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  • Articles  (144)
  • Latest Papers from Table of Contents or Articles in Press  (144)
  • *Biological Evolution  (97)
  • Models, Molecular
  • 2005-2009  (144)
  • 1980-1984
  • 1955-1959
  • 2006  (144)
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  • Articles  (144)
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  • Latest Papers from Table of Contents or Articles in Press  (144)
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  • 2005-2009  (144)
  • 1980-1984
  • 1955-1959
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  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-05-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stanley, George D Jr -- New York, N.Y. -- Science. 2006 May 12;312(5775):857-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Montana Paleontology Center, Missoula, MT 59812, USA. george.stanley@umontana.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16690848" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Animals ; Anthozoa/growth & development/*physiology ; *Biological Evolution ; Calcification, Physiologic ; Calcium Carbonate/metabolism ; Carbon Dioxide/metabolism ; Climate ; *Ecosystem ; Eukaryota/growth & development/*physiology ; Fossils ; Photosynthesis ; Sunlight ; *Symbiosis
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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
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  • 3
    Publication Date: 2006-01-10
    Description: Attine ants engage in a quadripartite symbiosis with fungi they cultivate for food, specialized garden parasites, and parasite-inhibiting bacteria. Molecular phylogenetic evidence supports an ancient host-pathogen association between the ant-cultivar mutualism and the garden parasite. Here we show that ants rear the antibiotic-producing bacteria in elaborate cuticular crypts, supported by unique exocrine glands, and that these structures have been highly modified across the ants' evolutionary history. This specialized structural evolution, together with the absence of these bacteria and modifications in other ant genera that do not grow fungus, indicate that the bacteria have an ancient and coevolved association with the ants, their fungal cultivar, and the garden parasite.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Currie, Cameron R -- Poulsen, Michael -- Mendenhall, John -- Boomsma, Jacobus J -- Billen, Johan -- New York, N.Y. -- Science. 2006 Jan 6;311(5757):81-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Bacteriology, University of Wisconsin at Madison, Madison, WI 53706, USA. currie@bact.wisc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16400148" target="_blank"〉PubMed〈/a〉
    Keywords: Actinomycetales/growth & development/*physiology ; Animals ; Anti-Bacterial Agents/biosynthesis ; Antibiosis ; Ants/*anatomy & histology/*microbiology/physiology/ultrastructure ; *Biological Evolution ; Exocrine Glands/anatomy & histology/microbiology ; Female ; Fungi/*growth & development ; Hypocreales/*growth & development ; Microscopy, Electron, Scanning ; Microscopy, Electron, Transmission ; Phylogeny ; Species Specificity ; *Symbiosis
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-04-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Redecker, Dirk -- New York, N.Y. -- Science. 2006 Apr 7;312(5770):53-4; author reply 53-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16601175" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Fungi/classification/genetics ; *Phylogeny
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-12-13
    Description: Humans behave altruistically in natural settings and experiments. A possible explanation-that groups with more altruists survive when groups compete-has long been judged untenable on empirical grounds for most species. But there have been no empirical tests of this explanation for humans. My empirical estimates show that genetic differences between early human groups are likely to have been great enough so that lethal intergroup competition could account for the evolution of altruism. Crucial to this process were distinctive human practices such as sharing food beyond the immediate family, monogamy, and other forms of reproductive leveling. These culturally transmitted practices presuppose advanced cognitive and linguistic capacities, possibly accounting for the distinctive forms of altruism found in our species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bowles, Samuel -- New York, N.Y. -- Science. 2006 Dec 8;314(5805):1569-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Santa Fe Institute, 1399 Hyde Park Road, Santa Fe, NM 87501, USA, and Universita di Siena, 17 Piazza San Francesco, Siena, Italy. bowles@santafe.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17158320" target="_blank"〉PubMed〈/a〉
    Keywords: *Altruism ; Archaeology ; *Biological Evolution ; Climate ; *Competitive Behavior ; Cultural Evolution ; Genetic Variation ; Genetics, Population ; *Group Processes ; Humans ; Mathematics ; Models, Theoretical ; Population Dynamics ; *Reproduction ; Selection, Genetic ; Violence ; Warfare
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  • 6
    Publication Date: 2006-06-10
    Description: Bacterial pathogens frequently use protein secretion to mediate interactions with their hosts. Here we found that a virulence locus (HSI-I) of Pseudomonas aeruginosa encodes a protein secretion apparatus. The apparatus assembled in discrete subcellular locations and exported Hcp1, a hexameric protein that forms rings with a 40 angstrom internal diameter. Regulatory patterns of HSI-I suggested that the apparatus functions during chronic infections. We detected Hcp1 in pulmonary secretions of cystic fibrosis (CF) patients and Hcp1-specific antibodies in their sera. Thus, HSI-I likely contributes to the pathogenesis of P. aeruginosa in CF patients. HSI-I-related loci are widely distributed among bacterial pathogens and may play a general role in mediating host interactions.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2800167/" 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/PMC2800167/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mougous, Joseph D -- Cuff, Marianne E -- Raunser, Stefan -- Shen, Aimee -- Zhou, Min -- Gifford, Casey A -- Goodman, Andrew L -- Joachimiak, Grazyna -- Ordonez, Claudia L -- Lory, Stephen -- Walz, Thomas -- Joachimiak, Andrzej -- Mekalanos, John J -- AI21451/AI/NIAID NIH HHS/ -- AI26289/AI/NIAID NIH HHS/ -- GM074942/GM/NIGMS NIH HHS/ -- GM62414/GM/NIGMS NIH HHS/ -- P50 GM062414/GM/NIGMS NIH HHS/ -- P50 GM062414-02/GM/NIGMS NIH HHS/ -- U54 GM074942/GM/NIGMS NIH HHS/ -- U54 GM074942-04S2/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Jun 9;312(5779):1526-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16763151" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins/*genetics/physiology/secretion ; Crystallography, X-Ray ; Cystic Fibrosis/complications/microbiology ; Humans ; Models, Molecular ; Protein Conformation ; Pseudomonas Infections/complications/microbiology ; Pseudomonas aeruginosa/*genetics/pathogenicity ; Rats ; Recombinant Fusion Proteins ; Sequence Alignment ; Virulence/genetics
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  • 7
    Publication Date: 2006-07-01
    Description: Although enzymes often incorporate molecular recognition elements to orient substrates selectively, such strategies are rarely achieved by synthetic catalysts. We combined molecular recognition through hydrogen bonding with C-H activation to obtain high-turnover catalytic regioselective functionalization of sp3 C-H bonds remote from the -COOH recognition group. The catalyst contains a Mn(mu-O)2Mn reactive center and a ligand based on Kemp's triacid that directs a -COOH group to anchor the carboxylic acid group of the substrate and thus modify the usual selectivity for oxidation. Control experiments supported the role of hydrogen bonding in orienting the substrate to achieve high selectivity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Das, Siddhartha -- Incarvito, Christopher D -- Crabtree, Robert H -- Brudvig, Gary W -- GM32715/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Jun 30;312(5782):1941-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Yale University, 225 Prospect Street, Post Office Box 208107, New Haven, CT 06520-8107, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16809537" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Carbon/*chemistry ; Carboxylic Acids/*chemistry ; *Catalysis ; Chemistry, Physical ; Hydrogen/*chemistry ; Hydrogen Bonding ; Ibuprofen/*chemistry ; Ligands ; Magnetic Resonance Spectroscopy ; Manganese/*chemistry ; Models, Chemical ; Models, Molecular ; Molecular Structure ; Organometallic Compounds/*chemistry ; Oxidation-Reduction ; Physicochemical Phenomena
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  • 8
    Publication Date: 2006-02-14
    Description: Development of the animal body plan is controlled by large gene regulatory networks (GRNs), and hence evolution of body plans must depend upon change in the architecture of developmental GRNs. However, these networks are composed of diverse components that evolve at different rates and in different ways. Because of the hierarchical organization of developmental GRNs, some kinds of change affect terminal properties of the body plan such as occur in speciation, whereas others affect major aspects of body plan morphology. A notable feature of the paleontological record of animal evolution is the establishment by the Early "Cambrian of virtually all phylum-level body plans. We identify a class of GRN component, the kernels" of the network, which, because of their developmental role and their particular internal structure, are most impervious to change. Conservation of phyletic body plans may have been due to the retention since pre-Cambrian time of GRN kernels, which underlie development of major body parts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davidson, Eric H -- Erwin, Douglas H -- HD37105/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2006 Feb 10;311(5762):796-800.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology 156-29, California Institute of Technology, Pasadena, CA 91125, USA. davidson@caltech.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16469913" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological/genetics ; Animals ; *Biological Evolution ; Body Patterning/*genetics ; Embryonic Development ; Fossils ; *Gene Expression Regulation, Developmental ; Genes, Regulator ; Genetic Speciation ; Morphogenesis/*genetics ; Signal Transduction/genetics ; Transcription Factors/genetics/metabolism
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  • 9
    Publication Date: 2006-03-11
    Description: Nisin is a posttranslationally modified antimicrobial peptide that is widely used as a food preservative. It contains five cyclic thioethers of varying sizes that are installed by a single enzyme, NisC. Reported here are the in vitro reconstitution of the cyclization process and the x-ray crystal structure of the NisC enzyme. The structure reveals similarities in fold and substrate activation with mammalian farnesyl transferases, suggesting that human homologs of NisC posttranslationally modify a cysteine of a protein substrate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Bo -- Yu, John Paul J -- Brunzelle, Joseph S -- Moll, Gert N -- van der Donk, Wilfred A -- Nair, Satish K -- GM58822/GM/NIGMS NIH HHS/ -- R01 GM079038/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Mar 10;311(5766):1464-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16527981" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anti-Bacterial Agents/*biosynthesis/chemistry ; Carbon-Sulfur Lyases/chemistry/genetics/*metabolism ; Crystallography, X-Ray ; Farnesyltranstransferase/chemistry ; Humans ; Lactococcus lactis/*enzymology ; Models, Molecular ; Molecular Sequence Data ; Nisin/*biosynthesis/chemistry ; Protein Conformation ; Protein Processing, Post-Translational ; Sequence Homology, Amino Acid ; Structure-Activity Relationship
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  • 10
    Publication Date: 2006-06-17
    Description: Vesicular stomatitis virus is a negative-stranded RNA virus. Its nucleoprotein (N) binds the viral genomic RNA and is involved in multiple functions including transcription, replication, and assembly. We have determined a 2.9 angstrom structure of a complex containing 10 molecules of the N protein and 90 bases of RNA. The RNA is tightly sequestered in a cavity at the interface between two lobes of the N protein. This serves to protect the RNA in the absence of polynucleotide synthesis. For the RNA to be accessed, some conformational change in the N protein should be necessary.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Green, Todd J -- Zhang, Xin -- Wertz, Gail W -- Luo, Ming -- AI050066/AI/NIAID NIH HHS/ -- R37 AI012464/AI/NIAID NIH HHS/ -- R37 AI012464-28/AI/NIAID NIH HHS/ -- R37 AI012464-29/AI/NIAID NIH HHS/ -- R37 AI012464-30/AI/NIAID NIH HHS/ -- R37 AI012464-31/AI/NIAID NIH HHS/ -- R37AI012464/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2006 Jul 21;313(5785):357-60. Epub 2006 Jun 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, School of Medicine, University of Alabama at Birmingham, 1025 18th Street South, Birmingham, AL 35294, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16778022" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Crystallography, X-Ray ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Nucleocapsid Proteins/*chemistry/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA, Viral/*chemistry/metabolism ; Ribonucleoproteins/*chemistry ; Sequence Alignment ; Vesicular stomatitis Indiana virus/*chemistry
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  • 11
    Publication Date: 2006-07-01
