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  • 1
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    Identification of a fourth mannose 6-phosphate binding site in the cation-independent mannose 6-phosphate receptor (2015)
    Oxford University Press
    Details
    Publication Date: 2015-04-28
    Description: The 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR) plays an essential role in lysosome biogenesis by targeting ~60 different phosphomannosyl-containing acid hydrolases to the lysosome. This type I membrane glycoprotein has a large extracellular region comprised of 15 homologous domains. Two mannose 6-phosphate (M6P) binding sites have been mapped to domains 3 and 9, whereas domain 5 binds preferentially to the phosphodiester, M6P- N -acetylglucosamine (GlcNAc). A structure-based sequence alignment predicts that the C-terminal domain 15 contains three out of the four conserved residues identified as essential for carbohydrate recognition by domains 3, 5 and 9 of the CI-MPR, but lacks two cysteine residues that are predicted to form a disulfide bond. To determine whether domain 15 of the CI-MPR has lectin activity and to probe its carbohydrate-binding specificity, truncated forms of the CI-MPR were tested for binding to acid hydrolases with defined N -glycans in surface plasmon resonance analyses, and used to interrogate a phosphorylated glycan microarray. The results show that a construct encoding domains 14–15 binds both M6P and M6P-GlcNAc with similar affinity ( K d = 13 and 17 μM, respectively). Site-directed mutagenesis studies demonstrate the essential role of the conserved Tyr residue in domain 15 for phosphomannosyl binding. A structural model of domain 15 was generated that predicted an Arg residue to be in the binding pocket and mutagenesis studies confirmed its important role in carbohydrate binding. Together, these results show that the CI-MPR contains a fourth carbohydrate-recognition site capable of binding both phosphomonoesters and phosphodiesters.
    Print ISSN: 0959-6658
    Electronic ISSN: 1460-2423
    Topics: Biology , Medicine
    Published by Oxford University Press
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  • 2
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    Energetic charged particles in the magnetosphere of neptune (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-12-15
    Description: The Voyager 2 cosmic ray system (CRS) measured significant fluxes of energetic [〉/=1 megaelectron volt (MeV)] trapped electrons and protons in the magnetosphere of Neptune. The intensities are maximum near a magnetic L shell of 7, decreasing closer to the planet because of absorption by satellites and rings. In the region of the inner satellites of Neptune, the radiation belts have a complicated structure, which provides some constraints on the magnetic field geometry of the inner magnetosphere. Electron phase-space densities have a positive radial gradient, indicating that they diffuse inward from a source in the outer magnetosphere. Electron spectra from 1 to 5 MeV are generally well represented by power laws with indices near 6, which harden in the region of peak flux to power law indices of 4 to 5. Protons have significantly lower fluxes than electrons throughout the magnetosphere, with large anisotropies due to radial intensity gradients. The radiation belts resemble those of Uranus to the extent allowed by the different locations of the satellites, which limit the flux at each planet.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, E C -- Cummings, A C -- Loooper, M D -- Selesnick, R S -- Lal, N -- McDonald, F B -- Trainor, J H -- Chenette, D L -- New York, N.Y. -- Science. 1989 Dec 15;246(4936):1489-94.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17756005" target="_blank"〉PubMed〈/a〉
    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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    Influenza binds phosphorylated glycans from human lung (2019)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2019
    Description: 〈p〉Influenza A viruses can bind sialic acid–terminating glycan receptors, and species specificity is often correlated with sialic acid linkage with avian strains recognizing α2,3-linked sialylated glycans and mammalian strains preferring α2,6-linked sialylated glycans. These paradigms derive primarily from studies involving erythrocyte agglutination, binding to synthetic receptor analogs or binding to undefined surface markers on cells or tissues. Here, we present the first examination of the N-glycome of the human lung for identifying natural receptors for a range of avian and mammalian influenza viruses. We found that the human lung contains many α2,3- and α2,6-linked sialylated glycan determinants bound by virus, but all viruses also bound to phosphorylated, nonsialylated glycans.〈/p〉
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Voyager 1 observes low-energy galactic cosmic rays in a region depleted of heliospheric ions (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-07-03
