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  • Mutation  (6)
  • American Association for the Advancement of Science (AAAS)  (6)
  • Elsevier
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  • American Association for the Advancement of Science (AAAS)  (6)
  • Elsevier
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  • 1
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    Dual positive and negative regulation of wingless signaling by adenomatous polyposis coli (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-01-19
    Description: The evolutionarily conserved Wnt/Wingless signal transduction pathway directs cell proliferation, cell fate, and cell death during development in metazoans and is inappropriately activated in several types of cancer. The majority of colorectal carcinomas contain truncating mutations in the adenomatous polyposis coli (APC) tumor suppressor, a negative regulator of Wnt/Wingless signaling. Here, we demonstrate that Drosophila Apc homologs also have an activating role in both physiological and ectopic Wingless signaling. The Apc amino terminus is important for its activating function, whereas the beta-catenin binding sites are dispensable. Apc likely promotes Wingless transduction through down-regulation of Axin, a negative regulator of Wingless signaling. Given the evolutionary conservation of APC in Wnt signal transduction, an activating role may also be present in vertebrates with relevance to development and cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takacs, Carter M -- Baird, Jason R -- Hughes, Edward G -- Kent, Sierra S -- Benchabane, Hassina -- Paik, Raehum -- Ahmed, Yashi -- KO8CA078532/CA/NCI NIH HHS/ -- R01 CA105038/CA/NCI NIH HHS/ -- R01CA105038/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2008 Jan 18;319(5861):333-6. doi: 10.1126/science.1151232.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics and the Norris Cotton Cancer Center, Dartmouth Medical School, Hanover, NH 03755, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18202290" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Apoptosis ; Armadillo Domain Proteins/metabolism ; Axin Protein ; Binding Sites ; Cytoskeletal Proteins/chemistry/genetics/*metabolism ; Down-Regulation ; Drosophila/genetics/growth & development/*metabolism ; Drosophila Proteins/chemistry/genetics/*metabolism ; Genes, Insect ; Mutation ; Photoreceptor Cells, Invertebrate/cytology ; Proto-Oncogene Proteins/*metabolism ; *Signal Transduction ; Transcription Factors/metabolism ; Tumor Suppressor Proteins/chemistry/genetics/*metabolism ; Wings, Animal/growth & development/metabolism ; Wnt1 Protein
    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
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    A role for Snf2-related nucleosome-spacing enzymes in genome-wide nucleosome organization (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-09-24
    Description: The positioning of nucleosomes within the coding regions of eukaryotic genes is aligned with respect to transcriptional start sites. This organization is likely to influence many genetic processes, requiring access to the underlying DNA. Here, we show that the combined action of Isw1 and Chd1 nucleosome-spacing enzymes is required to maintain this organization. In the absence of these enzymes, regular positioning of the majority of nucleosomes is lost. Exceptions include the region upstream of the promoter, the +1 nucleosome, and a subset of locations distributed throughout coding regions where other factors are likely to be involved. These observations indicate that adenosine triphosphate-dependent remodeling enzymes are responsible for directing the positioning of the majority of nucleosomes within the Saccharomyces cerevisiae genome.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3428865/" 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/PMC3428865/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gkikopoulos, Triantaffyllos -- Schofield, Pieta -- Singh, Vijender -- Pinskaya, Marina -- Mellor, Jane -- Smolle, Michaela -- Workman, Jerry L -- Barton, Geoffrey J -- Owen-Hughes, Tom -- 064414/Wellcome Trust/United Kingdom -- 095062/Wellcome Trust/United Kingdom -- G0900740/Medical Research Council/United Kingdom -- R01 GM047867/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2011 Sep 23;333(6050):1758-60. doi: 10.1126/science.1206097.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Trust Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dundee, DD1 5EH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21940898" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/genetics/*metabolism ; Adenosine Triphosphate/metabolism ; Chromatin Assembly and Disassembly ; DNA, Fungal/genetics ; DNA-Binding Proteins/genetics/*metabolism ; Gene Expression Regulation, Fungal ; Genes, Fungal ; *Genome, Fungal ; Mutation ; Nucleosomes/*genetics/physiology/ultrastructure ; Saccharomyces cerevisiae/*genetics/physiology ; Saccharomyces cerevisiae Proteins/genetics/*metabolism ; Transcription Initiation Site
    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
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    Molecular biology. Breaking the silence (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Owen-Hughes, Tom -- Bruno, Michael -- New York, N.Y. -- Science. 2004 Jan 16;303(5656):324-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK. t.a.owenhughes@dundee.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14726582" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Acetyltransferases/metabolism ; Adenosine Triphosphatases/genetics/*metabolism ; Adenosine Triphosphate/*metabolism ; Catalysis ; Chromatin/*metabolism ; Chromosomes, Fungal ; Dimerization ; *Gene Expression Regulation, Fungal ; *Gene Silencing ; Genes, Fungal ; Genetic Variation ; Heterochromatin/metabolism ; Histone Acetyltransferases ; Histones/*metabolism ; Mutation ; Nucleosomes/metabolism ; Protein Binding ; Saccharomyces cerevisiae/*genetics/metabolism ; Saccharomyces cerevisiae Proteins/genetics/*metabolism ; 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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  • 4
