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  • Animals  (39)
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  • American Association for the Advancement of Science (AAAS)  (39)
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2012-11-20
    Description: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3621126/" 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/PMC3621126/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martinez, Gustavo J -- Rao, Anjana -- R01 CA042471/CA/NCI NIH HHS/ -- R01 CA42471/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2012 Nov 16;338(6109):891-2. doi: 10.1126/science.1231310.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉La Jolla Institute for Allergy and Immunology, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23161983" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Humans ; Immunomodulation/*genetics ; Interferon Regulatory Factors/*metabolism ; *Regulatory Elements, Transcriptional ; Th17 Cells/*immunology ; Transcription Factor AP-1/*metabolism ; *Transcriptional Activation
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  • 12
    Publication Date: 2014-06-21
    Description: Seventeen Middle Pleistocene crania from the Sima de los Huesos site (Atapuerca, Spain) are analyzed, including seven new specimens. This sample makes it possible to thoroughly characterize a Middle Pleistocene hominin paleodeme and to address hypotheses about the origin and evolution of the Neandertals. Using a variety of techniques, the hominin-bearing layer could be reassigned to a period around 430,000 years ago. The sample shows a consistent morphological pattern with derived Neandertal features present in the face and anterior vault, many of which are related to the masticatory apparatus. This suggests that facial modification was the first step in the evolution of the Neandertal lineage, pointing to a mosaic pattern of evolution, with different anatomical and functional modules evolving at different rates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arsuaga, J L -- Martinez, I -- Arnold, L J -- Aranburu, A -- Gracia-Tellez, A -- Sharp, W D -- Quam, R M -- Falgueres, C -- Pantoja-Perez, A -- Bischoff, J -- Poza-Rey, E -- Pares, J M -- Carretero, J M -- Demuro, M -- Lorenzo, C -- Sala, N -- Martinon-Torres, M -- Garcia, N -- Alcazar de Velasco, A -- Cuenca-Bescos, G -- Gomez-Olivencia, A -- Moreno, D -- Pablos, A -- Shen, C-C -- Rodriguez, L -- Ortega, A I -- Garcia, R -- Bonmati, A -- Bermudez de Castro, J M -- Carbonell, E -- New York, N.Y. -- Science. 2014 Jun 20;344(6190):1358-63. doi: 10.1126/science.1253958.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centro Mixto UCM-ISCIII de Evolucion y Comportamiento Humanos, Madrid, Spain. Departamento de Paleontologia, Facultad Ciencias Geologicas, Universidad Complutense de Madrid, Spain. jlarsuaga@isciii.es. ; Area de Paleontologia, Departamento de Geologia, Geografia y Medio Ambiente, Universidad de Alcala, Spain.Centro Mixto UCM-ISCIII de Evolucion y Comportamiento Humanos, Madrid, Spain. ; Centro Nacional de Investigacion sobre la Evolucion Humana Burgos, Spain. School of Earth and Environmental Sciences, the Environment Institute, and the Institute for Photonics and Advanced Sensing (IPAS), University of Adelaide, Australia. ; Departamento Mineralogia y Petrologia, Facultad de Ciencia y Tecnologia, Universidad del Pais Vasco, Spain. ; Berkeley Geochronology Center, Berkeley, CA, USA. ; Department of Anthropology, Binghamton University (State University of New York), Binghamton, NY, USA. Division of Anthropology, American Museum of Natural History, New York, NY, USA.Centro Mixto UCM-ISCIII de Evolucion y Comportamiento Humanos, Madrid, Spain. ; Departement de Prehistoire, Museum National d'Histoire Naturelle, Paris, France. ; Centro Mixto UCM-ISCIII de Evolucion y Comportamiento Humanos, Madrid, Spain. Departamento de Paleontologia, Facultad Ciencias Geologicas, Universidad Complutense de Madrid, Spain. ; U.S. Geological Survey, Menlo Park, CA,USA. ; Centro Nacional de Investigacion sobre la Evolucion Humana Burgos, Spain. ; Laboratorio de Evolucion Humana, Departamento de Ciencias Historicas y Geografia, Universidad de Burgos, Spain. ; Centro Nacional de Investigacion