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  • Articles  (21)
  • Humans  (14)
  • Seawater/*chemistry  (7)
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  • Articles  (21)
  • 1
    Publication Date: 1999-11-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Brien, S J -- Eisenberg, J F -- Miyamoto, M -- Hedges, S B -- Kumar, S -- Wilson, D E -- Menotti-Raymond, M -- Murphy, W J -- Nash, W G -- Lyons, L A -- Menninger, J C -- Stanyon, R -- Wienberg, J -- Copeland, N G -- Jenkins, N A -- Gellin, J -- Yerle, M -- Andersson, L -- Womack, J -- Broad, T -- Postlethwait, J -- Serov, O -- Bailey, E -- James, M R -- Marshall Graves, J A -- New York, N.Y. -- Science. 1999 Oct 15;286(5439):463-78.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Cancer Institute, Frederick, MD, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10577209" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Chromosome Mapping ; Chromosome Painting ; *Genome ; *Genome, Human ; Humans ; Mammals/*genetics ; Nucleic Acid Hybridization ; Phylogeny
    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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  • 2
    Publication Date: 2001-07-21
    Description: Genetic variability of Plasmodium falciparum underlies its transmission success and thwarts efforts to control disease caused by this parasite. Genetic variation in antigenic, drug resistance, and pathogenesis determinants is abundant, consistent with an ancient origin of P. falciparum, whereas DNA variation at silent (synonymous) sites in coding sequences appears virtually absent, consistent with a recent origin of the parasite. To resolve this paradox, we analyzed introns and demonstrated that these are deficient in single-nucleotide polymorphisms, as are synonymous sites in coding regions. These data establish the recent origin of P. falciparum and further provide an explanation for the abundant diversity observed in antigen and other selected genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Volkman, S K -- Barry, A E -- Lyons, E J -- Nielsen, K M -- Thomas, S M -- Choi, M -- Thakore, S S -- Day, K P -- Wirth, D F -- Hartl, D L -- New York, N.Y. -- Science. 2001 Jul 20;293(5529):482-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Harvard-Oxford Malaria Genome Diversity Project, Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11463913" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Agriculture ; Alternative Splicing ; Animals ; Base Sequence ; *Biological Evolution ; Genes, Protozoan ; *Genetic Variation ; Humans ; *Introns ; Malaria, Falciparum/epidemiology/parasitology/transmission ; *Microsatellite Repeats ; Molecular Sequence Data ; Mutation ; Plasmodium/genetics ; Plasmodium falciparum/*genetics ; *Polymorphism, Single Nucleotide
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 1998-06-20
    Description: The shaker-2 mouse mutation, the homolog of human DFNB3, causes deafness and circling behavior. A bacterial artificial chromosome (BAC) transgene from the shaker-2 critical region corrected the vestibular defects, deafness, and inner ear morphology of shaker-2 mice. An unconventional myosin gene, Myo15, was discovered by DNA sequencing of this BAC. Shaker-2 mice were found to have an amino acid substitution at a highly conserved position within the motor domain of this myosin. Auditory hair cells of shaker-2 mice have very short stereocilia and a long actin-containing protrusion extending from their basal end. This histopathology suggests that Myo15 is necessary for actin organization in the hair cells of the cochlea.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Probst, F J -- Fridell, R A -- Raphael, Y -- Saunders, T L -- Wang, A -- Liang, Y -- Morell, R J -- Touchman, J W -- Lyons, R H -- Noben-Trauth, K -- Friedman, T B -- Camper, S A -- Z01 DC 00035/DC/NIDCD NIH HHS/ -- Z01 DC 00038/DC/NIDCD NIH HHS/ -- Z01 DC 02407/DC/NIDCD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 May 29;280(5368):1444-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Genetics, 4701 MSRB III, University of Michigan, 1500 West Medical Center Drive, Ann Arbor, MI 48109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9603735" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Brain/metabolism ; Chromosomes, Bacterial ; Deafness/*genetics/pathology/therapy ; Ear, Inner/metabolism ; Female ; Genetic Complementation Test ; Hair Cells, Auditory/ultrastructure ; Humans ; Liver/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Mutant Strains ; Mice, Transgenic ; Myosins/chemistry/*genetics/metabolism ; Phenotype ; Point Mutation ; Transgenes
