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  • Mutation  (16)
  • Cell Line  (12)
  • American Association for the Advancement of Science (AAAS)  (28)
  • American Association for the Advancement of Science
  • 2020-2023
  • 2005-2009  (28)
  • 1955-1959
  • 2008  (28)
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  • American Association for the Advancement of Science (AAAS)  (28)
  • American Association for the Advancement of Science
  • Nature Publishing Group (NPG)  (28)
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  • 2020-2023
  • 2005-2009  (28)
  • 1955-1959
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  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2008-03-29
    Description: The gradual modification of transcription circuits over evolutionary time scales is an important source of the diversity of life. Over the past decade, studies in animals have shown how seemingly small molecular changes in gene regulation can have large effects on morphology and physiology and how selective pressures can act on these changes. More recently, genome-wide studies, particularly those in single-cell yeasts, have uncovered evidence of extensive transcriptional rewiring, indicating that even closely related organisms regulate their genes using markedly different circuitries.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tuch, Brian B -- Li, Hao -- Johnson, Alexander D -- New York, N.Y. -- Science. 2008 Mar 28;319(5871):1797-9. doi: 10.1126/science.1152398.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco, CA, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18369141" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA-Binding Proteins ; *Evolution, Molecular ; *Gene Expression Regulation ; *Gene Regulatory Networks ; Humans ; Mutation ; Regulatory Sequences, Nucleic Acid ; Transcription Factors/*metabolism ; *Transcription, Genetic
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2008-03-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Armitage, Bruce A -- Berget, Peter B -- New York, N.Y. -- Science. 2008 Feb 29;319(5867):1195-6. doi: 10.1126/science.1155093.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Molecular Biosensor and Imaging Center (MBIC), Carnegie Mellon University, Pittsburgh, PA 15213, USA. army@cmu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18309067" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Antibodies, Monoclonal/*chemistry/genetics ; Antigen-Antibody Complex ; Binding Sites, Antibody ; Crystallization ; Fluorescence ; Fluorescent Dyes ; Hydrophobic and Hydrophilic Interactions ; Luminescence ; Molecular Structure ; Mutation ; Protein Conformation ; Spectrometry, Fluorescence ; Stilbenes/*chemistry/immunology ; Structure-Activity Relationship
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  • 3
    Publication Date: 2008-01-05
    Description: Fundamental processes influencing human growth can be revealed by studying extreme short stature. Using genetic linkage analysis, we find that biallelic loss-of-function mutations in the centrosomal pericentrin (PCNT) gene on chromosome 21q22.3 cause microcephalic osteodysplastic primordial dwarfism type II (MOPD II) in 25 patients. Adults with this rare inherited condition have an average height of 100 centimeters and a brain size comparable to that of a 3-month-old baby, but are of near-normal intelligence. Absence of PCNT results in disorganized mitotic spindles and missegregation of chromosomes. Mutations in related genes are known to cause primary microcephaly (MCPH1, CDK5RAP2, ASPM, and CENPJ).