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  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-02-05
    Description: The sterile alpha motif (SAM) domain is a protein interaction module that is present in diverse signal-transducing proteins. SAM domains are known to form homo- and hetero-oligomers. The crystal structure of the SAM domain from an Eph receptor tyrosine kinase, EphB2, reveals two large interfaces. In one interface, adjacent monomers exchange amino-terminal peptides that insert into a hydrophobic groove on each neighbor. A second interface is composed of the carboxyl-terminal helix and a nearby loop. A possible oligomer, constructed from a combination of these binding modes, may provide a platform for the formation of larger protein complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thanos, C D -- Goodwill, K E -- Bowie, J U -- New York, N.Y. -- Science. 1999 Feb 5;283(5403):833-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉UCLA-DOE Laboratory of Structural Biology and Molecular Medicine and Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9933164" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallization ; Crystallography, X-Ray ; Dimerization ; GRB10 Adaptor Protein ; Humans ; Hydrogen Bonding ; Kinesin/metabolism ; Models, Molecular ; Myosins/metabolism ; Phosphorylation ; *Protein Conformation ; Protein Structure, Secondary ; Protein Tyrosine Phosphatases/metabolism ; Proteins/metabolism ; Receptor Aggregation ; Receptor Protein-Tyrosine Kinases/*chemistry/metabolism ; Receptor, EphB2 ; Recombinant Proteins/chemistry/metabolism ; Surface Properties
    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: 2008-05-27
    Description: Understanding the energetics of molecular interactions is fundamental to all of the central quests of structural biology including structure prediction and design, mapping evolutionary pathways, learning how mutations cause disease, drug design, and relating structure to function. Hydrogen-bonding is widely regarded as an important force in a membrane environment because of the low dielectric constant of membranes and a lack of competition from water. Indeed, polar residue substitutions are the most common disease-causing mutations in membrane proteins. Because of limited structural information and technical challenges, however, there have been few quantitative tests of hydrogen-bond strength in the context of large membrane proteins. Here we show, by using a double-mutant cycle analysis, that the average contribution of eight interhelical side-chain hydrogen-bonding interactions throughout bacteriorhodopsin is only 0.6 kcal mol(-1). In agreement with these experiments, we find that 4% of polar atoms in the non-polar core regions of membrane proteins have no hydrogen-bond partner and the lengths of buried hydrogen bonds in soluble proteins and membrane protein transmembrane regions are statistically identical. Our results indicate that most hydrogen-bond interactions in membrane proteins are only modestly stabilizing. Weak hydrogen-bonding should be reflected in considerations of membrane protein folding, dynamics, design, evolution and function.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2734483/" 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/PMC2734483/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Joh, Nathan Hyunjoong -- Min, Andrew -- Faham, Salem -- Whitelegge, Julian P -- Yang, Duan -- Woods, Virgil L -- Bowie, James U -- R01 CA081000/CA/NCI NIH HHS/ -- R01 CA081000-07/CA/NCI NIH HHS/ -- R01 CA081000-08/CA/NCI NIH HHS/ -- R01 CA081000-09/CA/NCI NIH HHS/ -- R01 GM063919/GM/NIGMS NIH HHS/ -- R01 GM063919-06/GM/NIGMS NIH HHS/ -- R01 GM063919-07/GM/NIGMS NIH HHS/ -- R01 GM063919-08/GM/NIGMS NIH HHS/ -- England -- Nature. 2008 Jun 26;453(7199):1266-70. doi: 10.1038/nature06977. Epub 2008 May 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, UCLA-DOE Center for Genomics and Proteomics, Molecular Biology Institute, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18500332" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriorhodopsins/chemistry/genetics/metabolism ; Crystallography, X-Ray ; Deuterium Exchange Measurement ; Hydrogen Bonding ; Membrane Proteins/*chemistry/genetics/*metabolism ; Models, Molecular ; Mutation/genetics ; Protein Folding ; Solubility ; Thermodynamics
