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  • 1
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    Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-18
    Description: Mechanosensitive ion channels play a critical role in transducing physical stresses at the cell membrane into an electrochemical response. The MscL family of large-conductance mechanosensitive channels is widely distributed among prokaryotes and may participate in the regulation of osmotic pressure changes within the cell. In an effort to better understand the structural basis for the function of these channels, the structure of the MscL homolog from Mycobacterium tuberculosis was determined by x-ray crystallography to 3.5 angstroms resolution. This channel is organized as a homopentamer, with each subunit containing two transmembrane alpha helices and a third cytoplasmic alpha helix. From the extracellular side, a water-filled opening approximately 18 angstroms in diameter leads into a pore lined with hydrophilic residues which narrows at the cytoplasmic side to an occluded hydrophobic apex that may act as the channel gate. This structure may serve as a model for other mechanosensitive channels, as well as the broader class of pentameric ligand-gated ion channels exemplified by the nicotinic acetylcholine receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, G -- Spencer, R H -- Lee, A T -- Barclay, M T -- Rees, D C -- GM18486/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Dec 18;282(5397):2220-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9856938" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Cell Membrane/chemistry ; Cloning, Molecular ; Crystallization ; Crystallography, X-Ray ; *Escherichia coli Proteins ; *Ion Channel Gating ; Ion Channels/*chemistry/metabolism ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Molecular Weight ; Mycobacterium tuberculosis/*chemistry ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Temperature
    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 family of three mouse potassium channel genes with intronless coding regions (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-02-23
    Description: To understand the molecular mechanisms responsible for generating physiologically diverse potassium channels in mammalian cells, mouse genomic clones have been isolated with a potassium channel complementary DNA, MBK1, that is homologous to the Drosophila potassium channel gene, Shaker. A family of three closely related potassium channel genes (MK1, MK2, and MK3) that are encoded at distinct genomic loci has been isolated. Sequence analysis reveals that the coding region of each of these three genes exists as a single uninterrupted exon in the mouse genome. This organization precludes the generation of multiple forms of the protein by alternative RNA splicing, a mechanism known to characterize the Drosophila potassium channel genes Shaker and Shab. Thus, mammals may use a different strategy for generating diverse K+ channels by encoding related genes at multiple distinct genomic loci, each of which produces only a single protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chandy, K G -- Williams, C B -- Spencer, R H -- Aguilar, B A -- Ghanshani, S -- Tempel, B L -- Gutman, G A -- AI21366/AI/NIAID NIH HHS/ -- AI24783/AI/NIAID NIH HHS/ -- NS27206/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Feb 23;247(4945):973-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, Irvine 92717.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2305265" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; DNA/genetics ; DNA Probes ; Drosophila/genetics ; Exons ; *Introns ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Nucleic Acid Hybridization ; *Potassium Channels ; Restriction Mapping
    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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    Crystal structure of inhibitor-bound human 5-lipoxygenase-activating protein (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-06-30
    Description: Leukotrienes are proinflammatory products of arachidonic acid oxidation by 5-lipoxygenase that have been shown to be involved in respiratory and cardiovascular diseases. The integral membrane protein FLAP is essential for leukotriene biosynthesis. We describe the x-ray crystal structures of human FLAP in complex with two leukotriene biosynthesis inhibitors at 4.0 and 4.2 angstrom resolution, respectively. The structures show that inhibitors bind in membrane-embedded pockets of FLAP, which suggests how these inhibitors prevent arachidonic acid from binding to FLAP and subsequently being transferred to 5-lipoxygenase, thereby preventing leukotriene biosynthesis. This structural information provides a platform for the development of therapeutics for respiratory and cardiovascular diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferguson, Andrew D -- McKeever, Brian M -- Xu, Shihua -- Wisniewski, Douglas -- Miller, Douglas K -- Yamin, Ting-Ting -- Spencer, Robert H -- Chu, Lin -- Ujjainwalla, Feroze -- Cunningham, Barry R -- Evans, Jilly F -- Becker, Joseph W -- New York, N.Y. -- Science. 2007 Jul 27;317(5837):510-2. Epub 2007 Jun 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicinal Chemistry, Merck Research Laboratories, Rahway, NJ 07065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17600184" target="_blank"〉PubMed〈/a〉
    Keywords: 5-Lipoxygenase-Activating Proteins ; Arachidonate 5-Lipoxygenase/metabolism ; Arachidonic Acid/metabolism ; Binding Sites ; Carrier Proteins/antagonists & inhibitors/*chemistry/genetics/metabolism ; Catalytic Domain ; Crystallography, X-Ray ; Cytosol/chemistry ; Humans ; Hydrophobic and Hydrophilic Interactions ; Indoles/*chemistry/metabolism/pharmacology ; Membrane Proteins/antagonists & inhibitors/*chemistry/genetics/metabolism ; Models, Molecular ; Mutagenesis ; Nuclear Envelope/chemistry ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Quinolines/*chemistry/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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  • 4
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    Noise generation of upwind motor wind turbine generators (1981)
    In:  CASI
    Details
    Publication Date: 2016-06-07
    Description: Noise sources of wind turbines with rotors upstream of the support structure are discussed along with methodology for sound level prediction. Estimated noise levels for the MOD-2 wind turbine are presented operating in both the upwind and downwind configurations. Results indicate that upwind rotor configurations may be advantageous from an acoustical standpoint.
    Keywords: ENERGY PRODUCTION AND CONVERSION
    Type: NASA. Lewis Research Center Wind Turbine Dyn.; p 419-423
    Format: application/pdf
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    NASA TECHNICAL REPORTS
  • 5
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    Active control of helicopter transmission noise (1991)
    In:  Other Sources
    Details
    Publication Date: 2019-06-28
    Description: An account is given of an effort to reduce helicopter transmission noise by 10 dB, using active methods, as part of the NASA-Lewis/U.S. Army Propulsion Directorate Advanced Rotorcraft Transmission technology integration and demonstration program. The transmission used as a test stand is that of the CH-47C forward rotor. Attention is presently given to the active control system's actuators, sensors, and control algorithms.
    Keywords: ACOUSTICS
    Type: In: AHS and Royal Aeronautical Society, Technical Specialists' Meeting on Rotorcraft Acoustics(Fluid Dynamics, Philadelphia, PA, Oct. 15-17, 1991, Proceedings (A93-29401 10-71); 13 p.
    Format: text
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  • 6
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    Review and analysis of the DNW/Model 360 rotor acoustic data base (1989)
    In:  CASI
    Details
    Publication Date: 2019-07-13
    Description: A comprehensive model rotor aeroacoustic data base was collected in a large anechoic wind tunnel in 1986. Twenty-six microphones were positioned around the azimuth to collect acoustic data for approximately 150 different test conditions. A dynamically scaled, blade-pressure-instrumented model of the forward rotor of the BH360 helicopter simultaneously provided blade pressures for correlation with the acoustic data. High-speed impulsive noise, blade-vortex interaction noise, low-frequency noise, and broadband noise were all captured in this extensive data base. Trends are presentes for each noise source, with important parametric variations. The purpose of this paper is to introduce this data base and illustrate its potential for predictive code validation.
    Keywords: AERONAUTICS (GENERAL)
    Type: NASA-TM-102253 , A-89213 , NAS 1.15:102253 , USAAVSCOM-TM-89-A-002 , AD-A214865 , European Rotorcraft Forum; Sep 12, 1989 - Sep 15, 1989; Amsterdam; Netherlands
    Format: application/pdf
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