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  • 1
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    In:  Journal of Geophysical Research, Warszawa, Elsevier, vol. 103, no. B5, pp. 9691-9712, pp. 2382, (ISBN: 0-12-018847-3)
    Publication Date: 1998
    Keywords: Rheology ; Inelastic ; Laboratory measurements ; Physical properties of rocks ; JGR
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  • 2
    Publication Date: 1998-06-11
    Description: The mouse Clock gene encodes a bHLH-PAS protein that regulates circadian rhythms and is related to transcription factors that act as heterodimers. Potential partners of CLOCK were isolated in a two-hybrid screen, and one, BMAL1, was coexpressed with CLOCK and PER1 at known circadian clock sites in brain and retina. CLOCK-BMAL1 heterodimers activated transcription from E-box elements, a type of transcription factor-binding site, found adjacent to the mouse per1 gene and from an identical E-box known to be important for per gene expression in Drosophila. Mutant CLOCK from the dominant-negative Clock allele and BMAL1 formed heterodimers that bound DNA but failed to activate transcription. Thus, CLOCK-BMAL1 heterodimers appear to drive the positive component of per transcriptional oscillations, which are thought to underlie circadian rhythmicity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gekakis, N -- Staknis, D -- Nguyen, H B -- Davis, F C -- Wilsbacher, L D -- King, D P -- Takahashi, J S -- Weitz, C J -- New York, N.Y. -- Science. 1998 Jun 5;280(5369):1564-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Harvard Medical School, Boston MA 02115, USA. 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9616112" target="_blank"〉PubMed〈/a〉
    Keywords: ARNTL Transcription Factors ; Animals ; Basic Helix-Loop-Helix Transcription Factors ; Biological Clocks ; CLOCK Proteins ; Cell Cycle Proteins ; Circadian Rhythm/genetics/*physiology ; Cloning, Molecular ; Cricetinae ; DNA/metabolism ; Dimerization ; Feedback ; Gene Expression ; Helix-Loop-Helix Motifs ; Male ; Mesocricetus ; Mice ; Mutation ; Nuclear Proteins/*genetics/metabolism ; Period Circadian Proteins ; Promoter Regions, Genetic ; Retina/metabolism ; Suprachiasmatic Nucleus/metabolism ; Trans-Activators/genetics/*metabolism ; Transcription Factors/genetics/*metabolism ; *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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  • 3
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Using polymerase chain reaction, interleukin-6 (IL-6) cDNA fragments from harbor seal (Phoca vitulina), killer whale (Orcinus orca), and Southern sea otter (Enhydra lutris nereis) were cloned and sequenced. For all three species, a continuous open reading frame encoding 203 residues for harbor seal, 199 residues for killer whale, and 201 residues for sea otter with stop codons located at analogous positions were identified. These fragments correspond to nucleotides 71 – 753 of the human IL-6 transcript and represent 96% of the complete coding nucleotides. Comparison of these marine mammal sequences with other published mammalian IL-6 cDNA demonstrated that both harbor seal and sea otter IL-6 had most similarity to that of other terrestrial carnivores (Mustelidae and Canidae), while killer whale had highest identity with ruminants (Bovidae and Ovidae). Among the three marine mammal species characterized, as well as cDNA sequences from nine other species, 40 invariant amino acids, including a number of residues situated at the putative gp80 and gp130 receptor binding sites, were identified. The presence of invariant amino acids within the receptor-binding portion of IL-6 for twelve different species suggests these positions are essential for biological activity of IL-6 and, moreover, likely account for the cross-reactivity among different mammalian IL-6-like activities in mouse bioassays. An additional significant finding was the presence of several variant residues only within the mouse putative IL-6 receptor binding region, which may account for observations of restricted cross-reactivity of mouse IL-6-like activity in human bioassays. Together, these findings provide insights into the evolution of the mammalian IL-6 gene and additional valuable information regarding amino acid residues essential for the biological activity of mammalian IL-6.
    Type of Medium: Electronic Resource
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