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 1990-03-16
    Description: An amino acid sequence encodes a message that determines the shape and function of a protein. This message is highly degenerate in that many different sequences can code for proteins with essentially the same structure and activity. Comparison of different sequences with similar messages can reveal key features of the code and improve understanding of how a protein folds and how it performs its function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bowie, J U -- Reidhaar-Olson, J F -- Lim, W A -- Sauer, R T -- AI-15706/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1990 Mar 16;247(4948):1306-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2315699" target="_blank"〉PubMed〈/a〉
    Keywords: *Amino Acid Sequence ; Computer Graphics ; *DNA-Binding Proteins ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Proteins/*physiology/ultrastructure ; Repressor Proteins ; Structure-Activity Relationship ; Surface Properties ; Viral Proteins ; Viral Regulatory and Accessory Proteins
    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: 1991-07-12
    Description: The inverse protein folding problem, the problem of finding which amino acid sequences fold into a known three-dimensional (3D) structure, can be effectively attacked by finding sequences that are most compatible with the environments of the residues in the 3D structure. The environments are described by: (i) the area of the residue buried in the protein and inaccessible to solvent; (ii) the fraction of side-chain area that is covered by polar atoms (O and N); and (iii) the local secondary structure. Examples of this 3D profile method are presented for four families of proteins: the globins, cyclic AMP (adenosine 3',5'-monophosphate) receptor-like proteins, the periplasmic binding proteins, and the actins. This method is able to detect the structural similarity of the actins and 70- kilodalton heat shock proteins, even though these protein families share no detectable sequence similarity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bowie, J U -- Luthy, R -- Eisenberg, D -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):164-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Institute, University of California, Los Angeles 90024-1570.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1853201" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/chemistry/ultrastructure ; Algorithms ; Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry ; *Escherichia coli Proteins ; Molecular Structure ; Myoglobin/chemistry/ultrastructure ; *Periplasmic Binding Proteins ; *Protein Conformation ; Proteins/*chemistry ; Receptors, Cyclic AMP/chemistry/ultrastructure ; Structure-Activity Relationship
    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: 2006-01-28
    Description: The postsynaptic density (PSD) is a complex assembly of proteins associated with the postsynaptic membrane that organizes neurotransmitter receptors, signaling pathways, and regulatory elements within a cytoskeletal matrix. Here we show that the sterile alpha motif domain of rat Shank3/ProSAP2, a master scaffolding protein located deep within the PSD, can form large sheets composed of helical fibers stacked side by side. Zn2+, which is found in high concentrations in the PSD, binds tightly to Shank3 and may regulate assembly. Sheets of the Shank protein could form a platform for the construction of the PSD complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baron, Marisa K -- Boeckers, Tobias M -- Vaida, Bianca -- Faham, Salem -- Gingery, Mari -- Sawaya, Michael R -- Salyer, Danielle -- Gundelfinger, Eckart D -- Bowie, James U -- R01 CA081000/CA/NCI NIH HHS/ -- R01 GM063919/GM/NIGMS NIH HHS/ -- R01 GM063919-07/GM/NIGMS NIH HHS/ -- R01 GM063919-08/GM/NIGMS NIH HHS/ -- R01 GM075922/GM/NIGMS NIH HHS/ -- R01 GM075922-04/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Jan 27;311(5760):531-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, Molecular Biology Institute, University of California, Los Angeles, 611 Charles E. Young Drive East, Los Angeles, CA 90095-1570, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16439662" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/analysis/*chemistry/genetics/metabolism ; Animals ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; Hippocampus/chemistry ; Microscopy, Electron ; Models, Molecular ; Mutation ; Nerve Tissue Proteins ; Neurons/chemistry ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Rats ; Recombinant Fusion Proteins/analysis ; Solubility ; Synapses/*chemistry ; Zinc/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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  • 6
    Publication Date: 2008-06-28
    Description: Deep avian evolutionary relationships have been difficult to resolve as a result of a putative explosive radiation. Our study examined approximately 32 kilobases of aligned nuclear DNA sequences from 19 independent loci for 169 species, representing all major extant groups, and recovered a robust phylogeny from a genome-wide signal supported by multiple analytical methods. We documented well-supported, previously unrecognized interordinal relationships (such as a sister relationship between passerines and parrots) and corroborated previously contentious groupings (such as flamingos and grebes). Our conclusions challenge current classifications and alter our understanding of trait evolution; for example, some diurnal birds evolved from nocturnal ancestors. Our results provide a valuable resource for phylogenetic and comparative studies in birds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hackett, Shannon J -- Kimball, Rebecca T -- Reddy, Sushma -- Bowie, Rauri C K -- Braun, Edward L -- Braun, Michael J -- Chojnowski, Jena L -- Cox, W Andrew -- Han, Kin-Lan -- Harshman, John -- Huddleston, Christopher J -- Marks, Ben D -- Miglia, Kathleen J -- Moore, William S -- Sheldon, Frederick H -- Steadman, David W -- Witt, Christopher C -- Yuri, Tamaki -- New York, N.Y. -- Science. 2008 Jun 27;320(5884):1763-8. doi: 10.1126/science.1157704.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zoology Department, Field Museum of Natural History, 1400 South Lake Shore Drive, Chicago, IL 60605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18583609" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Animals ; Biological Evolution ; Birds/*classification/*genetics ; Ecosystem ; Flight, Animal ; *Genome ; *Genomics ; Molecular Sequence Data ; *Phylogeny ; Sequence Alignment ; Sequence Analysis, DNA
    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
    Publication Date: 2014-05-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rocha, L A -- Aleixo, A -- Allen, G -- Almeda, F -- Baldwin, C C -- Barclay, M V L -- Bates, J M -- Bauer, A M -- Benzoni, F -- Berns, C M -- Berumen, M L -- Blackburn, D C -- Blum, S -- Bolanos, F -- Bowie, R C K -- Britz, R -- Brown, R M -- Cadena, C D -- Carpenter, K -- Ceriaco, L M -- Chakrabarty, P -- Chaves, G -- Choat, J H -- Clements, K D -- Collette, B B -- Collins, A -- Coyne, J -- Cracraft, J -- Daniel, T -- de Carvalho, M R -- de Queiroz, K -- Di Dario, F -- Drewes, R -- Dumbacher, J P -- Engilis, A Jr -- Erdmann, M V -- Eschmeyer, W -- Feldman, C R -- Fisher, B L -- Fjeldsa, J -- Fritsch, P W -- Fuchs, J -- Getahun, A -- Gill, A -- Gomon, M -- Gosliner, T -- Graves, G R -- Griswold, C E -- Guralnick, R -- Hartel, K -- Helgen, K M -- Ho, H -- Iskandar, D T -- Iwamoto, T -- Jaafar, Z -- James, H F -- Johnson, D -- Kavanaugh, D -- Knowlton, N -- Lacey, E -- Larson, H K -- Last, P -- Leis, J M -- Lessios, H -- Liebherr, J -- Lowman, M -- Mahler, D L -- Mamonekene, V -- Matsuura, K -- Mayer, G C -- Mays, H Jr -- McCosker, J -- McDiarmid, R W -- McGuire, J -- Miller, M J -- Mooi, R -- Mooi, R D -- Moritz, C -- Myers, P -- Nachman, M W -- Nussbaum, R A -- Foighil, D O -- Parenti, L R -- Parham, J F -- Paul, E -- Paulay, G -- Perez-Eman, J -- Perez-Matus, A -- Poe, S -- Pogonoski, J -- Rabosky, D L -- Randall, J E -- Reimer, J D -- Robertson, D R -- Rodel, M-O -- Rodrigues, M T -- Roopnarine, P -- Ruber, L -- Ryan, M J -- Sheldon, F -- Shinohara, G -- Short, A -- Simison, W B -- Smith-Vaniz, W F -- Springer, V G -- Stiassny, M -- Tello, J G -- Thompson, C W -- Trnski, T -- Tucker, P -- Valqui, T -- Vecchione, M -- Verheyen, E -- Wainwright, P C -- Wheeler, T A -- White, W T -- Will, K -- Williams, J T -- Williams, G -- Wilson, E O -- Winker, K -- Winterbottom, R -- Witt, C C -- New York, N.Y. -- Science. 2014 May 23;344(6186):814-5. doi: 10.1126/science.344.6186.814.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉California Academy of Sciences, San Francisco, CA 94118, USA. LRocha@calacademy.org. ; Museu Paraense Emilio Goeldi, Belem, PA, 66040-170, Brazil. ; Western Australian Museum, Perth, WA, 6986, Australia. ; California Academy of Sciences, San Francisco, CA 94118, USA. ; Smithsonian Institution, Washington, DC 20560, USA. ; Natural History Museum, London, SW7 5BD, UK. ; Field Museum of Natural History, Chicago, IL 60605, USA. ; Villanova University, Villanova, PA 19085, USA. ; University of Milano-Bicocca, Milan, 20126, Italy. ; Utica College, Utica, NY 13502, USA. ; King Abdullah University of Science and Technology, Thuwal, 23955, Saudi Arabia. ; Universidad de Costa Rica, San Jose, 11501-2060, Costa Rica. ; University of California, Berkeley, CA 94720-3161, USA. ; University of Kansas, Lawrence, KS 66045, USA. ; Universidad de los Andes, Bogota, 4976, Colombia. ; Old Dominion University, Norfolk, VA 23529, USA. ; Museu Nacional de Historia Natural e da Ciencia, Lisbon, 7005-638, Portugal. ; Louisiana State University, Baton Rouge, LA 70803, USA. ; James Cook University, Townsville, 4811, Australia. ; University of Auckland, Auckland, 1142, New Zealand. ; NOAA Systematics Laboratory, Washington, DC 20013, USA. ; University of Chicago, Chicago, IL 60637, USA. ; American Museum of Natural History, New York, NY 10024, USA. ; Universidade de Sao Paulo, Sao Paulo, SP, 05508-090, Brazil. ; Universidade Federal do Rio de Janeiro, Macae, RJ, 27965-045, Brazil. ; University of California, Davis, CA 95616, USA. ; Conservation International, Denpasar, Bali, 80235, Indonesia. ; University of Nevada, Reno, NV 89557-0314, USA. ; Natural History Museum of Denmark, Copenhagen, DK-2100, Denmark. ; Museum National d'Histoire Naturelle, Paris, 75005, France. ; Addis Ababa University, Addis Ababa, 1176, Ethiopia. ; University of Sydney, Sydney, NSW, 2006, Australia. ; Museum Victoria, Melbourne, 3001, VIC, Australia. ; University of Colorado, Boulder, CO 80309-0334, USA. ; Harvard University, Cambridge, MA 02138, USA. ; Smithsonian Institution, Washington, DC 20560, USA. National University of Singapore, 117543, Singapore. ; Museum and Art Gallery of the Northern Territory, Darwin, 0820, NT, Australia. ; CSIRO Marine & Atmospheric Research, Hobart, TAS, 7000, Australia. ; Australian Museum, Sydney, NSW, 2010, Australia. ; Smithsonian Tropical Research Institute, Balboa, 0843-03092, Panama. ; Cornell University, Ithaca, NY 14853, USA. ; Universite Marien Ngouabi, Brazzaville, B.P. 69, Republic of Congo. ; National Museum of Nature and Science, Tsukuba, 305-0005, Japan. ; University of Wisconsin-Parkside, Kenosha, WI 53141-2000, USA. ; Cincinnati Museum Center, Cincinnati, OH 45203, USA. ; The Manitoba Museum, Winnipeg, MB, R3B 0N2, Canada. ; Australian National University, Canberra, ACT, 0200, Australia. ; University of Michigan, Ann Arbor, MI 48109-1079, USA. ; California State University, Fullerton, CA 92831, USA. ; The Ornithological Council, Chevy Chase, MD 20815, USA. ; University of Florida, Gainesville, fl32611, USA. ; Universidad Central de Venezuela, Caracas, 1041, Venezuela. ; Pontif cia Universidad Catolica de Chile, Santiago 6513677, Chile. ; University of New Mexico, Albuquerque, NM 87131-0001, USA. ; Bernice P. Bishop Museum, Honolulu, HI 96817, USA. ; University of the Ryukyus, Nishihara, 903-0213, Japan. ; Museum fur Naturkunde, Berlin, 10115, Germany. ; Naturhistorisches Museum der Burgergemeinde Bern, Bern, CH-3005, Switzerland. ; American Museum of Natural History, New York, NY 10024, USA. Long Island University, Brooklyn, NY 11201-8423, USA. ; Auckland Museum, Auckland, 1142, New Zealand. ; Centro de Ornitologia y Biodiversidad, Lima, 33, Peru. ; Royal Belgian Institute of Natural Sciences, Brussels, 1000, Belgium. ; McGill University, Montreal, QC, H9X 3V9, Canada. ; University of Alaska Museum, Fairbanks, AK 99775, USA. ; Royal Ontario Museum, Toronto, ON, M5S 2C6, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24855245" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biology/*methods ; Classification/*methods ; *Endangered Species ; *Extinction, Biological
