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  • 1
    Electronic Resource
    Electronic Resource
    Rates of synthesis and turnover of 5′ cap structures of hnRNA and mRNA and their changes during sea urchin development (1979)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 1 (1979), S. 151-165 
    Details
    ISSN: 0192-253X
    Keywords: sea urchin embryo ; hnRNA ; mRNA ; 5′ terminal cap ; turnover ; synthesis rate ; methylation ; developmental changes ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The relationship between heterogeneous nuclear RNA (hnRNA) and messenger RNA (mRNA) synthesis has been studied as a function of the development of the sea urchin embryo through the use of methyl incorporation. Several parameters in the metabolism of capped hnRNA and mRNA of early blastula and late gastrula stages have been investigated by measuring the kinetics of transfer of methyl groups from S-adenosylmethionine to the 5′ cap structures in nuclear and cytoplasmic RNA: 1The rate constants for the decay of hnRNA caps and the synthesis of mRNA caps are equal to within experimental error. This equality indicates a flux of precursor hnRNA caps to mRNA caps with a very high degree of conservation of the hnRNA caps. This conservation holds for each embryonic stage.2From literature data on the labeling kinetics of GTP and mRNA, we have calculated the decay constant of a putative mRNA precursor component of hnRNA. The value of this constant is very close to that for the decay constant of hnRNA caps. Hence, all hnRNA caps and some portion of their associated hnRNA sequences behave kinetically as the pre-mRNA fraction. This kinetically ascribed pre-mRNA comprises approximately 30% of the hnRNA mass.3The part of the hnRNA which does not serve as precursor to mRNA turns over at least twice as rapidly as the pre-mRNA fraction.4During development from early blastula to late gastrula, the rate of hnRNA cap synthesis drops from 2 × 103 molecules/min/cell to half of this value. This decline is parallel to the decline in total hnRNA synthesis and thereby confirms the constant degree of capping of hnRNA, as previously reported. We infer that the pre-mRNA fraction of hnRNA remains nearly constant during this developmental period.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020010204
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  • 2
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    Physical properties determining self-organization of motors and microtubules (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-05-12
    Description: In eukaryotic cells, microtubules and their associated motor proteins can be organized into various large-scale patterns. Using a simplified experimental system combined with computer simulations, we examined how the concentrations and kinetic parameters of the motors contribute to their collective behavior. We observed self-organization of generic steady-state structures such as asters, vortices, and a network of interconnected poles. We identified parameter combinations that determine the generation of each of these structures. In general, this approach may become useful for correlating the morphogenetic phenomena taking place in a biological system with the biophysical characteristics of its constituents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Surrey, T -- Nedelec, F -- Leibler, S -- Karsenti, E -- New York, N.Y. -- Science. 2001 May 11;292(5519):1167-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Biophysics Program, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11349149" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; Antibodies ; Biopolymers/chemistry/metabolism ; *Computer Simulation ; *Drosophila Proteins ; Guanosine Triphosphate/metabolism ; Kinesin/chemistry/metabolism ; Kinetics ; Macromolecular Substances ; Microtubules/*chemistry/drug effects/*metabolism ; Models, Molecular ; Molecular Motor Proteins/*chemistry/*metabolism ; Paclitaxel/pharmacology ; Protein Structure, Quaternary/drug effects ; Tubulin/chemistry/metabolism ; Viscosity
    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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  • 3
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    Hemoglobin I mutation encoded at both alpha-globin loci on the same chromosome: concerted evolution in the human genome (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-12-21
    Description: Genetic analysis of an individual expressing an unexpectedly high level of hemoglobin I, an alpha-globin structural mutant, reveals that the mutation is present at both the alpha 1- and the alpha 2-globin gene loci. Kindred analysis confirms that the two affected genes are located in cis. The most likely explanation for this finding is that a recent conversion event occurred within the human alpha-globin gene cluster.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liebhaber, S A -- Rappaport, E F -- Cash, F E -- Ballas, S K -- Schwartz, E -- Surrey, S -- AM 16691/AM/NIADDK NIH HHS/ -- AM 33975/AM/NIADDK NIH HHS/ -- HL 28157/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1984 Dec 21;226(4681):1449-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6505702" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Genes ; Globins/*genetics ; *Hemoglobins ; Hemoglobins, Abnormal/*genetics ; Humans ; *Mutation ; Nucleic Acid Hybridization ; Recombination, Genetic
    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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