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  • American Institute of Physics (AIP)  (8)
  • Nature Publishing Group (NPG)  (7)
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  • 1
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    A new method to induce molecular low bias negative differential resistance with multi-peaks (2016)
    American Institute of Physics (AIP)
    Details
    Publication Date: 2016-02-10
    Description: According to a first-principles study of the transport properties of two thiolated anthracene-9,10-diono molecules sandwiching ethyl, a new method to induce molecular low bias negative differential resistance with multi-peaks for strong n - or p -type molecules is proposed. The anthracene-9,10-diono molecule shows strong n -type characteristics when in contact with Au and Ag electrodes via a thiolate. The multiple negative differential resistance effect originated from the molecule–electrode couple is different between Ag and Au electrodes. Our investigations may promise potential for applications in molecular devices with low power dissipation and multifunction in the future.
    Print ISSN: 0021-9606
    Electronic ISSN: 1089-7690
    Topics: Chemistry and Pharmacology , Physics
    Published by American Institute of Physics (AIP)
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  • 2
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    Chemical mapping of a single molecule by plasmon-enhanced Raman scattering (2013)
    Nature Publishing Group (NPG)
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    Publication Date: 2013-06-07
    Description: Visualizing individual molecules with chemical recognition is a longstanding target in catalysis, molecular nanotechnology and biotechnology. Molecular vibrations provide a valuable 'fingerprint' for such identification. Vibrational spectroscopy based on tip-enhanced Raman scattering allows us to access the spectral signals of molecular species very efficiently via the strong localized plasmonic fields produced at the tip apex. However, the best spatial resolution of the tip-enhanced Raman scattering imaging is still limited to 3-15 nanometres, which is not adequate for resolving a single molecule chemically. Here we demonstrate Raman spectral imaging with spatial resolution below one nanometre, resolving the inner structure and surface configuration of a single molecule. This is achieved by spectrally matching the resonance of the nanocavity plasmon to the molecular vibronic transitions, particularly the downward transition responsible for the emission of Raman photons. This matching is made possible by the extremely precise tuning capability provided by scanning tunnelling microscopy. Experimental evidence suggests that the highly confined and broadband nature of the nanocavity plasmon field in the tunnelling gap is essential for ultrahigh-resolution imaging through the generation of an efficient double-resonance enhancement for both Raman excitation and Raman emission. Our technique not only allows for chemical imaging at the single-molecule level, but also offers a new way to study the optical processes and photochemistry of a single molecule.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, R -- Zhang, Y -- Dong, Z C -- Jiang, S -- Zhang, C -- Chen, L G -- Zhang, L -- Liao, Y -- Aizpurua, J -- Luo, Y -- Yang, J L -- Hou, J G -- England -- Nature. 2013 Jun 6;498(7452):82-6. doi: 10.1038/nature12151.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hefei National Laboratory for Physical Sciences at the Microscale, University of Science and Technology of China, Hefei, Anhui 230026, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23739426" target="_blank"〉PubMed〈/a〉
    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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  • 3
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    Structural basis for outer membrane lipopolysaccharide insertion (2014)
    Nature Publishing Group (NPG)
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    Publication Date: 2014-07-06
    Description: Lipopolysaccharide (LPS) is essential for most Gram-negative bacteria and has crucial roles in protection of the bacteria from harsh environments and toxic compounds, including antibiotics. Seven LPS transport proteins (that is, LptA-LptG) form a trans-envelope protein complex responsible for the transport of LPS from the inner membrane to the outer membrane, the mechanism for which is poorly understood. Here we report the first crystal structure of the unique integral membrane LPS translocon LptD-LptE complex. LptD forms a novel 26-stranded beta-barrel, which is to our knowledge the largest beta-barrel reported so far. LptE adopts a roll-like structure located inside the barrel of LptD to form an unprecedented two-protein 'barrel and plug' architecture. The structure, molecular dynamics simulations and functional assays suggest that the hydrophilic O-antigen and the core oligosaccharide of the LPS may pass through the barrel and the lipid A of the LPS may be inserted into the outer leaflet of the outer membrane through a lateral opening between strands beta1 and beta26 of LptD. These findings not only help us to understand important aspects of bacterial outer membrane biogenesis, but also have significant potential for the development of novel drugs against multi-drug resistant pathogenic bacteria.