    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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  • 4
    Publication Date: 2008-02-15
    Description: Choanoflagellates are the closest known relatives of metazoans. To discover potential molecular mechanisms underlying the evolution of metazoan multicellularity, we sequenced and analysed the genome of the unicellular choanoflagellate Monosiga brevicollis. The genome contains approximately 9,200 intron-rich genes, including a number that encode cell adhesion and signalling protein domains that are otherwise restricted to metazoans. Here we show that the physical linkages among protein domains often differ between M. brevicollis and metazoans, suggesting that abundant domain shuffling followed the separation of the choanoflagellate and metazoan lineages. The completion of the M. brevicollis genome allows us to reconstruct with increasing resolution the genomic changes that accompanied the origin of metazoans.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2562698/" 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/PMC2562698/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, Nicole -- Westbrook, M Jody -- Young, Susan L -- Kuo, Alan -- Abedin, Monika -- Chapman, Jarrod -- Fairclough, Stephen -- Hellsten, Uffe -- Isogai, Yoh -- Letunic, Ivica -- Marr, Michael -- Pincus, David -- Putnam, Nicholas -- Rokas, Antonis -- Wright, Kevin J -- Zuzow, Richard -- Dirks, William -- Good, Matthew -- Goodstein, David -- Lemons, Derek -- Li, Wanqing -- Lyons, Jessica B -- Morris, Andrea -- Nichols, Scott -- Richter, Daniel J -- Salamov, Asaf -- Sequencing, J G I -- Bork, Peer -- Lim, Wendell A -- Manning, Gerard -- Miller, W Todd -- McGinnis, William -- Shapiro, Harris -- Tjian, Robert -- Grigoriev, Igor V -- Rokhsar, Daniel -- R01 CA058530/CA/NCI NIH HHS/ -- R01 CA058530-14/CA/NCI NIH HHS/ -- R01 GM077197/GM/NIGMS NIH HHS/ -- R01 HG004164/HG/NHGRI NIH HHS/ -- R01 HG004164-01/HG/NHGRI NIH HHS/ -- R37 HD028315/HD/NICHD NIH HHS/ -- England -- Nature. 2008 Feb 14;451(7180):783-8. doi: 10.1038/nature06617.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology and the Center for Integrative Genomics, University of California, Berkeley, California 94720, USA. nking@berkeley.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18273011" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Adhesion ; Conserved Sequence ; Eukaryotic Cells/classification/cytology/*metabolism ; Evolution, Molecular ; Extracellular Matrix/metabolism ; Gene Expression Regulation ; Genetic Speciation ; Genome/*genetics ; Hedgehog Proteins/chemistry/genetics ; Humans ; Introns/genetics ; Phosphotyrosine/metabolism ; *Phylogeny ; Protein Structure, Tertiary/genetics ; Receptors, Notch/chemistry/genetics ; Signal Transduction/genetics ; Transcription Factors/genetics/metabolism ; Transcription, Genetic
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 2008-03-28
    Description: Biogeochemical signatures preserved in ancient sedimentary rocks provide clues to the nature and timing of the oxygenation of the Earth's atmosphere. Geochemical data suggest that oxygenation proceeded in two broad steps near the beginning and end of the Proterozoic eon (2,500 to 542 million years ago). The oxidation state of the Proterozoic ocean between these two steps and the timing of deep-ocean oxygenation have important implications for the evolutionary course of life on Earth but remain poorly known. Here we present a new perspective on ocean oxygenation based on the authigenic accumulation of the redox-sensitive transition element molybdenum in sulphidic black shales. Accumulation of authigenic