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  • 1
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    Public health. The Mexico City policy and U.S. family planning assistance (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-10-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cincotta, R P -- Crane, B B -- New York, N.Y. -- Science. 2001 Oct 19;294(5542):525-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research Department, Population Action International, 1300 19th Street, NW, Washington, DC 20036, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11641484" target="_blank"〉PubMed〈/a〉
    Keywords: *Abortion, Induced ; *Developing Countries ; *Family Planning Policy ; Family Planning Services/*economics/organization & administration ; Female ; Financing, Government ; Government Agencies/*economics ; Humans ; *International Cooperation ; United States ; Women's Health
    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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    Structure of nitric oxide synthase oxygenase dimer with pterin and substrate (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-16
    Description: Crystal structures of the murine cytokine-inducible nitric oxide synthase oxygenase dimer with active-center water molecules, the substrate L-arginine (L-Arg), or product analog thiocitrulline reveal how dimerization, cofactor tetrahydrobiopterin, and L-Arg binding complete the catalytic center for synthesis of the essential biological signal and cytotoxin nitric oxide. Pterin binding refolds the central interface region, recruits new structural elements, creates a 30 angstrom deep active-center channel, and causes a 35 degrees helical tilt to expose a heme edge and the adjacent residue tryptophan-366 for likely reductase domain interactions and caveolin inhibition. Heme propionate interactions with pterin and L-Arg suggest that pterin has electronic influences on heme-bound oxygen. L-Arginine binds to glutamic acid-371 and stacks with heme in an otherwise hydrophobic pocket to aid activation of heme-bound oxygen by direct proton donation and thereby differentiate the two chemical steps of nitric oxide synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crane, B R -- Arvai, A S -- Ghosh, D K -- Wu, C -- Getzoff, E D -- Stuehr, D J -- Tainer, J A -- HL58883/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1998 Mar 27;279(5359):2121-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Skaggs Institute for Chemical Biology, The 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/9516116" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arginine/chemistry/*metabolism ; Binding Sites ; Biopterin/*analogs & derivatives/chemistry/metabolism ; Citrulline/analogs & derivatives/chemistry/metabolism ; Crystallography, X-Ray ; Dimerization ; Hydrogen Bonding ; Isoenzymes/chemistry/metabolism ; Ligands ; Macrophages/enzymology ; Mice ; Models, Molecular ; Nitric Oxide/biosynthesis ; Nitric Oxide Synthase/*chemistry/metabolism ; Nitric Oxide Synthase Type II ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Thiourea/analogs & derivatives/chemistry/metabolism
    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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  • 3
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    Inhibition of a Mycobacterium tuberculosis beta-ketoacyl ACP synthase by isoniazid (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-11
    Description: Although isoniazid (isonicotinic acid hydrazide, INH) is widely used for the treatment of tuberculosis, its molecular target has remained elusive. In response to INH treatment, saturated hexacosanoic acid (C26:0) accumulated on a 12-kilodalton acyl carrier protein (AcpM) that normally carried mycolic acid precursors as long as C50. A protein species purified from INH-treated Mycobacterium tuberculosis was shown to consist of a covalent complex of INH, AcpM, and a beta-ketoacyl acyl carrier protein synthase, KasA. Amino acid-altering mutations in the KasA protein were identified in INH-resistant patient isolates that lacked other mutations associated with resistance to this drug.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mdluli, K -- Slayden, R A -- Zhu, Y -- Ramaswamy, S -- Pan, X -- Mead, D -- Crane, D D -- Musser, J M -- Barry, C E 3rd -- AI37004/AI/NIAID NIH HHS/ -- Z01 AI000783-11/Intramural NIH HHS/ -- New York, N.Y. -- Science. 1998 Jun 5;280(5369):1607-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tuberculosis Research Unit, Laboratory of Intracellular Parasites, Rocky Mountain Laboratories, National Institute for Allergy and Infectious Diseases (NIAID), National Institutes of Health, Hamilton, MT 59840, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9616124" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/*antagonists & ; inhibitors/chemistry/genetics ; Acyl Carrier Protein/chemistry/genetics/metabolism ; Amino Acid Sequence ; Antitubercular Agents/*pharmacology ; Drug Resistance, Microbial ; Enzyme Inhibitors/pharmacology ; Fatty Acids/metabolism ; Genes, Bacterial ; Humans ; Isoniazid/*pharmacology ; Molecular Sequence Data ; Molecular Weight ; Mutation ; Mycobacterium tuberculosis/drug effects/*enzymology/genetics ; Mycolic Acids/metabolism ; Tuberculosis/microbiology ; Up-Regulation
    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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  • 4
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    Time-critical social mobilization (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-10-29