    Description: The formation of glutaminyl transfer RNA (Gln-tRNA(Gln)) differs among the three domains of life. Most bacteria employ an indirect pathway to produce Gln-tRNA(Gln) by a heterotrimeric glutamine amidotransferase CAB (GatCAB) that acts on the misacylated Glu-tRNA(Gln). Here, we describe a series of crystal structures of intact GatCAB from Staphylococcus aureus in the apo form and in the complexes with glutamine, asparagine, Mn2+, and adenosine triphosphate analog. Two identified catalytic centers for the glutaminase and transamidase reactions are markedly distant but connected by a hydrophilic ammonia channel 30 A in length. Further, we show that the first U-A base pair in the acceptor stem and the D loop of tRNA(Gln) serve as identity elements essential for discrimination by GatCAB and propose a complete model for the overall concerted reactions to synthesize Gln-tRNA(Gln).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakamura, Akiyoshi -- Yao, Min -- Chimnaronk, Sarin -- Sakai, Naoki -- Tanaka, Isao -- New York, N.Y. -- Science. 2006 Jun 30;312(5782):1954-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Faculty of Advanced Life Sciences, Hokkaido University, Sapporo 060-0810, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16809541" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/metabolism ; Amino Acid Sequence ; Aminoacyltransferases/metabolism ; Ammonia/*metabolism ; Apoenzymes/chemistry/metabolism ; Asparagine/metabolism ; Base Pairing ; Catalytic Domain ; Crystallography, X-Ray ; Glutaminase/metabolism ; Glutamine/*chemistry/metabolism ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Magnesium/metabolism ; Manganese/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; RNA, Bacterial/chemistry/metabolism ; RNA, Transfer, Amino Acyl/chemistry/*metabolism ; RNA, Transfer, Gln/*chemistry/metabolism ; Staphylococcus aureus/*enzymology/genetics/metabolism
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-05-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, David L -- New York, N.Y. -- Science. 2006 May 19;312(5776):997-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16709765" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Birds ; Conservation of Natural Resources
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-09-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rokas, Antonis -- New York, N.Y. -- Science. 2006 Sep 29;313(5795):1897-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Broad Institute of Massachusetts Institute of Technology and Harvard University, Microbial Genome Analysis and Annotation, 7 Cambridge Center, Cambridge, MA 02142, USA. arokas@mit.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17008515" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Animals ; *Biological Evolution ; Computational Biology ; Genome ; *Genomics ; *Phylogeny ; Polymorphism, Genetic ; Sequence Analysis, DNA
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  • 14
    Publication Date: 2006-11-25
    Description: For microbial pathogens, phylogeographic differentiation seems to be relatively common. However, the neutral population structure of Salmonella enterica serovar Typhi reflects the continued existence of ubiquitous haplotypes over millennia. In contrast, clinical use of fluoroquinolones has yielded at least 15 independent gyrA mutations within a decade and stimulated clonal expansion of haplotype H58 in Asia and Africa. Yet, antibiotic-sensitive strains and haplotypes other than H58 still persist despite selection for antibiotic resistance. Neutral evolution in Typhi appears to reflect the asymptomatic carrier state, and adaptive evolution depends on the rapid transmission of phenotypic changes through acute infections.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2652035/" 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/PMC2652035/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roumagnac, Philippe -- Weill, Francois-Xavier -- Dolecek, Christiane -- Baker, Stephen -- Brisse, Sylvain -- Chinh, Nguyen Tran -- Le, Thi Anh Hong -- Acosta, Camilo J -- Farrar, Jeremy -- Dougan, Gordon -- Achtman, Mark -- 076962/Wellcome Trust/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2006 Nov 24;314(5803):1301-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Infektionsbiologie, Department of Molecular Biology, Chariteplatz 1, 10117 Berlin, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17124322" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Africa ; Alleles ; Anti-Bacterial Agents/pharmacology/therapeutic use ; Asia ; *Biological Evolution ; Carrier State/*microbiology ; DNA Gyrase/genetics ; Drug Resistance, Bacterial ; Drug Resistance, Multiple, Bacterial ; Fluoroquinolones/pharmacology/therapeutic use ; *Genes, Bacterial ; Genetic Variation ; Haplotypes ; Humans ; Molecular Sequence Data ; Mutation ; Polymorphism, Genetic ; Polymorphism, Single Nucleotide ; Salmonella typhi/drug effects/*genetics ; Selection, Genetic ; Typhoid Fever/drug therapy/*microbiology
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  • 15
    Publication Date: 2006-11-18
    Description: Our knowledge of Neanderthals is based on a limited number of remains and artifacts from which we must make inferences about their biology, behavior, and relationship to ourselves. Here, we describe the characterization of these extinct hominids from a new perspective, based on the development of a Neanderthal metagenomic library and its high-throughput sequencing and analysis. Several lines of evidence indicate that the 65,250 base pairs of hominid sequence so far identified in the library are of Neanderthal origin, the strongest being the ascertainment of sequence identities between Neanderthal and chimpanzee at sites where the human genomic sequence is different. These results enabled us to calculate the human-Neanderthal divergence time based on multiple randomly distributed autosomal loci. Our analyses suggest that on average the Neanderthal genomic sequence we obtained and the reference human genome sequence share a most recent common ancestor approximately 706,000 years ago, and that the human and Neanderthal ancestral populations split approximately 370,000 years ago, before the emergence of anatomically modern humans. Our finding that the Neanderthal and human genomes are at least 99.5% identical led us to develop and successfully implement a targeted method for recovering specific ancient DNA sequences from metagenomic libraries. This initial analysis of the Neanderthal genome advances our understanding of the evolutionary relationship of Homo sapiens and Homo neanderthalensis and signifies the dawn of Neanderthal genomics.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2583069/" 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/PMC2583069/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Noonan, James P -- Coop, Graham -- Kudaravalli, Sridhar -- Smith, Doug -- Krause, Johannes -- Alessi, Joe -- Chen, Feng -- Platt, Darren -- Paabo, Svante -- Pritchard, Jonathan K -- Rubin, Edward M -- 1-F32-GM074367/GM/NIGMS NIH HHS/ -- HL066681/HL/NHLBI NIH HHS/ -- R01 HG002772/HG/NHGRI NIH HHS/ -- R01 HG002772-01/HG/NHGRI NIH HHS/ -- R01 HG002772-1/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2006 Nov 17;314(5802):1113-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉U.S. Department of Energy Joint Genome Institute, 2800 Mitchell Drive, Walnut Creek, CA 94598, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17110569" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Bone and Bones ; Cell Nucleus ; DNA/*genetics/isolation & purification ; DNA, Mitochondrial ; *Fossils ; Gene Pool ; Genome ; Genome, Human ; Genomic Library ; History, Ancient ; Hominidae/*genetics ; Humans ; Male ; Molecular Sequence Data ; Pan troglodytes/genetics ; Polymerase Chain Reaction ; Sequence Alignment ; *Sequence Analysis, DNA/methods ; Time
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  • 16
    Publication Date: 2006-08-26
    Description: The most obvious key synapomorphy of the therian mammals is the tribosphenic pattern of their molars. Tribosphenic teeth are capable of both shearing and grinding, which substantially increase effectiveness of food processing and, in turn, permit evolution of a wide range of dietary specializations. Functional tribospheny developed repeatedly during mammalian evolution but was successful only in the Boreosphenida. The earliest stage in the development of boreosphenidan tribospheny has remained poorly understood, being documented only by lower molars of aegialodontids. Here, we report a known upper molar of an aegialodontid mammal, Kielantherium, from the Early Cretaceous of Mongolia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lopatin, Alexey V -- Averianov, Alexander O -- New York, N.Y. -- Science. 2006 Aug 25;313(5790):1092.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Paleontological Institute, Russian Academy of Sciences, Profsojuznaya ul. 123, Moscow 117997, Russia. alopat@paleo.ru〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16931755" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Dentition ; History, Ancient ; *Mammals/anatomy & histology ; Molar/*anatomy & histology ; Mongolia ; Paleodontology
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  • 17
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-12-13
    Description: Cooperation is needed for evolution to construct new levels of organization. Genomes, cells, multicellular organisms, social insects, and human society are all based on cooperation. Cooperation means that selfish replicators forgo some of their reproductive potential to help one another. But natural selection implies competition and therefore opposes cooperation unless a specific mechanism is at work. Here I discuss five mechanisms for the evolution of cooperation: kin selection, direct reciprocity, indirect reciprocity, network reciprocity, and group selection. For each mechanism, a simple rule is derived that specifies whether natural selection can lead to cooperation.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3279745/" 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/PMC3279745/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nowak, Martin A -- 1R01GM078986-01/GM/NIGMS NIH HHS/ -- R01 GM078986/GM/NIGMS NIH HHS/ -- R01 GM078986-04/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Dec 8;314(5805):1560-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program for Evolutionary Dynamics, Department of Organismic and Evolutionary Biology, and Department of Mathematics, Harvard University, Cambridge, MA 02138, USA. martin_nowak@harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17158317" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Community Networks ; *Cooperative Behavior ; Family ; Game Theory ; Helping Behavior ; Humans ; Mathematics ; Selection, Genetic
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  • 18
    Publication Date: 2006-03-18
    Description: Rapid evolution of asexual populations, such as that of cancer cells or of microorganisms developing drug resistance, can include the simultaneous spread of distinct beneficial mutations. We demonstrate that evolution in such cases is driven by the fitness effects and appearance times of only a small minority of favorable mutations. The complexity of the mutation-selection process is thereby greatly reduced, and much of the evolutionary dynamics can be encapsulated in two parameters-an effective selection coefficient and effective rate of beneficial mutations. We confirm this theoretical finding and estimate the effective parameters for evolving populations of fluorescently labeled Escherichia coli. The effective parameters constitute a simple description and provide a natural standard for comparing adaptation between species and across environments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hegreness, Matthew -- Shoresh, Noam -- Hartl, Daniel -- Kishony, Roy -- New York, N.Y. -- Science. 2006 Mar 17;311(5767):1615-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Bauer Center for Genomics Research, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16543462" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Bacterial Proteins/analysis/genetics ; *Biological Evolution ; Escherichia coli/*genetics/*physiology ; Genetics, Population ; Green Fluorescent Proteins/analysis/genetics ; Luminescent Proteins/analysis/genetics ; Mathematics ; Models, Genetic ; *Mutation
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  • 19
    Publication Date: 2006-07-15
    Description: The electric fields produced in folded proteins influence nearly every aspect of protein function. We present a vibrational spectroscopy technique that measures changes in electric field at a specific site of a protein as shifts in frequency (Stark shifts) of a calibrated nitrile vibration. A nitrile-containing inhibitor is used to deliver a unique probe vibration to the active site of human aldose reductase, and the response of the nitrile stretch frequency is measured for a series of mutations in the enzyme active site. These shifts yield quantitative information on electric fields that can be directly compared with electrostatics calculations. We show that extensive molecular dynamics simulations and ensemble averaging are required to reproduce the observed changes in field.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Suydam, Ian T -- Snow, Christopher D -- Pande, Vijay S -- Boxer, Steven G -- New York, N.Y. -- Science. 2006 Jul 14;313(5784):200-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Stanford University, Stanford, CA 94305-5080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16840693" target="_blank"〉PubMed〈/a〉
    Keywords: Aldehyde Reductase/antagonists & inhibitors/*chemistry/genetics/metabolism ; Binding Sites ; Circular Dichroism ; Computer Simulation ; *Electricity ; Enzyme Inhibitors/metabolism/pharmacology ; Humans ; Models, Molecular ; Mutation ; Nitriles/metabolism/pharmacology ; Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Spectrophotometry, Infrared ; Spectrum Analysis ; Static Electricity
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  • 20
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-10-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, Charles R -- New York, N.Y. -- Science. 2006 Oct 6;314(5796):66-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Organismic and Evolutionary Biology and Earth and Planetary Sciences, Harvard University, 26 Oxford Street Cambridge, MA 02138, USA. cmarshal@oeb.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17023640" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; *Biological Evolution ; *Bivalvia/anatomy & histology/classification ; *Fossils ; Geography ; Phylogeny ; Population Dynamics ; *Tropical Climate
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  • 21
    Publication Date: 2006-01-18