molybdenum from sea water is already seen in shales by 2,650 Myr ago; however, the small magnitudes of these enrichments reflect weak or transient sources of dissolved molybdenum before about 2,200 Myr ago, consistent with minimal oxidative weathering of the continents. Enrichments indicative of persistent and vigorous oxidative weathering appear in shales deposited at roughly 2,150 Myr ago, more than 200 million years after the initial rise in atmospheric oxygen. Subsequent expansion of sulphidic conditions after about 1,800 Myr ago (refs 8, 9) maintained a mid-Proterozoic molybdenum reservoir below 20 per cent of the modern inventory, which in turn may have acted as a nutrient feedback limiting the spatiotemporal distribution of euxinic (sulphidic) bottom waters and perhaps the evolutionary and ecological expansion of eukaryotic organisms. By 551 Myr ago, molybdenum contents reflect a greatly expanded oceanic reservoir due to oxygenation of the deep ocean and corresponding decrease in sulphidic conditions in the sediments and water column.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scott, C -- Lyons, T W -- Bekker, A -- Shen, Y -- Poulton, S W -- Chu, X -- Anbar, A D -- England -- Nature. 2008 Mar 27;452(7186):456-9. doi: 10.1038/nature06811.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth Sciences, University of California, Riverside, California 92521, USA. cscot002@ucr.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18368114" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere/chemistry ; Geologic Sediments/chemistry ; History, Ancient ; Molybdenum/analysis ; Oceans and Seas ; Oxygen/*analysis/chemistry ; Seawater/*chemistry ; Sulfides/chemistry ; Time Factors
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    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 2010-09-11
    Description: In most eukaryotic cells, subsets of microtubules are adapted for specific functions by post-translational modifications (PTMs) of tubulin subunits. Acetylation of the epsilon-amino group of K40 on alpha-tubulin is a conserved PTM on the luminal side of microtubules that was discovered in the flagella of Chlamydomonas reinhardtii. Studies on the significance of microtubule acetylation have been limited by the undefined status of the alpha-tubulin acetyltransferase. Here we show that MEC-17, a protein related to the Gcn5 histone acetyltransferases and required for the function of touch receptor neurons in Caenorhabditis elegans, acts as a K40-specific acetyltransferase for alpha-tubulin. In vitro, MEC-17 exclusively acetylates K40 of alpha-tubulin. Disruption of the Tetrahymena MEC-17 gene phenocopies the K40R alpha-tubulin mutation and makes microtubules more labile. Depletion of MEC-17 in zebrafish produces phenotypes consistent with neuromuscular defects. In C. elegans, MEC-17 and its paralogue W06B11.1 are redundantly required for acetylation of MEC-12 alpha-tubulin, and contribute to the function of touch receptor neurons partly via MEC-12 acetylation and partly via another function, possibly by acetylating another protein. In summary, we identify MEC-17 as an enzyme that acetylates the K40 residue of alpha-tubulin, the only PTM known to occur on the luminal surface of microtubules.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2938957/" 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/PMC2938957/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Akella, Jyothi S -- Wloga, Dorota -- Kim, Jihyun -- Starostina, Natalia G -- Lyons-Abbott, Sally -- Morrissette, Naomi S -- Dougan, Scott T -- Kipreos, Edward T -- Gaertig, Jacek -- R01 AI067981/AI/NIAID NIH HHS/ -- R01 AI067981-05/AI/NIAID NIH HHS/ -- R01 GM074212/GM/NIGMS NIH HHS/ -- R01 GM074212-03/GM/NIGMS NIH HHS/ -- R01 GM089912/GM/NIGMS NIH HHS/ -- R01 GM089912-01/GM/NIGMS NIH HHS/ -- R01AI067981/AI/NIAID NIH HHS/ -- R01GM074212/GM/NIGMS NIH HHS/ -- R01GM089912/GM/NIGMS NIH HHS/ -- England -- Nature. 2010 Sep 9;467(7312):218-22. doi: 10.1038/nature09324.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular Biology, University of Georgia, Athens, Georgia 30602, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20829795" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Acetyltransferases/*metabolism ; Animals ; Caenorhabditis elegans/*enzymology/metabolism ; Caenorhabditis elegans Proteins/*metabolism ; Cell Line ; Dipodomys ; Humans ; Protozoan Proteins/genetics/metabolism ; Tetrahymena/metabolism ; Touch ; Tubulin/chemistry/*metabolism ; Zebrafish/embryology/metabolism ; Zebrafish Proteins/*metabolism