    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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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2013-01-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bowie, James U -- R01GM063919/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2013 Jan 25;339(6118):398-9. doi: 10.1126/science.1228655.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, UCLA-DOE Institute of Genomics and Proteomics, University of California, Los Angeles, Los Angeles, CA 90095, USA. bowie@mbi.ucla.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23349275" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Membrane/*chemistry ; Hydrogen Bonding ; Lipid Bilayers/chemistry ; Membrane Proteins/*chemistry ; Models, Molecular ; Protein Conformation ; *Protein Folding ; Protein Structure, Secondary ; Protein Subunits/chemistry
    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: 2022-05-25
    Description: © The Author(s), 2018. This article is distributed under the terms of the Creative Commons Attribution License. The definitive version was published in Chemical Geology 493 (2018): 210-223, doi:10.1016/j.chemgeo.2018.05.040.
    Description: The GEOTRACES Intermediate Data Product 2017 (IDP2017) is the second publicly available data product of the international GEOTRACES programme, and contains data measured and quality controlled before the end of 2016. The IDP2017 includes data from the Atlantic, Pacific, Arctic, Southern and Indian oceans, with about twice the data volume of the previous IDP2014. For the first time, the IDP2017 contains data for a large suite of biogeochemical parameters as well as aerosol and rain data characterising atmospheric trace element and isotope (TEI) sources. The TEI data in the IDP2017 are quality controlled by careful assessment of intercalibration results and multi-laboratory data comparisons at crossover stations. The IDP2017 consists of two parts: (1) a compilation of digital data for more than 450 TEIs as well as standard hydrographic parameters, and (2) the eGEOTRACES Electronic Atlas providing an on-line atlas that includes more than 590 section plots and 130 animated 3D scenes. The digital data are provided in several formats, including ASCII, Excel spreadsheet, netCDF, and Ocean Data View collection. Users can download the full data packages or make their own custom selections with a new on-line data extraction service. In addition to the actual data values, the IDP2017 also contains data quality flags and 1-σ data error values where available. Quality flags and error values are useful for data filtering and for statistical analysis. Metadata about data originators, analytical methods and original publications related to the data are linked in an easily accessible way. The eGEOTRACES Electronic Atlas is the visual representation of the IDP2017 as section plots and rotating 3D scenes. The basin-wide 3D scenes combine data from many cruises and provide quick overviews of large-scale tracer distributions. These 3D scenes provide geographical and bathymetric context that is crucial for the interpretation and assessment of tracer plumes near ocean margins or along ridges. The IDP2017 is the result of a truly international effort involving 326 researchers from 25 countries. This publication provides the critical reference for unpublished data, as well as for studies that make use of a large cross-section of data from the IDP2017. This article is part of a special issue entitled: Conway GEOTRACES - edited by Tim M. Conway, Tristan Horner, Yves Plancherel, and Aridane G. González.
