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1P. K. Joshi ; T. Esko ; H. Mattsson ; N. Eklund ; I. Gandin ; T. Nutile ; A. U. Jackson ; C. Schurmann ; A. V. Smith ; W. Zhang ; Y. Okada ; A. Stancakova ; J. D. Faul ; W. Zhao ; T. M. Bartz ; M. P. Concas ; N. Franceschini ; S. Enroth ; V. Vitart ; S. Trompet ; X. Guo ; D. I. Chasman ; J. R. O'Connel ; T. Corre ; S. S. Nongmaithem ; Y. Chen ; M. Mangino ; D. Ruggiero ; M. Traglia ; A. E. Farmaki ; T. Kacprowski ; A. Bjonnes ; A. van der Spek ; Y. Wu ; A. K. Giri ; L. R. Yanek ; L. Wang ; E. Hofer ; C. A. Rietveld ; O. McLeod ; M. C. Cornelis ; C. Pattaro ; N. Verweij ; C. Baumbach ; A. Abdellaoui ; H. R. Warren ; D. Vuckovic ; H. Mei ; C. Bouchard ; J. R. Perry ; S. Cappellani ; S. S. Mirza ; M. C. Benton ; U. Broeckel ; S. E. Medland ; P. A. Lind ; G. Malerba ; A. Drong ; L. Yengo ; L. F. Bielak ; D. Zhi ; P. J. van der Most ; D. Shriner ; R. Magi ; G. Hemani ; T. Karaderi ; Z. Wang ; T. Liu ; I. Demuth ; J. H. Zhao ; W. Meng ; L. Lataniotis ; S. W. van der Laan ; J. P. 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Chambers ; J. S. Kooner ; D. P. Strachan ; H. Campbell ; J. N. Hirschhorn ; M. Perola ; O. Polasek ; J. F. Wilson
Nature Publishing Group (NPG)
Published 2015Staff ViewPublication Date: 2015-07-02Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Biological Evolution ; Blood Pressure/genetics ; Body Height/*genetics ; Cholesterol, LDL/genetics ; *Cognition ; Cohort Studies ; Educational Status ; Female ; Forced Expiratory Volume/genetics ; Genome, Human/genetics ; *Homozygote ; Humans ; Lung Volume Measurements ; Male ; PhenotypePublished by: -
2A. Okbay ; J. P. Beauchamp ; M. A. Fontana ; J. J. Lee ; T. H. Pers ; C. A. Rietveld ; P. Turley ; G. B. Chen ; V. Emilsson ; S. F. Meddens ; S. Oskarsson ; J. K. Pickrell ; K. Thom ; P. Timshel ; R. de Vlaming ; A. Abdellaoui ; T. S. Ahluwalia ; J. Bacelis ; C. Baumbach ; G. Bjornsdottir ; J. H. Brandsma ; M. Pina Concas ; J. Derringer ; N. A. Furlotte ; T. E. Galesloot ; G. Girotto ; R. Gupta ; L. M. Hall ; S. E. Harris ; E. Hofer ; M. Horikoshi ; J. E. Huffman ; K. Kaasik ; I. P. Kalafati ; R. Karlsson ; A. Kong ; J. Lahti ; S. J. van der Lee ; C. deLeeuw ; P. A. Lind ; K. O. Lindgren ; T. Liu ; M. Mangino ; J. Marten ; E. Mihailov ; M. B. Miller ; P. J. van der Most ; C. Oldmeadow ; A. Payton ; N. Pervjakova ; W. J. Peyrot ; Y. Qian ; O. Raitakari ; R. Rueedi ; E. Salvi ; B. Schmidt ; K. E. Schraut ; J. Shi ; A. V. Smith ; R. A. Poot ; B. St Pourcain ; A. Teumer ; G. Thorleifsson ; N. Verweij ; D. Vuckovic ; J. Wellmann ; H. J. Westra ; J. Yang ; W. Zhao ; Z. Zhu ; B. Z. Alizadeh ; N. Amin ; A. Bakshi ; S. E. Baumeister ; G. Biino ; K. Bonnelykke ; P. A. Boyle ; H. Campbell ; F. P. Cappuccio ; G. Davies ; J. E. De Neve ; P. Deloukas ; I. Demuth ; J. Ding ; P. Eibich ; L. Eisele ; N. Eklund ; D. M. Evans ; J. D. Faul ; M. F. Feitosa ; A. J. Forstner ; I. Gandin ; B. Gunnarsson ; B. V. Halldorsson ; T. B. Harris ; A. C. Heath ; L. J. Hocking ; E. G. Holliday ; G. Homuth ; M. A. Horan ; J. J. Hottenga ; P. L. de Jager ; P. K. Joshi ; A. Jugessur ; M. A. Kaakinen ; M. Kahonen ; S. Kanoni ; L. Keltigangas-Jarvinen ; L. A. Kiemeney ; I. Kolcic ; S. Koskinen ; A. T. Kraja ; M. Kroh ; Z. Kutalik ; A. Latvala ; L. J. Launer ; M. P. Lebreton ; D. F. Levinson ; P. Lichtenstein ; P. Lichtner ; D. C. Liewald ; A. Loukola ; P. A. Madden ; R. Magi ; T. Maki-Opas ; R. E. Marioni ; P. Marques-Vidal ; G. A. Meddens ; G. McMahon ; C. Meisinger ; T. Meitinger ; Y. Milaneschi ; L. Milani ; G. W. Montgomery ; R. Myhre ; C. P. Nelson ; D. R. Nyholt ; W. E. Ollier ; A. Palotie ; L. Paternoster ; N. L. Pedersen ; K. E. Petrovic ; D. J. Porteous ; K. Raikkonen ; S. M. Ring ; A. Robino ; O. Rostapshova ; I. Rudan ; A. Rustichini ; V. Salomaa ; A. R. Sanders ; A. P. Sarin ; H. Schmidt ; R. J. Scott ; B. H. Smith ; J. A. Smith ; J. A. Staessen ; E. Steinhagen-Thiessen ; K. Strauch ; A. Terracciano ; M. D. Tobin ; S. Ulivi ; S. Vaccargiu ; L. Quaye ; F. J. van Rooij ; C. Venturini ; A. A. Vinkhuyzen ; U. Volker ; H. Volzke ; J. M. Vonk ; D. Vozzi ; J. Waage ; E. B. Ware ; G. Willemsen ; J. R. Attia ; D. A. Bennett ; K. Berger ; L. Bertram ; H. Bisgaard ; D. I. Boomsma ; I. B. Borecki ; U. Bultmann ; C. F. Chabris ; F. Cucca ; D. Cusi ; I. J. Deary ; G. V. Dedoussis ; C. M. van Duijn ; J. G. Eriksson ; B. Franke ; L. Franke ; P. Gasparini ; P. V. Gejman ; C. Gieger ; H. J. Grabe ; J. Gratten ; P. J. Groenen ; V. Gudnason ; P. van der Harst ; C. Hayward ; D. A. Hinds ; W. Hoffmann ; E. Hypponen ; W. G. Iacono ; B. Jacobsson ; M. R. Jarvelin ; K. H. Jockel ; J. Kaprio ; S. L. Kardia ; T. Lehtimaki ; S. F. Lehrer ; P. K. Magnusson ; N. G. Martin ; M. McGue ; A. Metspalu ; N. Pendleton ; B. W. Penninx ; M. Perola ; N. Pirastu ; M. Pirastu ; O. Polasek ; D. Posthuma ; C. Power ; M. A. Province ; N. J. Samani ; D. Schlessinger ; R. Schmidt ; T. I. Sorensen ; T. D. Spector ; K. Stefansson ; U. Thorsteinsdottir ; A. R. Thurik ; N. J. Timpson ; H. Tiemeier ; J. Y. Tung ; A. G. Uitterlinden ; V. Vitart ; P. Vollenweider ; D. R. Weir ; J. F. Wilson ; A. F. Wright ; D. C. Conley ; R. F. Krueger ; G. Davey Smith ; A. Hofman ; D. I. Laibson ; S. E. Medland ; M. N. Meyer ; M. Johannesson ; P. M. Visscher ; T. Esko ; P. D. Koellinger ; D. Cesarini ; D. J. Benjamin
Nature Publishing Group (NPG)
Published 2016Staff ViewPublication Date: 2016-05-27Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsPublished by: -
3W. E. Feeney ; I. Medina ; M. Somveille ; R. Heinsohn ; M. L. Hall ; R. A. Mulder ; J. A. Stein ; R. M. Kilner ; N. E. Langmore
American Association for the Advancement of Science (AAAS)
Published 2013Staff ViewPublication Date: 2013-12-21Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Africa, Southern ; *Aggression ; Animal Distribution ; Animals ; Australia ; *Biological Evolution ; *Breeding ; *Cooperative Behavior ; *Nesting Behavior ; Passeriformes/classification/*physiology ; Phylogeny ; Vocalization, AnimalPublished by: -
4Staff View
Publication Date: 2018-01-12Publisher: American Heart Association (AHA)Print ISSN: 1942-325XElectronic ISSN: 1942-3268Topics: MedicineKeywords: Electrophysiology, Genetic, Association StudiesPublished by: -
5Schmidt-Nielsen, B. K. ; Gepner, J. I. ; Teng, N. N. H. ; Hall, L. M.
Oxford, UK : Blackwell Publishing Ltd
