pore in the protein complex beneath the active center may allow entry of substrates for polymerization and exit of the transcript during proofreading and passage through pause sites in the DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cramer, P -- Bushnell, D A -- Fu, J -- Gnatt, A L -- Maier-Davis, B -- Thompson, N E -- Burgess, R R -- Edwards, A M -- David, P R -- Kornberg, R D -- GM49985/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Apr 28;288(5466):640-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305-5126, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10784442" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Binding Sites ; Catalytic Domain ; Crystallization ; Crystallography, X-Ray ; DNA, Fungal/chemistry/metabolism ; Enzyme Stability ; Escherichia coli/enzymology ; Humans ; *Models, Molecular ; Protein Binding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; RNA Polymerase II/*chemistry/genetics/metabolism ; RNA, Fungal/chemistry/metabolism ; RNA, Messenger/chemistry/metabolism ; Thermus/enzymology ; Transcription Factors/chemistry/metabolism ; *Transcription Factors, General ; *Transcription, Genetic ; *Transcriptional Elongation Factors
    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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  • 2
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    The structural basis of ZMPSTE24-dependent laminopathies (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-03-30
    Description: Mutations in the nuclear membrane zinc metalloprotease ZMPSTE24 lead to diseases of lamin processing (laminopathies), such as the premature aging disease progeria and metabolic disorders. ZMPSTE24 processes prelamin A, a component of the nuclear lamina intermediate filaments, by cleaving it at two sites. Failure of this processing results in accumulation of farnesylated, membrane-associated prelamin A. The 3.4 angstrom crystal structure of human ZMPSTE24 has a seven transmembrane alpha-helical barrel structure, surrounding a large, water-filled, intramembrane chamber, capped by a zinc metalloprotease domain with the catalytic site facing into the chamber. The 3.8 angstrom structure of a complex with a CSIM tetrapeptide showed that the mode of binding of the substrate resembles that of an insect metalloprotease inhibitor in thermolysin. Laminopathy-associated mutations predicted to reduce ZMPSTE24 activity map to the zinc metalloprotease peptide-binding site and to the bottom of the chamber.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Quigley, Andrew -- Dong, Yin Yao -- Pike, Ashley C W -- Dong, Liang -- Shrestha, Leela -- Berridge, Georgina -- Stansfeld, Phillip J -- Sansom, Mark S P -- Edwards, Aled M -- Bountra, Chas -- von Delft, Frank -- Bullock, Alex N -- Burgess-Brown, Nicola A -- Carpenter, Elisabeth P -- 092809/Wellcome Trust/United Kingdom -- Canadian Institutes of Health Research/Canada -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2013 Mar 29;339(6127):1604-7. doi: 10.1126/science.1231513.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Structural Genomics Consortium, University of Oxford, Oxford, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23539603" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Catalytic Domain ; Crystallography, X-Ray ; Humans ; Lamin Type A ; Membrane Proteins/*chemistry/genetics ; Metabolism, Inborn Errors/genetics/*metabolism ; Metalloendopeptidases/*chemistry/genetics ; Molecular Sequence Data ; Nuclear Proteins/chemistry/genetics/*metabolism ; Progeria/genetics/metabolism ; Protein Conformation ; Protein Precursors/chemistry/genetics/*metabolism ; Substrate Specificity ; Thermolysin/chemistry
    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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  • 3
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    Too many roads not taken (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-02-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Edwards, Aled M -- Isserlin, Ruth -- Bader, Gary D -- Frye, Stephen V -- Willson, Timothy M -- Yu, Frank H -- England -- Nature. 2011 Feb 10;470(7333):163-5. doi: 10.1038/470163a.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Toronto, Toronto, Ontario M5G 1L7, Canada. aled.edwards@utoronto.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21307913" target="_blank"〉PubMed〈/a〉
    Keywords: *Bibliometrics ; Biomedical Research/*instrumentation/methods/*statistics & numerical data/trends ; Human Genome Project ; Humans ; Ion Channels ; Protein Kinases ; Receptors, Cytoplasmic and Nuclear
    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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  • 4
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    Publishing: Halt self-citation in impact measures (2014)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2014-01-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cameron, Elissa Z -- Edwards, Amy M -- White, Angela M -- England -- Nature. 2014 Jan 9;505(7482):160. doi: 10.1038/505160b.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Tasmania, Hobart, Australia. ; US Department of Agriculture Forest Service, Davis, California, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24402270" target="_blank"〉PubMed〈/a〉
    Keywords: Female ; Humans ; *Internationality ; Male ; Research Personnel/*statistics & numerical data ; Sexism/*statistics & numerical data
    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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  • 5
    Electronic Resource
    Electronic Resource
    Structural investigation of the initial interface region formed by thin titanium films on silicon (111) (1996)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 80 (1996), S. 183-187 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: A structural study of the initial interface region formed by titanium on silicon (111) was undertaken. Thin films (100 A(ring)) of titanium were deposited in ultrahigh vacuum (UHV) conditions onto atomically clean silicon(111) wafers and annealed in situ at 25 °C intervals between 300 and 475 °C. Structural characterization of the evolving interface was performed primarily via extended x-ray absorption fine structure (EXAFS) measurements. Results indicate that a major structural rearrangement takes place between 400 and 425 °C. EXAFS fitting analysis reveals this transition to be from a disordered TiSi-like phase to a more ordered C49-like disilicide state. The results are compared with those previously reported for the zirconium:silicon system. © 1996 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.362803
