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  • Animals  (4)
  • *Circadian Rhythm  (1)
  • 2010-2014  (3)
  • 2005-2009  (1)
  • 1965-1969
  • 1
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    Biochemistry. Nature's intricate clockwork (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2012-07-17
    Beschreibung: 〈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〉
    Schlagwort(e): ARNTL Transcription Factors/*chemistry ; Animals ; CLOCK Proteins/*chemistry ; *Circadian Rhythm ; Humans ; *Transcriptional Activation
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
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    Ecology: The Convention on Biological Diversity's 2010 target (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2005-01-18
    Beschreibung: 〈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〉
    Schlagwort(e): Animals ; *Biodiversity ; *Conservation of Natural Resources ; *Ecology ; Ecosystem ; Humans ; Interdisciplinary Communication ; International Cooperation ; Models, Biological ; Models, Theoretical ; Public Policy
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
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    Structure of full-length Drosophila cryptochrome (2011)
    Nature Publishing Group (NPG)
    Details
    Publikationsdatum: 2011-11-15
    Beschreibung: The cryptochrome/photolyase (CRY/PL) family of photoreceptors mediates adaptive responses to ultraviolet and blue light exposure in all kingdoms of life. Whereas PLs function predominantly in DNA repair of cyclobutane pyrimidine dimers (CPDs) and 6-4 photolesions caused by ultraviolet radiation, CRYs transduce signals important for growth, development, magnetosensitivity and circadian clocks. Despite these diverse functions, PLs/CRYs preserve a common structural fold, a dependence on flavin adenine dinucleotide (FAD) and an internal photoactivation mechanism. However, members of the CRY/PL family differ in the substrates recognized (protein or DNA), photochemical reactions catalysed and involvement of an antenna cofactor. It is largely unknown how the animal CRYs that regulate circadian rhythms act on their substrates. CRYs contain a variable carboxy-terminal tail that appends the conserved PL homology domain (PHD) and is important for function. Here, we report a 2.3-A resolution crystal structure of Drosophila CRY with an intact C terminus. The C-terminal helix docks in the analogous groove that binds DNA substrates in PLs. Conserved Trp 536 juts into the CRY catalytic centre to mimic PL recognition of DNA photolesions. The FAD anionic semiquinone found in the crystals assumes a conformation to facilitate restructuring of the tail helix. These results help reconcile the diverse functions of the CRY/PL family by demonstrating how conserved protein architecture and photochemistry can be elaborated into a range of light-driven functions.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3240699/" 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/PMC3240699/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zoltowski, Brian D -- Vaidya, Anand T -- Top, Deniz -- Widom, Joanne -- Young, Michael W -- Crane, Brian R -- GM054339/GM/NIGMS NIH HHS/ -- GM079679/GM/NIGMS NIH HHS/ -- R01 GM079679/GM/NIGMS NIH HHS/ -- R01 GM079679-06/GM/NIGMS NIH HHS/ -- R37 GM054339/GM/NIGMS NIH HHS/ -- R37 GM054339-16/GM/NIGMS NIH HHS/ -- England -- Nature. 2011 Nov 13;480(7377):396-9. doi: 10.1038/nature10618.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22080955" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Motifs ; Animals ; Arthropod Antennae ; Catalytic Domain ; Cryptochromes/*chemistry/metabolism ; Crystallography, X-Ray ; DNA/chemistry/metabolism ; Drosophila melanogaster/*chemistry ; Flavin-Adenine Dinucleotide/metabolism ; Models, Molecular ; Oxidation-Reduction ; Protein Conformation ; Substrate Specificity ; Tryptophan/chemistry/metabolism
    Print ISSN: 0028-0836
    Digitale ISSN: 1476-4687
    Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von Nature Publishing Group (NPG)
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
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    Updated structure of Drosophila cryptochrome (2013)
    Nature Publishing Group (NPG)
    Details
    Publikationsdatum: 2013-03-23
    Beschreibung: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3694752/" 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/PMC3694752/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levy, Colin -- Zoltowski, Brian D -- Jones, Alex R -- Vaidya, Anand T -- Top, Deniz -- Widom, Joanne -- Young, Michael W -- Scrutton, Nigel S -- Crane, Brian R -- Leys, David -- R01 GM079679/GM/NIGMS NIH HHS/ -- R37 GM054339/GM/NIGMS NIH HHS/ -- England -- Nature. 2013 Mar 21;495(7441):E3-4. doi: 10.1038/nature11995.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Manchester Institute of Biotechnology, Faculty of Life Sciences, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23518567" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Cryptochromes/chemistry ; Drosophila/*chemistry ; *Models, Molecular ; Protein Structure, Tertiary
    Print ISSN: 0028-0836
    Digitale ISSN: 1476-4687
    Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von Nature Publishing Group (NPG)
    Standort Signatur Erwartet Verfügbarkeit
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