    Print ISSN: 0028-0836
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    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 1990-08-10
    Description: Somatic mutations in a subset of growth hormone (GH)-secreting pituitary tumors convert the gene for the alpha polypeptide chain (alpha s) of Gs into a putative oncogene, termed gsp. These mutations, which activate alpha s by inhibiting its guanosine triphosphatase (GTPase) activity, are found in codons for either of two amino acids, each of which is completely conserved in all known G protein alpha chains. The likelihood that similar mutations would activate other G proteins prompted a survey of human tumors for mutations that replace either of these two amino acids in other G protein alpha chain genes. The first gene so far tested, which encodes the alpha chain of Gi2, showed mutations that replaced arginine-179 with either cysteine or histidine in 3 of 11 tumors of the adrenal cortex and 3 of 10 endocrine tumors of the ovary. The mutant alpha i2 gene is a putative oncogene, referred to as gip2. In addition, gsp mutations were found in 18 of 42 GH-secreting pituitary tumors and in an autonomously functioning thyroid adenoma. These findings suggest that human tumors may harbor oncogenic mutations in various G protein alpha chain genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lyons, J -- Landis, C A -- Harsh, G -- Vallar, L -- Grunewald, K -- Feichtinger, H -- Duh, Q Y -- Clark, O H -- Kawasaki, E -- Bourne, H R -- New York, N.Y. -- Science. 1990 Aug 10;249(4969):655-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Genetics, Cetus Corporation, Emeryville CA 94608.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2116665" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA, Neoplasm/genetics ; Endocrine System Diseases/*genetics ; Female ; GTP Phosphohydrolases/genetics/metabolism ; GTP-Binding Proteins/*genetics/metabolism ; Humans ; Male ; Molecular Sequence Data ; *Mutation ; Neoplasms/*genetics ; Oligonucleotide Probes ; *Oncogenes ; Pituitary Neoplasms/*genetics ; Polymerase Chain Reaction
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2008-08-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lyons, Timothy W -- New York, N.Y. -- Science. 2008 Aug 15;321(5891):923-4. doi: 10.1126/science.1162870.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth Sciences, University of California, Riverside, CA 92521, USA. timothy.lyons@ucr.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18703731" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Atmosphere ; Biological Evolution ; Geologic Sediments/chemistry ; Hydrogen Sulfide/analysis ; Ice Cover ; Iron/*analysis ; Oceans and Seas ; Oxygen/*analysis ; Seawater/*chemistry ; Sulfates/analysis ; Sulfides/analysis ; Time
    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
    Publication Date: 2009-05-13
    Description: A novel influenza A (H1N1) virus has spread rapidly across the globe. Judging its pandemic potential is difficult with limited data, but nevertheless essential to inform appropriate health responses. By analyzing the outbreak in Mexico, early data on international spread, and viral genetic diversity, we make an early assessment of transmissibility and severity. Our estimates suggest that 23,000 (range 6000 to 32,000) individuals had been infected in Mexico by late April, giving an estimated case fatality ratio (CFR) of 0.4% (range: 0.3 to 1.8%) based on confirmed and suspected deaths reported to that time. In a community outbreak in the small community of La Gloria, Veracruz, no deaths were attributed to infection, giving an upper 95% bound on CFR of 0.6%. Thus, although substantial uncertainty remains, clinical severity appears