Published 1977Staff ViewISSN: 1471-4159Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: Abstract— We describe an α-bungarotoxin binding component from Dromphila melanoyaster that has the properties expected of an acetylcholine receptor. Toxin binding to a paniculate form of this component has been shown to be proportional to amount of extract, to be saturable and to be destroyed by heat. Localization studies using 125I-α-bungarotoxin binding to frozen sections has shown toxin binding to be restricted to synaptic areas of the Drosophila CNS. We have also shown that this toxinbinding component can be treated with Triton X-100 without significantly altering its toxin-binding and pharmacological specificity. The ability of preincubation with cholinergic ligands to block labeled α-bungarotoxin binding to both particulate and detergent treated extracts has been studied. The nicotinic agents nicotine, d-tubocurarine, and acetylcholine are the most effective blocking agents. All of the muscarinic agents tested and the nicotinic agent decamethonium were less effective than acetylcholine in preventing α-bungarotoxin binding.Type of Medium: Electronic ResourceURL: -
6Rashid, A ; Newman, J C ; O'Donovan, J T ; Robinson, D ; Maurice, D ; Poisson, D ; Hall, L M
Oxford, UK : Blackwell Science Ltd
Published 2003Staff ViewISSN: 1365-3180Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, NutritionNotes: Summary Two Sonchus asper (spiny annual sow-thistle) biotypes, suspected of being resistant to the sulfonylurea herbicide metsulfuron-methyl, were collected in 1996 from two barley (Hordeum vulgare) fields in central Alberta, Canada. Both fields had received at least six applications of acetolactate synthase (ALS)-inhibiting herbicide(s). The responses of the two resistant (R) biotypes and two susceptible (S) biotypes to several sulfonylurea herbicides, and to herbicides and herbicide mixtures with other mechanisms of action, were compared. Both R biotypes were highly resistant to all sulfonylurea herbicides, but their control with other herbicides and mixtures was effective and comparable to that of the S biotypes. ALS extracted from an R biotype was about 440 times more resistant to metsulfuron-methyl than that of an S biotype, indicating that resistance was conferred by an ALS enzyme that was less sensitive to inhibition by the herbicide. Competitiveness and seed production of S. asper varied among biotypes, but the differences were probably the result of ecotype differences rather than resistance or susceptibility to sulfonylurea herbicides. This is the first reported occurrence of target site-based S. asper resistance to ALS-inhibiting herbicides.Type of Medium: Electronic ResourceURL: -
7Staff View
ISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] 2-Isothiocyanatoethyltrimethylammonium iodide, synthe-sised as a potential insecticide, was found to be a potent inhibitor of choline acetyltransferase partially purified from fly heads4. In the same study the dissociation constant for the enzyme-inhibitor complex was found to be 0.06 µM. No ...Type of Medium: Electronic ResourceURL: -
8Staff View
ISSN: 1932-7110Topics: SociologyURL: -
9Staff View
ISSN: 1932-7110Topics: SociologyNotes: PAPERS OF THE HEALTH DEPARTMENTURL: -
10Staff View
ISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] It was desired to ascertain which, if any, of these glutamyl derivatives is the naturally occurring stimulator of citrulline synthesis. Observation of the occurrence of such a stimulator and preliminary progress in the purification of this substance has been previously reported4. A concentrated ...Type of Medium: Electronic ResourceURL: -
11Staff View