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rauch, Anita -- Thiel, Christian T -- Schindler, Detlev -- Wick, Ursula -- Crow, Yanick J -- Ekici, Arif B -- van Essen, Anthonie J -- Goecke, Timm O -- Al-Gazali, Lihadh -- Chrzanowska, Krystyna H -- Zweier, Christiane -- Brunner, Han G -- Becker, Kristin -- Curry, Cynthia J -- Dallapiccola, Bruno -- Devriendt, Koenraad -- Dorfler, Arnd -- Kinning, Esther -- Megarbane, Andre -- Meinecke, Peter -- Semple, Robert K -- Spranger, Stephanie -- Toutain, Annick -- Trembath, Richard C -- Voss, Egbert -- Wilson, Louise -- Hennekam, Raoul -- de Zegher, Francis -- Dorr, Helmuth-Gunther -- Reis, Andre -- 062346/Z/00/Z/Wellcome Trust/United Kingdom -- 080952/Z/06/Z/Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2008 Feb 8;319(5864):816-9. doi: 10.1126/science.1151174. Epub 2008 Jan 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Human Genetics, University Hospital Erlangen, Friedrich-Alexander University Erlangen-Nuremberg, Erlangen, Germany. Anita.Rauch@humgenet.uni-erlangen.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18174396" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens/*genetics/metabolism/*physiology ; Apoptosis ; Cell Line ; Centrosome/physiology ; Dwarfism/*genetics/pathology/physiopathology ; Female ; Fibroblasts/cytology ; Humans ; Lod Score ; Lymphocytes/metabolism ; Male ; Microcephaly/*genetics/pathology/physiopathology ; Mitosis ; *Mutation ; Pedigree ; RNA, Messenger/genetics/metabolism ; Spindle Apparatus/physiology/ultrastructure ; Syndrome
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  • 4
    Publication Date: 2008-03-01
    Description: The blue-emissive antibody EP2-19G2 that has been elicited against trans-stilbene has unprecedented ability to produce bright luminescence and has been used as a biosensor in various applications. We show that the prolonged luminescence is not stilbene fluorescence. Instead, the emissive species is a charge-transfer excited complex of an anionic stilbene and a cationic, parallel pi-stacked tryptophan. Upon charge recombination, this complex generates exceptionally bright blue light. Complex formation is enabled by a deeply penetrating ligand-binding pocket, which in turn results from a noncanonical interface between the two variable domains of the antibody.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Debler, Erik W -- Kaufmann, Gunnar F -- Meijler, Michael M -- Heine, Andreas -- Mee, Jenny M -- Pljevaljcic, Goran -- Di Bilio, Angel J -- Schultz, Peter G -- Millar, David P -- Janda, Kim D -- Wilson, Ian A -- Gray, Harry B -- Lerner, Richard A -- DK19038/DK/NIDDK NIH HHS/ -- GM38273/GM/NIGMS NIH HHS/ -- GM56528/GM/NIGMS NIH HHS/ -- R01 GM038273/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2008 Feb 29;319(5867):1232-5. doi: 10.1126/science.1153445.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18309081" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal/*chemistry/genetics/immunology ; Antigen-Antibody Complex ; Binding Sites, Antibody ; Crystallization ; Crystallography, X-Ray ; *Electrons ; Fluorescence ; Fluorescence Polarization ; Haptens/chemistry/immunology ; Hydrophobic and Hydrophilic Interactions ; Immunoglobulin Variable Region/*chemistry/immunology ; Ligands ; Luminescence ; Mutation ; Oxidation-Reduction ; Protein Structure, Tertiary ; Spectrometry, Fluorescence ; Spectrum Analysis ; Stilbenes/*chemistry/immunology ; Tryptophan/chemistry
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  • 5
    Publication Date: 2008-07-26
    Description: Ribonucleoprotein complexes consisting of Argonaute-like proteins and small regulatory RNAs function in a wide range of biological processes. Many of these small regulatory RNAs are predicted to act, at least in part, within the nucleus. We conducted a genetic screen to identify factors essential for RNA interference (RNAi) in nuclei of Caenorhabditis elegans and identified the Argonaute protein NRDE-3. In the absence of small interfering RNAs (siRNAs), NRDE-3 resides in the cytoplasm. NRDE-3 binds siRNAs generated by RNA-dependent RNA polymerases acting on messenger RNA templates in the cytoplasm and redistributes to the nucleus. Nuclear redistribution of NRDE-3 requires a functional nuclear localization signal, is required for nuclear RNAi, and results in NRDE-3 association with nuclear-localized nascent transcripts. Thus, specific Argonaute proteins can transport specific classes of small regulatory RNAs to distinct cellular compartments to regulate gene expression.