sobre la Evolucion Humana Burgos, Spain. Institute for Photonics and Advanced Sensing (IPAS), School of Chemistry and Physics, University of Adelaide, Australia. ; Area de Prehistoria, Departamento d'Historia i Historia de l'Art, Universitat Rovira i Virgili (URV), Tarragona, Spain. Institut Catala de Paleoecologia Humana i Evolucio Social, Tarragona, Spain.Centro Mixto UCM-ISCIII de Evolucion y Comportamiento Humanos, Madrid, Spain. ; Centro Mixto UCM-ISCIII de Evolucion y Comportamiento Humanos, Madrid, Spain. ; Paleontologia, Aragosaurus-IUCA and Facultad Ciencias, Universidad de Zaragoza, Spain. ; Centro Mixto UCM-ISCIII de Evolucion y Comportamiento Humanos, Madrid, Spain. Departement de Prehistoire, Museum National d'Histoire Naturelle, Paris, France. PAVE Research Group, Division of Biological Anthropology, Cambridge, UK. ; Departement de Prehistoire, Museum National d'Histoire Naturelle, Paris, France. Laboratorio de Evolucion Humana, Departamento de Ciencias Historicas y Geografia, Universidad de Burgos, Spain. ; Centro Mixto UCM-ISCIII de Evolucion y Comportamiento Humanos, Madrid, Spain. Centro Nacional de Investigacion sobre la Evolucion Humana Burgos, Spain. Laboratorio de Evolucion Humana, Departamento de Ciencias Historicas y Geografia, Universidad de Burgos, Spain. ; High-Precision Mass Spectrometry and Environment Change Laboratory (HISPEC), Department of Geosciences, National Taiwan University, Taiwan ROC. ; Institut Catala de Paleoecologia Humana i Evolucio Social, Tarragona, Spain. Area de Prehistoria, Departamento d'Historia i Historia de l'Art, Universitat Rovira i Virgili (URV), Tarragona, Spain. Institute of Vertebrate Paleontology and Paleoanthropology of Beijing (IVPP), China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24948730" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/anatomy & histology ; Extinction, Biological ; *Fossils ; Genetic Drift ; Humans ; Neanderthals/*anatomy & histology/*genetics ; Organ Size ; Reproductive Isolation ; Skull/*anatomy & histology ; Spain
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  • 13
    Publication Date: 1997-08-22
    Description: It has been suggested that European Middle Pleistocene humans, Neandertals, and prehistoric modern humans had a greater sexual dimorphism than modern humans. Analysis of body size variation and cranial capacity variation in the large sample from the Sima de los Huesos site in Spain showed instead that the sexual dimorphism is comparable in Middle Pleistocene and modern populations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arsuaga, J L -- Carretero, J M -- Lorenzo, C -- Gracia, A -- Martinez, I -- Bermudez de Castro, J M -- Carbonell, E -- New York, N.Y. -- Science. 1997 Aug 22;277(5329):1086-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departamento de Paleontologia, Instituto de Geologia Economica, Facultad de Ciencias Geologicas, Universidad Complutense de Madrid, Ciudad Universitaria 28040 Madrid, Spain.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9262474" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Body Constitution ; Female ; *Fossils ; Hominidae/*anatomy & histology ; Humans ; Male ; *Sex Characteristics ; Skull/*anatomy & histology ; Spain
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  • 14
    Publication Date: 1997-05-30
    Description: Human fossil remains recovered from the TD6 level (Aurora stratum) of the lower Pleistocene cave site of Gran Dolina, Sierra de Atapuerca, Spain, exhibit a unique combination of cranial, mandibular, and dental traits and are suggested as a new species of Homo-H. antecessor sp. nov. The fully modern midfacial morphology of the fossils antedates other evidence of this feature by about 650, 000 years. The midfacial and subnasal morphology of modern humans may be a retention of a juvenile pattern that was not yet present in H. ergaster. Homo antecessor may represent the last common ancestor for Neandertals and modern humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bermudez de Castro, J M -- Arsuaga, J L -- Carbonell, E -- Rosas, A -- Martinez, I -- Mosquera, M -- New York, N.Y. -- Science. 1997 May 30;276(5317):1392-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Museo Nacional de Ciencias Naturales, Consejo Superior de Investigaciones Cientificas (CSIC), Departamento de Paleobiologia, J. Gutierrez Abascal 2, 28006 Madrid, Spain.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9162001" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Animals ; Child ; Dentition ; Facial Bones ; *Fossils ; *Hominidae/classification ; Humans ; Mandible ; Skull ; Spain