    Description: The specialized ribonuclease Dicer initiates RNA interference by cleaving double-stranded RNA (dsRNA) substrates into small fragments about 25 nucleotides in length. In the crystal structure of an intact Dicer enzyme, the PAZ domain, a module that binds the end of dsRNA, is separated from the two catalytic ribonuclease III (RNase III) domains by a flat, positively charged surface. The 65 angstrom distance between the PAZ and RNase III domains matches the length spanned by 25 base pairs of RNA. Thus, Dicer itself is a molecular ruler that recognizes dsRNA and cleaves a specified distance from the helical end.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Macrae, Ian J -- Zhou, Kaihong -- Li, Fei -- Repic, Adrian -- Brooks, Angela N -- Cande, W Zacheus -- Adams, Paul D -- Doudna, Jennifer A -- New York, N.Y. -- Science. 2006 Jan 13;311(5758):195-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16410517" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Conserved Sequence ; Crystallography, X-Ray ; Giardia lamblia/enzymology ; Humans ; Lanthanoid Series Elements/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Structure, Tertiary ; RNA Interference ; RNA, Double-Stranded/*metabolism ; RNA, Protozoan/metabolism ; Recombinant Fusion Proteins/genetics/metabolism ; Ribonuclease III/*chemistry/metabolism ; Schizosaccharomyces/genetics ; Structure-Activity Relationship
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  • 22
    Publication Date: 2006-03-25
    Description: Tracheal cytotoxin (TCT), a naturally occurring fragment of Gram-negative peptidoglycan, is a potent elicitor of innate immune responses in Drosophila. It induces the heterodimerization of its recognition receptors, the peptidoglycan recognition proteins (PGRPs) LCa and LCx, which activates the immune deficiency pathway. The crystal structure at 2.1 angstrom resolution of TCT in complex with the ectodomains of PGRP-LCa and PGRP-LCx shows that TCT is bound to and presented by the LCx ectodomain for recognition by the LCa ectodomain; the latter lacks a canonical peptidoglycan-docking groove conserved in other PGRPs. The interface, revealed in atomic detail, between TCT and the receptor complex highlights the importance of the anhydro-containing disaccharide in bridging the two ectodomains together and the critical role of diaminopimelic acid as the specificity determinant for PGRP interaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, Chung-I -- Chelliah, Yogarany -- Borek, Dominika -- Mengin-Lecreulx, Dominique -- Deisenhofer, Johann -- New York, N.Y. -- Science. 2006 Mar 24;311(5768):1761-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Texas Southwestern Medical Center at Dallas, 6001 Forest Park Road, Dallas, TX 75390-9050, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16556841" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/*chemistry/metabolism ; Crystallization ; Crystallography, X-Ray ; Cytotoxins/*chemistry/metabolism ; Drosophila melanogaster ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Molecular Sequence Data ; Peptidoglycan/*chemistry/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary
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  • 23
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-07-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Szathmary, Eors -- New York, N.Y. -- Science. 2006 Jul 21;313(5785):306-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Biology, Eotvos University Budapest, and Collegium Budapest (Institute for Advanced Study), 2 Szentharomsag utca, H-1014 Budapest, Hungary. szathmary@colbud.hu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16857926" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Chemical Phenomena ; Chemistry ; Computational Biology ; Cooperative Behavior ; Cultural Evolution ; Exobiology ; Humans ; Language ; Models, Biological ; Models, Theoretical ; Molecular Biology ; Origin of Life ; *Research ; Selection, Genetic
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  • 24
    Publication Date: 2006-02-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kerr, Richard A -- New York, N.Y. -- Science. 2006 Feb 17;311(5763):931.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16484458" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Fossils ; Geologic Sediments ; *Paleontology ; Regression Analysis ; Time
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  • 25
    Publication Date: 2006-07-11
    Description: The evolution of new combinations of bacterial properties contributes to biodiversity and the emergence of new diseases. We investigated the capacity for bacterial divergence with a chemostat culture of Escherichia coli. A clonal population radiated into more than five phenotypic clusters within 26 days, with multiple variations in global regulation, metabolic strategies, surface properties, and nutrient permeability pathways. Most isolates belonged to a single ecotype, and neither periodic selection events nor ecological competition for a single niche prevented an adaptive radiation with a single resource. The multidirectional exploration of fitness space is an underestimated ingredient to bacterial success even in unstructured environments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maharjan, Ram -- Seeto, Shona -- Notley-McRobb, Lucinda -- Ferenci, Thomas -- New York, N.Y. -- Science. 2006 Jul 28;313(5786):514-7. Epub 2006 Jul 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Molecular and Microbial Biosciences, University of Sydney, Sydney, New South Wales 2006, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16825532" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; *Biological Evolution ; Cell Membrane Permeability ; Culture Media ; *Ecosystem ; Environment ; Escherichia coli/classification/*genetics/growth & development/*physiology ; Gene Expression Regulation, Bacterial ; *Genetic Variation ; Genotype ; Glucose/metabolism ; Mutation ; Phenotype ; Phylogeny ; Selection, Genetic ; Surface Properties
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  • 26
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-12-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Irene A -- New York, N.Y. -- Science. 2006 Dec 8;314(5805):1558-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Health Sciences and Technology at Harvard Medical School and Massachusetts Institute of Technology, Boston, MA 02115, USA. ichen@post.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17158315" target="_blank"〉PubMed〈/a〉
    Keywords: Awards and Prizes ; *Biological Evolution ; *Cells ; Hydrogen-Ion Concentration ; Lipid Bilayers ; *Liposomes/chemistry ; Models, Biological ; *Origin of Life ; Osmotic Pressure ; *Rna ; RNA, Catalytic
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  • 27
    Publication Date: 2006-03-04
    Description: The homodimeric mammalian fatty acid synthase is one of the most complex cellular multienzymes, in that each 270-kilodalton polypeptide chain carries all seven functional domains required for fatty acid synthesis. We have calculated a 4.5 angstrom-resolution x-ray crystallographic map of porcine fatty acid synthase, highly homologous to the human multienzyme, and placed homologous template structures of all individual catalytic domains responsible for the cyclic elongation of fatty acid chains into the electron density. The positioning of domains reveals the complex architecture of the multienzyme forming an intertwined dimer with two lateral semicircular reaction chambers, each containing a full set of catalytic domains required for fatty acid elongation. Large distances between active sites and conformational differences between the reaction chambers demonstrate that mobility of the acyl carrier protein and general flexibility of the multienzyme must accompany handover of the reaction intermediates during the reaction cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maier, Timm -- Jenni, Simon -- Ban, Nenad -- New York, N.Y. -- Science. 2006 Mar 3;311(5765):1258-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology and Biophysics, Department of Biology, Swiss Federal Institute of Technology (ETH Zurich), 8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16513975" target="_blank"〉PubMed〈/a〉
    Keywords: Acyl Carrier Protein/chemistry/metabolism ; Animals ; Binding Sites ; Catalytic Domain ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Fatty Acid Synthases/*chemistry/isolation & purification/metabolism ; Fatty Acids/biosynthesis ; Mammary Glands, Animal/enzymology ; Models, Molecular ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Swine
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-09-09
    Description: The origin and possible antiquity of faunas at deep-sea hydrothermal vents and seeps have been debated since their discovery. We used the fossil record of seep mollusks to show that the living seep genera have significantly longer geologic ranges than the marine mollusks in general, but have ranges similar to those of deep-sea taxa, suggesting that seep faunas may be shaped by the factors that drive the evolution of life in the deep sea in general. Our data indicate that deep-sea anoxic/dysoxic events did not affect seep faunas, casting doubt on the suggested anoxic nature and/or global extent of these events.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kiel, Steffen -- Little, Crispin T S -- New York, N.Y. -- Science. 2006 Sep 8;313(5792):1429-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Earth and Environment, University of Leeds, Leeds LS2 9JT, UK. steffen.kiel@gmx.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16960004" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Bivalvia/classification/physiology ; Cold Temperature ; *Ecosystem ; *Fossils ; Gastropoda/classification/physiology ; *Mollusca/classification/physiology ; Polyplacophora/classification/physiology ; *Seawater ; Symbiosis
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  • 29
    Publication Date: 2006-04-15
    Description: Nee et al. (Reports, 19 August 2005, p. 1236) used a null model to argue that life history invariants are illusions. We show that their results are largely inconsequential for life history theory because the authors confound two definitions of invariance, and rigorous analysis of their null model demonstrates that it does not match observed data.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Savage, Van M -- White, Ethan P -- Moses, Melanie E -- Ernest, S K Morgan -- Enquist, Brian J -- Charnov, Eric L -- New York, N.Y. -- Science. 2006 Apr 14;312(5771):198; author reply 198.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Bauer Center for Genomics Research, Harvard University, Cambridge, MA 02138, USA. vsavage@cgr.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16614200" target="_blank"〉PubMed〈/a〉
    Keywords: Analysis of Variance ; Animals ; *Biological Evolution ; Body Size ; *Body Weight ; Clutch Size ; *Growth ; Longevity ; Mathematics ; *Models, Biological ; Regression Analysis ; *Reproduction ; Sexual Maturation
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  • 30
    Publication Date: 2006-07-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holden, Constance -- New York, N.Y. -- Science. 2006 Jun 30;312(5782):1867.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16809505" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Brain/*anatomy & histology ; Genetic Variation ; Humans ; Intelligence ; Organ Size ; Selection, Genetic
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  • 31
    Publication Date: 2006-09-02
    Description: The AcrA/AcrB/TolC complex spans the inner and outer membranes of Escherichia coli and serves as its major drug-resistance pump. Driven by the proton motive force, it mediates the efflux of bile salts, detergents, organic solvents, and many structurally unrelated antibiotics. Here, we report a crystallographic structure of trimeric AcrB determined at 2.9 and 3.0 angstrom resolution in space groups that allow asymmetry of the monomers. This structure reveals three different monomer conformations representing consecutive states in a transport cycle. The structural data imply an alternating access mechanism and a novel peristaltic mode of drug transport by this type of transporter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seeger, Markus A -- Schiefner, Andre -- Eicher, Thomas -- Verrey, Francois -- Diederichs, Kay -- Pos, Klaas M -- New York, N.Y. -- Science. 2006 Sep 1;313(5791):1295-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Physiology and Zurich Centre for Integrative Human Physiology (ZIHP), University of Zurich, Winterthurerstrasse 190, Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16946072" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Transport ; Crystallization ; Crystallography, X-Ray ; Diffusion ; Drug Resistance, Multiple, Bacterial ; Escherichia coli/*chemistry/drug effects ; Escherichia coli Proteins/*chemistry/*metabolism ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Membrane Transport Proteins/*chemistry/metabolism ; Models, Molecular ; Multidrug Resistance-Associated Proteins/*chemistry/*metabolism ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protons
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  • 32
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-06-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holden, Constance -- New York, N.Y. -- Science. 2006 Jun 2;312(5778):1292.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16741084" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Biology/*education/legislation & jurisprudence ; Georgia ; Religion and Science ; Teaching/*legislation & jurisprudence ; *Textbooks as Topic
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  • 33
    Publication Date: 2006-02-25
    Description: DNA glycosylases must interrogate millions of base pairs of undamaged DNA in order to locate and then excise one damaged nucleobase. The nature of this search process remains poorly understood. Here we report the use of disulfide cross-linking (DXL) technology to obtain structures of a bacterial DNA glycosylase, MutM, interrogating undamaged DNA. These structures, solved to 2.0 angstrom resolution, reveal the nature of the search process: The protein inserts a probe residue into the helical stack and severely buckles the target base pair, which remains intrahelical. MutM therefore actively interrogates the intact DNA helix while searching for damage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Banerjee, Anirban -- Santos, Webster L -- Verdine, Gregory L -- F32 GM067380/GM/NIGMS NIH HHS/ -- GM044853/GM/NIGMS NIH HHS/ -- R01 CA100742/CA/NCI NIH HHS/ -- R01 GM044853/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Feb 24;311(5764):1153-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16497933" target="_blank"〉PubMed〈/a〉