ISSN: 1476-5535Keywords: metallothionein ; cyanobacteria ; metals ; bioremediationSource: Springer Online Journal Archives 1860-2000Topics: BiologyProcess Engineering, Biotechnology, Nutrition TechnologyNotes: Abstract A cDNA encoding mouse metallothionein was cloned into the shuttle vector pUC303, creating a translational fusion with the bacterial chloramphenicol acetyltransferase gene. The resulting fusion protein has been expressed in the cyanobacteriumSynechococcus PCC7942. Cyanobacterial transformants expressed mouse metallothionein-specific mRNA species as detected by RNA slot blots. In addition, the transformants expressed a unique cadmium ionbinding protein corresponding to the predicted size of the mouse metallothionein fusion protein. Expression of this fusion protein conferred a two-to five-fold increase in cadmium ion tolerance and accumulation onSynechococcus PCC7942.Type of Medium: Electronic ResourceURL: -
12Staff View
ISSN: 1476-5535Keywords: cyanobacteria ; biosensor ; heavy metal ; luxSource: Springer Online Journal Archives 1860-2000Topics: BiologyProcess Engineering, Biotechnology, Nutrition TechnologyNotes: Abstract The metal-responsivesmt operator/promoter region ofSynechococcus PCC7942 was fused to theluxCDABE genes ofVibrio fischeri. Plasmid DNA (pJLE23) carrying this fusion conferred metal ion-inducible luminescence to transformed cyanobacteria.Synechococcus PCC7942 (pJLE23) was sensitive to ZnCl2 concentrations within a range of 0.5–4 μM as demonstrated by induction of luminescence. Trace levels of CuSO4, and CdCl2 were also detected.Type of Medium: Electronic ResourceURL: -
13Staff View
ISSN: 1573-4927Keywords: Drosophila melanogaster ; GTP cyclohydrolase ; pteridine biosynthesis ; development ; mutantsSource: Springer Online Journal Archives 1860-2000Topics: BiologyChemistry and PharmacologyNotes: Abstract The enzyme guanosine triphosphate cyclohydrolase (GTP cyclohydrolase), which in bacteria is known to be the first enzyme in the biosynthetic pathway for the synthesis of pteridines, has been discovered in extracts of Drosophila melanogaster. Most of the enzyme (80%) is located in the head of the adult fly. An analysis of enzyme activity during development in Drosophila has revealed the presence of a relatively small peak of activity at pupariation and a much larger peak that appears at about the time of eclosion. Enzyme activity declines rapidly as the fly ages. Analyses for the production of the typical pteridine pigments of Drosophila have indicated that the small peak of GTP cyclohydrolase activity evident at pupariation coincides with the appearance of isoxanthopterin, sepiapterin, and pterin, and the larger peak at eclosion roughly corresponds to the accumulation of drosopterin as well as to the appearance in larger amounts of pterin and sepiapterin. These observations strongly suggest that in Drosophila, like bacteria, GTP cyclohydrolase is involved in the biosynthesis of pteridines. Analyses of a variety of zeste mutants of Drosophila melanogaster have shown that these mutants all contain GTP cyclohydrolase equal approximately to the amount found in the wild-type fly. These observations do not support the suggestions made by Rasmusson et al. (1973) that zeste is the structural locus for GTP cyclohydrolase.Type of Medium: Electronic ResourceURL: -
14Staff View