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dong, Haohao -- Xiang, Quanju -- Gu, Yinghong -- Wang, Zhongshan -- Paterson, Neil G -- Stansfeld, Phillip J -- He, Chuan -- Zhang, Yizheng -- Wang, Wenjian -- Dong, Changjiang -- 083501/Z/07/Z/Wellcome Trust/United Kingdom -- England -- Nature. 2014 Jul 3;511(7507):52-6. doi: 10.1038/nature13464. Epub 2014 Jun 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Biomedical Research Centre, Norwich Medical School, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK [2] Biomedical Sciences Research Complex, School of Chemistry, University of St Andrews, North Haugh, St Andrews KY16 9ST, UK. ; 1] Biomedical Sciences Research Complex, School of Chemistry, University of St Andrews, North Haugh, St Andrews KY16 9ST, UK [2] Department of Microbiology, College of Resource and Environment Science, Sichuan Agriculture University, Yaan 625000, China. ; Biomedical Research Centre, Norwich Medical School, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK. ; 1] Biomedical Research Centre, Norwich Medical School, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK [2] Biomedical Sciences Research Complex, School of Chemistry, University of St Andrews, North Haugh, St Andrews KY16 9ST, UK [3] College of Life Sciences, Sichuan University, Chengdu 610065, China. ; Diamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, UK. ; Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. ; 1] Biomedical Sciences Research Complex, School of Chemistry, University of St Andrews, North Haugh, St Andrews KY16 9ST, UK [2] School of Electronics and Information, Wuhan Technical College of Communications, No.6 Huangjiahu West Road, Hongshan District, Wuhan, Hubei 430065, China. ; College of Life Sciences, Sichuan University, Chengdu 610065, China. ; Laboratory of Department of Surgery, the First Affiliated Hospital, Sun Yat-sen University, 58 Zhongshan Road II, Guangzhou, Guangdong 510080, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24990744" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Outer Membrane Proteins/*chemistry/*metabolism ; Cell Membrane/chemistry/metabolism ; Cell Wall/chemistry/metabolism ; Crystallography, X-Ray ; Lipopolysaccharides/chemistry/*metabolism ; Models, Molecular ; Multiprotein Complexes/*chemistry/*metabolism ; Protein Binding ; Protein Structure, Secondary ; Salmonella typhimurium/*chemistry/cytology ; Structure-Activity Relationship
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 4
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    Transcription factor achaete-scute homologue 2 initiates follicular T-helper-cell development (2014)
    Nature Publishing Group (NPG)
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    Publication Date: 2014-01-28
    Description: In immune responses, activated T cells migrate to B-cell follicles and develop into follicular T-helper (TFH) cells, a recently identified subset of CD4(+) T cells specialized in providing help to B lymphocytes in the induction of germinal centres. Although Bcl6 has been shown to be essential in TFH-cell function, it may not regulate the initial migration of T cells or the induction of the TFH program, as exemplified by C-X-C chemokine receptor type 5 (CXCR5) upregulation. Here we show that expression of achaete-scute homologue 2 (Ascl2)--a basic helix-loop-helix (bHLH) transcription factor--is selectively upregulated in TFH cells. Ectopic expression of Ascl2 upregulates CXCR5 but not Bcl6, and downregulates C-C chemokine receptor 7 (CCR7) expression in T cells in vitro, as well as accelerating T-cell migration to the follicles and TFH-cell development in vivo in mice. Genome-wide analysis indicates that Ascl2 directly regulates TFH-related genes whereas it inhibits expression of T-helper cell 1 (TH1) and TH17 signature genes. Acute deletion of Ascl2, as well as blockade of its function with the Id3 protein in CD4(+) T cells, results in impaired TFH-cell development and germinal centre response. Conversely, mutation of Id3, known to cause antibody-mediated autoimmunity, greatly enhances TFH-cell generation. Thus, Ascl2 directly initiates TFH-cell development.