ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Publication Date: 2002-12-14
    Description: The master circadian oscillator in the hypothalamic suprachiasmatic nucleus is entrained to the day/night cycle by retinal photoreceptors. Melanopsin (Opn4), an opsin-based photopigment, is a primary candidate for photoreceptor-mediated entrainment. To investigate the functional role of melanopsin in light resetting of the oscillator, we generated melanopsin-null mice (Opn4-/-). These mice entrain to a light/dark cycle and do not exhibit any overt defect in circadian activity rhythms under constant darkness. However, they display severely attenuated phase resetting in response to brief pulses of monochromatic light, highlighting the critical role of melanopsin in circadian photoentrainment in mammals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Panda, Satchidananda -- Sato, Trey K -- Castrucci, Ana Maria -- Rollag, Mark D -- DeGrip, Willem J -- Hogenesch, John B -- Provencio, Ignacio -- Kay, Steve A -- MH 62405/MH/NIMH NIH HHS/ -- MH51573/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2002 Dec 13;298(5601):2213-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genomics Institute of the Novartis Research Foundation, 10675 John J. Hopkins Drive, San Diego, CA 92121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12481141" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Clocks/physiology ; Circadian Rhythm/*physiology ; Darkness ; Female ; Gene Targeting ; *Light ; Light Signal Transduction ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Motor Activity ; Retinal Ganglion Cells/physiology ; Rod Opsins/genetics/*physiology ; Suprachiasmatic Nucleus/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 2
    Publication Date: 2001-12-01
    Description: Phosphoinositide (PI)-binding domains play critical roles in the intracellular localization of a variety of cell-signaling proteins. The 120-amino acid Phox homology (PX) domain targets proteins to organelle membranes through interactions between two conserved basic motifs within the PX domain and specific PIs. The combination of protein-lipid and protein-protein interactions ensures the proper localization and regulation of PX domain-containing proteins. Upon proper localization, PX domain-containing proteins can then bind to additional proteins and execute their functions in a diverse set of biological pathways, including intracellular protein transport, cell growth and survival, cytoskeletal organization, and neutrophil defense.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sato, T K -- Overduin, M -- Emr, S D -- New York, N.Y. -- Science. 2001 Nov 30;294(5548):1881-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Medicine and Howard Hughes Medical Institute, University of California at San Diego School of Medicine, La Jolla, CA 92093-0668, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11729306" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Animals ; Carrier Proteins/chemistry/metabolism ; Humans ; Intracellular Membranes/*metabolism ; Models, Molecular ; NADPH Oxidase ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphatidylinositols/*metabolism ; Phosphoproteins/*chemistry/*metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Protein Transport ; Signal Transduction ; Structure-Activity Relationship ; src Homology Domains
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 3
    Publication Date: 2003-06-28
    Description: Although mice lacking rod and cone photoreceptors are blind, they retain many eye-mediated responses to light, possibly through photosensitive retinal ganglion cells. These cells express melanopsin, a photopigment that confers this photosensitivity. Mice lacking melanopsin still retain nonvisual photoreception, suggesting that rods and cones could operate in this capacity. We observed that mice with both outer-retinal degeneration and a deficiency in melanopsin exhibited complete loss of photoentrainment of the circadian oscillator, pupillary light responses, photic suppression of arylalkylamine-N-acetyltransferase transcript, and acute suppression of locomotor activity by light. This indicates the importance of both nonvisual and classical visual photoreceptor systems for nonvisual photic responses in mammals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Panda, Satchidananda -- Provencio, Ignacio -- Tu, Daniel C -- Pires, Susana S -- Rollag, Mark D -- Castrucci, Ana Maria -- Pletcher, Mathew T -- Sato, Trey K -- Wiltshire, Tim -- Andahazy, Mary -- Kay, Steve A -- Van Gelder, Russell N -- Hogenesch, John B -- K08-EY00403/EY/NEI