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  • 6
    Electronic Resource
    Electronic Resource
    Structural and electrical properties of (Ti0.9Zr0.1)Si2 thin films on Si(111) (1994)
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 65 (1994), S. 2413-2415 
    Details
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: Alloy films of Ti and up to 20% Zr were prepared by codeposition onto Si(111) surfaces in ultrahigh vacuum. After in situ thermal annealing at temperatures of ∼600 °C, the films form the C49 phase and are stable in this phase up to at least 910 °C. In contrast, Ti films on Si(111) initially react to form the C49 phase and transform to the C54 phase at ∼700 °C. The surfaces of the (Ti0.9Zr0.1)Si2 alloy films are studied by atomic force microscopy and are shown to be smoother than the surfaces of TiSi2 films on Si substrates. In addition the tendency to island formation is also not observed for annealing temperatures less than 910 °C. The sheet resistivity of the (Ti0.9Zr0.1)Si2 alloy films is found to be ∼46 μΩ cm for annealing temperatures from 600 to 910 °C. © 1994 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.112692
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  • 7
    Electronic Resource
    Electronic Resource
    Silicon depletions in some Norfolk rivers (1974)
    Oxford, UK : Blackwell Publishing Ltd
    Freshwater biology 4 (1974), S. 0 
    Details
    ISSN: 1365-2427
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Water samples collected weekly from the rivers Yare, Tud, Wensum and Tas in Norfolk, England, displayed marked depletions in the spring and summer of the concentration of dissolved silicon. These were unconnected with any hydrological event and were assumed to be due to the assimilation of silicon by diatoms. Equilibrium concentrations were maintained in the Yare and Tud during the weeks prior to and following the spring bloom. It was estimated that 35 Mg (51%) of the predicted load were removed from the Yare during the 11 weeks of this depletion and 6-0 Mg (45%) from the Tud. The lowest observed concentration (0-4 mg/l) occurred during the first week in May when over 90% of the silicon had been removed. However, the maximum amount of removal and hence maximum diatom productivity occurred earlier at a time of higher water discharge. A similar pattern was observed in the Yare during the spring of 1971. Two small blooms occurred later in the summer of 1970 in the Yare and Tud. It was estimated that 15% ofthe Yare's dissolved silicon load of 263 Mg was in the assimilated form and 12-5%of the Tud's output of 56-6 Mg. The weathering of silicate minerals was probably the source of almost all the silicon and the outputs represented a silicon erosion rate of 1-15 Mg/km2/year for the Yare and 0-77 Mg/kmVyear for the Tud.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2427.1974.tb00096.x
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  • 8
    Electronic Resource
    Electronic Resource
    Structural investigation of the initial interface region formed by thin zirconium films on silicon (111) (1994)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 76 (1994), S. 4630-4635 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: A structural study of the initial interface region formed by zirconium on silicon (111) was undertaken. Thin films (100 A(ring)) of zirconium were deposited in ultrahigh-vacuum conditions onto atomically, clean silicon (111) wafers and annealed in situ at 25 °C intervals between 300 and 425 °C, over which range Auger spectroscopy indicated silicon diffusion to the surface. Structural characterization of the evolving interface was performed primarily via extended x-ray-absorption fine-structure (EXAFS) measurements. Results indicate that a major structural rearrangement takes place between 350 and 375 °C. EXAFS fitting analysis reveals this transition to be from a disordered-intermixed phase to a more ordered state having interatomic distances closely resembling those of ZrSi, but lower coordination numbers. Ordering continues with progressively higher annealing temperatures until the interface region assumes the ZrSi structure at ∼425 °C. The results are discussed in terms of the free energy and strain of the interface film.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.357299
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  • 9
    Electronic Resource
    Electronic Resource
    Water and Wastewater Minimization: the Aire and Calder Project (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Water and environment journal 10 (1996), S. 0 
    Details
    ISSN: 1747-6593
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Energy, Environment Protection, Nuclear Power Engineering
    Notes: The reduction of the waste of raw materials at source using clean technologies, recycling, and good housekeeping has considerable benefits for both the environment and industry. A demonstration project on wastewater minimization was completed in 1995 in the Aire and Calder catchments of West Yorkshire. The findings indicated cost savings for eleven firms of over $3 million/annum and further opportunities which, when implemented, could realize another $1 million/annum. The reduction in the amount of wastewater discharged either to sewer or river was 27%, with a potential to increase to over 40%. The payback period for 63% of the waste minimization opportunities is less than one year and many involve only a small initial investment. Waste minimization when widely adopted has prospects for cutting industry's costs, reducing demand for water and reducing the volume of effluent produced.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1747-6593.1996.tb00040.x
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  • 10
    Electronic Resource
    Electronic Resource
    Polarized XAS on vectorially oriented single monolayers of cytochrome c (1999)
    Chester : International Union of Crystallography (IUCr)
    Journal of synchrotron radiation 6 (1999), S. 411-413 
    Details
    ISSN: 1600-5775
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0909049598016847
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