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  • Molecular Sequence Data  (4)
  • American Association for the Advancement of Science (AAAS)  (4)
  • Wiley
  • 2010-2014  (3)
  • 1995-1999  (1)
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Keywords
Publisher
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Year
  • 1
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    Interaction of a Golgi-associated kinesin-like protein with Rab6 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-07
    Description: Rab guanosine triphosphatases regulate vesicular transport and membrane traffic within eukaryotic cells. Here, a kinesin-like protein that interacts with guanosine triphosphate (GTP)-bound forms of Rab6 was identified. This protein, termed Rabkinesin-6, was localized to the Golgi apparatus and shown to play a role in the dynamics of this organelle. The carboxyl-terminal domain of Rabkinesin-6, which contains the Rab6-interacting domain, inhibited the effects of Rab6-GTP on intracellular transport. Thus, a molecular motor is a potential effector of a Rab protein, and coordinated action between members of these two families of proteins could control membrane dynamics and directional vesicular traffic.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Echard, A -- Jollivet, F -- Martinez, O -- Lacapere, J J -- Rousselet, A -- Janoueix-Lerosey, I -- Goud, B -- New York, N.Y. -- Science. 1998 Jan 23;279(5350):580-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite Mixte de Recherche CNRS 144 et 168, Institut Curie, 26 rue d'Ulm, 75248 Paris Cedex 05, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9438855" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; Alkaline Phosphatase/metabolism ; Amino Acid Sequence ; Biological Transport ; Carrier Proteins/*metabolism ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus/chemistry/*metabolism/ultrastructure ; Guanosine Triphosphate/metabolism ; HeLa Cells ; Humans ; Kinesin/analysis/chemistry/genetics/*metabolism ; Microtubules/metabolism/ultrastructure ; Molecular Sequence Data ; Molecular Weight ; *rab GTP-Binding Proteins ; ras Proteins/*metabolism
    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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  • 2
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    Archaeorhizomycetes: unearthing an ancient class of ubiquitous soil fungi (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-08-13
    Description: Estimates suggest that only one-tenth of the true fungal diversity has been described. Among numerous fungal lineages known only from environmental DNA sequences, Soil Clone Group 1 is the most ubiquitous. These globally distributed fungi may dominate below-ground fungal communities, but their placement in the fungal tree of life has been uncertain. Here, we report cultures of this group and describe the class, Archaeorhizomycetes, phylogenetically placed within subphylum Taphrinomycotina in the Ascomycota. Archaeorhizomycetes comprises hundreds of cryptically reproducing filamentous species that do not form recognizable mycorrhizal structures and have saprotrophic potential, yet are omnipresent in roots and rhizosphere soil and show ecosystem and host root habitat specificity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosling, Anna -- Cox, Filipa -- Cruz-Martinez, Karelyn -- Ihrmark, Katarina -- Grelet, Gwen-Aelle -- Lindahl, Bjorn D -- Menkis, Audrius -- James, Timothy Y -- New York, N.Y. -- Science. 2011 Aug 12;333(6044):876-9. doi: 10.1126/science.1206958.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Forest Mycology and Pathology, Uppsala BioCentre, SLU, Box 7026, 750 07 Uppsala, Sweden. anna.rosling@slu.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21836015" target="_blank"〉PubMed〈/a〉
    Keywords: *Ascomycota/classification/genetics/growth & development/isolation & purification ; Coniferophyta/microbiology ; *Ecosystem ; Genes, Fungal ; Genes, rRNA ; Meristem/*microbiology ; Molecular Sequence Data ; *Mycorrhizae/classification/genetics ; Phylogeny ; Rhizosphere ; *Soil Microbiology
    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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  • 3
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    HSPC117 is the essential subunit of a human tRNA splicing ligase complex (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-02-12