less than that seen in the 1918 influenza pandemic but comparable with that seen in the 1957 pandemic. Clinical attack rates in children in La Gloria were twice that in adults (〈15 years of age: 61%; 〉/=15 years: 29%). Three different epidemiological analyses gave basic reproduction number (R0) estimates in the range of 1.4 to 1.6, whereas a genetic analysis gave a central estimate of 1.2. This range of values is consistent with 14 to 73 generations of human-to-human transmission having occurred in Mexico to late April. Transmissibility is therefore substantially higher than that of seasonal flu, and comparable with lower estimates of R0 obtained from previous influenza pandemics.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3735127/" 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/PMC3735127/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fraser, Christophe -- Donnelly, Christl A -- Cauchemez, Simon -- Hanage, William P -- Van Kerkhove, Maria D -- Hollingsworth, T Deirdre -- Griffin, Jamie -- Baggaley, Rebecca F -- Jenkins, Helen E -- Lyons, Emily J -- Jombart, Thibaut -- Hinsley, Wes R -- Grassly, Nicholas C -- Balloux, Francois -- Ghani, Azra C -- Ferguson, Neil M -- Rambaut, Andrew -- Pybus, Oliver G -- Lopez-Gatell, Hugo -- Alpuche-Aranda, Celia M -- Chapela, Ietza Bojorquez -- Zavala, Ethel Palacios -- Guevara, Dulce Ma Espejo -- Checchi, Francesco -- Garcia, Erika -- Hugonnet, Stephane -- Roth, Cathy -- WHO Rapid Pandemic Assessment Collaboration -- G0600719/Medical Research Council/United Kingdom -- GR082623MA/Wellcome Trust/United Kingdom -- U54 GM088491/GM/NIGMS NIH HHS/ -- Biotechnology and Biological Sciences Research Council/United Kingdom -- Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2009 Jun 19;324(5934):1557-61. doi: 10.1126/science.1176062. Epub 2009 May 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Centre for Outbreak Analysis and Modelling, Department of Infectious Disease Epidemiology, Imperial College London, Faculty of Medicine, Norfolk Place, London W2 1PG, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19433588" target="_blank"〉PubMed〈/a〉
    Keywords: *Disease Outbreaks ; Global Health ; Humans ; *Influenza A Virus, H1N1 Subtype ; Influenza, Human/*epidemiology/mortality/transmission/virology ; Mexico/epidemiology ; Molecular Sequence Data ; Travel
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
    Publication Date: 2010-02-13
    Description: The Ediacaran Period (635 to 542 million years ago) was a time of fundamental environmental and evolutionary change, culminating in the first appearance of macroscopic animals. Here, we present a detailed spatial and temporal record of Ediacaran ocean chemistry for the Doushantuo Formation in the Nanhua Basin, South China. We find evidence for a metastable zone of euxinic (anoxic and sulfidic) waters impinging on the continental shelf and sandwiched within ferruginous [Fe(II)-enriched] deep waters. A stratified ocean with coeval oxic, sulfidic, and ferruginous zones, favored by overall low oceanic sulfate concentrations, was maintained dynamically throughout the Ediacaran Period. Our model reconciles seemingly conflicting geochemical redox conditions proposed previously for Ediacaran deep oceans and helps to explain the patchy temporal record of early metazoan fossils.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Chao -- Love, Gordon D -- Lyons, Timothy W -- Fike, David A -- Sessions, Alex L -- Chu, Xuelei -- New York, N.Y. -- Science. 2010 Apr 2;328(5974):80-3. doi: 10.1126/science.1182369. Epub 2010 Feb 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth Sciences, University of California, Riverside, CA 92521, USA. chaoli@ucr.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20150442" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Carbonates/analysis ; China ; Ferrous Compounds/analysis ; *Fossils ; Geologic Sediments/*chemistry ; Hydrogen Sulfide ; Iron ; Oceans and Seas ; Oxidation-Reduction ; Oxygen/*analysis ; Seawater/*chemistry ; Sulfates/analysis
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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