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2771369/" 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/PMC2771369/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guang, Shouhong -- Bochner, Aaron F -- Pavelec, Derek M -- Burkhart, Kirk B -- Harding, Sandra -- Lachowiec, Jennifer -- Kennedy, Scott -- R01 GM076619/GM/NIGMS NIH HHS/ -- R01 GM076619-01/GM/NIGMS NIH HHS/ -- R01 GM076619-02/GM/NIGMS NIH HHS/ -- R01 GM076619-03/GM/NIGMS NIH HHS/ -- R01 GM088289/GM/NIGMS NIH HHS/ -- R01 GM088289-01/GM/NIGMS NIH HHS/ -- T32 GM007133/GM/NIGMS NIH HHS/ -- T32 GM007133-24/GM/NIGMS NIH HHS/ -- T32 GM007133-25/GM/NIGMS NIH HHS/ -- T32 GM007133-26/GM/NIGMS NIH HHS/ -- T32 GM007133-27/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2008 Jul 25;321(5888):537-41. doi: 10.1126/science.1157647.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Wisconsin-Madison, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18653886" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Animals ; Caenorhabditis elegans/embryology/*genetics/growth & development/*metabolism ; Caenorhabditis elegans Proteins/chemistry/genetics/*metabolism ; Cell Nucleus/*metabolism ; Cytoplasm/*metabolism ; Genes, Helminth ; Mutation ; Nuclear Localization Signals ; Protein Structure, Tertiary ; *RNA Interference ; RNA Precursors/genetics/metabolism ; RNA Replicase/metabolism ; RNA, Double-Stranded/chemistry/genetics/metabolism ; RNA, Helminth/chemistry/genetics/metabolism ; RNA, Messenger/genetics/metabolism ; RNA, Small Interfering/chemistry/genetics/*metabolism ; RNA-Binding Proteins/chemistry/genetics/*metabolism ; Up-Regulation
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  • 6
    Publication Date: 2008-03-01
    Description: Intraluminal vesicles of multivesicular endosomes are either sorted for cargo degradation into lysosomes or secreted as exosomes into the extracellular milieu. The mechanisms underlying the sorting of membrane into the different populations of intraluminal vesicles are unknown. Here, we find that cargo is segregated into distinct subdomains on the endosomal membrane and that the transfer of exosome-associated domains into the lumen of the endosome did not depend on the function of the ESCRT (endosomal sorting complex required for transport) machinery, but required the sphingolipid ceramide. Purified exosomes were enriched in ceramide, and the release of exosomes was reduced after the inhibition of neutral sphingomyelinases. These results establish a pathway in intraendosomal membrane transport and exosome formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Trajkovic, Katarina -- Hsu, Chieh -- Chiantia, Salvatore -- Rajendran, Lawrence -- Wenzel, Dirk -- Wieland, Felix -- Schwille, Petra -- Brugger, Britta -- Simons, Mikael -- New York, N.Y. -- Science. 2008 Feb 29;319(5867):1244-7. doi: 10.1126/science.1153124.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for Biochemistry and Molecular Cell Biology, University of Gottingen, 37073 Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18309083" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Line, Tumor ; Ceramides/analysis/*metabolism ; Cytoplasmic Vesicles/chemistry/*metabolism/ultrastructure ; Endosomes/*metabolism/ultrastructure ; Humans ; Intracellular Membranes/*metabolism/ultrastructure ; Membrane Microdomains/*metabolism/ultrastructure ; Mice ; Myelin Proteolipid Protein/*metabolism ; Oligodendroglia/metabolism/ultrastructure ; Protein Transport ; Receptor, Epidermal Growth Factor/metabolism ; Recombinant Fusion Proteins/metabolism ; Sphingomyelin Phosphodiesterase/antagonists & inhibitors/metabolism
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  • 7
    Publication Date: 2008-10-25
