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  • Chemistry  (36)
  • Crystallography, X-Ray  (30)
  • Magnetism  (18)
  • Superfluidity and superconductivity  (17)
  • 1
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    Modification of structural disorder by hydrostatic pressure in the superconducting cuprate ${\mathrm{YBa}}_{2}{\mathrm{Cu}}_{3}{\mathrm{O}}_{6.73}$ (2018)
    American Physical Society (APS)
    Details
    Publication Date: 2018-05-10
    Description: Author(s): H. Huang, H. Jang, M. Fujita, T. Nishizaki, Y. Lin, J. Wang, J. Ying, J. S. Smith, C. Kenney-Benson, G. Shen, W. L. Mao, C.-C. Kao, Y.-J. Liu, and J.-S. Lee Compelling efforts to improve the critical temperature ( T c ) of superconductors have been made through high-pressure application. Understanding the underlying mechanism behind such improvements is critically important; however, much remains unclear. Here we studied ortho-III YBa 2 Cu 3 O 6.73 (YBCO) using... [Phys. Rev. B 97, 174508] Published Wed May 09, 2018
    Keywords: Superfluidity and superconductivity
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
    Published by American Physical Society (APS)
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  • 2
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    Thermal melting of magnetic stripe domains (2011)
    American Physical Society (APS)
    Details
    Publication Date: 2011-05-28
    Description: Author(s): W. Kuch, K. Fukumoto, J. Wang, F. Nolting, C. Quitmann, and T. Ramsvik We present a microscopic investigation of the temperature dependence of stripe domains in perpendicularly magnetized Ni films on Cu(001) using photoelectron emission microscopy in combination with x-ray magnetic circular dichroism (XMCD) in the resonant absorption of soft x rays. When the temperatur... [Phys. Rev. B 83, 172406] Published Fri May 27, 2011
    Keywords: Magnetism
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
    Published by American Physical Society (APS)
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  • 3
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    Intrinsic ferroelectric polarization of orthorhombic manganites with E-type spin order (2012)
    American Physical Society (APS)
    Details
    Publication Date: 2012-05-08
    Description: Author(s): Y. S. Chai, Y. S. Oh, L. J. Wang, N. Manivannan, S. M. Feng, Y. S. Yang, L. Q. Yan, C. Q. Jin, and Kee Hoon Kim By directly measuring electrical hysteresis loops using the Positive-Up Negative-Down (PUND) method, we determined accurately the remanent ferroelectric polarization P r of orthorhombic R MnO 3 ( R = Ho, Tm, Yb, and Lu) compounds below their E -type spin ordering temperatures. We found that LuMnO 3 has th... [Phys. Rev. B 85, 184406] Published Mon May 07, 2012
    Keywords: Magnetism
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
    Published by American Physical Society (APS)
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  • 4
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    Large and inverted spin signals in nonlocal spin valves (2011)
    American Physical Society (APS)
    Details
    Publication Date: 2011-03-04
    Description: Author(s): Han Zou, S. T. Chui, X. J. Wang, and Yi Ji A nonlocal spin valve (NLSV) is a nanoscale planar heterostructure, consisting of a spin injector, a spin detector, and a nonmagnetic channel. A pure spin current can be induced in the nonmagnetic channel by electrical spin injection. We report large but inverted spin signals in a set of NLSV struct... [Phys. Rev. B 83, 094402] Published Thu Mar 03, 2011
    Keywords: Magnetism
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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  • 5
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    Magnetic domain-wall motion twisted by nanoscale probe-induced spin transfer (2014)
    American Physical Society (APS)
    Details
    Publication Date: 2014-12-10
    Description: Author(s): J. Wang, L. S. Xie, C. S. Wang, H. Z. Zhang, L. Shu, J. Bai, Y. S. Chai, X. Zhao, J. C. Nie, C. B. Cao, C. Z. Gu, C. M. Xiong, Y. Sun, J. Shi, S. Salahuddin, K. Xia, C. W. Nan, and J. X. Zhang A method for deterministic control of magnetism using an electrical stimulus is highly desired for the new generation of magnetoelectronic devices. Much effort has been focused on magnetic domain-wall (DW) motion manipulated by a successive injection of spin-polarized current into a magnetic nanostr... [Phys. Rev. B 90, 224407] Published Fri Dec 05, 2014
    Keywords: Magnetism
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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  • 6
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    Transverse currents in triplet Josephson junction with spin-orbit coupling (2012)
    American Physical Society (APS)
    Details
    Publication Date: 2012-01-04
    Description: Author(s): Huan Zhang, K. S. Chan, Zijing Lin, and J. Wang [Phys. Rev. B 85, 024501] Published Tue Jan 03, 2012
