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  • Mutation  (1,000)
  • Astronomy
  • Earth Resources and Remote Sensing
  • American Association for the Advancement of Science (AAAS)  (1,019)
  • 2000-2004  (831)
  • 1985-1989  (188)
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  • 1
    Publication Date: 2004-12-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Easton, Douglas F -- Hopper, John L -- Thomas, Duncan C -- Antoniou, Antonis -- Pharoah, Paul D P -- Whittemore, Alice S -- Haile, Robert W -- New York, N.Y. -- Science. 2004 Dec 24;306(5705):2187-91; author reply 2187-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15622557" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Breast Neoplasms/epidemiology/*genetics ; Female ; *Genes, BRCA1 ; *Genes, BRCA2 ; *Genetic Predisposition to Disease ; Heterozygote ; Humans ; Jews/genetics ; Middle Aged ; Mutation ; Penetrance ; Risk ; Selection Bias
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2004-12-25
    Description: The position-dependent specification of root epidermal cells in Arabidopsis provides an elegant paradigm for cell patterning during development. Here, we describe a new gene, SCRAMBLED (SCM), required for cells to appropriately interpret their location within the developing root epidermis. SCM encodes a receptor-like kinase protein with a predicted extracellular domain of six leucine-rich repeats and an intracellular serine-threonine kinase domain. SCM regulates the expression of the GLABRA2, CAPRICE, WEREWOLF, and ENHANCER OF GLABRA3 transcription factor genes that define the cell fates. Further, the SCM gene is expressed throughout the developing root. Therefore, SCM likely enables developing epidermal cells to detect positional cues and establish an appropriate cell-type pattern.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kwak, Su-Hwan -- Shen, Ronglai -- Schiefelbein, John -- New York, N.Y. -- Science. 2005 Feb 18;307(5712):1111-3. Epub 2004 Dec 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1048, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15618487" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/cytology/*enzymology/*genetics/growth & development ; Arabidopsis Proteins/chemistry/*genetics/*metabolism ; Cell Division ; Cloning, Molecular ; Gene Expression Regulation, Plant ; Genes, Plant ; Genes, Reporter ; Hydrophobic and Hydrophilic Interactions ; In Situ Hybridization ; Molecular Sequence Data ; Mutation ; Plant Epidermis/cytology/enzymology/growth & development ; Plant Roots/cytology/enzymology/growth & development ; Plants, Genetically Modified ; Protein Sorting Signals ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/chemistry/*genetics/*metabolism ; RNA, Messenger/genetics/metabolism ; RNA, Plant/genetics/metabolism ; Receptor Protein-Tyrosine Kinases/chemistry/*genetics/*metabolism ; *Signal Transduction ; Transcription Factors/genetics/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 2004-12-25
    Description: beta-arrestins are multifunctional proteins that act as scaffolds and transducers of intracellular signals from heptahelical transmembrane-spanning receptors (7TMR). Hedgehog (Hh) signaling, which uses the putative 7TMR, Smoothened, is established as a fundamental pathway in development, and unregulated Hh signaling is associated with certain malignancies. Here, we show that the functional knockdown of beta-arrestin 2 in zebrafish embryos recapitulates the many phenotypes of Hh pathway mutants. Expression of wild-type beta-arrestin 2, or constitutive activation of the Hh pathway downstream of Smoothened, rescues the phenotypes caused by beta-arrestin 2 deficiency. These results suggest that a functional interaction between beta-arrestin 2 and Smoothened may be critical to regulate Hh signaling in zebrafish development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilbanks, Alyson M -- Fralish, Gregory B -- Kirby, Margaret L -- Barak, Larry S -- Li, Yin-Xiong -- Caron, Marc G -- GM069086-01/GM/NIGMS NIH HHS/ -- HL36059/HL/NHLBI NIH HHS/ -- HL61365/HL/NHLBI NIH HHS/ -- NS19576/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2004 Dec 24;306(5705):2264-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Center for Models of Human Disease, Institute for Genome Science and Policy, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15618520" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arrestins/genetics/*physiology ; Cell Differentiation ; Cyclic AMP-Dependent Protein Kinases/genetics/metabolism ; Embryo, Nonmammalian/metabolism ; Gene Expression Regulation, Developmental ; Hedgehog Proteins ; Homeodomain Proteins/genetics/metabolism ; In Situ Hybridization ; Membrane Proteins/genetics/metabolism ; Muscle Cells/cytology ; Muscle Fibers, Skeletal/cytology ; Mutation ; Phenotype ; Receptors, Cell Surface ; Receptors, G-Protein-Coupled/genetics/physiology ; Repressor Proteins/genetics/metabolism ; *Signal Transduction ; Trans-Activators/genetics/*metabolism ; Transcription Factors/genetics/metabolism ; Zebrafish/*embryology/genetics/*metabolism ; Zebrafish Proteins/genetics/metabolism/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-12-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beutler, Ernest -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2051-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Experimental Medicine, Scripps Research Institute, La Jolla, CA 92037, USA. beutler@scripps.