NIH HHS/ -- MH 62405/MH/NIMH NIH HHS/ -- MH51573/MH/NIMH NIH HHS/ -- R01-EY14988/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2003 Jul 25;301(5632):525-7. Epub 2003 Jun 26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genomics Institute of the Novartis Research Foundation, 10675 John J. Hopkins Drive, San Diego, CA 92121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12829787" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arylamine N-Acetyltransferase/genetics/metabolism ; Blindness/genetics/*physiopathology ; Circadian Rhythm ; *Light ; *Light Signal Transduction ; Mice ; Mice, Inbred C3H ; Motor Activity ; Photoreceptor Cells, Vertebrate/*physiology ; Reflex, Pupillary ; Retinal Degeneration/genetics/physiopathology ; Retinal Ganglion Cells/physiology ; Rod Opsins/deficiency/genetics/*physiology ; Signal Transduction ; Suprachiasmatic Nucleus/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 4
    Publication Date: 2014-09-23
    Description: Experimental investigations of transactinoide elements provide benchmark results for chemical theory and probe the predictive power of trends in the periodic table. So far, in gas-phase chemical reactions, simple inorganic compounds with the transactinoide in its highest oxidation state have been synthesized. Single-atom production rates, short half-lives, and harsh experimental conditions limited the number of experimentally accessible compounds. We applied a gas-phase carbonylation technique previously tested on short-lived molybdenum (Mo) and tungsten (W) isotopes to the preparation of a carbonyl complex of seaborgium, the 106th element. The volatile seaborgium complex showed the same volatility and reactivity with a silicon dioxide surface as those of the hexacarbonyl complexes of the lighter homologs Mo and W. Comparison of the product's adsorption enthalpy with theoretical predictions and data for the lighter congeners supported a Sg(CO)6 formulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Even, J -- Yakushev, A -- Dullmann, Ch E -- Haba, H -- Asai, M -- Sato, T K -- Brand, H -- Di Nitto, A -- Eichler, R -- Fan, F L -- Hartmann, W -- Huang, M -- Jager, E -- Kaji, D -- Kanaya, J -- Kaneya, Y -- Khuyagbaatar, J -- Kindler, B -- Kratz, J V -- Krier, J -- Kudou, Y -- Kurz, N -- Lommel, B -- Miyashita, S -- Morimoto, K -- Morita, K -- Murakami, M -- Nagame, Y -- Nitsche, H -- Ooe, K -- Qin, Z -- Schadel, M -- Steiner, J -- Sumita, T -- Takeyama, M -- Tanaka, K -- Toyoshima, A -- Tsukada, K -- Turler, A -- Usoltsev, I -- Wakabayashi, Y -- Wang, Y -- Wiehl, N -- Yamaki, S -- New York, N.Y. -- Science. 2014 Sep 19;345(6203):1491-3. doi: 10.1126/science.1255720.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Helmholtz-Institut Mainz, 55099 Mainz, Germany. ; GSI Helmholtzzentrum fur Schwerionenforschung GmbH, 64291 Darmstadt, Germany. ; Helmholtz-Institut Mainz, 55099 Mainz, Germany. GSI Helmholtzzentrum fur Schwerionenforschung GmbH, 64291 Darmstadt, Germany. Institut fur Kernchemie, Johannes Gutenberg-Universitat Mainz, 55099 Mainz, Germany. duellman@uni-mainz.de. ; RIKEN, Wako, Saitama 351-0198, Japan. ; Japan Atomic Energy Agency, Tokai, Ibaraki 319-1195, Japan. ; Institut fur Kernchemie, Johannes Gutenberg-Universitat Mainz, 55099 Mainz, Germany. ; Department of Chemistry and Biochemistry, University of Bern, 3012 Bern, Switzerland. Paul Scherrer Institute, 5232 Villigen, Switzerland. ; Institute of Modern Physics, Chinese Academy of Sciences, 730000 Lanzhou, China. ; Japan Atomic Energy Agency, Tokai, Ibaraki 319-1195, Japan. Department of Chemistry, Hiroshima University, Kagamiyama, Higashi-Hiroshima 739-8526, Japan. ; RIKEN, Wako, Saitama 351-0198, Japan. Department of Physics, Kyushu University, Higashi-Ku, Fukuoka, 812-8581, Japan. ; RIKEN, Wako, Saitama 351-0198, Japan. Department of Chemistry, Niigata University, Niigata, Niigata 950-2181, Japan. ; Department of Chemistry, University of California, Berkeley, CA 94720-1460, USA. Lawrence Berkeley National Laboratory, Berkeley, CA 94720-8169, USA. ; Department of Chemistry, Niigata University, Niigata, Niigata 950-2181, Japan. ; Helmholtz-Institut Mainz, 55099 Mainz, Germany. Institut fur Kernchemie, Johannes Gutenberg-Universitat Mainz, 55099 Mainz, Germany. ; RIKEN, Wako, Saitama 351-0198, Japan. Department of Physics, Saitama University, Saitama 338-8570, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25237098" 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
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 5
    Publication Date: 2015-04-10
