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  • 1
    Publication Date: 2008-03-07
    Description: Long-held ideas regarding the evolutionary relationships among animals have recently been upended by sometimes controversial hypotheses based largely on insights from molecular data. These new hypotheses include a clade of moulting animals (Ecdysozoa) and the close relationship of the lophophorates to molluscs and annelids (Lophotrochozoa). Many relationships remain disputed, including those that are required to polarize key features of character evolution, and support for deep nodes is often low. Phylogenomic approaches, which use data from many genes, have shown promise for resolving deep animal relationships, but are hindered by a lack of data from many important groups. Here we report a total of 39.9 Mb of expressed sequence tags from 29 animals belonging to 21 phyla, including 11 phyla previously lacking genomic or expressed-sequence-tag data. Analysed in combination with existing sequences, our data reinforce several previously identified clades that split deeply in the animal tree (including Protostomia, Ecdysozoa and Lophotrochozoa), unambiguously resolve multiple long-standing issues for which there was strong conflicting support in earlier studies with less data (such as velvet worms rather than tardigrades as the sister group of arthropods), and provide molecular support for the monophyly of molluscs, a group long recognized by morphologists. In addition, we find strong support for several new hypotheses. These include a clade that unites annelids (including sipunculans and echiurans) with nemerteans, phoronids and brachiopods, molluscs as sister to that assemblage, and the placement of ctenophores as the earliest diverging extant multicellular animals. A single origin of spiral cleavage (with subsequent losses) is inferred from well-supported nodes. Many relationships between a stable subset of taxa find strong support, and a diminishing number of lineages remain recalcitrant to placement on the tree.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dunn, Casey W -- Hejnol, Andreas -- Matus, David Q -- Pang, Kevin -- Browne, William E -- Smith, Stephen A -- Seaver, Elaine -- Rouse, Greg W -- Obst, Matthias -- Edgecombe, Gregory D -- Sorensen, Martin V -- Haddock, Steven H D -- Schmidt-Rhaesa, Andreas -- Okusu, Akiko -- Kristensen, Reinhardt Mobjerg -- Wheeler, Ward C -- Martindale, Mark Q -- Giribet, Gonzalo -- England -- Nature. 2008 Apr 10;452(7188):745-9. doi: 10.1038/nature06614. Epub 2008 Mar 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Kewalo Marine Laboratory, PBRC, University of Hawaii, 41 Ahui Street, Honolulu, Hawaii 96813, USA. casey_dunn@brown.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18322464" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bayes Theorem ; Classification/*methods ; Computational Biology ; Databases, Genetic ; Evolution, Molecular ; Expressed Sequence Tags ; Gene Library ; Humans ; Markov Chains ; *Phylogeny ; Reproducibility of Results ; Sample Size ; Sensitivity and Specificity
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2006-12-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Glenner, Henrik -- Thomsen, Philip Francis -- Hebsgaard, Martin Bay -- Sorensen, Martin Vinther -- Willerslev, Eske -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2006 Dec 22;314(5807):1883-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for Ancient Genetics, Department of Evolutionary Biology, Biological Institute, University of Copenhagen, Universitetsparken 15, DK-2100 Copenhagen, Denmark. ewillerslev@bi.ku.dk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17185588" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Animals ; *Biological Evolution ; *Crustacea/anatomy & histology/classification/genetics/physiology ; Ecosystem ; Fossils ; Fresh Water ; *Insects/anatomy & histology/classification/genetics/physiology ; Phylogeny ; Seawater ; 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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  • 3
    ISSN: 1432-1327
    Keywords: Key words Matrix metalloproteinase ; Metal chelating agent ; Metal hybrid ; Fluorescent peptide substrate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  We have selectively replaced the catalytic zinc of the catalytic domain of stromelysin-1 (SCD) with other transition metals. Dialysis of the enzyme against 2 mM 1,10-phenanthroline, 20 mM Hepes, pH 7.5 in the presence of 10 mM CaCl2 removes the catalytic zinc, leaving the structural zinc site intact. Dialysis with metal-free buffer followed by the new metal ion replaces the catalytic zinc forming a metal hybrid enzyme. Full incorporation of 1 mol Co2+, Ni2+, or Cd2+/mol enzyme is confirmed by atomic absorption spectrometry while the weaker binding Mn2+ yields a value of 0.4 mol Mn2+/mol enzyme after dialysis against 1 μM Mn2+. The activity of the monozinc enzyme is 〈10% while its activity is restored upon the addition of zinc and other transition metals. The k cat values for the Co2+, Mn2+, Cd2+, and Ni2+ enzymes are respectively 99%, 54%, 19%, and 17% of the value for the native enzyme, while the respective k cat/K m values are 36%, 29%, 7%, and 16% toward the fluorescent heptapeptide substrate, DnsPLALRAR. The zinc and metal hybrid SCD cleave DnsPLA↓LRAR, and DnsPLE↓LFAR, exclusively at one bond, while DnsPLA↓L↓WAR and DnsPLA↓L↓FAR are cleaved at two positions. The double cleavage of DnsPLALWAR and DnsPLALFAR catalyzed by SCD is in marked contrast to the close structurally related matrilysin. A notable feature of SCD catalysis is the different cleavage site specificity of the metal hybrids toward the A-L and L-W bonds of the DnsPLALWAR substrate. Thus the k cat values of the Co/Zn hybrid for the cleavage of the A-L bond in the DnsPLALRAR and DnsPLAWAR substrates are 5- and 8-fold greater than those for the Cd/Zn hybrid compared to a 140-fold difference for the corresponding k cat values for the L-W bond cleavage. These results imply that the catalytic metal of SCD is not only involved in catalysis but also influences the substrate specificity of the enzyme.
    Type of Medium: Electronic Resource
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  • 4
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