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  • 15
    Publication Date: 2002-12-10
    Description: We have catalogued the protein kinase complement of the human genome (the "kinome") using public and proprietary genomic, complementary DNA, and expressed sequence tag (EST) sequences. This provides a starting point for comprehensive analysis of protein phosphorylation in normal and disease states, as well as a detailed view of the current state of human genome analysis through a focus on one large gene family. We identify 518 putative protein kinase genes, of which 71 have not previously been reported or described as kinases, and we extend or correct the protein sequences of 56 more kinases. New genes include members of well-studied families as well as previously unidentified families, some of which are conserved in model organisms. Classification and comparison with model organism kinomes identified orthologous groups and highlighted expansions specific to human and other lineages. We also identified 106 protein kinase pseudogenes. Chromosomal mapping revealed several small clusters of kinase genes and revealed that 244 kinases map to disease loci or cancer amplicons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Manning, G -- Whyte, D B -- Martinez, R -- Hunter, T -- Sudarsanam, S -- New York, N.Y. -- Science. 2002 Dec 6;298(5600):1912-34.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉SUGEN Inc., 230 East Grand Avenue, South San Francisco, CA 94080, USA. gerard-manning@sugen.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12471243" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Catalysis ; Chromosome Mapping ; Computational Biology ; Databases, Genetic ; Genes ; *Genome, Human ; Humans ; Neoplasms/genetics ; Phylogeny ; Protein Kinases/chemistry/classification/*genetics/*metabolism ; Protein Structure, Tertiary ; Pseudogenes ; Sequence Analysis, DNA ; Signal Transduction
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  • 16
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-11-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martinez Arias, Alfonso -- New York, N.Y. -- Science. 2005 Nov 25;310(5752):1284-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, University of Cambridge, Cambridge CB2 3EH, UK. ama11@hermes.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16311322" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Animals ; Cell Nucleus/metabolism ; Drosophila Proteins/chemistry/*metabolism ; Drosophila melanogaster/genetics/*metabolism ; Endocytosis ; Frizzled Receptors ; Models, Neurological ; Mutation ; Neuromuscular Junction/*metabolism ; Protein Structure, Tertiary ; Proto-Oncogene Proteins/*metabolism ; Receptors, G-Protein-Coupled ; Receptors, Neurotransmitter/chemistry/*metabolism ; *Signal Transduction ; Wnt1 Protein
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  • 17
    Publication Date: 2005-02-26
    Description: Apical membrane antigen 1 from Plasmodium is a leading malaria vaccine candidate. The protein is essential for host-cell invasion, but its molecular function is unknown. The crystal structure of the three domains comprising the ectoplasmic region of the antigen from P. vivax, solved at 1.8 angstrom resolution, shows that domains I and II belong to the PAN motif, which defines a superfamily of protein folds implicated in receptor binding. We also mapped the epitope of an invasion-inhibitory monoclonal antibody specific for the P. falciparum ortholog and modeled this to the structure. The location of the epitope and current knowledge on structure-function correlations for PAN domains together suggest a receptor-binding role during invasion in which domain II plays a critical part. These results are likely to aid vaccine and drug design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pizarro, Juan Carlos -- Vulliez-Le Normand, Brigitte -- Chesne-Seck, Marie-Laure -- Collins, Christine R -- Withers-Martinez, Chrislaine -- Hackett, Fiona -- Blackman, Michael J -- Faber, Bart W -- Remarque, Edmond J -- Kocken, Clemens H M -- Thomas, Alan W -- Bentley, Graham A -- MC_U117532063/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2005 Apr 15;308(5720):408-11. Epub 2005 Feb 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite d'Immunologie Structurale, Centre National de la Recherche Scientifique, URA 2185, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15731407" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Antigens, Protozoan/*chemistry/immunology ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; Epitope Mapping ; Epitopes ; Heparin/metabolism ; Malaria Vaccines ; Membrane Proteins/*chemistry/immunology ; Models, Molecular ; Molecular Sequence Data ; Plasmodium falciparum/chemistry/immunology ; Plasmodium vivax/chemistry/*immunology ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protozoan Proteins/*chemistry/immunology ; Recombinant Proteins/chemistry ; Sequence Alignment
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  • 18
    Publication Date: 2004-10-02
    Description: Diatoms are unicellular algae with plastids acquired by secondary endosymbiosis. They are responsible for approximately 20% of global carbon fixation. We report the 34 million-base pair draft nuclear genome of the marine diatom Thalassiosira pseudonana and its 129 thousand-base pair plastid and 44 thousand-base pair mitochondrial genomes. Sequence and optical restriction mapping revealed 24 diploid nuclear chromosomes. We identified novel genes for silicic acid transport and formation of silica-based cell walls, high-affinity iron uptake, biosynthetic enzymes for several types of polyunsaturated fatty acids, use of a range of nitrogenous compounds, and a complete urea cycle, all attributes that allow diatoms to prosper in aquatic environments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Armbrust, E Virginia -- Berges, John A -- Bowler, Chris -- Green, Beverley R -- Martinez, Diego -- Putnam, Nicholas H -- Zhou, Shiguo -- Allen, Andrew E -- Apt, Kirk E -- Bechner, Michael -- Brzezinski, Mark A -- Chaal, Balbir K -- Chiovitti, Anthony -- Davis, Aubrey K -- Demarest, Mark S -- Detter, J Chris -- Glavina, Tijana -- Goodstein, David -- Hadi, Masood Z -- Hellsten, Uffe -- Hildebrand, Mark -- Jenkins, Bethany D -- Jurka, Jerzy -- Kapitonov, Vladimir V -- Kroger, Nils -- Lau, Winnie W Y -- Lane, Todd W -- Larimer, Frank W -- Lippmeier, J Casey -- Lucas, Susan -- Medina, Monica -- Montsant, Anton -- Obornik, Miroslav -- Parker, Micaela Schnitzler -- Palenik, Brian -- Pazour, Gregory J -- Richardson, Paul M -- Rynearson, Tatiana A -- Saito, Mak A -- Schwartz, David C -- Thamatrakoln, Kimberlee -- Valentin, Klaus -- Vardi, Assaf -- Wilkerson, Frances P -- Rokhsar, Daniel S -- New York, N.Y. -- Science. 2004 Oct 1;306(5693):79-86.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Oceanography, University of Washington, Seattle, WA 98195, USA. armbrust@ocean.washington.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15459382" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Algal Proteins/chemistry/genetics/physiology ; Animals ; *Biological Evolution ; Cell Nucleus/genetics ; Chromosomes ; DNA/genetics ; Diatoms/chemistry/cytology/*genetics/metabolism ; *Ecosystem ; Energy Metabolism ; *Genome ; Iron/metabolism ; Light ; Light-Harvesting Protein Complexes/chemistry/genetics/metabolism ; Mitochondria/genetics ; Molecular Sequence Data ; Nitrogen/metabolism ; Photosynthesis ; Plastids/genetics ; Restriction Mapping ; Sequence Alignment ; *Sequence Analysis, DNA ; Silicic Acid/metabolism ; Symbiosis ; Urea/metabolism
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  • 19
    Publication Date: 2004-01-06
