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  • 1
    Publication Date: 2019-07-13
    Description: An inexpensive, laboratory-based, strain gauge valve gape monitor (SGM) was developed to monitor the valve gape behavior of bivalve molluscs in response to diel-cycling hypoxia. A Wheatstone bridge was connected to strain gauges that were attached to the shells of oysters (Crassostrea virginica). The recorded signals allowed for the opening and closing of the bivalves to be recorded continuously over two-day periods of experimentally-induced diel-cycling hypoxia and diel-cycling changes in pH. Here, we describe a protocol for developing an inexpensive strain gauge monitor and describe, in an example laboratory experiment, how we used it to measure the valve gape behavior of Eastern oysters (C. virginica), in response to diel-cycling hypoxia and cyclical changes in pH. Valve gape was measured on oysters subjected to cyclical severe hypoxic (0.6 mg/L) dissolved oxygen conditions with and without cyclical changes in pH, cyclical mild hypoxic (1.7 mg/L) conditions and normoxic (7.3 mg/L) conditions. We demonstrate that when oysters encounter repeated diel cycles, they rapidly close their shells in response to severe hypoxia and close with a time lag to mild hypoxia. When normoxia is restored, they rapidly open again. Oysters did not respond to cyclical pH conditions superimposed on diel cycling severe hypoxia. At reduced oxygen conditions, more than one third of the oysters closed simultaneously. We demonstrate that oysters respond to diel-cycling hypoxia, which must be considered when assessing the behavior of bivalves to dissolved oxygen. The valve SGM can be used to assess responses of bivalve molluscs to changes in dissolved oxygen or contaminants. Sealing techniques to better seal the valve gape strain gauges from sea water need further improvement to increase the longevity of the sensors.
    Keywords: Astrophysics
    Type: GSFC-E-DAA-TN54019 , Journal of Visualized Experiments (e-ISSN 1940-087X); 138
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  • 2
    Publication Date: 1999-09-25
    Description: Mass mortalities due to disease outbreaks have recently affected major taxa in the oceans. For closely monitored groups like corals and marine mammals, reports of the frequency of epidemics and the number of new diseases have increased recently. A dramatic global increase in the severity of coral bleaching in 1997-98 is coincident with high El Nino temperatures. Such climate-mediated, physiological stresses may compromise host resistance and increase frequency of opportunistic diseases. Where documented, new diseases typically have emerged through host or range shifts of known pathogens. Both climate and human activities may have also accelerated global transport of species, bringing together pathogens and previously unexposed host populations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harvell, C D -- Kim, K -- Burkholder, J M -- Colwell, R R -- Epstein, P R -- Grimes, D J -- Hofmann, E E -- Lipp, E K -- Osterhaus, A D -- Overstreet, R M -- Porter, J W -- Smith, G W -- Vasta, G R -- 1PO1 ES09563/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1999 Sep 3;285(5433):1505-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ecology and Evolutionary Biology, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10498537" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aquaculture ; *Climate ; Cnidaria ; *Disease Outbreaks/*veterinary ; Humans ; Infection/epidemiology/*etiology/transmission/*veterinary ; *Marine Biology ; Oceans and Seas ; Water Pollution
    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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  • 3
    Publication Date: 1998-06-11
    Description: Veratrum alkaloids and distal inhibitors of cholesterol biosynthesis have been studied for more than 30 years as potent teratogens capable of inducing cyclopia and other birth defects. Here, it is shown that these compounds specifically block the Sonic hedgehog (Shh) signaling pathway. These teratogens did not prevent the sterol modification of Shh during autoprocessing but rather inhibited the response of target tissues to Shh, possibly acting through the sterol sensing domain within the Patched protein regulator of Shh response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cooper, M K -- Porter, J A -- Young, K E -- Beachy, P A -- New York, N.Y. -- Science. 1998 Jun 5;280(5369):1603-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9616123" target="_blank"〉PubMed〈/a〉
    Keywords: Abnormalities, Drug-Induced/etiology ; Animals ; Cell Membrane/metabolism ; Central Nervous System/drug effects/*embryology/metabolism ; Chick Embryo ; Cholesterol/biosynthesis/*metabolism ; Culture Techniques ; DNA-Binding Proteins/biosynthesis ; Endoplasmic Reticulum/metabolism ; Hedgehog Proteins ; Hepatocyte Nuclear Factor 3-beta ; Holoprosencephaly/chemically induced ; Homeodomain Proteins/biosynthesis ; LIM-Homeodomain Proteins ; Membrane Proteins/metabolism ; Muscle Proteins/biosynthesis ; Nerve Tissue Proteins/biosynthesis ; Nuclear Proteins/biosynthesis ; PAX7 Transcription Factor ; Proteins/*metabolism ; Receptors, Cell Surface ; Signal Transduction/drug effects ; Teratogens/*pharmacology ; Tomatine/analogs & derivatives/pharmacology ; *Trans-Activators ; *Transcription Factors ; Triparanol/pharmacology ; Veratrum Alkaloids/*pharmacology ; trans-1,4-Bis(2-chlorobenzaminomethyl)cyclohexane Dihydrochloride/pharmacology