    Keywords: *Base Pairing ; Binding Sites ; Cross-Linking Reagents ; Crystallography, X-Ray ; DNA/*chemistry/metabolism ; *DNA Damage ; DNA Glycosylases/*chemistry/*metabolism ; Geobacillus stearothermophilus/*enzymology ; Guanine/*analogs & derivatives/analysis/metabolism ; Hydrogen Bonding ; Models, Molecular ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/chemistry/metabolism ; Protein Conformation ; Protein Structure, Secondary
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  • 34
    Publication Date: 2006-09-02
    Description: Draft genome sequences have been determined for the soybean pathogen Phytophthora sojae and the sudden oak death pathogen Phytophthora ramorum. Oomycetes such as these Phytophthora species share the kingdom Stramenopila with photosynthetic algae such as diatoms, and the presence of many Phytophthora genes of probable phototroph origin supports a photosynthetic ancestry for the stramenopiles. Comparison of the two species' genomes reveals a rapid expansion and diversification of many protein families associated with plant infection such as hydrolases, ABC transporters, protein toxins, proteinase inhibitors, and, in particular, a superfamily of 700 proteins with similarity to known oomycete avirulence genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tyler, Brett M -- Tripathy, Sucheta -- Zhang, Xuemin -- Dehal, Paramvir -- Jiang, Rays H Y -- Aerts, Andrea -- Arredondo, Felipe D -- Baxter, Laura -- Bensasson, Douda -- Beynon, Jim L -- Chapman, Jarrod -- Damasceno, Cynthia M B -- Dorrance, Anne E -- Dou, Daolong -- Dickerman, Allan W -- Dubchak, Inna L -- Garbelotto, Matteo -- Gijzen, Mark -- Gordon, Stuart G -- Govers, Francine -- Grunwald, Niklaus J -- Huang, Wayne -- Ivors, Kelly L -- Jones, Richard W -- Kamoun, Sophien -- Krampis, Konstantinos -- Lamour, Kurt H -- Lee, Mi-Kyung -- McDonald, W Hayes -- Medina, Monica -- Meijer, Harold J G -- Nordberg, Eric K -- Maclean, Donald J -- Ospina-Giraldo, Manuel D -- Morris, Paul F -- Phuntumart, Vipaporn -- Putnam, Nicholas H -- Rash, Sam -- Rose, Jocelyn K C -- Sakihama, Yasuko -- Salamov, Asaf A -- Savidor, Alon -- Scheuring, Chantel F -- Smith, Brian M -- Sobral, Bruno W S -- Terry, Astrid -- Torto-Alalibo, Trudy A -- Win, Joe -- Xu, Zhanyou -- Zhang, Hongbin -- Grigoriev, Igor V -- Rokhsar, Daniel S -- Boore, Jeffrey L -- BB/C509123/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2006 Sep 1;313(5791):1261-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Virginia Bioinformatics Institute, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, USA. bmtyler@vt.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16946064" target="_blank"〉PubMed〈/a〉
    Keywords: Algal Proteins/genetics/physiology ; *Biological Evolution ; DNA, Algal/*genetics ; Genes ; *Genome ; Hydrolases/genetics/metabolism ; Photosynthesis/genetics ; Phylogeny ; Physical Chromosome Mapping ; Phytophthora/classification/*genetics/*pathogenicity/physiology ; Plant Diseases/microbiology ; Polymorphism, Single Nucleotide ; Repetitive Sequences, Nucleic Acid ; Sequence Analysis, DNA ; Symbiosis ; Toxins, Biological/genetics
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  • 35
    Publication Date: 2006-07-22
    Description: CorA family members are ubiquitously distributed transporters of divalent metal cations and are considered to be the primary Mg2+ transporter of Bacteria and Archaea. We have determined a 2.9 angstrom resolution structure of CorA from Thermotoga maritima that reveals a pentameric cone-shaped protein. Two potential regulatory metal binding sites are found in the N-terminal domain that bind both Mg2+ and Co2+. The structure of CorA supports an efflux system involving dehydration and rehydration of divalent metal ions potentially mediated by a ring of conserved aspartate residues at the cytoplasmic entrance and a carbonyl funnel at the periplasmic side of the pore.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eshaghi, Said -- Niegowski, Damian -- Kohl, Andreas -- Martinez Molina, Daniel -- Lesley, Scott A -- Nordlund, Par -- New York, N.Y. -- Science. 2006 Jul 21;313(5785):354-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biophysics, Department of Medical Biochemistry and Biophysics, Karolinska Institute, SE-171 77 Stockholm, Sweden. Said.Eshaghi@ki.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16857941" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Cation Transport Proteins/*chemistry/metabolism ; Chlorides/analysis/metabolism ; Cobalt/chemistry/*metabolism ; Crystallography, X-Ray ; Hydrophobic and Hydrophilic Interactions ; Magnesium/chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Sequence Alignment ; Thermotoga maritima/*chemistry ; Water/chemistry
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  • 36
    Publication Date: 2006-02-14
    Description: Kaposi's sarcoma-associated herpesvirus (KSHV) latency-associated nuclear antigen (LANA) mediates viral genome attachment to mitotic chromosomes. We find that N-terminal LANA docks onto chromosomes by binding nucleosomes through the folded region of histones H2A-H2B. The same LANA residues were required for both H2A-H2B binding and chromosome association. Further, LANA did not bind Xenopus sperm chromatin, which is deficient in H2A-H2B; chromatin binding was rescued after assembly of nucleosomes containing H2A-H2B. We also describe the 2.9-angstrom crystal structure of a nucleosome complexed with the first 23 LANA amino acids. The LANA peptide forms a hairpin that interacts exclusively with an acidic H2A-H2B region that is implicated in the formation of higher order chromatin structure. Our findings present a paradigm for how nucleosomes may serve as binding platforms for viral and cellular proteins and reveal a previously unknown mechanism for KSHV latency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barbera, Andrew J -- Chodaparambil, Jayanth V -- Kelley-Clarke, Brenna -- Joukov, Vladimir -- Walter, Johannes C -- Luger, Karolin -- Kaye, Kenneth M -- CA82036/CA/NCI NIH HHS/ -- GM067777/GM/NIGMS NIH HHS/ -- GM62267/GM/NIGMS NIH HHS/ -- R01 GM067777/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Feb 10;311(5762):856-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Channing Laboratory, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16469929" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; Antigens, Viral/*chemistry/*metabolism ; Cell Line, Tumor ; Chromatin/metabolism ; Chromosomes/metabolism ; Chromosomes, Human/metabolism ; Chromosomes, Mammalian/metabolism ; Crystallography, X-Ray ; Dimerization ; Herpesvirus 8, Human/chemistry/*metabolism ; Histones/chemistry/*metabolism ; Humans ; Models, Molecular ; Mutation ; Nuclear Proteins/*chemistry/*metabolism ; Nucleosomes/*chemistry/*metabolism ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; Xenopus laevis
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  • 37
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-02-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holden, Constance -- New York, N.Y. -- Science. 2006 Feb 24;311(5764):1083.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16497892" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Biological Science Disciplines/*education ; *Curriculum ; Ohio ; Religion and Science
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  • 38
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-02-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holden, Constance -- New York, N.Y. -- Science. 2006 Feb 10;311(5762):769-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16469893" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Culture ; Curriculum ; Earth (Planet) ; Geological Phenomena ; Geology ; Humans ; *Religion and Science ; *Students ; Teaching ; United States ; *Universities
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  • 39
    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
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  • 40
    Publication Date: 2006-12-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balter, Michael -- New York, N.Y. -- Science. 2006 Dec 22;314(5807):1871-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17185582" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; *Brain/anatomy & histology/physiology ; China ; Chromosomes, Human, Y/genetics ; *Cognition ; History, 20th Century ; History, 21st Century ; Humans ; Intelligence/genetics ; Nerve Tissue Proteins/genetics ; Selection, Genetic ; United States
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  • 41
    Publication Date: 2006-09-09
    Description: The crystal structure of the bacterial 70S ribosome refined to 2.8 angstrom resolution reveals atomic details of its interactions with messenger RNA (mRNA) and transfer RNA (tRNA). A metal ion stabilizes a kink in the mRNA that demarcates the boundary between A and P sites, which is potentially important to prevent slippage of mRNA. Metal ions also stabilize the intersubunit interface. The interactions of E-site tRNA with the 50S subunit have both similarities and differences compared to those in the archaeal ribosome. The structure also rationalizes much biochemical and genetic data on translation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Selmer, Maria -- Dunham, Christine M -- Murphy, Frank V 4th -- Weixlbaumer, Albert -- Petry, Sabine -- Kelley, Ann C -- Weir, John R -- Ramakrishnan, V -- GM67624/GM/NIGMS NIH HHS/ -- MC_U105184332/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2006 Sep 29;313(5795):1935-42. Epub 2006 Sep 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16959973" target="_blank"〉PubMed〈/a〉
    Keywords: Anticodon ; Bacterial Proteins/*chemistry/metabolism ; Codon ; Crystallization ; Crystallography, X-Ray ; Magnesium/metabolism ; Models, Molecular ; Nucleic Acid Conformation ; Peptidyl Transferases/chemistry/metabolism ; Protein Biosynthesis ; Protein Conformation ; RNA, Bacterial/chemistry/metabolism ; RNA, Messenger/chemistry/*metabolism ; RNA, Transfer/chemistry/*metabolism ; RNA, Transfer, Met/chemistry/metabolism ; RNA, Transfer, Phe/chemistry/metabolism ; Ribosomal Proteins/*chemistry/metabolism ; Ribosomes/*chemistry/metabolism/*ultrastructure ; Thermus thermophilus/*chemistry/ultrastructure
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  • 42
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-11-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balter, Michael -- New York, N.Y. -- Science. 2006 Nov 17;314(5802):1071.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17110550" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Evolution, Molecular ; Genome, Human ; History, Ancient ; Hominidae/*genetics ; Humans ; Nerve Tissue Proteins/genetics ; Paleontology ; Selection, Genetic ; Sexual Behavior ; tau Proteins/genetics
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-03-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Falkowski, Paul G -- New York, N.Y. -- Science. 2006 Mar 24;311(5768):1724-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Environmental Biophysics and Molecular Ecology Program, Institute of Marine and Coastal Sciences and Department of Geological Sciences, Rutgers University, New Brunswick, NJ 08901, USA. falko@imcs.rutgers.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16556831" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Computational Biology ; Electron Transport ; Electrons ; Energy Metabolism ; Eukaryotic Cells/metabolism ; *Evolution, Molecular ; Gene Duplication ; Gene Transfer, Horizontal ; *Metabolism ; Oxidation-Reduction ; Oxygen/*metabolism ; Photosynthesis ; Reactive Oxygen Species/metabolism ; Selection, Genetic ; Water/metabolism
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  • 44
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-11-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2006 Nov 17;314(5802):1068-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17110549" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Bone and Bones ; Cell Nucleus ; DNA/genetics/history/*isolation & purification ; DNA, Mitochondrial ; Equipment Contamination ; *Fossils ; Genome, Human ; Genomics/methods ; History, Ancient ; Hominidae/*genetics ; Humans ; Polymerase Chain Reaction ; Sequence Analysis, DNA
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  • 45
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-10-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2006 Oct 13;314(5797):244-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17038601" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Brain/physiology ; Brain Chemistry ; Cognition ; Evolution, Molecular ; Gene Expression Profiling ; Humans ; Invertebrates/anatomy & histology/physiology ; Membrane Proteins/*analysis/genetics/metabolism ; Multiprotein Complexes/*analysis/genetics/metabolism ; Nerve Tissue Proteins/*analysis/genetics/metabolism ; Organ Size ; Receptors, Neurotransmitter/analysis/genetics/metabolism ; Signal Transduction ; Synaptic Membranes/*chemistry/physiology ; Synaptic Transmission ; Vertebrates/anatomy & histology/physiology
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  • 46
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-09-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2006 Sep 29;313(5795):1908-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17008520" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Brain/anatomy & histology/embryology/physiology ; Cerebral Cortex/embryology/metabolism ; Evolution, Molecular ; Gene Dosage ; Gene Expression Profiling ; Gene Expression Regulation ; Genome ; *Genome, Human ; Genomics ; Humans ; Microcephaly/genetics ; Oligonucleotide Array Sequence Analysis ; Pan troglodytes/genetics ; Primates/*genetics ; Proteins/genetics/physiology ; RNA/genetics/physiology ; Selection, Genetic
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  • 47
    Publication Date: 2006-04-08