    Description: On 25 August 2012, Voyager 1 was at 122 astronomical units when the steady intensity of low-energy ions it had observed for the previous 6 years suddenly dropped for a third time and soon completely disappeared as the ions streamed away into interstellar space. Although the magnetic field observations indicate that Voyager 1 remained inside the heliosphere, the intensity of cosmic ray nuclei from outside the heliosphere abruptly increased. We report the spectra of galactic cosmic rays down to ~3 x 10(6) electron volts per nucleon, revealing H and He energy spectra with broad peaks from 10 x 10(6) to 40 x 10(6) electron volts per nucleon and an increasing galactic cosmic-ray electron intensity down to ~10 x 10(6) electron volts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, E C -- Cummings, A C -- McDonald, F B -- Heikkila, B C -- Lal, N -- Webber, W R -- New York, N.Y. -- Science. 2013 Jul 12;341(6142):150-3. doi: 10.1126/science.1236408. Epub 2013 Jun 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉California Institute of Technology, Pasadena, CA 91125, USA. ecs@srl.caltech.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23811227" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Murine model of Niemann-Pick C disease: mutation in a cholesterol homeostasis gene (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-11
    Description: An integrated human-mouse positional candidate approach was used to identify the gene responsible for the phenotypes observed in a mouse model of Niemann-Pick type C (NP-C) disease. The predicted murine NPC1 protein has sequence homology to the putative transmembrane domains of the Hedgehog signaling molecule Patched, to the cholesterol-sensing regions of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase and SREBP cleavage-activating protein (SCAP), and to the NPC1 orthologs identified in human, the nematode Caenorhabditis elegans, and the yeast Saccharomyces cerevisiae. The mouse model may provide an important resource for studying the role of NPC1 in cholesterol homeostasis and neurodegeneration and for assessing the efficacy of new drugs for NP-C disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Loftus, S K -- Morris, J A -- Carstea, E D -- Gu, J Z -- Cummings, C -- Brown, A -- Ellison, J -- Ohno, K -- Rosenfeld, M A -- Tagle, D A -- Pentchev, P G -- Pavan, W J -- New York, N.Y. -- Science. 1997 Jul 11;277(5323):232-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genetic Disease Research, National Human Genome Research Institute, National Institutes of Health (NIH), Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9211850" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cholesterol/*metabolism ; *Disease Models, Animal ; Homeostasis ; Humans ; Hydroxymethylglutaryl CoA Reductases/chemistry ; Intracellular Signaling Peptides and Proteins ; Lysosomes/metabolism ; Membrane Proteins/chemistry ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Mice, Mutant Strains ; Molecular Sequence Data ; Mutation ; Niemann-Pick Diseases/*genetics/metabolism ; Phenotype ; Protein Sorting Signals/chemistry ; Proteins/chemistry/*genetics/physiology ; Sequence Homology, Amino Acid
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Niemann-Pick C1 disease gene: homology to mediators of cholesterol homeostasis (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-11
    Description: Niemann-Pick type C (NP-C) disease, a fatal neurovisceral disorder, is characterized by lysosomal accumulation of low density lipoprotein (LDL)-derived cholesterol. By positional cloning methods, a gene (NPC1) with insertion, deletion, and missense mutations has been identified in NP-C patients. Transfection of NP-C fibroblasts with wild-type NPC1 cDNA resulted in correction of their excessive lysosomal storage of LDL cholesterol, thereby defining the critical role of NPC1 in regulation of intracellular cholesterol trafficking. The 1278-amino acid NPC1 protein has sequence similarity to the morphogen receptor PATCHED and the putative sterol-sensing regions of SREBP cleavage-activating protein (SCAP) and 3-hydroxy-3-methyl-glutaryl coenzyme A (HMG-CoA) reductase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carstea, E D -- Morris, J A -- Coleman, K G -- Loftus, S K -- Zhang, D -- Cummings, C -- Gu, J -- Rosenfeld, M A -- Pavan, W J -- Krizman, D B -- Nagle, J -- Polymeropoulos, M H -- Sturley, S L -- Ioannou, Y A -- Higgins, M E -- Comly, M -- Cooney, A -- Brown, A -- Kaneski, C R -- Blanchette-Mackie, E J -- Dwyer, N K -- Neufeld, E B -- Chang, T Y -- Liscum, L -- Strauss, J F 3rd -- Ohno, K -- Zeigler, M -- Carmi, R -- Sokol, J -- Markie, D -- O'Neill, R R -- van Diggelen, O P -- Elleder, M -- Patterson, M C -- Brady, R O -- Vanier, M T -- Pentchev, P G -- Tagle, D A -- New York, N.Y. -- Science. 1997 Jul 11;277(5323):228-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9211849" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Carrier Proteins ; Cholesterol/*metabolism ; Cholesterol, LDL/metabolism ; Chromosome Mapping ; Chromosomes, Human, Pair 18 ; Cloning, Molecular ; *Drosophila Proteins ; Homeostasis ; Humans ; Hydroxymethylglutaryl CoA Reductases/chemistry ; Insect Proteins/chemistry ; Intracellular Signaling Peptides and Proteins ; Lysosomes/metabolism ; *Membrane Glycoproteins ; Membrane Proteins/chemistry ; Molecular Sequence Data ; Mutation ; Niemann-Pick Diseases/*genetics/metabolism ; Polymorphism, Single-Stranded Conformational ; Proteins/chemistry/*genetics/physiology ; Receptors, Cell Surface/chemistry ; Sequence Homology, Amino Acid ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Voyager 1 explores the termination shock region and the heliosheath beyond (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-09-24