    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: 1991-01-18
    Description: Concerted evolution is the production and maintenance of homogeneity within repeated families of DNA. Two mechanisms--unequal crossing over and biased gene conversion--have been the principal explanations of concerted evolution. Concerted evolution of ribosomal DNA (rDNA) arrays is thought to be largely the result of unequal crossing over. However, concerted evolution of rDNA in parthenogenetic lizards of hybrid origin is strongly biased toward one of two parental sequences, which is consistent with biased gene conversion as the operative mechanism. The apparent gene conversions are independent of initial genome dosage and result in homogenization of rDNA arrays across all nucleolar organizer regions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hillis, D M -- Moritz, C -- Porter, C A -- Baker, R J -- New York, N.Y. -- Science. 1991 Jan 18;251(4991):308-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Texas, Austin 78712.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1987647" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Blotting, Southern ; DNA, Ribosomal/*genetics ; Gene Conversion ; Karyotyping ; Lizards ; Nucleic Acid Hybridization ; Parthenogenesis ; Restriction Mapping
    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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  • 5
    Publication Date: 2015-03-25
    Description: No large group of recently extinct placental mammals remains as evolutionarily cryptic as the approximately 280 genera grouped as 'South American native ungulates'. To Charles Darwin, who first collected their remains, they included perhaps the 'strangest animal[s] ever discovered'. Today, much like 180 years ago, it is no clearer whether they had one origin or several, arose before or after the Cretaceous/Palaeogene transition 66.2 million years ago, or are more likely to belong with the elephants and sirenians of superorder Afrotheria than with the euungulates (cattle, horses, and allies) of superorder Laurasiatheria. Morphology-based analyses have proved unconvincing because convergences are pervasive among unrelated ungulate-like placentals. Approaches using ancient DNA have also been unsuccessful, probably because of rapid DNA degradation in semitropical and temperate deposits. Here we apply proteomic analysis to screen bone samples of the Late Quaternary South American native ungulate taxa Toxodon (Notoungulata) and Macrauchenia (Litopterna) for phylogenetically informative protein sequences. For each ungulate, we obtain approximately 90% direct sequence coverage of type I collagen alpha1- and alpha2-chains, representing approximately 900 of 1,140 amino-acid residues for each subunit. A phylogeny is estimated from an alignment of these fossil sequences with collagen (I) gene transcripts from available mammalian genomes or mass spectrometrically derived sequence data obtained for this study. The resulting consensus tree agrees well with recent higher-level mammalian phylogenies. Toxodon and Macrauchenia form a monophyletic group whose sister taxon is not Afrotheria or any of its constituent clades as recently claimed, but instead crown Perissodactyla (horses, tapirs, and rhinoceroses). These results are consistent with the origin of at least some South American native ungulates from 'condylarths', a paraphyletic assembly of archaic placentals. With ongoing improvements in instrumentation and analytical procedures, proteomics may produce a revolution in systematics such as that achieved by genomics, but with the possibility of reaching much further back in time.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Welker, Frido -- Collins, Matthew J -- Thomas, Jessica A -- Wadsley, Marc -- Brace, Selina -- Cappellini, Enrico -- Turvey, Samuel T -- Reguero, Marcelo -- Gelfo, Javier N -- Kramarz, Alejandro -- Burger, Joachim -- Thomas-Oates, Jane -- Ashford, David A -- Ashton, Peter D -- Rowsell, Keri -- Porter, Duncan M -- Kessler, Benedikt -- Fischer, Roman -- Baessmann, Carsten -- Kaspar, Stephanie -- Olsen, Jesper V -- Kiley, Patrick -- Elliott, James A -- Kelstrup, Christian D -- Mullin, Victoria -- Hofreiter, Michael -- Willerslev, Eske -- Hublin, Jean-Jacques -- Orlando, Ludovic -- Barnes, Ian -- MacPhee, Ross D E -- England -- Nature. 