    Description: Biological responses to histone methylation critically depend on the faithful readout and transduction of the methyl-lysine signal by "effector" proteins, yet our understanding of methyl-lysine recognition has so far been limited to the study of histone binding by chromodomain and WD40-repeat proteins. The double tudor domain of JMJD2A, a Jmjc domain-containing histone demethylase, binds methylated histone H3-K4 and H4-K20. We found that the double tudor domain has an interdigitated structure, and the unusual fold is required for its ability to bind methylated histone tails. The cocrystal structure of the JMJD2A double tudor domain with a trimethylated H3-K4 peptide reveals that the trimethyl-K4 is bound in a cage of three aromatic residues, two of which are from the tudor-2 motif, whereas the binding specificity is determined by side-chain interactions involving amino acids from the tudor-1 motif. Our study provides mechanistic insights into recognition of methylated histone tails by tudor domains and reveals the structural intricacy of methyl-lysine recognition by two closely spaced effector domains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Ying -- Fang, Jia -- Bedford, Mark T -- Zhang, Yi -- Xu, Rui-Ming -- DK62248/DK/NIDDK NIH HHS/ -- GM 63718/GM/NIGMS NIH HHS/ -- GM68804/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 May 5;312(5774):748-51. Epub 2006 Apr 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉W. M. Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16601153" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; DNA-Binding Proteins/*chemistry/genetics/*metabolism ; Histones/*chemistry/*metabolism ; Humans ; Hydrogen Bonding ; Jumonji Domain-Containing Histone Demethylases ; Lysine/metabolism ; Methylation ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Oxidoreductases, N-Demethylating ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Static Electricity ; Transcription Factors/*chemistry/genetics/*metabolism
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-09-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2006 Sep 8;313(5792):1381.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16959986" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Crustacea/physiology ; Female ; Fundulidae/*genetics/*physiology ; *Genetic Variation ; Hermaphroditic Organisms ; Male ; Microsatellite Repeats ; *Reproduction ; Sex Determination Processes ; Sexual Behavior, Animal
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-07-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2006 Jul 14;313(5784):156.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16840668" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Beak/*anatomy & histology ; *Biological Evolution ; Competitive Behavior ; Diet ; Disasters ; Ecosystem ; Ecuador ; Feeding Behavior ; *Finches/anatomy & histology/physiology ; *Food ; Population Dynamics ; *Seeds ; *Selection, Genetic
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  • 50
    Publication Date: 2006-06-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2006 Jun 23;312(5781):1737.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16794056" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Cognition ; Comprehension ; Cooperative Behavior ; Cues ; Dogs/*psychology ; *Intelligence ; *Social Behavior
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  • 51
    Publication Date: 2006-04-15
    Description: Protein dynamics plays an important role in protein function. Many functionally important motions occur on the microsecond and low millisecond time scale and can be characterized by nuclear magnetic resonance relaxation experiments. We describe the different states of a peptidyl carrier protein (PCP) that play a crucial role in its function as a peptide shuttle in the nonribosomal peptide synthetases of the tyrocidine A system. Both apo-PCP (without the bound 4'-phosphopantetheine cofactor) and holo-PCP exist in two different stable conformations. We show that one of the apo conformations and one of the holo conformations are identical, whereas the two remaining conformations are only detectable by nuclear magnetic resonance spectroscopy in either the apo or holo form. We further demonstrate that this conformational diversity is an essential prerequisite for the directed movement of the 4'-PP cofactor and its interaction with externally acting proteins such as thioesterases and 4'-PP transferase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koglin, Alexander -- Mofid, Mohammad R -- Lohr, Frank -- Schafer, Birgit -- Rogov, Vladimir V -- Blum, Marc-Michael -- Mittag, Tanja -- Marahiel, Mohamed A -- Bernhard, Frank -- Dotsch, Volker -- New York, N.Y. -- Science. 2006 Apr 14;312(5771):273-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Biophysical Chemistry, Centre for Biomolecular Magnetic Resonance (BMRZ), J.W. Goethe University of Frankfurt, Marie-Curie-Strasse, D-60439 Frankfurt/Main, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16614225" target="_blank"〉PubMed〈/a〉
    Keywords: Apoproteins/chemistry/metabolism ; Bacterial Proteins/chemistry/metabolism ; Binding Sites ; Carrier Proteins/*chemistry/*metabolism ; Crystallography, X-Ray ; Fatty Acid Synthases/metabolism ; Holoenzymes/chemistry/metabolism ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; Pantetheine/analogs & derivatives/metabolism ; Peptide Synthases/*chemistry/*metabolism ; *Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Thiolester Hydrolases/metabolism ; Transferases/metabolism
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  • 52
    Publication Date: 2006-05-06
    Description: Ediacaran assemblages immediately predate the Cambrian explosion of metazoans and should have played a crucial role in this radiation. Their wider relationships, however, have remained refractory and difficult to integrate with early metazoan phylogeny. Here, we describe a frondlike fossil, Stromatoveris (S. psygmoglena sp. nov.), from the Lower Cambrian Chengjiang Lagerstatte (Yunnan, China) that is strikingly similar to Ediacaran vendobionts. The exquisite preservation reveals closely spaced branches, probably ciliated, that appear to represent precursors of the diagnostic comb rows of ctenophores. Therefore, this finding has important implications for the early evolution of this phylum and related diploblasts, some of which independently evolved a frondose habit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shu, D-G -- Morris, S Conway -- Han, J -- Li, Y -- Zhang, X-L -- Hua, H -- Zhang, Z-F -- Liu, J-N -- Guo, J-F -- Yao, Y -- Yasui, K -- New York, N.Y. -- Science. 2006 May 5;312(5774):731-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Early Life Institute and Key Laboratory of Continental Dynamics, Northwest University, Xi'an 710069, China. elidgshu@nwu.edu.cn〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16675697" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; China ; *Fossils ; Geologic Sediments ; Invertebrates/*anatomy & histology/*classification ; Phylogeny
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  • 53
    Publication Date: 2006-12-13
    Description: The crystal structure of a putative metal-chelate-type adenosine triphosphate (ATP)-binding cassette (ABC) transporter encoded by genes HI1470 and HI1471 of Haemophilus influenzae has been solved at 2.4 angstrom resolution. The permeation pathway exhibits an inward-facing conformation, in contrast to the outward-facing state previously observed for the homologous vitamin B12 importer BtuCD. Although the structures of both HI1470/1 and BtuCD have been solved in nucleotide-free states, the pairs of ABC subunits in these two structures differ by a translational shift in the plane of the membrane that coincides with a repositioning of the membrane-spanning subunits. The differences observed between these ABC transporters involve relatively modest rearrangements and may serve as structural models for inward- and outward-facing conformations relevant to the alternating access mechanism of substrate translocation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pinkett, H W -- Lee, A T -- Lum, P -- Locher, K P -- Rees, D C -- GM45162/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Jan 19;315(5810):373-7. Epub 2006 Dec 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, Howard Hughes Medical Institute, MC 114-96, California Institute of Technology (Caltech), Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17158291" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/*chemistry ; Bacterial Proteins/*chemistry ; Catalytic Domain ; Crystallography, X-Ray ; Dimerization ; Haemophilus influenzae/*chemistry ; Metals/metabolism ; Models, Molecular ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry
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  • 54
    Publication Date: 2006-12-13
    Description: Because animals require oxygen, an increase in late-Neoproterozoic oxygen concentrations has been suggested as a stimulus for their evolution. The iron content of deep-sea sediments shows that the deep ocean was anoxic and ferruginous before and during the Gaskiers glaciation 580 million years ago and that it became oxic afterward. The first known members of the Ediacara biota arose shortly after the Gaskiers glaciation, suggesting a causal link between their evolution and this oxygenation event. A prolonged stable oxic environment may have permitted the emergence of bilateral motile animals some 25 million years later.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Canfield, Don E -- Poulton, Simon W -- Narbonne, Guy M -- New York, N.Y. -- Science. 2007 Jan 5;315(5808):92-5. Epub 2006 Dec 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nordic Center for Earth Evolution (NordCEE) and Institute of Biology, University of Southern Denmark, Campusvej 55, 5230 Odense M, Denmark. dec@biology.sdu.dk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17158290" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Atmosphere ; *Biological Evolution ; *Fossils ; Geologic Sediments/chemistry ; Ice Cover ; Iron/analysis ; Newfoundland and Labrador ; Oxidation-Reduction ; Oxygen/*analysis ; Seawater/*chemistry ; Sulfates/analysis ; Time
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  • 55
    Publication Date: 2006-06-03
    Description: The hexavalent state, considered to be the highest oxidation level accessible for iron, has previously been found only in the tetrahedral ferrate dianion, FeO4(2-). We report the photochemical synthesis of another Fe(VI) compound, an octahedrally coordinated dication bearing a terminal nitrido ligand. Mossbauer and x-ray absorption spectra, supported by density functional theory, are consistent with the octahedral structure having an FeN triple bond of 1.57 angstroms and a singlet d2(xy) ground electronic configuration. The compound is stable at 77 kelvin and yields a high-spin Fe(III) species upon warming.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berry, John F -- Bill, Eckhard -- Bothe, Eberhard -- George, Serena DeBeer -- Mienert, Bernd -- Neese, Frank -- Wieghardt, Karl -- New York, N.Y. -- Science. 2006 Jun 30;312(5782):1937-41. Epub 2006 Jun 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Bioanorganische Chemie, Stiftstrasse 34-36, D-45470 Mulheim an der Ruhr, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16741074" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; Cold Temperature ; Electrochemistry ; Iron/*chemistry ; Isomerism ; Models, Molecular ; Molecular Structure ; Nitrogen/chemistry ; Organometallic Compounds/*chemistry ; Oxidation-Reduction ; Photochemistry ; Photolysis ; Physicochemical Phenomena ; Spectrophotometry, Infrared ; Spectroscopy, Mossbauer ; Spectrum Analysis
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  • 56
    Publication Date: 2006-06-03
    Description: In Gram-negative bacteria, the import of essential micronutrients across the outer membrane requires a transporter, an electrochemical gradient of protons across the inner membrane, and an inner membrane protein complex (ExbB, ExbD, TonB) that couples the proton-motive force to the outer membrane transporter. The inner membrane protein TonB binds directly to a conserved region, called the Ton-box, of the transporter. We solved the structure of the cobalamin transporter BtuB in complex with the C-terminal domain of TonB. In contrast to its conformations in the absence of TonB, the Ton-box forms a beta strand that is recruited to the existing beta sheet of TonB, which is consistent with a mechanical pulling model of transport.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shultis, David D -- Purdy, Michael D -- Banchs, Christian N -- Wiener, Michael C -- DK59999/DK/NIDDK NIH HHS/ -- GM00Z055/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Jun 2;312(5778):1396-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16741124" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Outer Membrane Proteins/*chemistry/metabolism ; Biological Transport, Active ; Crystallography, X-Ray ; Escherichia coli ; Escherichia coli Proteins/*chemistry/metabolism ; Magnetic Resonance Spectroscopy ; Membrane Proteins/*chemistry/metabolism ; Membrane Transport Proteins/*chemistry/metabolism ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-05-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2006 May 19;312(5776):985-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16709756" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Dna ; Evolution, Molecular ; Fossils ; Genome ; *Genome, Human ; Humans ; Hybridization, Genetic ; Pan troglodytes/*genetics ; Time
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  • 58
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-03-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2006 Mar 10;311(5766):1372-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16527944" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Animals ; *Biological Evolution ; Birds ; Cichlids ; Ecology ; Female ; Finches ; Geography ; Insects ; Lizards ; Male ; Sexual Behavior, Animal
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-11-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bhattacharjee, Yudhijit -- New York, N.Y. -- Science. 2006 Nov 17;314(5802):1063.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17110543" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; *Embryo Research ; *Embryonic Stem Cells ; Federal Government ; *Politics ; United States
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-02-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2006 Feb 10;311(5762):766-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16469892" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Cypriniformes/anatomy & histology/genetics ; Databases, Factual ; *Fishes/anatomy & histology/embryology/growth & development ; Gastrula ; Interdisciplinary Communication ; *Research ; Terminology as Topic ; *Zebrafish/embryology/genetics/growth & development