    Description: During the development of multicellular organisms, organogenesis and pattern formation depend on formative divisions to specify and maintain pools of stem cells. In higher plants, these activities are essential to shape the final root architecture because the functioning of root apical meristems and the de novo formation of lateral roots entirely rely on it. We used transcript profiling on sorted pericycle cells undergoing lateral root initiation to identify the receptor-like kinase ACR4 of Arabidopsis as a key factor both in promoting formative cell divisions in the pericycle and in constraining the number of these divisions once organogenesis has been started. In the root tip meristem, ACR4 shows a similar action by controlling cell proliferation activity in the columella cell lineage. Thus, ACR4 function reveals a common mechanism of formative cell division control in the main root tip meristem and during lateral root initiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉De Smet, Ive -- Vassileva, Valya -- De Rybel, Bert -- Levesque, Mitchell P -- Grunewald, Wim -- Van Damme, Daniel -- Van Noorden, Giel -- Naudts, Mirande -- Van Isterdael, Gert -- De Clercq, Rebecca -- Wang, Jean Y -- Meuli, Nicholas -- Vanneste, Steffen -- Friml, Jiri -- Hilson, Pierre -- Jurgens, Gerd -- Ingram, Gwyneth C -- Inze, Dirk -- Benfey, Philip N -- Beeckman, Tom -- New York, N.Y. -- Science. 2008 Oct 24;322(5901):594-7. doi: 10.1126/science.1160158.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Systems Biology, Flanders Institute for Biotechnology (VIB), B-9052 Ghent, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18948541" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*cytology/*enzymology/genetics/growth & development ; Arabidopsis Proteins/*genetics/*metabolism ; *Cell Division ; Cell Lineage ; Gene Expression Profiling ; Gene Expression Regulation, Plant ; Genes, Plant ; Meristem/*cytology/enzymology/growth & development ; Mutation ; Plant Roots/*cytology/enzymology/growth & development ; Protein-Serine-Threonine Kinases ; Receptors, Cell Surface/*genetics/*metabolism
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  • 8
    Publication Date: 2008-05-03
    Description: Golgins, long stringlike proteins, tether cisternae and transport vesicles at the Golgi apparatus. We examined the attachment of golgin GMAP-210 to lipid membranes. GMAP-210 connected highly curved liposomes to flatter ones. This asymmetric tethering relied on motifs that sensed membrane curvature both in the N terminus of GMAP-210 and in ArfGAP1, which controlled the interaction of the C terminus of GMAP-210 with the small guanine nucleotide-binding protein Arf1. Because membrane curvature constantly changes during vesicular trafficking, this mode of tethering suggests a way to maintain the Golgi architecture without compromising membrane flow.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Drin, Guillaume -- Morello, Vincent -- Casella, Jean-Francois -- Gounon, Pierre -- Antonny, Bruno -- New York, N.Y. -- Science. 2008 May 2;320(5876):670-3. doi: 10.1126/science.1155821.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Pharmacologie Moleculaire et Cellulaire, Universite de Nice Sophia Antipolis and CNRS, 660 route des lucioles, 06560 Valbonne, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18451304" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factor 1/metabolism ; Binding Sites ; Cell Line ; GTPase-Activating Proteins/metabolism ; Golgi Apparatus/chemistry/metabolism ; HeLa Cells ; Humans ; Intracellular Membranes/*chemistry/metabolism ; Liposomes ; Membrane Lipids/*chemistry ; Nuclear Proteins/*chemistry/metabolism ; Recombinant Proteins/chemistry/metabolism
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  • 9
    Publication Date: 2008-01-19