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4012617/" 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/PMC4012617/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Xindong -- Chen, Xin -- Zhong, Bo -- Wang, Aibo -- Wang, Xiaohu -- Chu, Fuliang -- Nurieva, Roza I -- Yan, Xiaowei -- Chen, Ping -- van der Flier, Laurens G -- Nakatsukasa, Hiroko -- Neelapu, Sattva S -- Chen, Wanjun -- Clevers, Hans -- Tian, Qiang -- Qi, Hai -- Wei, Lai -- Dong, Chen -- AI106654/AI/NIAID NIH HHS/ -- P30 CA016672/CA/NCI NIH HHS/ -- R01 AI106654/AI/NIAID NIH HHS/ -- R01 AR050772/AR/NIAMS NIH HHS/ -- RC2 AR059010/AR/NIAMS NIH HHS/ -- Intramural NIH HHS/ -- England -- Nature. 2014 Mar 27;507(7493):513-8. doi: 10.1038/nature12910. Epub 2014 Jan 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Tsinghua University School of Medicine, Beijing 100084, China [2] Department of Immunology, MD Anderson Cancer Center, Houston, Texas 77054, USA. ; Tsinghua University School of Medicine, Beijing 100084, China. ; 1] Department of Immunology, MD Anderson Cancer Center, Houston, Texas 77054, USA [2] College of Life Sciences, Wuhan University, Wuhan 430072, China (B.Z.); SomantiX B.V., Padualaan 8, 3584 CH Utrecht, the Netherlands (L.G.v.d.F.). ; Department of Lymphoma and Myeloma, MD Anderson Cancer Center, Houston, Texas 77054, USA. ; Department of Immunology, MD Anderson Cancer Center, Houston, Texas 77054, USA. ; Institute for Systems Biology, Seattle, Washington 98103, USA. ; Laboratory of Immunology, National Eye Institute, NIH, Bethesda, Maryland 20892-1858, USA. ; 1] Hubrecht Institute-KNAW and University Medical Center Utrecht, Uppsalalaan 8, 3584 CT Utrecht, the Netherlands [2] College of Life Sciences, Wuhan University, Wuhan 430072, China (B.Z.); SomantiX B.V., Padualaan 8, 3584 CH Utrecht, the Netherlands (L.G.v.d.F.). ; National Institute of Dental and Craniofacial Research, NIH, Bethesda, Maryland 20892-2190, USA. ; Hubrecht Institute-KNAW and University Medical Center Utrecht, Uppsalalaan 8, 3584 CT Utrecht, the Netherlands. ; State Key Laboratory of Ophthalmology, Sun Yat-sen University, Guangzhou 510275, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24463518" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Basic Helix-Loop-Helix Transcription Factors/antagonists & ; inhibitors/deficiency/genetics/*metabolism ; *Cell Differentiation/genetics ; Cell Movement ; DNA-Binding Proteins/metabolism ; Down-Regulation ; Germinal Center/*cytology/immunology ; Humans ; Inhibitor of Differentiation Proteins/genetics/metabolism ; Mice ; Mutation/genetics ; Receptors, CCR7/metabolism ; Receptors, CXCR5/metabolism ; T-Lymphocytes, Helper-Inducer/*cytology/immunology/*metabolism ; Th17 Cells/cytology/immunology/metabolism ; Transcription, Genetic/genetics ; Up-Regulation
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 5
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    Cap binding and immune evasion revealed by Lassa nucleoprotein structure (2010)
    Nature Publishing Group (NPG)
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    Publication Date: 2010-11-19
    Description: Lassa virus, the causative agent of Lassa fever, causes thousands of deaths annually and is a biological threat agent, for which there is no vaccine and limited therapy. The nucleoprotein (NP) of Lassa virus has essential roles in viral RNA synthesis and immune suppression, the molecular mechanisms of which are poorly understood. Here we report the crystal structure of Lassa virus NP at 1.80 A resolution, which reveals amino (N)- and carboxy (C)-terminal domains with structures unlike any of the reported viral NPs. The N domain folds into a novel structure with a deep cavity for binding the m7GpppN cap structure that is required for viral RNA transcription, whereas the C domain contains 3'-5' exoribonuclease activity involved in suppressing interferon induction. To our knowledge this is the first X-ray crystal structure solved for an arenaviral NP, which reveals its unexpected functions and indicates unique mechanisms in cap binding and immune evasion. These findings provide great potential for vaccine and drug development.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3057469/" 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/PMC3057469/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Qi, Xiaoxuan -- Lan, Shuiyun -- Wang, Wenjian -- Schelde, Lisa McLay -- Dong, Haohao -- Wallat, Gregor D -- Ly, Hinh -- Liang, Yuying -- Dong, Changjiang -- 083501/Z/07/Z/Wellcome Trust/United Kingdom -- 5-U19-AI057266-07/AI/NIAID NIH HHS/ -- 5-U54-AI-057157-06/AI/NIAID NIH HHS/ -- AI067704/AI/NIAID NIH HHS/ -- DK64399/DK/NIDDK NIH HHS/ -- R01 AI083409/AI/NIAID NIH HHS/ -- R01 AI083409-01A1/AI/NIAID NIH HHS/ -- R01 AI083409-02/AI/NIAID NIH HHS/ -- R01 AI093580/AI/NIAID NIH HHS/ -- R01AI083409/AI/NIAID NIH HHS/ -- England -- Nature. 