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-02-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2006 Feb 3;311(5761):591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16456043" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological/*genetics ; Animals ; *Biological Evolution ; Genes, Insect ; *Genetic Variation ; Juvenile Hormones/physiology ; Larva/genetics/physiology ; Manduca/*genetics/physiology ; Mutation ; Phenotype ; Pigmentation/*genetics ; Temperature
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  • 62
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-08-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Jon D -- Scott, Eugenie C -- Okamoto, Shinji -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):765-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Michigan State University, East Lansing, MI 48824-1115, USA. jdmiller@msu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902112" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Age Factors ; *Attitude ; *Biological Evolution ; Educational Status ; Europe ; Female ; Genetics ; Humans ; Japan ; Male ; Politics ; *Public Opinion ; Public Policy ; Religion ; Religion and Science ; Sex Factors ; Surveys and Questionnaires ; United States
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  • 63
    Publication Date: 2006-06-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bhattacharjee, Yudhijit -- New York, N.Y. -- Science. 2006 Jun 23;312(5781):1727.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16794045" target="_blank"〉PubMed〈/a〉
    Keywords: *Altruism ; *Biological Evolution ; Cross-Cultural Comparison ; *Cultural Evolution ; Games, Experimental ; Humans ; *Punishment ; Social Behavior
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  • 64
    Publication Date: 2006-02-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bhattacharjee, Yudhijit -- New York, N.Y. -- Science. 2006 Feb 3;311(5761):588-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16456041" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Kansas ; *Politics ; *Religion and Science ; Science/*education
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  • 65
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-03-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johns, David -- New York, N.Y. -- Science. 2006 Mar 10;311(5766):1376.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16527949" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Confidentiality ; Korea ; *Religion and Science ; Science/education/standards ; *Scientific Misconduct ; United States
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  • 66
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-08-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kramer, Elena M -- Donohue, Kathleen -- New York, N.Y. -- Science. 2006 Aug 18;313(5789):924-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Organismic and Evolutionary Biology, Harvard University, Cambridge, MA 02138, USA. ekramer@oeb.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16917048" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptation, Biological ; Alleles ; Antirrhinum/*genetics ; *Biological Evolution ; Flowers/*genetics ; Genes, Plant ; *Genetic Speciation ; Genotype ; Hybridization, Genetic ; Models, Genetic ; Phenotype ; Pigmentation/*genetics ; Selection, Genetic
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-04-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, Ann -- New York, N.Y. -- Science. 2006 Apr 14;312(5771):178.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16614183" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Bone and Bones/anatomy & histology ; Ethiopia ; Female ; *Fossils ; Geologic Sediments ; *Hominidae/anatomy & histology/classification ; Paleodontology ; Paleontology ; Posture
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  • 68
    Publication Date: 2006-09-02
    Description: On the basis of new information from the 10th specimen of Archaeopteryx, Mayr et al. (Reports, 2 December 2005, p. 1483) suggested that birds, or avian flight, originated twice. We investigate the statistical support for this phylogenetic hypothesis and show that it is no better supported by available morphological character data than the hypothesis of a single avian origin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corfe, Ian J -- Butler, Richard J -- New York, N.Y. -- Science. 2006 Sep 1;313(5791):1238; author reply 1238.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth Sciences, University of Bristol, Wills Memorial Building, Queens Road, Bristol, BS8 1RJ, UK. ian.corfe@bristol.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16946054" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Birds/anatomy & histology/classification ; Bone and Bones/anatomy & histology ; *Dinosaurs ; Flight, Animal ; Fossils ; Phylogeny
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  • 69
    Publication Date: 2006-08-19
    Description: To understand evolutionary paths connecting diverse biological forms, we defined a three-dimensional genotypic space separating two flower color morphs of Antirrhinum. A hybrid zone between morphs showed a steep cline specifically at genes controlling flower color differences, indicating that these loci are under selection. Antirrhinum species with diverse floral phenotypes formed a U-shaped cloud within the genotypic space. We propose that this cloud defines an evolutionary path that allows flower color to evolve while circumventing less-adaptive regions. Hybridization between morphs located in different arms of the U-shaped path yields low-fitness genotypes, accounting for the observed steep clines at hybrid zones.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Whibley, Annabel C -- Langlade, Nicolas B -- Andalo, Christophe -- Hanna, Andrew I -- Bangham, Andrew -- Thebaud, Christophe -- Coen, Enrico -- New York, N.Y. -- Science. 2006 Aug 18;313(5789):963-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Developmental Biology, John Innes Centre, Colney Lane, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16917061" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Alleles ; Antirrhinum/classification/*genetics ; Base Sequence ; *Biological Evolution ; Crosses, Genetic ; Flowers/*genetics ; Gene Flow ; Gene Frequency ; Genes, Plant ; *Genetic Speciation ; Genotype ; Haplotypes ; Hybridization, Genetic ; Models, Genetic ; Molecular Sequence Data ; Phenotype ; Phylogeny ; Pigmentation/*genetics ; Pigments, Biological/genetics ; Principal Component Analysis ; Selection, Genetic
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  • 70
    Publication Date: 2006-10-07
    Description: The evolutionary dynamics underlying the latitudinal gradient in biodiversity have been controversial for over a century. Using a spatially explicit approach that incorporates not only origination and extinction but immigration, a global analysis of genera and subgenera of marine bivalves over the past 11 million years supports an "out of the tropics" model, in which taxa preferentially originate in the tropics and expand toward the poles without losing their tropical presence. The tropics are thus both a cradle and a museum of biodiversity, contrary to the conceptual dichotomy dominant since 1974; a tropical diversity crisis would thus have profound evolutionary effects at all latitudes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jablonski, David -- Roy, Kaustuv -- Valentine, James W -- New York, N.Y. -- Science. 2006 Oct 6;314(5796):102-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Geophysical Sciences, University of Chicago, 5734 South Ellis Avenue, Chicago, IL 60637, USA. djablons@uchicago.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17023653" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; *Biological Evolution ; *Bivalvia/classification ; *Fossils ; Geography ; Models, Biological ; Phylogeny ; Population Dynamics ; *Tropical Climate
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  • 71
    Publication Date: 2006-03-25
    Description: Prochlorococcus ecotypes are a useful system for exploring the origin and function of diversity among closely related microbes. The genetic variability between phenotypically distinct strains that differ by less that 1% in 16S ribosomal RNA sequences occurs mostly in genomic islands. Island genes appear to have been acquired in part by phage-mediated lateral gene transfer, and some are differentially expressed under light and nutrient stress. Furthermore, genome fragments directly recovered from ocean ecosystems indicate that these islands are variable among cooccurring Prochlorococcus cells. Genomic islands in this free-living photoautotroph share features with pathogenicity islands of parasitic bacteria, suggesting a general mechanism for niche differentiation in microbial species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coleman, Maureen L -- Sullivan, Matthew B -- Martiny, Adam C -- Steglich, Claudia -- Barry, Kerrie -- Delong, Edward F -- Chisholm, Sallie W -- New York, N.Y. -- Science. 2006 Mar 24;311(5768):1768-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Massachusetts Institute of Technology, Department of Civil and Environmental Engineering, 15 Vassar Street, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16556843" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Atlantic Ocean ; Bacteriophages/*genetics/physiology ; *Biological Evolution ; *Ecosystem ; Gene Expression Regulation, Bacterial ; Gene Transfer, Horizontal ; Genes, Bacterial ; Genome, Bacterial ; *Genomic Islands ; Light ; Molecular Sequence Data ; Pacific Ocean ; Phylogeny ; Prochlorococcus/classification/*genetics/isolation & purification/*physiology ; Seawater/*microbiology
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  • 72
    Publication Date: 2006-12-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wares, John P -- Barber, Paul H -- Ross-Ibarra, Jeffrey -- Sotka, Erik E -- Toonen, Robert J -- New York, N.Y. -- Science. 2006 Dec 1;314(5804):1388-90; author reply 1388-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17144000" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; DNA, Mitochondrial/*genetics ; *Genetic Variation ; Invertebrates/*genetics ; Meta-Analysis as Topic ; *Polymorphism, Genetic ; Population Density ; Vertebrates/*genetics
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  • 73
    Publication Date: 2006-11-25
    Description: Canonical cap-dependent translation initiation requires a large number of protein factors that act in a stepwise assembly process. In contrast, internal ribosomal entry sites (IRESs) are cis-acting RNAs that in some cases completely supplant these factors by recruiting and activating the ribosome using a single structured RNA. Here we present the crystal structures of the ribosome-binding domain from a Dicistroviridae intergenic region IRES at 3.1 angstrom resolution, providing a view of the prefolded architecture of an all-RNA translation initiation apparatus. Docking of the structure into cryo-electron microscopy reconstructions of an IRES-ribosome complex suggests a model for ribosome manipulation by a dynamic IRES RNA.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2669756/" 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/PMC2669756/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pfingsten, Jennifer S -- Costantino, David A -- Kieft, Jeffrey S -- R01 GM072560/GM/NIGMS NIH HHS/ -- R01 GM072560-01/GM/NIGMS NIH HHS/ -- R01 GM072560-02/GM/NIGMS NIH HHS/ -- R01 GM072560-03/GM/NIGMS NIH HHS/ -- R01 GM072560-04/GM/NIGMS NIH HHS/ -- R01 GM072560-05/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Dec 1;314(5804):1450-4. Epub 2006 Nov 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Genetics, University of Colorado at Denver and Health Sciences Center, Mail Stop 8101, Post Office Box 6511, Aurora, CO 80045, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17124290" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cryoelectron Microscopy ; Crystallization ; Crystallography, X-Ray ; Models, Molecular ; Mutation ; Nucleic Acid Conformation ; *Protein Biosynthesis ; RNA Viruses/*genetics ; RNA, Viral/*chemistry/genetics/metabolism ; *Regulatory Sequences, Ribonucleic Acid/genetics ; Ribosomes/*metabolism
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  • 74
    Publication Date: 2006-05-20
    Description: Large-scale comparative genomics in harness with proteomics has substantiated fundamental features of eukaryote cellular evolution. The evolutionary trajectory of modern eukaryotes is distinct from that of prokaryotes. Data from many sources give no direct evidence that eukaryotes evolved by genome fusion between archaea and bacteria. Comparative genomics shows that, under certain ecological settings, sequence loss and cellular simplification are common modes of evolution. Subcellular architecture of eukaryote cells is in part a physical-chemical consequence of molecular crowding; subcellular compartmentation with specialized proteomes is required for the efficient functioning of proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kurland, C G -- Collins, L J -- Penny, D -- New York, N.Y. -- Science. 2006 May 19;312(5776):1011-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbial Ecology, Lund University, Lund, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16709776" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Cell Compartmentation ; *Eukaryotic Cells ; Evolution, Molecular ; *Genomics ; Phagocytosis ; Prokaryotic Cells ; Proteome ; Selection, Genetic
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  • 75
    Publication Date: 2006-03-04