    Description: The chemical properties of an element are primarily governed by the configuration of electrons in the valence shell. Relativistic effects influence the electronic structure of heavy elements in the sixth row of the periodic table, and these effects increase dramatically in the seventh row--including the actinides--even affecting ground-state configurations. Atomic s and p1/2 orbitals are stabilized by relativistic effects, whereas p3/2, d and f orbitals are destabilized, so that ground-state configurations of heavy elements may differ from those of lighter elements in the same group. The first ionization potential (IP1) is a measure of the energy required to remove one valence electron from a neutral atom, and is an atomic property that reflects the outermost electronic configuration. Precise and accurate experimental determination of IP1 gives information on the binding energy of valence electrons, and also, therefore, on the degree of relativistic stabilization. However, such measurements are hampered by the difficulty in obtaining the heaviest elements on scales of more than one atom at a time. Here we report that the experimentally obtained IP1 of the heaviest actinide, lawrencium (Lr, atomic number 103), is 4.96(+0.08)(-0.07) electronvolts. The IP1 of Lr was measured with (256)Lr (half-life 27 seconds) using an efficient surface ion-source and a radioisotope detection system coupled to a mass separator. The measured IP1 is in excellent agreement with the value of 4.963(15) electronvolts predicted here by state-of-the-art relativistic calculations. The present work provides a reliable benchmark for theoretical calculations and also opens the way for IP1 measurements of superheavy elements (that is, transactinides) on an atom-at-a-time scale.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sato, T K -- Asai, M -- Borschevsky, A -- Stora, T -- Sato, N -- Kaneya, Y -- Tsukada, K -- Dullmann, Ch E -- Eberhardt, K -- Eliav, E -- Ichikawa, S -- Kaldor, U -- Kratz, J V -- Miyashita, S -- Nagame, Y -- Ooe, K -- Osa, A -- Renisch, D -- Runke, J -- Schadel, M -- Thorle-Pospiech, P -- Toyoshima, A -- Trautmann, N -- England -- Nature. 2015 Apr 9;520(7546):209-11. doi: 10.1038/nature14342.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Japan Atomic Energy Agency (JAEA), Tokai, Ibaraki 319-1195, Japan. ; 1] Centre for Theoretical Chemistry and Physics, New Zealand Institute for Advanced Study, Massey University, 0745 North Shore MSC, Auckland, New Zealand [2] Helmholtz-Institut Mainz, 55099 Mainz, Germany. ; ISOLDE, CERN, CH-1211 Geneva 23, Switzerland. ; 1] Japan Atomic Energy Agency (JAEA), Tokai, Ibaraki 319-1195, Japan [2] Graduate School of Science and Engineering, Ibaraki University, Mito, Ibaraki 310-8512, Japan. ; 1] Helmholtz-Institut Mainz, 55099 Mainz, Germany [2] GSI Helmholtzzentrum fur Schwerionenforschung, 64291 Darmstadt, Germany [3] Institut fur Kernchemie, Johannes Gutenberg-Universitat Mainz, 55099 Mainz, Germany. ; 1] Helmholtz-Institut Mainz, 55099 Mainz, Germany [2] Institut fur Kernchemie, Johannes Gutenberg-Universitat Mainz, 55099 Mainz, Germany. ; School of Chemistry, Tel Aviv University, 69978 Tel Aviv, Israel. ; 1] Japan Atomic Energy Agency (JAEA), Tokai, Ibaraki 319-1195, Japan [2] Nishina Center for Accelerator-Based Science, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. ; Institut fur Kernchemie, Johannes Gutenberg-Universitat Mainz, 55099 Mainz, Germany. ; Graduate School of Science, Hiroshima University, Kagamiyama, Higashi-Hiroshima 739-8526, Japan. ; Institute of Science and Technology, Niigata University, Niigata 910-2181, Japan. ; GSI Helmholtzzentrum fur Schwerionenforschung, 64291 Darmstadt, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25855457" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 6
    Publication Date: 2013-08-31
    Description: Author(s): M. Murakami, S. Goto, H. Murayama, T. Kojima, H. Kudo, D. Kaji, K. Morimoto, H. Haba, Y. Kudou, T. Sumita, R. Sakai, A. Yoneda, K. Morita, Y. Kasamatsu, H. Kikunaga, and T. K. Sato Production cross sections of Rf isotopes in the 248 Cm +  18 O reaction were measured at the beam energy range of 88.2 to 101.3 MeV by use of a gas-filled recoil ion separator. The excitation functions of 260 Rf, 261 Rf a , and 262 Rf were obtained together with those of spontaneously fissioning nuclides wh... [Phys. Rev. C 88, 024618] Published Fri Aug 30, 2013
    Keywords: Nuclear Reactions
    Print ISSN: 0556-2813
    Electronic ISSN: 1089-490X
    Topics: Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 7
  • 8
  • 9
  • 10
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...