    Description: To initiate studies on how protein-protein interaction (or "interactome") networks relate to multicellular functions, we have mapped a large fraction of the Caenorhabditis elegans interactome network. Starting with a subset of metazoan-specific proteins, more than 4000 interactions were identified from high-throughput, yeast two-hybrid (HT=Y2H) screens. Independent coaffinity purification assays experimentally validated the overall quality of this Y2H data set. Together with already described Y2H interactions and interologs predicted in silico, the current version of the Worm Interactome (WI5) map contains approximately 5500 interactions. Topological and biological features of this interactome network, as well as its integration with phenome and transcriptome data sets, lead to numerous biological hypotheses.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1698949/" 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/PMC1698949/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Siming -- Armstrong, Christopher M -- Bertin, Nicolas -- Ge, Hui -- Milstein, Stuart -- Boxem, Mike -- Vidalain, Pierre-Olivier -- Han, Jing-Dong J -- Chesneau, Alban -- Hao, Tong -- Goldberg, Debra S -- Li, Ning -- Martinez, Monica -- Rual, Jean-Francois -- Lamesch, Philippe -- Xu, Lai -- Tewari, Muneesh -- Wong, Sharyl L -- Zhang, Lan V -- Berriz, Gabriel F -- Jacotot, Laurent -- Vaglio, Philippe -- Reboul, Jerome -- Hirozane-Kishikawa, Tomoko -- Li, Qianru -- Gabel, Harrison W -- Elewa, Ahmed -- Baumgartner, Bridget -- Rose, Debra J -- Yu, Haiyuan -- Bosak, Stephanie -- Sequerra, Reynaldo -- Fraser, Andrew -- Mango, Susan E -- Saxton, William M -- Strome, Susan -- Van Den Heuvel, Sander -- Piano, Fabio -- Vandenhaute, Jean -- Sardet, Claude -- Gerstein, Mark -- Doucette-Stamm, Lynn -- Gunsalus, Kristin C -- Harper, J Wade -- Cusick, Michael E -- Roth, Frederick P -- Hill, David E -- Vidal, Marc -- R01 AG011085/AG/NIA NIH HHS/ -- R01 GM034059/GM/NIGMS NIH HHS/ -- R01 GM034059-18/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jan 23;303(5657):540-3. Epub 2004 Jan 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute and Department of Genetics, Harvard Medical School, 44 Binney Street, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14704431" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/genetics/*metabolism ; Caenorhabditis elegans Proteins/genetics/*metabolism ; Computational Biology ; Evolution, Molecular ; Genes, Helminth ; Genomics ; Open Reading Frames ; Phenotype ; Protein Binding ; Proteome/*metabolism ; Transcription, Genetic ; Two-Hybrid System Techniques
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  • 20
    Publication Date: 2004-11-20
    Description: To act as guides in the RNA interference (RNAi) pathway, small interfering RNAs (siRNAs) must be unwound into their component strands, then assembled with proteins to form the RNA-induced silencing complex (RISC), which catalyzes target messenger RNA cleavage. Thermodynamic differences in the base-pairing stabilities of the 5' ends of the two approximately 21-nucleotide siRNA strands determine which siRNA strand is assembled into the RISC. We show that in Drosophila, the orientation of the Dicer-2/R2D2 protein heterodimer on the siRNA duplex determines which siRNA strand associates with the core RISC protein Argonaute 2. R2D2 binds the siRNA end with the greatest double-stranded character, thereby orienting the heterodimer on the siRNA duplex. Strong R2D2 binding requires a 5'-phosphate on the siRNA strand that is excluded from the RISC. Thus, R2D2 is both a protein sensor for siRNA thermodynamic asymmetry and a licensing factor for entry of authentic siRNAs into the RNAi pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tomari, Yukihide -- Matranga, Christian -- Haley, Benjamin -- Martinez, Natalia -- Zamore, Phillip D -- GM62862-01/GM/NIGMS NIH HHS/ -- GM65236-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Nov 19;306(5700):1377-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15550672" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Argonaute Proteins ; Dimerization ; Drosophila/embryology/metabolism ; Drosophila Proteins/*metabolism ; Light ; Luciferases/genetics ; Nucleic Acid Conformation ; RNA Helicases/*metabolism ; *RNA Interference ; RNA, Double-Stranded/chemistry/metabolism ; RNA, Small Interfering/*chemistry/*metabolism ; RNA-Binding Proteins/*metabolism ; RNA-Induced Silencing Complex/*metabolism ; Ribonuclease III ; Superoxide Dismutase/genetics ; Thermodynamics ; Uracil/*analogs & derivatives/analysis
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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