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
Filter
  • American Association for the Advancement of Science (AAAS)  (5)
  • 2005-2009  (5)
  • 1
    Publication Date: 2005-10-08
    Description: The proton transfer mechanism between aqueous Bronsted acids and bases, forming an encounter pair, has been studied in real time with ultrafast infrared spectroscopy. The transient intermediacy of a hydrated proton, formed by ultrafast dissociation from an optically triggered photoacid proton donor ROH, is implicated by the appearance of an infrared absorption marker band before protonation of the base, B-. Thus, proton exchange between an acid and a base in aqueous solution is shown to proceed by a sequential, von Grotthuss-type, proton-hopping mechanism through water bridges. The spectra suggest a hydronium cation H3O+ structure for the intermediate, stabilized in the Eigen configuration in the ionic complex RO-...H3O+...B-.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mohammed, Omar F -- Pines, Dina -- Dreyer, Jens -- Pines, Ehud -- Nibbering, Erik T J -- New York, N.Y. -- Science. 2005 Oct 7;310(5745):83-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Born Institut fur Nichtlineare Optik und Kurzzeitspektroskopie, Max Born Strasse 2A, D-12489 Berlin, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16210532" 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 ...
  • 2
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-12-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berry, Oliver F -- New York, N.Y. -- Science. 2006 Dec 1;314(5804):1388-90; author reply 1388-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17138882" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; DNA, Mitochondrial/*genetics ; *Genetic Variation ; Genetics, Population ; Population Density
    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: 2008-04-19
    Description: We investigated whether fluoxetine, a widely prescribed medication for treatment of depression, restores neuronal plasticity in the adult visual system of the rat. We found that chronic administration of fluoxetine reinstates ocular dominance plasticity in adulthood and promotes the recovery of visual functions in adult amblyopic animals, as tested electrophysiologically and behaviorally. These effects were accompanied by reduced intracortical inhibition and increased expression of brain-derived neurotrophic factor in the visual cortex. Cortical administration of diazepam prevented the effects induced by fluoxetine, indicating that the reduction of intracortical inhibition promotes visual cortical plasticity in the adult. Our results suggest a potential clinical application for fluoxetine in amblyopia as well as new mechanisms for the therapeutic effects of antidepressants and for the pathophysiology of mood disorders.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maya Vetencourt, Jose Fernando -- Sale, Alessandro -- Viegi, Alessandro -- Baroncelli, Laura -- De Pasquale, Roberto -- O'Leary, Olivia F -- Castren, Eero -- Maffei, Lamberto -- New York, N.Y. -- Science. 2008 Apr 18;320(5874):385-8. doi: 10.1126/science.1150516.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Scuola Normale Superiore, Piazza dei Cavalieri, I-56100 Pisa, Italy. jf.maya@in.cnr.it〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18420937" target="_blank"〉PubMed〈/a〉
    Keywords: Amblyopia/drug therapy/physiopathology ; Animals ; Antidepressive Agents, Second-Generation/pharmacology ; Brain-Derived Neurotrophic Factor/metabolism ; Diazepam/pharmacology ; Dominance, Ocular/drug effects ; Evoked Potentials, Visual/drug effects ; Fluoxetine/administration & dosage/*pharmacology ; Long-Term Potentiation ; Long-Term Synaptic Depression ; Neuronal Plasticity/*drug effects ; Rats ; Serotonin/physiology ; Serotonin Uptake Inhibitors/*pharmacology ; Synaptic Transmission/drug effects ; Visual Cortex/*drug effects/physiology ; gamma-Aminobutyric Acid/metabolism
    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: 2008-06-17
    Description: Protein dynamics are essential for protein function, and yet it has been challenging to access the underlying atomic motions in solution on nanosecond-to-microsecond time scales. We present a structural ensemble of ubiquitin, refined against residual dipolar couplings (RDCs), comprising solution dynamics up to microseconds. The ensemble covers the complete structural heterogeneity observed in 46 ubiquitin crystal structures, most of which are complexes with other proteins. Conformational selection, rather than induced-fit motion, thus suffices to explain the molecular recognition dynamics of ubiquitin. Marked correlations are seen between the flexibility of the ensemble and contacts formed in ubiquitin complexes. A large part of the solution dynamics is concentrated in one concerted mode, which accounts for most of ubiquitin's molecular recognition heterogeneity and ensures a low entropic complex formation cost.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lange, Oliver F -- Lakomek, Nils-Alexander -- Fares, Christophe -- Schroder, Gunnar F -- Walter, Korvin F A -- Becker, Stefan -- Meiler, Jens -- Grubmuller, Helmut -- Griesinger, Christian -- de Groot, Bert L -- New York, N.Y. -- Science. 2008 Jun 13;320(5882):1471-5. doi: 10.1126/science.1157092.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Theoretical and Computational Biophysics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18556554" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Animals ; Anisotropy ; Chemistry, Physical ; Crystallography, X-Ray ; Entropy ; Kinetics ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; Physicochemical Phenomena ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Solutions ; Ubiquitin/*chemistry/*metabolism ; Xenopus laevis
    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: 2007-02-03
    Description: Femtosecond time-resolved infrared spectroscopy was used to study the formation of cyclobutane dimers in the all-thymine oligodeoxynucleotide (dT)18 by ultraviolet light at 272 nanometers. The appearance of marker bands in the time-resolved spectra indicates that the dimers are fully formed approximately 1 picosecond after ultraviolet excitation. The ultrafast appearance of this mutagenic photolesion points to an excited-state reaction that is approximately barrierless for bases that are properly oriented at the instant of light absorption. The low quantum yield of this photoreaction is proposed to result from infrequent conformational states in the unexcited polymer, revealing a strong link between conformation before light absorption and photodamage.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2792699/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2792699/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schreier, Wolfgang J -- Schrader, Tobias E -- Koller, Florian O -- Gilch, Peter -- Crespo-Hernandez, Carlos E -- Swaminathan, Vijay N -- Carell, Thomas -- Zinth, Wolfgang -- Kohler, Bern -- GM064563/GM/NIGMS NIH HHS/ -- R01 GM064563-04/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Feb 2;315(5812):625-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department fur Physik, Ludwig-Maximilians-Universitat, Oettingenstrasse 67, D-80538 Munchen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17272716" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/*chemistry ; DNA Damage ; Dimerization ; Kinetics ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/*chemistry ; Photons ; Pyrimidine Dimers/*chemistry ; Spectroscopy, Fourier Transform Infrared ; Temperature ; Ultraviolet Rays
    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 ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...