    Description: All steps of fatty acid synthesis in fungi are catalyzed by the fatty acid synthase, which forms a 2.6-megadalton alpha6beta6 complex. We have determined the molecular architecture of this multienzyme by fitting the structures of homologous enzymes that catalyze the individual steps of the reaction pathway into a 5 angstrom x-ray crystallographic electron density map. The huge assembly contains two separated reaction chambers, each equipped with three sets of active sites separated by distances up to approximately 130 angstroms, across which acyl carrier protein shuttles substrates during the reaction cycle. Regions of the electron density arising from well-defined structural features outside the catalytic domains separate the two reaction chambers and serve as a matrix in which domains carrying the various active sites are embedded. The structure rationalizes the compartmentalization of fatty acid synthesis, and the spatial arrangement of the active sites has specific implications for our understanding of the reaction cycle mechanism and of the architecture of multienzymes in general.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jenni, Simon -- Leibundgut, Marc -- Maier, Timm -- Ban, Nenad -- New York, N.Y. -- Science. 2006 Mar 3;311(5765):1263-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology and Biophysics, Department of Biology, Swiss Federal Institute of Technology (ETH Zurich), 8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16513976" target="_blank"〉PubMed〈/a〉
    Keywords: Acyl Carrier Protein/chemistry/metabolism ; Ascomycota/*enzymology ; Binding Sites ; Catalytic Domain ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Fatty Acid Synthases/*chemistry/isolation & purification/metabolism ; Fatty Acids/biosynthesis ; Models, Molecular ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Sequence Homology, Amino Acid
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  • 76
    Publication Date: 2006-12-23
    Description: Iron regulatory protein 1 (IRP1) binds iron-responsive elements (IREs) in messenger RNAs (mRNAs), to repress translation or degradation, or binds an iron-sulfur cluster, to become a cytosolic aconitase enzyme. The 2.8 angstrom resolution crystal structure of the IRP1:ferritin H IRE complex shows an open protein conformation compared with that of cytosolic aconitase. The extended, L-shaped IRP1 molecule embraces the IRE stem-loop through interactions at two sites separated by approximately 30 angstroms, each involving about a dozen protein:RNA bonds. Extensive conformational changes related to binding the IRE or an iron-sulfur cluster explain the alternate functions of IRP1 as an mRNA regulator or enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walden, William E -- Selezneva, Anna I -- Dupuy, Jerome -- Volbeda, Anne -- Fontecilla-Camps, Juan C -- Theil, Elizabeth C -- Volz, Karl -- DK20251/DK/NIDDK NIH HHS/ -- DK47281/DK/NIDDK NIH HHS/ -- GM47522/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Dec 22;314(5807):1903-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of Illinois at Chicago, Chicago, IL 60612-7344, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17185597" target="_blank"〉PubMed〈/a〉
    Keywords: Apoferritins/*genetics ; Binding Sites ; Crystallography, X-Ray ; Hydrogen Bonding ; Iron/metabolism ; Iron Regulatory Protein 1/*chemistry/*metabolism ; Models, Molecular ; Nucleic Acid Conformation ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA, Messenger/chemistry/genetics/metabolism ; *Regulatory Sequences, Ribonucleic Acid ; *Response Elements ; Sulfur/metabolism ; Untranslated Regions/*chemistry/*metabolism
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  • 77
    Publication Date: 2006-09-02
    Description: Extreme gene duplication is a major source of evolutionary novelty. A genome-wide survey of gene copy number variation among human and great ape lineages revealed that the most striking human lineage-specific amplification was due to an unknown gene, MGC8902, which is predicted to encode multiple copies of a protein domain of unknown function (DUF1220). Sequences encoding these domains are virtually all primate-specific, show signs of positive selection, and are increasingly amplified generally as a function of a species' evolutionary proximity to humans, where the greatest number of copies (212) is found. DUF1220 domains are highly expressed in brain regions associated with higher cognitive function, and in brain show neuron-specific expression preferentially in cell bodies and dendrites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Popesco, Magdalena C -- Maclaren, Erik J -- Hopkins, Janet -- Dumas, Laura -- Cox, Michael -- Meltesen, Lynne -- McGavran, Loris -- Wyckoff, Gerald J -- Sikela, James M -- AA11853/AA/NIAAA NIH HHS/ -- New York, N.Y. -- Science. 2006 Sep 1;313(5791):1304-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Human Medical Genetics, University of Colorado at Denver and Health Sciences Center, Aurora, CO 80045, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16946073" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Biological Evolution ; Brain/*metabolism ; Cognition ; Exons ; *Gene Amplification ; Gene Dosage ; Gene Duplication ; Gene Expression ; Genome, Human ; Humans ; Macaca mulatta/genetics ; Mice ; Molecular Sequence Data ; Neocortex/metabolism ; Neurons/*metabolism ; Pan troglodytes/genetics ; Phylogeny ; Polymerase Chain Reaction ; *Protein Structure, Tertiary ; Proteins/*chemistry/genetics ; Rats ; *Selection, Genetic
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  • 78
    Publication Date: 2006-09-16
    Description: We used nuclear magnetic resonance relaxation dispersion to characterize higher energy conformational substates of Escherichia coli dihydrofolate reductase. Each intermediate in the catalytic cycle samples low-lying excited states whose conformations resemble the ground-state structures of preceding and following intermediates. Substrate and cofactor exchange occurs through these excited substates. The maximum hydride transfer and steady-state turnover rates are governed by the dynamics of transitions between ground and excited states of the intermediates. Thus, the modulation of the energy landscape by the bound ligands funnels the enzyme through its reaction cycle along a preferred kinetic path.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boehr, David D -- McElheny, Dan -- Dyson, H Jane -- Wright, Peter E -- GM56879/GM/NIGMS NIH HHS/ -- GM75995/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Sep 15;313(5793):1638-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Skaggs Institute for Chemical Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16973882" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Escherichia coli/*enzymology ; Kinetics ; Ligands ; Models, Molecular ; NADP/metabolism ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; *Protein Conformation ; Tetrahydrofolate Dehydrogenase/*chemistry/*metabolism ; Tetrahydrofolates/metabolism ; Thermodynamics
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  • 79
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-07-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steven, Alasdair C -- Spear, Patricia G -- New York, N.Y. -- Science. 2006 Jul 14;313(5784):177-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Structural Biology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, 50 South Drive, Bethesda, MD 20892, USA. stevena@mail.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16840685" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophages/chemistry/genetics ; Capsid Proteins/chemistry ; Crystallography, X-Ray ; *Evolution, Molecular ; Genome, Viral ; Herpesvirus 1, Human/*chemistry/genetics ; Hydrogen-Ion Concentration ; Membrane Glycoproteins/*chemistry/genetics ; Models, Molecular ; Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Vesicular stomatitis Indiana virus/*chemistry/genetics ; Viral Envelope Proteins/*chemistry/genetics ; Viral Fusion Proteins/*chemistry/genetics
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  • 80
    Publication Date: 2006-01-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mervis, Jeffrey -- New York, N.Y. -- Science. 2006 Jan 6;311(5757):34.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16400124" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Biological Science Disciplines/*education ; Curriculum ; Education/legislation & jurisprudence ; Pennsylvania
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  • 81
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-11-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stokstad, Erik -- New York, N.Y. -- Science. 2006 Nov 10;314(5801):921.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17095675" target="_blank"〉PubMed〈/a〉
    Keywords: *Amphibians ; Animals ; *Biological Evolution ; Fossils ; Paleodontology ; *Paleontology ; *Whales
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  • 82
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-12-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boyd, Robert -- New York, N.Y. -- Science. 2006 Dec 8;314(5805):1555-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anthropology, University of California, Los Angeles, CA 90095, USA. rboyd@anthro.ucla.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17158313" target="_blank"〉PubMed〈/a〉
    Keywords: *Altruism ; Animals ; *Biological Evolution ; Competitive Behavior ; *Cooperative Behavior ; Cultural Evolution ; Family ; *Genetic Variation ; Humans ; Language ; Selection, Genetic ; *Social Behavior
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  • 83
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-09-30
    Description: The family of Hox genes, which number 4 to 48 per genome depending on the animal, control morphologies on the main body axis of nearly all metazoans. The conventional wisdom is that Hox genes are arranged in chromosomal clusters in colinear order with their expression patterns on the body axis. However, recent evidence has shown that Hox gene clusters are fragmented, reduced, or expanded in many animals-findings that correlate with interesting morphological changes in evolution. Hox gene clusters also contain many noncoding RNAs, such as intergenic regulatory transcripts and evolutionarily conserved microRNAs, some of whose developmental functions have recently been explored.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lemons, Derek -- McGinnis, William -- R37 HD028315/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2006 Sep 29;313(5795):1918-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Cell and Developmental Biology, 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/17008523" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Body Patterning/genetics ; Evolution, Molecular ; Gene Dosage ; Gene Expression Regulation, Developmental ; Gene Order ; *Genes, Homeobox ; Humans ; Invertebrates/*genetics ; MicroRNAs/genetics ; *Multigene Family ; RNA, Untranslated/genetics ; Transcription Factors/*genetics/physiology ; Vertebrates/*genetics
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  • 84
    Publication Date: 2006-05-20
    Description: The endemic species richness on Madagascar, relative to landmass area, is unparalleled in the world. Many organisms on the island have restricted geographical ranges. A comprehensive hypothesis explaining the evolution of this microendemism has yet to be developed. Using an analysis of watersheds in the context of Quaternary climatic shifts, we provide a new mechanistic model to explain the process of explosive speciation on the island. River catchments with sources at relatively low elevations were zones of isolation and hence led to the speciation of locally endemic taxa, whereas those at higher elevations were zones of retreat and dispersion and hence contain proportionately lower levels of microendemism. These results provide a framework for biogeographic and phylogeographic studies, as well as a basis for prioritizing conservation actions of the remaining natural forest habitats on the island.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilme, Lucienne -- Goodman, Steven M -- Ganzhorn, Jorg U -- New York, N.Y. -- Science. 2006 May 19;312(5776):1063-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Missouri Botanical Garden, Boite Postale 3391, Antananarivo (101), Madagascar.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16709785" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; *Biological Evolution ; Climate ; Genetic Speciation ; Geography ; Madagascar ; Models, Biological ; Rivers ; Trees ; Vertebrates
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  • 85
    Publication Date: 2006-01-21
    Description: Scaffold proteins organize signaling proteins into pathways and are often viewed as passive assembly platforms. We found that the Ste5 scaffold has a more active role in the yeast mating pathway: A fragment of Ste5 allosterically activated autophosphorylation of the mitogen-activated protein kinase Fus3. The resulting form of Fus3 is partially active-it is phosphorylated on only one of two key residues in the activation loop. Unexpectedly, at a systems level, autoactivated Fus3 appears to have a negative regulatory role, promoting Ste5 phosphorylation and a decrease in pathway transcriptional output. Thus, scaffolds not only direct basic pathway connectivity but can precisely tune quantitative pathway input-output properties.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bhattacharyya, Roby P -- Remenyi, Attila -- Good, Matthew C -- Bashor, Caleb J -- Falick, Arnold M -- Lim, Wendell A -- New York, N.Y. -- Science. 2006 Feb 10;311(5762):822-6. Epub 2006 Jan 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California-San Francisco, 600 16th Street, San Francisco, CA 94143-2240, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16424299" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/*chemistry/genetics/*metabolism ; Allosteric Regulation ; Amino Acid Motifs ; Binding Sites ; Crystallography, X-Ray ; Down-Regulation ; Enzyme Activation ; *MAP Kinase Signaling System ; Mitogen-Activated Protein Kinases/*chemistry/*metabolism ; Models, Biological ; Models, Molecular ; Mutation ; Pheromones/*physiology ; Phosphorylation ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/*chemistry/genetics/*metabolism ; Transcription, Genetic
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  • 86
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-08-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bhattarcharjee, Yudhijit -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):743.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902095" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Biology/*education ; Education/*standards ; Kansas ; Politics ; *Religion and Science
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  • 87