    Description: Splicing of mammalian precursor transfer RNA (tRNA) molecules involves two enzymatic steps. First, intron removal by the tRNA splicing endonuclease generates separate 5' and 3' exons. In animals, the second step predominantly entails direct exon ligation by an elusive RNA ligase. Using activity-guided purification of tRNA ligase from HeLa cell extracts, we identified HSPC117, a member of the UPF0027 (RtcB) family, as the essential subunit of a tRNA ligase complex. RNA interference-mediated depletion of HSPC117 inhibited maturation of intron-containing pre-tRNA both in vitro and in living cells. The high sequence conservation of HSPC117/RtcB proteins is suggestive of RNA ligase roles of this protein family in various organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Popow, Johannes -- Englert, Markus -- Weitzer, Stefan -- Schleiffer, Alexander -- Mierzwa, Beata -- Mechtler, Karl -- Trowitzsch, Simon -- Will, Cindy L -- Luhrmann, Reinhard -- Soll, Dieter -- Martinez, Javier -- New York, N.Y. -- Science. 2011 Feb 11;331(6018):760-4. doi: 10.1126/science.1197847.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), A-1030 Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21311021" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Exons ; HeLa Cells ; Humans ; Introns ; Molecular Sequence Data ; Proteins/*chemistry/isolation & purification/*metabolism ; RNA Interference ; RNA Ligase (ATP)/*chemistry/isolation & purification/*metabolism ; RNA Precursors/*metabolism ; *RNA Splicing ; RNA, Transfer/*metabolism ; Spliceosomes/metabolism
    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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  • 4
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    Potential for chemolithoautotrophy among ubiquitous bacteria lineages in the dark ocean (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-09-03
    Description: Recent studies suggest that unidentified prokaryotes fix inorganic carbon at globally significant rates in the immense dark ocean. Using single-cell sorting and whole-genome amplification of prokaryotes from two subtropical gyres, we obtained genomic DNA from 738 cells representing most cosmopolitan lineages. Multiple cells of Deltaproteobacteria cluster SAR324, Gammaproteobacteria clusters ARCTIC96BD-19 and Agg47, and some Oceanospirillales from the lower mesopelagic contained ribulose-1,5-bisphosphate carboxylase-oxygenase and sulfur oxidation genes. These results corroborated community DNA and RNA profiling from diverse geographic regions. The SAR324 genomes also suggested C(1) metabolism and a particle-associated life-style. Microautoradiography and fluorescence in situ hybridization confirmed bicarbonate uptake and particle association of SAR324 cells. Our study suggests potential chemolithoautotrophy in several uncultured Proteobacteria lineages that are ubiquitous in the dark oxygenated ocean and provides new perspective on carbon cycling in the ocean's largest habitat.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Swan, Brandon K -- Martinez-Garcia, Manuel -- Preston, Christina M -- Sczyrba, Alexander -- Woyke, Tanja -- Lamy, Dominique -- Reinthaler, Thomas -- Poulton, Nicole J -- Masland, E Dashiell P -- Gomez, Monica Lluesma -- Sieracki, Michael E -- DeLong, Edward F -- Herndl, Gerhard J -- Stepanauskas, Ramunas -- New York, N.Y. -- Science. 2011 Sep 2;333(6047):1296-300. doi: 10.1126/science.1203690.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Bigelow Laboratory for Ocean Sciences, 180 McKown Point Road, Post Office Box 475, West Boothbay Harbor, ME 04575, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21885783" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/genetics/metabolism ; Carbon Cycle ; Carbon Dioxide/metabolism ; *Chemoautotrophic Growth ; Darkness ; Deltaproteobacteria/classification/genetics/growth & development/*metabolism ; Gammaproteobacteria/classification/genetics/growth & development/*metabolism ; Genes, Bacterial ; Genome, Bacterial ; Metagenome ; Molecular Sequence Data ; Oceans and Seas ; Oxidation-Reduction ; Phylogeny ; Ribulose-Bisphosphate Carboxylase/genetics ; Seawater/*microbiology ; Sulfur/metabolism ; Sulfur Compounds/metabolism
    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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