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    DNA topoisomerase IIbeta and neural development (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-30
    Description: DNA topoisomerase IIbeta is shown to have an unsuspected and critical role in neural development. Neurogenesis was normal in IIbeta mutant mice, but motor axons failed to contact skeletal muscles, and sensory axons failed to enter the spinal cord. Despite an absence of innervation, clusters of acetylcholine receptors were concentrated in the central region of skeletal muscles, thereby revealing patterning mechanisms that are autonomous to skeletal muscle. The defects in motor axon growth in IIbeta mutant mice resulted in a breathing impairment and death of the pups shortly after birth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, X -- Li, W -- Prescott, E D -- Burden, S J -- Wang, J C -- NS10537/NS/NINDS NIH HHS/ -- NS27963/NS/NINDS NIH HHS/ -- NS36193/NS/NINDS NIH HHS/ -- R01 NS036193/NS/NINDS NIH HHS/ -- R01 NS036193-02/NS/NINDS NIH HHS/ -- R01 NS041311/NS/NINDS NIH HHS/ -- R01 NS041311-03/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 2000 Jan 7;287(5450):131-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Skirball Institute of Molecular Medicine, New York University Medical School, 540 First Avenue, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10615047" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/*physiology/ultrastructure ; Cell Lineage ; Cues ; DNA Repair ; DNA Topoisomerases, Type II/genetics/*metabolism ; DNA-Binding Proteins ; Diaphragm/chemistry/embryology/innervation ; Embryonic and Fetal Development ; Gene Targeting ; Intercostal Muscles/innervation ; Mice ; Mice, Knockout ; Motor Neurons/physiology/ultrastructure ; Muscle, Skeletal/embryology/*innervation ; Neuromuscular Junction/*embryology/growth & development ; Neurons, Afferent/physiology/ultrastructure ; Presynaptic Terminals/ultrastructure ; Receptors, Cholinergic/analysis ; Skin/innervation ; Spinal Cord/embryology/ultrastructure
    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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    A modular PIP2 binding site as a determinant of capsaicin receptor sensitivity (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-05-24
    Description: The capsaicin receptor (TRPV1), a heat-activated ion channel of the pain pathway, is sensitized by phosphatidylinositol-4,5-bisphosphate (PIP2) hydrolysis after phospholipase C activation. We identify a site within the C-terminal domain of TRPV1 that is required for PIP2-mediated inhibition of channel gating. Mutations that weaken PIP2-TRPV1 interaction reduce thresholds for chemical or thermal stimuli, whereas TRPV1 channels in which this region is replaced with a lipid-binding domain from PIP2-activated potassium channels remain inhibited by PIP2. The PIP2-interaction domain therefore serves as a critical determinant of thermal threshold and dynamic sensitivity range, tuning TRPV1, and thus the sensory neuron, to appropriately detect heat under normal or pathophysiological conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prescott, Elizabeth D -- Julius, David -- New York, N.Y. -- Science. 2003 May 23;300(5623):1284-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143-2140, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12764195" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arsenicals/pharmacology ; Binding Sites ; Capsaicin/metabolism/pharmacology ; Carrier Proteins ; Hot Temperature ; Humans ; Ion Channel Gating ; Membrane Proteins ; Molecular Sequence Data ; Mutation ; Oocytes ; Patch-Clamp Techniques ; Phosphatidylinositol 4,5-Diphosphate/*metabolism ; Phosphorylation ; Potassium Channels, Inwardly Rectifying/chemistry/genetics/metabolism ; Protein Structure, Tertiary ; Rats ; Receptor, Epidermal Growth Factor/metabolism ; Receptor, trkA/metabolism ; Receptors, Drug/*chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Sequence Deletion ; Type C Phospholipases/metabolism ; Xenopus
    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)
    Location Call Number Expected Availability
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