2010 Dec 9;468(7325):779-83. doi: 10.1038/nature09605. Epub 2010 Nov 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biomedical Sciences Research Complex, School of Chemistry, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21085117" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography, X-Ray ; Exoribonucleases/chemistry/genetics/metabolism ; Immune Evasion/*immunology ; Interferons/biosynthesis/immunology ; Lassa virus/*chemistry/genetics/*immunology ; Models, Molecular ; Nucleoproteins/*chemistry/genetics/immunology/*metabolism ; Protein Structure, Tertiary ; RNA Cap Analogs/chemistry/metabolism ; RNA Caps/chemistry/*metabolism ; RNA, Viral/biosynthesis/genetics/metabolism ; RNA-Binding Proteins/chemistry/genetics/metabolism ; Transcription, Genetic ; Viral Proteins/*chemistry/genetics/immunology/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 6
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    Structural basis of outer membrane protein insertion by the BAM complex (2016)
    Nature Publishing Group (NPG)
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    Publication Date: 2016-02-24
    Description: All Gram-negative bacteria, mitochondria and chloroplasts have outer membrane proteins (OMPs) that perform many fundamental biological processes. The OMPs in Gram-negative bacteria are inserted and folded into the outer membrane by the beta-barrel assembly machinery (BAM). The mechanism involved is poorly understood, owing to the absence of a structure of the entire BAM complex. Here we report two crystal structures of the Escherichia coli BAM complex in two distinct states: an inward-open state and a lateral-open state. Our structures reveal that the five polypeptide transport-associated domains of BamA form a ring architecture with four associated lipoproteins, BamB-BamE, in the periplasm. Our structural, functional studies and molecular dynamics simulations indicate that these subunits rotate with respect to the integral membrane beta-barrel of BamA to induce movement of the beta-strands of the barrel and promote insertion of the nascent OMP.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gu, Yinghong -- Li, Huanyu -- Dong, Haohao -- Zeng, Yi -- Zhang, Zhengyu -- Paterson, Neil G -- Stansfeld, Phillip J -- Wang, Zhongshan -- Zhang, Yizheng -- Wang, Wenjian -- Dong, Changjiang -- G1100110/1/Medical Research Council/United Kingdom -- WT106121MA/Wellcome Trust/United Kingdom -- England -- Nature. 2016 Mar 3;531(7592):64-9. doi: 10.1038/nature17199. Epub 2016 Feb 22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biomedical Research Centre, Norwich Medical School, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK. ; Diamond Light Source, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, UK. ; Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. ; Jiangsu Province Key Laboratory of Anesthesiology, Xuzhou Medical College, Xuzhou 221004, China. ; Key Laboratory of Bio-resources and Eco-environment, Ministry of Education, Sichuan Key Laboratory of Molecular Biology and Biotechnology, College of Life Sciences, Sichuan University, Chengdu 610064, China. ; Laboratory of Department of Surgery, the First Affiliated Hospital, Sun Yat-sen University, 58 Zhongshan Road II, Guangzhou, Guangdong 510080, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26901871" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Outer Membrane Proteins/*chemistry/*metabolism ; Crystallography, X-Ray ; Escherichia coli/*chemistry ; Escherichia coli Proteins/*chemistry/*metabolism ; Lipoproteins/chemistry/metabolism ; Models, Molecular ; Molecular Dynamics Simulation ; Movement ; Multiprotein Complexes/*chemistry/*metabolism ; Periplasm/metabolism ; Protein Binding ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism ; Rotation
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 7
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    Visualizing coherent intermolecular dipole-dipole coupling in real space (2016)
    Nature Publishing Group (NPG)
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    Publication Date: 2016-04-01
    Description: Many important energy-transfer and optical processes, in both biological and artificial systems, depend crucially on excitonic coupling that spans several chromophores. Such coupling can in principle be described in a straightforward manner by considering the coherent intermolecular dipole-dipole interactions involved. However, in practice, it is challenging to directly observe in real space the coherent dipole coupling and the related exciton delocalizations, owing to the diffraction limit in conventional optics. Here we demonstrate that the highly localized excitations that are produced by electrons tunnelling from the tip of a scanning tunnelling microscope, in conjunction with imaging of the resultant luminescence, can