    Description: Voyager 1 crossed the termination shock of the supersonic flow of the solar wind on 16 December 2004 at a distance of 94.01 astronomical units from the Sun, becoming the first spacecraft to begin exploring the heliosheath, the outermost layer of the heliosphere. The shock is a steady source of low-energy protons with an energy spectrum approximately E(-1.41 +/- 0.15) from 0.5 to approximately 3.5 megaelectron volts, consistent with a weak termination shock having a solar wind velocity jump ratio r=2.6(-0.2)(+0.4). However, in contradiction to many predictions, the intensity of anomalous cosmic ray (ACR) helium did not peak at the shock, indicating that the ACR source is not in the shock region local to Voyager 1. The intensities of approximately 10-megaelectron volt electrons, ACRs, and galactic cosmic rays have steadily increased since late 2004 as the effects of solar modulation have decreased.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, E C -- Cummings, A C -- McDonald, F B -- Heikkila, B C -- Lal, N -- Webber, W R -- New York, N.Y. -- Science. 2005 Sep 23;309(5743):2017-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉California Institute of Technology, Pasadena, CA 91125, USA. ecs@srl.caltech.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16179468" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Observation of the (6)(0)Fe nucleosynthesis-clock isotope in galactic cosmic rays (2016)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2016-04-23
    Description: Iron-60 ((60)Fe) is a radioactive isotope in cosmic rays that serves as a clock to infer an upper limit on the time between nucleosynthesis and acceleration. We have used the ACE-CRIS instrument to collect 3.55 x 10(5) iron nuclei, with energies ~195 to ~500 mega-electron volts per nucleon, of which we identify 15 (60)Fe nuclei. The (60)Fe/(56)Fe source ratio is (7.5 +/- 2.9) x 10(-5) The detection of supernova-produced (60)Fe in cosmic rays implies that the time required for acceleration and transport to Earth does not greatly exceed the (60)Fe half-life of 2.6 million years and that the (60)Fe source distance does not greatly exceed the distance cosmic rays can diffuse over this time, 1 kiloparsec. A natural place for (60)Fe origin is in nearby clusters of massive stars.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Binns, W R -- Israel, M H -- Christian, E R -- Cummings, A C -- de Nolfo, G A -- Lave, K A -- Leske, R A -- Mewaldt, R A -- Stone, E C -- von Rosenvinge, T T -- Wiedenbeck, M E -- New York, N.Y. -- Science. 2016 May 6;352(6286):677-80. doi: 10.1126/science.aad6004. Epub 2016 Apr 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Washington University, St. Louis, MO 63130, USA. wrb@wustl.edu mhi@wustl.edu. ; NASA/Goddard Space Flight Center, Greenbelt, MD 20771, USA. ; California Institute of Technology, Pasadena, CA 91125, USA. ; Washington University, St. Louis, MO 63130, USA. ; Jet Propulsion Laboratory, California Institute of Technology, Pasadena, CA 91109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/27103666" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Energetic Charged Particles in Saturn's Magnetosphere: Voyager 1 Results (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-04-10
    Description: Voyager 1 provided the first look at Saturn's magnetotail and magnetosphere during relatively quiet interplanetary conditions. This report discusses the energetic particle populations of the outer magnetosphere of Saturn and absorption features associated with Titan and Rhea, and compares these observations with Pioneer 11 data of a year earlier. The trapped proton fluxes had soft spectra, represented by power laws E(-gamma) in kinetic energy E, with gamma approximately 7 in the outer magnetosphere and gamma approximately 9 in the magnetotail. Structure associated with the magnetotial was observed as close as 10 Saturn radii (R(s)) on the outbound trajectory. The proton and electron fluxes in the outer magnetosphere and in the magnetotail were variable and appeared to respond to changes in interplanetary conditions. Protons with energies 〉/= 2 million electron volts had free access to the magnetosphere from interplanetary space and were not stably trapped outside approximately 7.5 R(s).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogt, R E -- Chenette, D L -- Cummings, A C -- Garrard, T L -- Stone, E C -- Schardt, A W -- Trainor, J H -- Lal, N -- McDonald, F B -- New York, N.Y. -- Science. 1981 Apr 10;212(4491):231-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17783835" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Energetic Charged Particles in Saturn's Magnetosphere: Voyager 2 Results (1982)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1982-01-29
    Description: Results from the cosmic-ray system on Voyager 2 in Saturn's magnetosphere are presented. During the inbound pass through the outer magnetosphere, the 〉/= 0.43-million-electron-volt proton flux was more intense, and both the proton and electron fluxes were more variable, than previously observed. These changes are attributed to the influence on the magnetosphere of variations in the solar wind conditions. Outbound, beyond 18 Saturn radii, impulsive bursts of 0.14- to 〉 1.0- million-electron-volt electrons were observed. In the inner magnetosphere, the charged particle absorption signatures of Mimas, Enceladus, and Tethys are used to constrain the possible tilt and offset of Saturn's internal magnetic dipole. At approximately 3 Saturn radii, a transient decrease was observed in the electron flux which was not due to Mimas. Characteristics of this decrease suggest the existence of additional material, perhaps another satellite, in the orbit of Mimas.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogt, R E -- Chenette, D L -- Cummings, A C -- Garrard, T L -- Stone, E C -- Schardt, A W -- Trainor, J H -- Lal, N -- McDonald, F B -- New York, N.Y. -- Science. 1982 Jan 29;215(4532):577-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17771281" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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