    Description: The World Wide Web is commonly seen as a platform that can harness the collective abilities of large numbers of people to accomplish tasks with unprecedented speed, accuracy, and scale. To explore the Web's ability for social mobilization, the Defense Advanced Research Projects Agency (DARPA) held the DARPA Network Challenge, in which competing teams were asked to locate 10 red weather balloons placed at locations around the continental United States. Using a recursive incentive mechanism that both spread information about the task and incentivized individuals to act, our team was able to find all 10 balloons in less than 9 hours, thus winning the Challenge. We analyzed the theoretical and practical properties of this mechanism and compared it with other approaches.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pickard, Galen -- Pan, Wei -- Rahwan, Iyad -- Cebrian, Manuel -- Crane, Riley -- Madan, Anmol -- Pentland, Alex -- New York, N.Y. -- Science. 2011 Oct 28;334(6055):509-12. doi: 10.1126/science.1205869.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Media Laboratory, Massachusetts Institute of Technology (MIT), Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22034432" target="_blank"〉PubMed〈/a〉
    Keywords: Altruism ; *Communication ; *Cooperative Behavior ; Humans ; *Internet ; *Motivation ; *Social Facilitation ; Time Factors
    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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  • 5
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    Biochemistry. Nature's intricate clockwork (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-07-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crane, Brian R -- New York, N.Y. -- Science. 2012 Jul 13;337(6091):165-6. doi: 10.1126/science.1224611.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14850, USA. bc69@cornell.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22798591" target="_blank"〉PubMed〈/a〉
    Keywords: ARNTL Transcription Factors/*chemistry ; Animals ; CLOCK Proteins/*chemistry ; *Circadian Rhythm ; Humans ; *Transcriptional Activation
    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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    Ecology: The Convention on Biological Diversity's 2010 target (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-01-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balmford, Andrew -- Bennun, Leon -- Brink, Ben Ten -- Cooper, David -- Cote, Isabelle M -- Crane, Peter -- Dobson, Andrew -- Dudley, Nigel -- Dutton, Ian -- Green, Rhys E -- Gregory, Richard D -- Harrison, Jeremy -- Kennedy, Elizabeth T -- Kremen, Claire -- Leader-Williams, Nigel -- Lovejoy, Thomas E -- Mace, Georgina -- May, Robert -- Mayaux, Phillipe -- Morling, Paul -- Phillips, Joanna -- Redford, Kent -- Ricketts, Taylor H -- Rodriguez, Jon Paul -- Sanjayan, M -- Schei, Peter J -- van Jaarsveld, Albert S -- Walther, Bruno A -- New York, N.Y. -- Science. 2005 Jan 14;307(5707):212-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cambridge University and University of Cape Town.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15653489" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; *Conservation of Natural Resources ; *Ecology ; Ecosystem ; Humans ; Interdisciplinary Communication ; International Cooperation ; Models, Biological ; Models, Theoretical ; Public Policy
    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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    Tryptophan-accelerated electron flow through proteins (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-06-28
    Description: Energy flow in biological structures often requires submillisecond charge transport over long molecular distances. Kinetics modeling suggests that charge-transfer rates can be greatly enhanced by multistep electron tunneling in which redox-active amino acid side chains act as intermediate donors or acceptors. We report transient optical and infrared spectroscopic experiments that quantify the extent to which an intervening tryptophan residue can facilitate electron transfer between distant metal redox centers in a mutant Pseudomonas aeruginosa azurin. Cu(I) oxidation by a photoexcited Re(I)-diimine at position 124 on a histidine(124)-glycine(123)-tryptophan(122)-methionine(121) beta strand occurs in a few nanoseconds, fully two orders of magnitude faster than documented for single-step electron tunneling at a 19 angstrom donor-acceptor distance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shih, Crystal -- Museth, Anna Katrine -- Abrahamsson, Malin -- Blanco-Rodriguez, Ana Maria -- Di Bilio, Angel J -- Sudhamsu, Jawahar -- Crane, Brian R -- Ronayne, Kate L -- Towrie, Mike -- Vlcek, Antonin Jr -- Richards, John H -- Winkler, Jay R -- Gray, Harry B -- DK19038/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2008 Jun 27;320(5884):1760-2. doi: 10.1126/science.1158241.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Beckman Institute, 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/18583608" target="_blank"〉PubMed〈/a〉
    Keywords: Azurin/*chemistry ; Copper/*chemistry ; Crystallography, X-Ray ; *Electrons ; Energy Transfer ; Kinetics ; Ligands ; Models, Chemical ; Mutant Proteins/chemistry ; Oxidation-Reduction ; Phenylalanine/chemistry ; Pseudomonas aeruginosa/chemistry ; Rhenium/chemistry ; Spectrum Analysis ; Thermodynamics ; Tryptophan/*chemistry ; Tyrosine/chemistry
    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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    Vertebrate cell cycle modulates infection by protozoan parasites (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-11-27
    Description: Synchronized HeLa cell populations were exposed to Trypanosoma cruzi or Toxoplasma gondii, obligate intracellular protozoan parasites that cause Chagas' disease and toxoplasmosis, respectively, in humans. The ability of the two parasites to infect HeLa cells increased as the HeLa cells proceeded from the G1 phase to the S phase of their growth cycle and decreased as the cells entered G2-M. Characterization of the S-phase cell surface components responsible for this phenomenon could be beneficial in the development of vaccines against these parasitic diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dvorak, J A -- Crane, M S -- New York, N.Y. -- Science. 1981 Nov 27;214(4524):1034-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7029713" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Cycle ; HeLa Cells/physiology ; Humans ; Kinetics ; Toxoplasma/pathogenicity/*physiology ; Trypanosoma cruzi/pathogenicity/*physiology
    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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