2015 Jun 4;522(7554):81-4. doi: 10.1038/nature14249. Epub 2015 Mar 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] BioArCh, University of York, York YO10 5DD, UK [2] Department of Human Evolution, Max Planck Institute for Evolutionary Anthropology, 04103 Leipzig, Germany. ; BioArCh, University of York, York YO10 5DD, UK. ; Department of Earth Sciences, Natural History Museum, London SW7 5BD, UK. ; Centre for GeoGenetics, Natural History Museum of Denmark, University of Copenhagen, Oster Voldgade 5-7, 1350 Copenhagen K, Denmark. ; Institute of Zoology, Zoological Society of London, London NW1 4RY, UK. ; CONICET- Division Paleontologia de Vertebrados, Museo de La Plata. Facultad de Ciencias Naturales y Museo de La Plata, Universidad Nacional de La Plata. Paseo del Bosque s/n, B1900FWA, La Plata, Argentina. ; Seccion Paleontologia de Vertebrados. Museo Argentino de Ciencias Naturales "Bernardino Rivadavia", 470 Angel Gallardo Av., C1405DJR, Buenos Aires, Argentina. ; Institute of Anthropology, Johannes Gutenberg-University, Anselm-Franz-von-Bentzel-Weg 7, D-55128 Mainz, Germany. ; Department of Chemistry, University of York, York YO10 5DD, UK. ; Bioscience Technology Facility, Department of Biology, University of York, York YO10 5DD, UK. ; Department of Biological Sciences, Virginia Polytechnic Institute and State University, Blacksburg, Virginia 24061, USA. ; Target Discovery Institute, Nuffield Department of Medicine, University of Oxford, Roosevelt Drive, Oxford OX3 7FZ, UK. ; Applications Development, Bruker Daltonik GmbH, 28359 Bremen, Germany. ; Novo Nordisk Foundation Center for Protein Research, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3b, 2200 Copenhagen, Denmark. ; Department of Materials Science and Metallurgy, University of Cambridge, Cambridge CB3 0FS, UK. ; Smurfit Institute of Genetics, Trinity College Dublin, Dublin 2, Ireland. ; 1] BioArCh, University of York, York YO10 5DD, UK [2] Institute for Biochemistry and Biology, Karl-Liebknecht-Strasse 24-25, 14476 Potsdam OT Golm, Germany. ; Department of Human Evolution, Max Planck Institute for Evolutionary Anthropology, 04103 Leipzig, Germany. ; Department of Mammalogy, American Museum of Natural History, New York, New York 10024, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25799987" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bone and Bones/chemistry ; Cattle ; Collagen Type I/*chemistry/genetics ; Female ; *Fossils ; Mammals/*classification ; Perissodactyla/classification ; *Phylogeny ; Placenta ; Pregnancy ; Proteomics ; South America
    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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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1996-10-11
    Description: Hedgehog (Hh) proteins comprise a family of secreted signaling molecules essential for patterning a variety of structures in animal embryogenesis. During biosynthesis, Hh undergoes an autocleavage reaction, mediated by its carboxyl-terminal domain, that produces a lipid-modified amino-terminal fragment responsible for all known Hh signaling activity. Here it is reported that cholesterol is the lipophilic moiety covalently attached to the amino-terminal signaling domain during autoprocessing and that the carboxyl-terminal domain acts as an intramolecular cholesterol transferase. This use of cholesterol to modify embryonic signaling proteins may account for some of the effects of perturbed cholesterol biosynthesis on animal development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Porter, J A -- Young, K E -- Beachy, P A -- New York, N.Y. -- Science. 1996 Oct 11;274(5285):255-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8824192" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cells, Cultured ; Cholesterol/*metabolism ; Dithiothreitol/pharmacology ; Drosophila ; *Drosophila Proteins ; *Embryonic Induction ; Embryonic and Fetal Development ; Hedgehog Proteins ; Humans ; Protein Processing, Post-Translational ; Proteins/genetics/*metabolism ; Signal Transduction ; *Trans-Activators
    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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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-11-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maruyama, Y -- Fontanesi, J -- Porter, A T -- Wierzbicki, J G -- Gaspar, L -- New York, N.Y. -- Science. 1994 Nov 4;266(5186):714-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973620" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Boron Neutron Capture Therapy ; Brain Neoplasms/*radiotherapy ; Californium/*therapeutic use ; Humans ; Neutron Capture Therapy/*methods ; Rats
    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
    Publication Date: 1994-12-02
    Description: Extracellular signaling proteins encoded by the hedgehog (hh) multigene family are responsible for the patterning of a variety of embryonic structures in vertebrates and invertebrates. The Drosophila hh gene has now been shown to generate two predominant protein species that are derived by an internal autoproteolytic cleavage of a larger precursor. Mutations that reduced the efficiency of autoproteolysis in vitro diminished precursor cleavage in vivo and also impaired the signaling and patterning activities of the HH protein. The two HH protein species exhibited distinctive biochemical properties and tissue distribution, and these differences suggest a mechanism that could account for the long- and short-range signaling activities of HH in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, J J -- Ekker, S C -- von Kessler, D P -- Porter, J A -- Sun, B I -- Beachy, P A -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1528-37.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7985023" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Drosophila/embryology/genetics/*metabolism ; *Drosophila Proteins ; Embryo, Nonmammalian/*metabolism ; Embryonic Induction ; Gene Expression Regulation, Developmental ; Genes, Insect ; Hedgehog Proteins ; Models, Biological ; Molecular Sequence Data ; Mutation ; Protein Precursors/chemistry/genetics/metabolism ; *Protein Processing, Post-Translational ; Proteins/chemistry/genetics/*metabolism ; Serine Endopeptidases/chemistry ; *Signal Transduction
    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: 1993-11-12
    Description: Calmodulin is a highly conserved regulatory protein found in all eukaryotic organisms which mediates a variety of calcium ion-dependent signalling pathways. In the Drosophila retina, calmodulin was concentrated in the photoreceptor cell microvillar structure, the rhabdomere, and was found in lower amounts in the sub-rhabdomeral cytoplasm. This calmodulin localization was dependent on the NINAC (neither inactivation nor afterpotential C) unconventional myosins. Mutant flies lacking the rhabdomere-specific p174 NINAC protein did not concentrate calmodulin in the rhabdomere, whereas flies lacking the sub-rhabdomeral p132 isoform had no detectable cytoplasmic calmodulin. Furthermore, a defect in vision resulted when calmodulin was not concentrated in the rhabdomeres, suggesting a role for calmodulin in the regulation of fly phototransduction. A general function of unconventional myosins may be to control the subcellular distribution of calmodulin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Porter, J A -- Yu, M -- Doberstein, S K -- Pollard, T D -- Montell, C -- EY08117/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 12;262(5136):1038-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235618" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Calmodulin/*metabolism ; Drosophila ; *Drosophila Proteins ; Electroretinography ; Eye Proteins/*metabolism ; Mutation ; *Myosin Heavy Chains ; Myosins/*metabolism ; Nerve Degeneration ; Photoreceptor Cells, Invertebrate/*metabolism ; Retina/metabolism
    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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  • 10
    Publication Date: 2015-07-04
    Description: Whereas the predominant shapes of most animal tails are cylindrical, seahorse tails are square prisms. Seahorses use their tails as flexible grasping appendages, in spite of a rigid bony armor that fully encases their bodies. We explore the mechanics of two three-dimensional-printed models that mimic either the natural (square prism) or hypothetical (cylindrical) architecture of a seahorse tail to uncover whether or not the square geometry provides any functional advantages. Our results show that the square prism is more resilient when crushed and provides a mechanism for preserving articulatory organization upon extensive bending and twisting, as compared with its cylindrical counterpart. Thus, the square architecture is better than the circular one in the context of two integrated functions: grasping ability and crushing resistance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Porter, Michael M -- Adriaens, Dominique -- Hatton, Ross L -- Meyers, Marc A -- McKittrick, Joanna -- New York, N.Y. -- Science. 2015 Jul 3;349(6243):aaa6683. doi: 10.1126/science.aaa6683. Epub 2015 Jul 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Mechanical Engineering, Clemson University, Clemson, SC 29634, USA. mmporte@clemson.edu. ; Evolutionary Morphology of Vertebrates, Ghent University, K.L. Ledeganckstraat 35, B-9000 Ghent, Belgium. ; School of Mechanical, Industrial, and Manufacturing Engineering, Oregon State University, Corvallis, OR 97330, USA. ; Materials Science and Engineering Program, University of California, San Diego, La Jolla, CA 92093, USA. Department of Mechanical and Aerospace Engineering, University of California, San Diego, La Jolla, CA 92093, USA. Department of NanoEngineering, University of California, San Diego, La Jolla, CA 92093, USA. ; Materials Science and Engineering Program, University of California, San Diego, La Jolla, CA 92093, USA. Department of Mechanical and Aerospace Engineering, University of California, San Diego, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26138983" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Bioengineering ; Biomechanical Phenomena ; Computer Simulation ; Models, Anatomic ; Printing, Three-Dimensional ; Smegmamorpha/*anatomy & histology/*physiology ; Tail/*anatomy & histology/*physiology
    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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