be used to map the spatial distribution of the excitonic coupling in well-defined arrangements of a few zinc-phthalocyanine molecules. The luminescence patterns obtained for excitons in a dimer, which are recorded for different energy states and found to resemble sigma and pi molecular orbitals, reveal the local optical response of the system and the dependence of the local optical response on the relative orientation and phase of the transition dipoles of the individual molecules in the dimer. We generate an in-line arrangement up to four zinc-phthalocyanine molecules, with a larger total transition dipole, and show that this results in enhanced 'single-molecule' superradiance from the oligomer upon site-selective excitation. These findings demonstrate that our experimental approach provides detailed spatial information about coherent dipole-dipole coupling in molecular systems, which should enable a greater understanding and rational engineering of light-harvesting structures and quantum light sources.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Yang -- Luo, Yang -- Zhang, Yao -- Yu, Yun-Jie -- Kuang, Yan-Min -- Zhang, Li -- Meng, Qiu-Shi -- Luo, Yi -- Yang, Jin-Long -- Dong, Zhen-Chao -- Hou, J G -- England -- Nature. 2016 Mar 31;531(7596):623-7. doi: 10.1038/nature17428.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hefei National Laboratory for Physical Sciences at the Microscale and Synergetic Innovation Center of Quantum Information and Quantum Physics, University of Science and Technology of China, Hefei, Anhui 230026, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/27029277" target="_blank"〉PubMed〈/a〉
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    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 8
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    Materials science: Share corrosion data (2015)
    Nature Publishing Group (NPG)
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    Publication Date: 2015-11-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Xiaogang -- Zhang, Dawei -- Liu, Zhiyong -- Li, Zhong -- Du, Cuiwei -- Dong, Chaofang -- England -- Nature. 2015 Nov 26;527(7579):441-2. doi: 10.1038/527441a.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Key Laboratory for Corrosion and Protection of the Ministry of Education, Institute of Advanced Materials & Technology, University of Science and Technology Beijing, Beijing, China, and is at the Ningbo Institute of Material Technology & Engineering, Chinese Academy of Sciences, Ningbo, Zhejiang, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26607528" target="_blank"〉PubMed〈/a〉
    Keywords: Accidents/mortality ; *Corrosion ; Disasters/*prevention & control/statistics & numerical data ; Humans ; *Information Dissemination ; Materials Testing ; Safety Management/*methods
    Print ISSN: 0028-0836
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    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 9
    Electronic Resource
    Electronic Resource
    Ion beam syntheses and microstructure studies of a new FeSi2 phase (1996)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 80 (1996), S. 3306-3309 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: Iron-silicide has been formed by ion implantation of iron into silicon (111). In the as-implanted sample, a new type of orthorhombic FeSi2 phase was found. Although the lattice parameters of the new phase are the same as those of the known semiconductor β-FeSi2, its point group and space group were different and determined to be mmm and Pbca, respectively. © 1996 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.363240
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  • 10
    Electronic Resource
    Electronic Resource
    X-ray reflectivity studies of the effect of surfactant on the growth of GeSi superlattices (1995)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 78 (1995), S. 1681-1684 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: X-ray reflectivity is applied to investigate the effect of a surfactant on the growth of Ge1−xSix/Si superlattices. It is demonstrated that the antimony layer deposited on the surface can effectively prevent the intermixing of silicon and germanium. The specular reflectivity curves show that the width of the interface is sufficiently reduced by the surfactant. The transverse scans show that the interface roughening exponent h for the sample with surfactant is larger than for the sample without surfactant, and the in-plane correlation length for the former is much larger than for the latter. This indicates that the surfactant makes less jagged and smoother interfaces and induces a different surface growth mode. © 1995 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.360264
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