    Description: We gratefully acknowledge financial support by the Scientific Committee on Oceanic Research (SCOR) through grants from the U.S. National Science Foundation, including grants OCE-0608600, OCE-0938349, OCE-1243377, and OCE-1546580. Financial support was also provided by the UK Natural Environment Research Council (NERC), the Ministry of Earth Science of India, the Centre National de Recherche Scientifique, l'Université Paul Sabatier de Toulouse, the Observatoire Midi-Pyrénées Toulouse, the Universitat Autònoma de Barcelona, the Kiel Excellence Cluster The Future Ocean, the Swedish Museum of Natural History, The University of Tokyo, The University of British Columbia, The Royal Netherlands Institute for Sea Research, the GEOMAR-Helmholtz Centre for Ocean Research Kiel, and the Alfred Wegener Institute.
    Keywords: GEOTRACES ; Trace elements ; Isotopes ; Electronic atlas ; IDP2017
    Repository Name: Woods Hole Open Access Server
    Type: Article
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  • 10
    Publication Date: 2022-05-25
    Description: Author Posting. © The Author(s), 2011. This is the author's version of the work. It is posted here by permission of Elsevier B.V. for personal use, not for redistribution. The definitive version was published in Marine Chemistry 126 (2011): 108-113, doi:10.1016/j.marchem.2011.04.004.
    Description: Photosynthesis by marine phytoplankton requires bioavailable forms of several trace elements that are found in extremely low concentrations in the open ocean. We have compared the concentration, lability and size distribution (〈 1 nm and 〈 10 nm) of a suite of trace elements that are thought to be limiting to primary productivity as well as a toxic element (Pb) in two High Nutrient Low Chlorophyll (HNLC) regions using a new dynamic speciation technique, Diffusive Gradients in Thin-film (DGT). The labile species trapped within the DGT probes have a size that is smaller or similar than the pore size of algal cell walls and thus present a proxy for bioavailable species. Total Dissolvable trace element concentrations (TD concentration) varied between 0.05 nM (Co) and 4.0 nM (Ni) at K2 (Northwest Pacific Ocean) and between 0.026 nM (Co) and 4.7 nM (Ni) in the Southern Ocean. The smallest size fractionated labile concentrations (〈 1 nm) observed at Southern Ocean sampling stations ranged between 0.002 nM (Co) and 2.1 nM (Ni). Moreover, large differences in bioavailable fractions (ratio of labile to TD concentration) were observed between the trace elements. In the Northwest Pacific Ocean Fe, Cu and Mn had lower labile fractions (between 10 and 44%) than Co, Cd, Ni and Pb (between 80 and 100%). In the Southern Ocean a similar trend was observed, and in addition: (1) Co, Cd, Ni and Pb have lower labile fractions in the Southern Ocean than in the Northwest Pacific and (2) the ratios of 〈1nm to dissolvable element concentrations at some Southern Ocean stations were very low and varied between 4 and16 %.
    Description: This research was supported by Federal Science Policy Office, Brussels, through contracts EV/03/7A, SD/CA/03A, the Research Foundation Flanders through grant G.0021.04 and Vrije Universiteit Brussel via grant GOA 22, as well as for K2, the VERTIGO program funding primarily by the US National Science Foundation programs in Chemical and Biological Oceanography
    Keywords: Trace elements ; Speciation ; Bioavailability ; Pacific Ocean ; Southern Ocean
    Repository Name: Woods Hole Open Access Server
    Type: Preprint
    Format: application/pdf
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