ISSN: 1617-4623Source: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Summary Drosophila melanogaster cells and tissues respond to heat shock by dramatically altering their pattern of transcription and translation, leading to the rapid synthesis of a small number of polypeptides, the heat shock proteins (hsps). By using cloned hsp DNA we have detected sequences complementary to heat shock genes in RNA prepared from non-heat-shocked animals of different developmental stages. Hsp 83 mRNA is present at high levels in all stages examined. Hsp 68 and 70 mRNAs are present at very low levels in most stages and at slightly higher concentration in pupae. Hsp 26 and 27 mRNAs are detected in embryos. Hsp 23, 26 and 27 mRNA are barely detectable in early third instar larvae but are major components of late third instar and early pupal RNA. Hsp 22 mRNA is also detected in early pupae. Later in development the levels of the small hsp mRNAs decrease but a further peak in abundance of hsp 26 and 27 mRNAs is found in mature adult females.Type of Medium: Electronic ResourceURL: -
15Reuter, G. ; Gausz, J. ; Gyurkovics, H. ; Friede, B. ; Bang, R. ; Spierer, A. ; Hall, L. M. C. ; Spierer, P.
Springer
Published 1987Staff ViewISSN: 1617-4623Keywords: Drosophila melanogaster ; Position-effect variegation ; Cytogenetic mappingSource: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Summary Four dominant suppressor and one enhancer of variegation loci were mapped in the polytene chromosome region extending from section 86C to section 88B of the Drosophila melanogaster third chromosome using a set of deficiencies. The suppressor locus Su-var(3) 14 maps in 86CD, Su-var(3) 13 in 86F4-7, Su-var(3)6 in 87B4-7 and Su-var(3)7 in 87E4-5. The enhancer locus E-var(3)3 maps in 87E12-F11. Su-var(3)13, Su-var(3)6 and Su-var(3)7 are also defined by point mutant alleles originally identified by other criteria (Reuter et al. 1986). Duplications covering the suppressor loci Su-var(3)14, Su-var(3)13, Su-var(3)6 and Su-var(3)7 were found to reduce considerably the haplo-abnormal effect of heterozygous point mutants of the corresponding loci. One suppressor locus, Su-var(3)7, maps within a region which has previously been cloned. The positions of deficiency breakpoints delimiting the suppressor locus indicate that all the necessary sequences for its function are located within 10 kb of cloned DNA.Type of Medium: Electronic ResourceURL: -
16Staff View
ISSN: 1435-4373Source: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: Abstract A combination of universal and species-specific primers was used to detect and differentiate by nested polymerase chain reaction (PCR) the four species most commonly causing bacterial meningitis. Primers recognising conserved sequences in the 16S and 23S ribosomal RNA genes were employed to amplify the 16S–23S spacer region fromNeisseria meningitidis, Haemophilus influenzae (type b),Streptococcus pneumoniae, andStreptococcus agalactiae (group B streptococcus). The sequence of the most abundant spacer product was determined in each case and used to deduce species-specific primers. A nested PCR using universal primers in the first round and a species-specific primer in the second were able to detect and distinguish between the four common pathogens, in the presence of human DNA.Streptococcus pneumoniae DNA was detected in the cerebrospinal fluid of a meningitis patient with negative culture and Gram-stain results.Type of Medium: Electronic ResourceURL: