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  • 1
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    Mismatch between the eye and the optic lobe in the giant squid (2017)
    Royal Society
    Details
    Publication Date: 2017-07-20
    Description: Giant squids ( Architeuthis ) are a legendary species among the cephalopods. They live in the deep sea and are well known for their enormous body and giant eyes. It has been suggested that their giant eyes are not adapted for the detection of either mates or prey at distance, but rather are best suited for monitoring very large predators, such as sperm whales, at distances exceeding 120 m and at a depth below 600 m (Nilsson et al. 2012 Curr. Biol. 22 , 683–688. ( doi:10.1016/j.cub.2012.02.031 )). However, it is not clear how the brain of giant squids processes visual information. In this study, the optic lobe of a giant squid ( Architeuthis dux , male, mantle length 89 cm), which was caught by local fishermen off the northeastern coast of Taiwan, was scanned using high-resolution magnetic resonance imaging in order to examine its internal structure. It was evident that the volume ratio of the optic lobe to the eye in the giant squid is much smaller than that in the oval squid ( Sepioteuthis lessoniana ) and the cuttlefish ( Sepia pharaonis ). Furthermore, the cell density in the cortex of the optic lobe is significantly higher in the giant squid than in oval squids and cuttlefish, with the relative thickness of the cortex being much larger in Architeuthis optic lobe than in cuttlefish. This indicates that the relative size of the medulla of the optic lobe in the giant squid is disproportionally smaller compared with these two cephalopod species. This morphological study of the giant squid brain, though limited only to the optic lobe, provides the first evidence to support that the optic lobe cortex, the visual information processing area in cephalopods, is well developed in the giant squid. In comparison, the optic lobe medulla, the visuomotor integration centre in cephalopods, is much less developed in the giant squid than other species. This finding suggests that, despite the giant eye and a full-fledged cortex within the optic lobe, the brain of giant squids has not evolved proportionally in terms of performing complex tasks compared with shallow-water cephalopod species.
    Keywords: neuroscience, behaviour, evolution
    Electronic ISSN: 2054-5703
    Topics: Natural Sciences in General
    Published by Royal Society
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  • 2
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    Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-09-25
    Description: Gram-negative bacteria, such as Escherichia coli, frequently use tripartite efflux complexes in the resistance-nodulation-cell division (RND) family to expel various toxic compounds from the cell. The efflux system CusCBA is responsible for extruding biocidal Cu(I) and Ag(I) ions. No previous structural information was available for the heavy-metal efflux (HME) subfamily of the RND efflux pumps. Here we describe the crystal structures of the inner-membrane transporter CusA in the absence and presence of bound Cu(I) or Ag(I). These CusA structures provide new structural information about the HME subfamily of RND efflux pumps. The structures suggest that the metal-binding sites, formed by a three-methionine cluster, are located within the cleft region of the periplasmic domain. This cleft is closed in the apo-CusA form but open in the CusA-Cu(I) and CusA-Ag(I) structures, which directly suggests a plausible pathway for ion export. Binding of Cu(I) and Ag(I) triggers significant conformational changes in both the periplasmic and transmembrane domains. The crystal structure indicates that CusA has, in addition to the three-methionine metal-binding site, four methionine pairs-three located in the transmembrane region and one in the periplasmic domain. Genetic analysis and transport assays suggest that CusA is capable of actively picking up metal ions from the cytosol, using these methionine pairs or clusters to bind and export metal ions. These structures suggest a stepwise shuttle mechanism for transport between these sites.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2946090/" 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/PMC2946090/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Long, Feng -- Su, Chih-Chia -- Zimmermann, Michael T -- Boyken, Scott E -- Rajashankar, Kanagalaghatta R -- Jernigan, Robert L -- Yu, Edward W -- GM 072014/GM/NIGMS NIH HHS/ -- GM 074027/GM/NIGMS NIH HHS/ -- GM 081680/GM/NIGMS NIH HHS/ -- GM 086431/GM/NIGMS NIH HHS/ -- R01 GM072014/GM/NIGMS NIH HHS/ -- R01 GM074027/GM/NIGMS NIH HHS/ -- R01 GM074027-05/GM/NIGMS NIH HHS/ -- R01 GM086431/GM/NIGMS NIH HHS/ -- R01 GM086431-01A2/GM/NIGMS NIH HHS/ -- RR-15301/RR/NCRR NIH HHS/ -- England -- Nature. 2010 Sep 23;467(7314):484-8. doi: 10.1038/nature09395.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular, Cellular and Developmental Biology Interdepartmental Graduate Program, Iowa State University, Iowa 50011, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20865003" target="_blank"〉PubMed〈/a〉
    Keywords: Apoproteins/chemistry/metabolism ; Binding Sites ; Cell Membrane/metabolism ; Copper/chemistry/*metabolism ; Crystallography, X-Ray ; Cytosol/metabolism ; Escherichia coli/*chemistry ; Escherichia coli Proteins/*chemistry/*metabolism ; Ion Transport ; Membrane Transport Proteins/*chemistry/*metabolism ; Methionine/*metabolism ; Models, Biological ; Models, Molecular ; Periplasm/metabolism ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Silver/chemistry/*metabolism ; Structure-Activity Relationship
    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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    Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-02-26
    Description: Gram-negative bacteria, such as Escherichia coli, expel toxic chemicals through tripartite efflux pumps that span both the inner and outer membrane. The three parts are an inner membrane, substrate-binding transporter; a membrane fusion protein; and an outer-membrane-anchored channel. The fusion protein connects the transporter to the channel within the periplasmic space. A crystallographic model of this tripartite efflux complex has been unavailable because co-crystallization of the various components of the system has proven to be extremely difficult. We previously described the crystal structures of both the inner membrane transporter CusA and the membrane fusion protein CusB of the CusCBA efflux system of E. coli. Here we report the co-crystal structure of the CusBA efflux complex, showing that the transporter (or pump) CusA, which is present as a trimer, interacts with six CusB protomers and that the periplasmic domain of CusA is involved in these interactions. The six CusB molecules seem to form a continuous channel. The affinity of the CusA and CusB interaction was found to be in the micromolar range. Finally, we have predicted a three-dimensional structure for the trimeric CusC outer membrane channel and developed a model of the tripartite efflux assemblage. This CusC(3)-CusB(6)-CusA(3) model shows a 750-kilodalton efflux complex that spans the entire bacterial cell envelope and exports Cu I and Ag I ions.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3078058/" 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/PMC3078058/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Su, Chih-Chia -- Long, Feng -- Zimmermann, Michael T -- Rajashankar, Kanagalaghatta R -- Jernigan, Robert L -- Yu, Edward W -- R01 GM072014/GM/NIGMS NIH HHS/ -- R01 GM074027/GM/NIGMS NIH HHS/ -- R01 GM074027-05/GM/NIGMS NIH HHS/ -- R01 GM086431/GM/NIGMS NIH HHS/ -- R01 GM086431-01A2/GM/NIGMS NIH HHS/ -- R01GM072014/GM/NIGMS NIH HHS/ -- R01GM074027/GM/NIGMS NIH HHS/ -- R01GM081680/GM/NIGMS NIH HHS/ -- R01GM086431/GM/NIGMS NIH HHS/ -- RR-15301/RR/NCRR NIH HHS/ -- England -- Nature. 2011 Feb 24;470(7335):558-62. doi: 10.1038/nature09743.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Iowa State University, Ames, Iowa 50011, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21350490" target="_blank"〉PubMed〈/a〉
    Keywords: Copper/metabolism ; Crystallization ; Crystallography, X-Ray ; Escherichia coli/*chemistry ; Escherichia coli Proteins/*chemistry/metabolism ; Membrane Transport Proteins/*chemistry/metabolism ; Metals, Heavy/*metabolism ; Models, Molecular ; Multiprotein Complexes/*chemistry/metabolism ; Protein Binding ; Protein Multimerization ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Silver/metabolism ; Static Electricity
    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
    Electronic Resource
    Electronic Resource
    Hydrothermal synthesis and structural characterization of two calcium vanadium(III) phosphates: Ca2V(PO4)(HPO4)2.cntdot.H2O and Ca2V(PO4)(P2O7) (1992)
    s.l. : American Chemical Society
    Inorganic chemistry 31 (1992), S. 439-442 
    Details
    ISSN: 1520-510X
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ic00029a017
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  • 5
    Electronic Resource
    Electronic Resource
    Chemical interactions in blends of bisphenol A polycarbonate with tetraglycidyl-4,4'-diaminodiphenylmethane epoxy (1995)