    Publication Date: 2006-03-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉von Grotthuss, Marcin -- Rychlewski, Leszek -- New York, N.Y. -- Science. 2006 Mar 3;311(5765):1241-2; author reply 1241-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16513967" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; Dog Diseases/virology ; Dogs ; Glycosylation ; Hemagglutinin Glycoproteins, Influenza Virus/*chemistry/*genetics/immunology ; Horse Diseases/virology ; Horses ; Influenza A Virus, H3N8 Subtype/*genetics ; Models, Molecular ; *Mutation ; Orthomyxoviridae Infections/*veterinary/virology ; Protein Conformation
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  • 88
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-03-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, Stuart -- New York, N.Y. -- Science. 2006 Mar 3;311(5765):1251-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Children's Hospital Oakland Research Institute, Oakland, CA 94609, USA. ssmith@chori.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16513973" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Catalytic Domain ; Crystallography, X-Ray ; Dimerization ; Evolution, Molecular ; Fatty Acid Synthases/*chemistry/metabolism ; Fatty Acids/biosynthesis ; Fungi/enzymology ; Models, Molecular ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Protein Subunits/chemistry
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  • 89
    Publication Date: 2006-01-10
    Description: Modern felid species descend from relatively recent (〈11 million years ago) divergence and speciation events that produced successful predatory carnivores worldwide but that have confounded taxonomic classifications. A highly resolved molecular phylogeny with divergence dates for all living cat species, derived from autosomal, X-linked, Y-linked, and mitochondrial gene segments (22,789 base pairs) and 16 fossil calibrations define eight principal lineages produced through at least 10 intercontinental migrations facilitated by sea-level fluctuations. A ghost lineage analysis indicates that available felid fossils underestimate (i.e., unrepresented basal branch length) first occurrence by an average of 76%, revealing a low representation of felid lineages in paleontological remains. The phylogenetic performance of distinct gene classes showed that Y-chromosome segments are appreciably more informative than mitochondrial DNA, X-linked, or autosomal genes in resolving the rapid Felidae species radiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, Warren E -- Eizirik, Eduardo -- Pecon-Slattery, Jill -- Murphy, William J -- Antunes, Agostinho -- Teeling, Emma -- O'Brien, Stephen J -- N01-CO-12400/CO/NCI NIH HHS/ -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2006 Jan 6;311(5757):73-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genomic Diversity, National Cancer Institute, Frederick, MD 21702-1201, USA. johnsonw@ncifcrf.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16400146" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Americas ; Animals ; Asia ; *Biological Evolution ; Cats/classification/genetics ; DNA/genetics ; DNA, Mitochondrial/genetics ; Europe ; Felidae/*classification/*genetics ; Felis/classification/genetics ; Fossils ; Genes ; *Genetic Speciation ; Lynx/classification/genetics ; Panthera/classification/genetics ; Phylogeny ; Puma/classification/genetics ; X Chromosome/genetics ; Y Chromosome/genetics
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  • 90
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-04-08
    Description: In female heterogamous (ZW) species, sex-linked genes coding for maternal products that are packaged into the egg open a unique arena for genetic conflict that does not occur in male heterogamous (XY) species. Z-linked maternal-effect alleles that help sons and harm daughters are expected to go to fixation, as are W-linked alleles that help daughters and harm sons. This conflict differs from known cases of meiotic drive, because sex-specific ontogeny, physiology, and gene expression greatly simplify the genetic interactions that lead to sexual conflict. Selection on maternal-effect genes may substantially alter the evolution of ZW compared with XY systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Paige M -- Gavrilets, Sergey -- Rice, William R -- GM56693/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Apr 7;312(5770):73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology, Evolution, and Marine Biology, University of California, Santa Barbara, CA 93106, USA. pmiller@lifesci.ucsb.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16601185" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; *Biological Evolution ; Female ; *Genes ; Male ; Mathematics ; *Selection, Genetic ; Sex Chromosomes/*genetics
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  • 91
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-06-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, Ann -- New York, N.Y. -- Science. 2006 Jun 23;312(5781):1739-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16794057" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Fossils ; *Hominidae ; Humans ; *Paleontology ; Posture ; Walking
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  • 92
    Publication Date: 2006-03-18
    Description: The hemagglutinin (HA) structure at 2.9 angstrom resolution, from a highly pathogenic Vietnamese H5N1 influenza virus, is more related to the 1918 and other human H1 HAs than to a 1997 duck H5 HA. Glycan microarray analysis of this Viet04 HA reveals an avian alpha2-3 sialic acid receptor binding preference. Introduction of mutations that can convert H1 serotype HAs to human alpha2-6 receptor specificity only enhanced or reduced affinity for avian-type receptors. However, mutations that can convert avian H2 and H3 HAs to human receptor specificity, when inserted onto the Viet04 H5 HA framework, permitted binding to a natural human alpha2-6 glycan, which suggests a path for this H5N1 virus to gain a foothold in the human population.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stevens, James -- Blixt, Ola -- Tumpey, Terrence M -- Taubenberger, Jeffery K -- Paulson, James C -- Wilson, Ian A -- AI058113/AI/NIAID NIH HHS/ -- AI42266/AI/NIAID NIH HHS/ -- CA55896/CA/NCI NIH HHS/ -- GM060938/GM/NIGMS NIH HHS/ -- GM062116/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Apr 21;312(5772):404-10. Epub 2006 Mar 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. jstevens@scripps.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16543414" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Antigenic Variation ; Binding Sites ; Birds ; Carbohydrate Conformation ; Cloning, Molecular ; Crystallography, X-Ray ; Glycosylation ; Hemagglutinin Glycoproteins, Influenza ; Virus/*chemistry/genetics/immunology/*metabolism ; Humans ; Influenza A Virus, H5N1 Subtype/*chemistry/genetics/metabolism/*pathogenicity ; Lung/virology ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Polysaccharides/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Receptors, Virus/chemistry/*metabolism ; Respiratory Mucosa/virology ; Sialic Acids/chemistry/metabolism ; Species Specificity ; Virulence
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  • 93
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-02-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Culotta, Elizabeth -- New York, N.Y. -- Science. 2006 Feb 10;311(5762):770.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16469894" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Biological Science Disciplines/*education ; Curriculum ; Humans ; *Teaching ; United States
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  • 94
    Publication Date: 2006-03-25
    Description: The evolution of oxygenic photosynthesis and ensuing oxygenation of Earth's atmosphere represent a major transition in the history of life. Although many organisms retreated to anoxic environments, others evolved to use oxygen as a high-potential redox couple while concomitantly mitigating its toxicity. To understand the changes in biochemistry and enzymology that accompanied adaptation to O2, we integrated network analysis with information on enzyme evolution to infer how oxygen availability changed the architecture of metabolic networks. Our analysis revealed the existence of four discrete groups of networks of increasing complexity, with transitions between groups being contingent on the presence of key metabolites, including molecular oxygen, which was required for transition into the largest networks.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Raymond, Jason -- Segre, Daniel -- New York, N.Y. -- Science. 2006 Mar 24;311(5768):1764-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Microbial Systems Division, Biosciences Directorate, Lawrence Livermore National Laboratory, Livermore, CA 94550, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16556842" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Aerobiosis ; Anaerobiosis ; Animals ; *Biological Evolution ; Coenzyme A/metabolism ; Computational Biology ; Computer Simulation ; Databases, Genetic ; Enzymes/metabolism ; Eukaryotic Cells ; *Evolution, Molecular ; Gene Duplication ; *Metabolism ; Monte Carlo Method ; Oxidation-Reduction ; Oxygen/*metabolism ; Photosynthesis ; Phylogeny ; Sulfur/metabolism ; Thermodynamics
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  • 95
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-08-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stokstad, Erik -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):745.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902097" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Animals ; *Biological Evolution ; Bivalvia/anatomy & histology/*physiology ; *Brachyura ; *Ecosystem ; Predatory Behavior
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  • 96
    Publication Date: 2006-06-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bradshaw, William E -- Holzapfel, Christina M -- New York, N.Y. -- Science. 2006 Jun 9;312(5779):1477-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Ecology and Evolutionary Biology, University of Oregon, Eugene, OR 97403, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16763134" target="_blank"〉PubMed〈/a〉
    Keywords: *Acclimatization/genetics ; Animals ; *Biological Evolution ; Climate
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  • 97
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-05-20
    Description: Planning for future needs, not just current ones, is one of the most formidable human cognitive achievements. Whether this skill is a uniquely human adaptation is a controversial issue. In a study we conducted, bonobos and orangutans selected, transported, and saved appropriate tools above baseline levels to use them 1 hour later (experiment 1). Experiment 2 extended these results to a 14-hour delay between collecting and using the tools. Experiment 3 showed that seeing the apparatus during tool selection was not necessary to succeed. These findings suggest that the precursor skills for planning for the future evolved in great apes before 14 million years ago, when all extant great ape species shared a common ancestor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mulcahy, Nicholas J -- Call, Josep -- New York, N.Y. -- Science. 2006 May 19;312(5776):1038-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute for Evolutionary Anthropology, Deutscher Platz 6, D-04103 Leipzig, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16709782" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Association Learning ; *Biological Evolution ; *Cognition ; *Mental Processes ; *Pan paniscus ; Pan troglodytes ; *Pongo pygmaeus
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  • 98
    Publication Date: 2006-06-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stokstad, Erik -- New York, N.Y. -- Science. 2006 Jun 23;312(5781):1730.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16794049" target="_blank"〉PubMed〈/a〉
    Keywords: *Amber ; Animals ; *Biological Evolution ; DNA, Complementary ; Fibroins/*genetics ; *Fossils ; Genes ; *Silk/genetics ; *Spiders/genetics/physiology
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  • 99
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-03-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gordon, Kenneth R -- New York, N.Y. -- Science. 2006 Mar 3;311(5765):1240-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16513966" target="_blank"〉PubMed〈/a〉
    Keywords: Bias (Epidemiology) ; *Biological Evolution ; Humans ; *Language ; *Mutation ; *Science
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  • 100
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-07-15
    Description: Competitor species can have evolutionary effects on each other that result in ecological character displacement; that is, divergence in resource-exploiting traits such as jaws and beaks. Nevertheless, the process of character displacement occurring in nature, from the initial encounter of competitors to the evolutionary change in one or more of them, has not previously been investigated. Here we report that a Darwin's finch species (Geospiza fortis) on an undisturbed Galapagos island diverged in beak size from a competitor species (G. magnirostris) 22 years after the competitor's arrival, when they jointly and severely depleted the food supply. The observed evolutionary response to natural selection was the strongest recorded in 33 years of study, and close to the value predicted from the high heritability of beak size. These findings support the role of competition in models of community assembly, speciation, and adaptive radiations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grant, Peter R -- Grant, B Rosemary -- New York, N.Y. -- Science. 2006 Jul 14;313(5784):224-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and Evolutionary Biology, Princeton University, Princeton, NJ 08544-1003, USA. prgrant@princeton.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16840700" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Beak/*anatomy & histology ; *Biological Evolution ; Biomass ; Body Size ; Competitive Behavior ; Disasters ; Ecosystem ; Ecuador ; Feeding Behavior ; Female ; *Finches/anatomy & histology/physiology ; *Food ; Male ; Organ Size ; Population Density ; Population Dynamics ; *Seeds ; *Selection, Genetic ; Time Factors
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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