    Keywords: Superfluidity and superconductivity
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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  • 7
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    Insights into editing from an ile-tRNA synthetase structure with tRNAile and mupirocin (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-08-14
    Description: Isoleucyl-transfer RNA (tRNA) synthetase (IleRS) joins Ile to tRNA(Ile) at its synthetic active site and hydrolyzes incorrectly acylated amino acids at its editing active site. The 2.2 angstrom resolution crystal structure of Staphylococcus aureus IleRS complexed with tRNA(Ile) and Mupirocin shows the acceptor strand of the tRNA(Ile) in the continuously stacked, A-form conformation with the 3' terminal nucleotide in the editing active site. To position the 3' terminus in the synthetic active site, the acceptor strand must adopt the hairpinned conformation seen in tRNA(Gln) complexed with its synthetase. The amino acid editing activity of the IleRS may result from the incorrect products shuttling between the synthetic and editing active sites, which is reminiscent of the editing mechanism of DNA polymerases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Silvian, L F -- Wang, J -- Steitz, T A -- GM22778/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Aug 13;285(5430):1074-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics, Yale University, and Howard Hughes Medical Institute, New Haven, CT 06520-8114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10446055" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Adenosine Monophosphate/analogs & derivatives/metabolism ; Amino Acids/metabolism ; Binding Sites ; Crystallography, X-Ray ; DNA-Directed DNA Polymerase/metabolism ; Glutamate-tRNA Ligase/chemistry/metabolism ; Isoleucine/metabolism ; Isoleucine-tRNA Ligase/*chemistry/*metabolism ; Models, Molecular ; Mupirocin/chemistry/*metabolism ; Nucleic Acid Conformation ; Oligopeptides/metabolism ; Protein Conformation ; Protein Structure, Secondary ; RNA, Transfer, Gln/chemistry/metabolism ; RNA, Transfer, Ile/*chemistry/*metabolism ; Staphylococcus aureus/enzymology ; Substrate Specificity
    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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  • 8
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    The crystal structure of a T cell receptor in complex with peptide and MHC class II (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-03
    Description: The crystal structure of a complex involving the D10 T cell receptor (TCR), 16-residue foreign peptide antigen, and the I-Ak self major histocompatibility complex (MHC) class II molecule is reported at 3.2 angstrom resolution. The D10 TCR is oriented in an orthogonal mode relative to its peptide-MHC (pMHC) ligand, necessitated by the amino-terminal extension of peptide residues projecting from the MHC class II antigen-binding groove as part of a mini beta sheet. Consequently, the disposition of D10 complementarity-determining region loops is altered relative to that of most pMHCI-specific TCRs; the latter TCRs assume a diagonal orientation, although with substantial variability. Peptide recognition, which involves P-1 to P8 residues, is dominated by the Valpha domain, which also binds to the class II MHC beta1 helix. That docking is limited to one segment of MHC-bound peptide offers an explanation for epitope recognition and altered peptide ligand effects, suggests a structural basis for alloreactivity, and illustrates how bacterial superantigens can span the TCR-pMHCII surface.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reinherz, E L -- Tan, K -- Tang, L -- Kern, P -- Liu, J -- Xiong, Y -- Hussey, R E -- Smolyar, A -- Hare, B -- Zhang, R -- Joachimiak, A -- Chang, H C -- Wagner, G -- Wang, J -- AI/CA37581/AI/NIAID NIH HHS/ -- AI19807/AI/NIAID NIH HHS/ -- GM56008/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Dec 3;286(5446):1913-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunobiology, Dana-Farber Cancer Institute, Department of Medicine, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10583947" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens/*chemistry/immunology/metabolism ; Binding Sites ; CD4-Positive T-Lymphocytes/immunology ; CD8-Positive T-Lymphocytes/immunology ; Conalbumin/chemistry/immunology ; Crystallization ; Crystallography, X-Ray ; Histocompatibility Antigens Class I/immunology ; Histocompatibility Antigens Class II/*chemistry/immunology/metabolism ; Hydrogen Bonding ; Ligands ; Mice ; Mice, Inbred AKR ; Models, Molecular ; Oligopeptides/chemistry/immunology/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Receptors, Antigen, T-Cell, alpha-beta/*chemistry/immunology/metabolism ; Superantigens/immunology/metabolism ; Thymus Gland/cytology/immunology