    Description: The earliest step in creating the cerebral cortex is the specification of neuroepithelium to a cortical fate. Using mouse genetic mosaics and timed inactivations, we demonstrated that Lhx2 acts as a classic selector gene and essential intrinsic determinant of cortical identity. Lhx2 selector activity is restricted to an early critical period when stem cells comprise the cortical neuroepithelium, where it acts cell-autonomously to specify cortical identity and suppress alternative fates in a spatially dependent manner. Laterally, Lhx2 null cells adopt antihem identity, whereas medially they become cortical hem cells, which can induce and organize ectopic hippocampal fields. In addition to providing functional evidence for Lhx2 selector activity, these findings show that the cortical hem is a hippocampal organizer.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2494603/" 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/PMC2494603/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mangale, Vishakha S -- Hirokawa, Karla E -- Satyaki, Prasad R V -- Gokulchandran, Nandini -- Chikbire, Satyadeep -- Subramanian, Lakshmi -- Shetty, Ashwin S -- Martynoga, Ben -- Paul, Jolly -- Mai, Mark V -- Li, Yuqing -- Flanagan, Lisa A -- Tole, Shubha -- Monuki, Edwin S -- 056684/Z/99/Z/Wellcome Trust/United Kingdom -- AG23583/AG/NIA NIH HHS/ -- MH02029/MH/NIMH NIH HHS/ -- NS053511/NS/NINDS NIH HHS/ -- NS07444/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2008 Jan 18;319(5861):304-9. doi: 10.1126/science.1151695.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Tata Institute of Fundamental Research, Mumbai 400005, India.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18202285" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Aggregation ; Cerebral Cortex/cytology/*embryology/metabolism ; Chimera ; Dentate Gyrus/cytology/embryology/metabolism ; Embryonic Induction ; Embryonic Stem Cells/metabolism ; Epithelium/embryology/metabolism ; Gene Expression Regulation, Developmental ; Hippocampus/cytology/*embryology ; Homeodomain Proteins/*genetics/*metabolism ; LIM-Homeodomain Proteins ; Mice ; Mice, Knockout ; Mutation ; Neuroepithelial Cells/cytology/metabolism ; Organizers, Embryonic/embryology/*physiology ; Prosencephalon/embryology/metabolism ; Pyramidal Cells/cytology/embryology ; Recombination, Genetic ; Telencephalon/cytology/embryology ; Transcription Factors/*genetics/*metabolism
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  • 10
    Publication Date: 2008-03-15
    Description: DEET (N,N-diethyl-meta-toluamide) is the world's most widely used topical insect repellent, with broad effectiveness against most insects. Its mechanism of action and molecular target remain unknown. Here, we show that DEET blocks electrophysiological responses of olfactory sensory neurons to attractive odors in Anopheles gambiae and Drosophila melanogaster. DEET inhibits behavioral attraction to food odors in Drosophila, and this inhibition requires the highly conserved olfactory co-receptor OR83b. DEET inhibits odor-evoked currents mediated by the insect odorant receptor complex, comprising a ligand-binding subunit and OR83b. We conclude that DEET masks host odor by inhibiting subsets of heteromeric insect odorant receptors that require the OR83b co-receptor. The identification of candidate molecular targets for the action of DEET may aid in the design of safer and more effective insect repellents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ditzen, Mathias -- Pellegrino, Maurizio -- Vosshall, Leslie B -- DC008600/DC/NIDCD NIH HHS/ -- New York, N.Y. -- Science. 2008 Mar 28;319(5871):1838-42. doi: 10.1126/science.1153121. Epub 2008 Mar 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Neurogenetics and Behavior, Rockefeller University, 1230 York Avenue, Box 63, New York, NY 10065 USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18339904" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anopheles gambiae/*drug effects/physiology ; Behavior, Animal/drug effects ; DEET/metabolism/*pharmacology ; Drosophila Proteins/antagonists & inhibitors/metabolism ; Drosophila melanogaster/*drug effects/genetics/physiology ; Electrophysiology ; Feeding Behavior/drug effects ; Food ; Insect Repellents/metabolism/*pharmacology ; Ligands ; Mutation ; Odors ; Olfactory Receptor Neurons/*drug effects/physiology ; Oocytes ; Patch-Clamp Techniques ; Receptors, Odorant/*antagonists & inhibitors/metabolism ; Xenopus laevis
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