    s.l. : American Chemical Society
    Macromolecules 28 (1995), S. 6779-6786 
    Details
    ISSN: 1520-5835
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ma00124a012
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  • 6
    Electronic Resource
    Electronic Resource
    Bonding properties of Cu(II)-imidazole chromophores: spectroscopic and electrochemical properties of monosubstituted imidazole copper(II) complexes. Molecular structure of [Cu(4-methylimidazole)"4(ClO"4)"2]
    Amsterdam : Elsevier
    Inorganica Chimica Acta 196 (1992), S. 231-240 
    Details
    ISSN: 0020-1693
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0020-1693(00)86128-9
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  • 7
    Electronic Resource
    Electronic Resource
    Dielectric properties of material with random off-center defects: Monte Carlo simulation of relaxor ferroelectrics (2001)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 90 (2001), S. 6345-6356 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: A Ginzburg–Landau type theory of interaction of randomly distributed local dipoles in a paraelectric crystal is developed. The interaction is caused by the polarization of the host lattice generated by these dipoles. The obtained effective Hamiltonian of the dipole–dipole interaction is employed for the Monte Carlo simulation of ferroelectric properties of a system with off-center dopant ions producing local dipoles. The computer simulation shows that at low dopant ion concentration the paraelectric state transforms into a macroscopically paraelectric state consisting of randomly oriented polar clusters. These clusters amplify the effective dipole moment and dramatically increase the dielectric constant. The interaction between the clusters results in a spectrum of relaxation time and transition to the relaxor state. The real and imaginary parts of the susceptibility of this state are calculated. At intermediate dopant concentration, the material undergoes a diffuse phase transition into a ferroelectric state smeared within a temperature range. A further increase in the dopant concentration makes the transition sharper and closer to the conventional ferroelectric transition. The results obtained are compared with the behavior of the K1−xLixTaO3 relaxor ferroelectric. © 2001 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.1415759
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  • 8
    Electronic Resource
    Electronic Resource
    Mechanism of cholesterol gallstone dissolution. Analysis of the kinetics of cholesterol monohydrate dissolution in taurocholate/lecithin solutions by the Mazer, Benedek, and Carey model (1981)
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 85 (1981), S. 127-129 
    Details
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/j150602a002
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  • 9
    Electronic Resource
    Electronic Resource
    A new locus for resistance to brown planthopper identified in the indica rice variety DV85 (2005)
    Oxford, UK : Blackwell Publishing Ltd
    Plant breeding 124 (2005), S. 0 
    Details
    ISSN: 1439-0523
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: The brown planthopper (BPH) is one of the most destructive insect pests of rice. Resistant varieties have proved to be one of the most economic and effective measures for BPH management. In this study, an indica rice ‘DV85’ showed resistance to biotype 2 of BPH by bulked seedling test, and a recombinant inbred line (RIL) population derived from a cross between a susceptible rice ‘Kinmaze’ and ‘DV85’ was phenotyped to map genetic factors conferring BPH resistance in ‘DV85′. Composite interval mapping revealed that one quantitative trait locus (QTL) with a LOD score of 10.1 was detected between XNpb202 and C1172 on chromosome 11. This QTL was designated as Qbph11. Qbph11 explained 68.4% of the phenotypic variance of BPH resistance in this population. The allele from the resistant parent ‘DV85’ at Qbph11 reduced the damage caused by BPH feeding and would be very useful in breeding resistant rice varieties via marker-assisted selection.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1439-0523.2004.01011.x
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  • 10
    Electronic Resource
    Electronic Resource
    The application of ESCA to the study of bonding in nitrosyls
    Amsterdam : Elsevier
    Journal of Organometallic Chemistry 84 (1975), S. 53-64 
    Details
    ISSN: 0022-328X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0022-328X(00)88774-4
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