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604397" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antimicrobial Cationic Peptides/*metabolism ; Biological Transport ; Cation Transport Proteins/genetics/*metabolism ; Enterocytes/metabolism ; Erythropoiesis ; Erythropoietin/genetics/metabolism ; Gene Expression Regulation ; Hemochromatosis/genetics ; Hepatocytes/metabolism ; Hepcidins ; Histocompatibility Antigens Class I/genetics ; Homeostasis ; Iron/*metabolism ; Iron Regulatory Protein 1/*metabolism ; Iron Regulatory Protein 2/*metabolism ; Membrane Proteins/genetics ; Mice ; Models, Biological ; Mutation ; Nitric Oxide/metabolism ; Oxygen/physiology ; Response Elements ; Signal Transduction ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 2004-12-18
    Description: The inositol pyrophosphates IP7 and IP8 contain highly energetic pyrophosphate bonds. Although implicated in various biologic functions, their molecular sites of action have not been clarified. Using radiolabeled IP7, we detected phosphorylation of multiple eukaryotic proteins. We also observed phosphorylation of endogenous proteins by endogenous IP7 in yeast. Phosphorylation by IP7 is nonenzymatic and may represent a novel intracellular signaling mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saiardi, Adolfo -- Bhandari, Rashna -- Resnick, Adam C -- Snowman, Adele M -- Snyder, Solomon H -- DA00074/DA/NIDA NIH HHS/ -- MH068830-02/MH/NIMH NIH HHS/ -- MH18501/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2101-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University, School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604408" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Drosophila Proteins/metabolism ; Drosophila melanogaster ; Escherichia coli Proteins/metabolism ; Humans ; Inositol Phosphates/*metabolism ; Kinetics ; Magnesium/metabolism ; Mice ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/chemistry/*metabolism ; Phosphates/metabolism ; Phosphorylation ; Phosphotransferases (Phosphate Group Acceptor)/metabolism ; Protein Kinases/genetics/metabolism ; Proteins/*metabolism ; RNA-Binding Proteins/chemistry/*metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry/*metabolism ; Serine/metabolism ; Signal Transduction ; Temperature
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 2004-12-18
    Description: Nutrient availability regulates life-span in a wide range of organisms. We demonstrate that in mammalian cells, acute nutrient withdrawal simultaneously augments expression of the SIRT1 deacetylase and activates the Forkhead transcription factor Foxo3a. Knockdown of Foxo3a expression inhibited the starvation-induced increase in SIRT1 expression. Stimulation of SIRT1 transcription by Foxo3a was mediated through two p53 binding sites present in the SIRT1 promoter, and a nutrient-sensitive physical interaction was observed between Foxo3a and p53. SIRT1 expression was not induced in starved p53-deficient mice. Thus, in mammalian cells, p53, Foxo3a, and SIRT1, three proteins separately implicated in aging, constitute a nutrient-sensing pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nemoto, Shino -- Fergusson, Maria M -- Finkel, Toren -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2105-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cardiovascular Branch, National Heart, Lung, and Blood Institute (NHLBI), Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604409" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/metabolism ; Animals ; Binding Sites ; Culture Media ; Culture Media, Serum-Free ; DNA-Binding Proteins/*metabolism ; Forkhead Transcription Factors ; Gene Deletion ; Genes, p53 ; Glucose ; HeLa Cells ; Humans ; Mice ; Mice, Inbred C57BL ; Mutation ; PC12 Cells ; Promoter Regions, Genetic ; RNA, Small Interfering/pharmacology ; Rats ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/metabolism ; Serum ; Sirtuin 1 ; Sirtuins/genetics/*metabolism ; *Starvation ; Transcription Factors/*metabolism ; Transcription, Genetic ; Tumor Suppressor Protein p53/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 2004-12-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stivers, James T -- GM56834-09/GM/NIGMS NIH HHS/ -- R01 GM056834/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2042; author reply 2042.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Johns Hopkins Medical School, 725 North Wolfe Street, Baltimore, MD 21205, USA. jstivers@jhmi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604391" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/enzymology/immunology/*physiology ; Catalysis ; DNA/*metabolism ; DNA Damage ; DNA Glycosylases/*metabolism ; DNA Repair ; Humans ; *Immunoglobulin Class Switching ; Mice ; Mutation ; Recombination, Genetic ; Uracil/metabolism ; Uracil-DNA Glycosidase ; Viral Proteins/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