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    The kinase domain of titin controls muscle gene expression and protein turnover (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-04-02
    Description: The giant sarcomeric protein titin contains a protein kinase domain (TK) ideally positioned to sense mechanical load. We identified a signaling complex where TK interacts with the zinc-finger protein nbr1 through a mechanically inducible conformation. Nbr1 targets the ubiquitin-associated p62/SQSTM1 to sarcomeres, and p62 in turn interacts with MuRF2, a muscle-specific RING-B-box E3 ligase and ligand of the transactivation domain of the serum response transcription factor (SRF). Nuclear translocation of MuRF2 was induced by mechanical inactivity and caused reduction of nuclear SRF and repression of transcription. A human mutation in the titin protein kinase domain causes hereditary muscle disease by disrupting this pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lange, Stephan -- Xiang, Fengqing -- Yakovenko, Andrey -- Vihola, Anna -- Hackman, Peter -- Rostkova, Elena -- Kristensen, Jakob -- Brandmeier, Birgit -- Franzen, Gereon -- Hedberg, Birgitta -- Gunnarsson, Lars Gunnar -- Hughes, Simon M -- Marchand, Sylvie -- Sejersen, Thomas -- Richard, Isabelle -- Edstrom, Lars -- Ehler, Elisabeth -- Udd, Bjarne -- Gautel, Mathias -- G0200496(63216)/Medical Research Council/United Kingdom -- G0300213/Medical Research Council/United Kingdom -- PG/03/049/15364/British Heart Foundation/United Kingdom -- New York, N.Y. -- Science. 2005 Jun 10;308(5728):1599-603. Epub 2005 Mar 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Muscle Signalling and Development, Randall Division, King's College London, London SE1 1UL, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15802564" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Catalytic Domain ; Cell Line ; Cell Nucleus/metabolism ; Connectin ; *Gene Expression Regulation ; Heat-Shock Proteins/metabolism ; Humans ; Ligands ; Mice ; Mice, Inbred C3H ; Molecular Sequence Data ; Muscle Proteins/*chemistry/genetics/*metabolism ; Muscle, Skeletal/*metabolism ; Muscular Diseases/genetics ; Mutation ; Myocytes, Cardiac/*metabolism ; Protein Binding ; Protein Conformation ; Protein Kinases/*chemistry/genetics/*metabolism ; Protein Structure, Tertiary ; Proteins/metabolism ; Rats ; Respiratory Insufficiency/genetics/metabolism ; Sarcomeres/metabolism ; Serum Response Factor/metabolism ; Signal Transduction ; Two-Hybrid System Techniques ; Ubiquitin-Protein Ligases/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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  • 5
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    Cdc13p: a single-strand telomeric DNA-binding protein with a dual role in yeast telomere maintenance (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-11
    Description: The CDC13 gene has previously been implicated in the maintenance of telomere integrity in Saccharomyces cerevisiae. With the use of two classes of mutations, here it is shown that CDC13 has two discrete roles at the telomere. The cdc13-2est mutation perturbs a function required in vivo for telomerase regulation but not in vitro for enzyme activity, whereas cdc13-1ts defines a separate essential role at the telomere. In vitro, purified Cdc13p binds to single-strand yeast telomeric DNA. Therefore, Cdc13p is a telomere-binding protein required to protect the telomere and mediate access of telomerase to the chromosomal terminus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nugent, C I -- Hughes, T R -- Lue, N F -- Lundblad, V -- New York, N.Y. -- Science. 1996 Oct 11;274(5285):249-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Human Genetics and Cell and Molecular Biology Program, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8824190" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Cloning, Molecular ; Cyclin B ; Cyclins/genetics/*metabolism ; DNA, Fungal/metabolism ; DNA, Single-Stranded/metabolism ; DNA-Binding Proteins/*metabolism ; Fungal Proteins/genetics ; Genes, Fungal ; Molecular Sequence Data ; Mutation ; Phenotype ; Saccharomyces cerevisiae/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Telomerase/genetics/*metabolism ; Telomere/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Sampling the antibiotic resistome (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-01-21
    Description: Microbial resistance to antibiotics currently spans all known classes of natural and synthetic compounds. It has not only hindered our treatment of infections but also dramatically reshaped drug discovery, yet its origins have not been systematically studied. Soil-dwelling bacteria produce and encounter a myriad of antibiotics, evolving corresponding sensing and evading strategies. They are a reservoir of resistance determinants that can be mobilized into the microbial community. Study of this reservoir could provide an early warning system for future clinically relevant antibiotic resistance mechanisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉D'Costa, Vanessa M -- McGrann, Katherine M -- Hughes, Donald W -- Wright, Gerard D -- New York, N.Y. -- Science. 2006 Jan 20;311(5759):374-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Antimicrobial Research Centre, Department of Biochemistry and Biomedical Sciences, McMaster University, Ontario, Canada, L8N 3Z5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16424339" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Anti-Bacterial Agents/metabolism/*pharmacology ; Ciprofloxacin/pharmacology ; Daptomycin/metabolism/pharmacology ; *Drug Resistance, Multiple, Bacterial/genetics ; Erythromycin/metabolism/pharmacology ; Genes, Bacterial ; Ketolides/metabolism/pharmacology ; Macrolides/pharmacology ; Microbial Sensitivity Tests ; Molecular Sequence Data ; Mutation ; Rifampin/metabolism/pharmacology ; *Soil Microbiology ; Streptomyces/*drug effects/enzymology/genetics/isolation & purification ; Trimethoprim Resistance ; Vancomycin Resistance/genetics ; Virginiamycin/metabolism/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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