    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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  • 9
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    Mechanism of substrate recognition and transport by an amino acid antiporter (2010)
    Nature Publishing Group (NPG)
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    Publication Date: 2010-01-22
    Description: In extremely acidic environments, enteric bacteria such as Escherichia coli rely on the amino acid antiporter AdiC to expel protons by exchanging intracellular agmatine (Agm(2+)) for extracellular arginine (Arg(+)). AdiC is a representative member of the amino acid-polyamine-organocation (APC) superfamily of membrane transporters. The structure of substrate-free AdiC revealed a homodimeric assembly, with each protomer containing 12 transmembrane segments and existing in an outward-open conformation. The overall folding of AdiC is similar to that of the Na(+)-coupled symporters. Despite these advances, it remains unclear how the substrate (arginine or agmatine) is recognized and transported by AdiC. Here we report the crystal structure of an E. coli AdiC variant bound to Arg at 3.0 A resolution. The positively charged Arg is enclosed in an acidic binding chamber, with the head groups of Arg hydrogen-bonded to main chain atoms of AdiC and the aliphatic portion of Arg stacked by hydrophobic side chains of highly conserved residues. Arg binding induces pronounced structural rearrangement in transmembrane helix 6 (TM6) and, to a lesser extent, TM2 and TM10, resulting in an occluded conformation. Structural analysis identified three potential gates, involving four aromatic residues and Glu 208, which may work in concert to differentially regulate the upload and release of Arg and Agm.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gao, Xiang -- Zhou, Lijun -- Jiao, Xuyao -- Lu, Feiran -- Yan, Chuangye -- Zeng, Xin -- Wang, Jiawei -- Shi, Yigong -- England -- Nature. 2010 Feb 11;463(7282):828-32. doi: 10.1038/nature08741. Epub 2010 Jan 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ministry of Education Protein Science Laboratory, Tsinghua University, Beijing 100084, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20090677" target="_blank"〉PubMed〈/a〉
    Keywords: Agmatine/metabolism ; Amino Acid Transport Systems/*chemistry/*metabolism ; Antiporters/*chemistry/*metabolism ; Arginine/chemistry/*metabolism ; Biological Transport ; Conserved Sequence ; Crystallography, X-Ray ; Escherichia coli Proteins/*chemistry/*metabolism ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; Protein Conformation ; Protein Folding ; Protein Multimerization ; Protons ; Static Electricity ; Structure-Activity Relationship ; Substrate Specificity
    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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  • 10
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    Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-11-27
    Description: FocA is a representative member of the formate-nitrite transporter family, which transports short-chain acids in bacteria, archaea, fungi, algae and parasites. The structure and transport mechanism of the formate-nitrite transporter family remain unknown. Here we report the crystal structure of Escherichia coli FocA at 2.25 A resolution. FocA forms a symmetric pentamer, with each protomer consisting of six transmembrane segments. Despite a lack of sequence homology, the overall structure of the FocA protomer closely resembles that of aquaporin and strongly argues that FocA is a channel, rather than a transporter. Structural analysis identifies potentially important channel residues, defines the channel path and reveals two constriction sites. Unlike aquaporin, FocA is impermeable to water but allows the passage of formate. A structural and biochemical investigation provides mechanistic insights into the channel activity of FocA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Yi -- Huang, Yongjian -- Wang, Jiawei -- Cheng, Chao -- Huang, Weijiao -- Lu, Peilong -- Xu, Ya-Nan -- Wang, Pengye -- Yan, Nieng -- Shi, Yigong -- England -- Nature. 2009 Nov 26;462(7272):467-72. doi: 10.1038/nature08610.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ministry of Education Protein Science Laboratory, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19940917" target="_blank"〉PubMed〈/a〉
    Keywords: Aquaporins/*chemistry/metabolism ; Crystallography, X-Ray ; Escherichia coli/chemistry/genetics/metabolism ; Escherichia coli Proteins/*chemistry/genetics/metabolism ; Formates/metabolism ; Liposomes/chemistry/metabolism ; Membrane Transport Proteins/*chemistry/genetics/metabolism ; Models, Molecular ; Molecular Mimicry ; Mutation ; Permeability ; Protein Structure, Quaternary ; Structure-Activity Relationship ; Water/analysis/metabolism
    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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