    Publication Date: 2004-12-14
    Description: Cells from Werner syndrome patients are characterized by slow growth rates, premature senescence, accelerated telomere shortening rates, and genome instability. The syndrome is caused by the loss of the RecQ helicase WRN, but the underlying molecular mechanism is unclear. Here we report that cells lacking WRN exhibit deletion of telomeres from single sister chromatids. Only telomeres replicated by lagging strand synthesis were affected, and prevention of loss of individual telomeres was dependent on the helicase activity of WRN. Telomere loss could be counteracted by telomerase activity. We propose that WRN is necessary for efficient replication of G-rich telomeric DNA, preventing telomere dysfunction and consequent genomic instability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crabbe, Laure -- Verdun, Ramiro E -- Haggblom, Candy I -- Karlseder, Jan -- GM069525/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Dec 10;306(5703):1951-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Salk Institute for Biological Studies, 10010 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/15591207" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Anaphase ; Ataxia Telangiectasia Mutated Proteins ; Cell Cycle Proteins ; Cell Line ; Cells, Cultured ; Chromatids/metabolism ; Chromosomes, Human/physiology ; DNA Damage ; DNA Helicases/genetics/*metabolism ; DNA-Binding Proteins ; Exodeoxyribonucleases ; Genomic Instability ; HeLa Cells ; Humans ; In Situ Hybridization, Fluorescence ; Models, Genetic ; Mutation ; Protein-Serine-Threonine Kinases/metabolism ; RecQ Helicases ; S Phase ; Telomerase/metabolism ; Telomere/*metabolism ; Tumor Suppressor Proteins ; Werner Syndrome/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
    Publication Date: 2004-12-14
    Description: Sex and recombination are driving forces in the evolution of eukaryotes. Homologous recombination is known to be the dominant process in the divergence of many bacterial species. For Archaea, the only direct evidence bearing on the importance or natural occurrence of homologous recombination is anecdotal reports of mosaicism from comparative genomic studies. Genetic studies, however, reveal that recombination may play a significant role in generating diversity among members of at least one archaeal group, the haloarchaea. We used multi-locus sequence typing to demonstrate that haloarchaea exchange genetic information promiscuously, exhibiting a degree of linkage equilibrium approaching that of a sexual population.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Papke, R Thane -- Koenig, Jeremy E -- Rodriguez-Valera, Francisco -- Doolittle, W Ford -- New York, N.Y. -- Science. 2004 Dec 10;306(5703):1928-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Dalhousie University, 5859 University Avenue, Halifax, Nova Scotia B3H 4H7, Canada. rpapke@dal.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15591201" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; DNA, Archaeal ; Genes, Archaeal ; Genes, rRNA ; Genetic Linkage ; Genetic Variation ; Halobacteriaceae/classification/*genetics/isolation & purification ; Linkage Disequilibrium ; Molecular Sequence Data ; Mutation ; Phylogeny ; Polymerase Chain Reaction ; *Recombination, Genetic ; Ribotyping ; Sequence Analysis, DNA ; Sodium Chloride ; Spain ; *Water Microbiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-12-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crabb, Charlene -- New York, N.Y. -- Science. 2004 Dec 3;306(5702):1670-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15576583" target="_blank"〉PubMed〈/a〉
    Keywords: Academies and Institutes ; *Accidents, Occupational ; Antidotes/therapeutic use ; Biomedical Research ; *Chemical Industry/legislation & jurisprudence ; Cohort Studies ; *Disasters ; Female ; Gas Poisoning/*complications ; Hospitals ; Humans ; India ; Isocyanates/*poisoning ; Male ; Mutation ; Neoplasms/chemically induced/epidemiology ; Publishing ; Pulmonary Surfactants/analysis ; Thiosulfates/therapeutic use
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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