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  • 1
    Electronic Resource
    Electronic Resource
    Proto-oncogene fos: Factors Affecting Expression and Covalent Modification of the Gene Product (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 511 (1987), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Notes: Expression of proto-oncogene fos is induced in response to a variety of growth factors and differentiation-specific agents. However, the induction of fos gene expression is not influenced by inhibition of protein synthesis. We, therefore, entertained the notion that expression of the fos gene may be governed by posttranslational modification of cellular transcriptional factors. We report here that transcription of the human c-fos gene is modulated by negatively and positively acting cellular factors.The nuclear protein products of the resident oncogene of the FBJ-murine osteosar-coma virus (v-fos) and its corresponding cellular proto-oncogene (c-fos) are stoichiometrically phosphorylated on serine and threonine residues. The c-fos protein is more highly phosphorylated than the v-fos protein due to the phosphorylation of unique sites tentatively localized to the c-terminal 20 amino acid residues. The protein kinase C agonist, TPA, stimulates phosphorylation of the c-fos, but not the v-fos protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1987.tb36242.x
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  • 2
    Electronic Resource
    Electronic Resource
    THE USE OF ACRYLAMIDE GEL ELECTROPHORESIS IN THE INVESTIGATION OF THE SOLUBLE PROTEINS OF PLANTS (1964)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 121 (1964), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1964.tb14223.x
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  • 3
    Electronic Resource
    Electronic Resource
    The molecular anatomy and function of thylakoid proteins (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Plant, cell & environment 12 (1989), S. 0 
    Details
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract. The structure of chloroplast membrane proteins and their organization into photosynthetically-active multimeric complexes is described. Extensive use has been made of information derived from gene sequencing and other biochemical studies to predict likely protein conformations. These predictions have been assimilated into structural models of the various thylakoid complexes. The enzymatic activities of the complexes have also been described and where possible related to individual polypeptides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3040.1989.tb01228.x
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  • 4
    Electronic Resource
    Electronic Resource
    Uptake and Distribution of Mercury within Higher Plants (1977)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 39 (1977), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The uptake and distribution of inorganic mercury (HgCl2) within higher plants (Pisum sativum and Mentha spicata) was examined using solution culture and radiotracer techniques. Plants were found to tolerate an external level of 1 mgHg/kg of solution but both physiological and biochemical processes were affected at 5 mgHg/kg and 10 mgHg/kg. The uptake of Hg into plants grown in hydroponic solution was a function of external concentration. Over the concentration range considered the accumulation of Hg in the roots was linear on a log-log basis although the uptake of the element into the shoots appeared to be two-phased. The distribution of Hg in plants was asymmetrical with much greater amounts of the element in the roots than the shoots. Although the level of Hg increased generally in plant tissues with increasing external levels, the proportion retained in the roots, relative to the shoots, was constant (approximately 95%). Two binding characteristics of the Hg within plant tissue were detected. A major proportion of Hg was tightly bound, being unaffected by treatment with ethanol and hydrochloric acid. The remaining Hg in the tissue was removed by either water or hydrochloric acid treatment. Cell fractionation indicated that the major binding component of Hg in plant tissues was the cell wall.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1977.tb01880.x
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  • 5
    Electronic Resource
    Electronic Resource
    The structure, function and dynamics of photosystem two (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 100 (1997), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: One of the greatest challenges in modern photosynthesis research is to elucidate fully the structural and functional properties of photosystem two (PSII). This water-plasto-quinone oxidoreductase is located in a membrane complex composed of more than 25 subunits. The primary and secondary structures of all known subunits which constitute the central core of PSII are reviewed. How these subunits interact with each other to produce the tertiary and quaternary structure of PSII in vivo is not fully understood. However, electron microscopy is helping to fill this gap in our knowledge both by single particle analysis and electron crystallography. These studies suggest that active PSII is dimeric, although the functional significance of this oligomeric state is not yet understood. Moreover, the elucidation of the structure of photosystem one (PSI) by X-ray crystallography has revealed features which are likely to be relevant to PSII structure. It seems highly likely that the D1 protein with CP43 and D2 protein with CP47 (summing 11 transmembrane helices in each case) will have structural similarities to the organisation of PsaA and PsaB. It is likely that the turnover of the D1 protein is aided by the relatively easy removal of CP43 from this arrangement of the PSII core.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1997.tb00008.x
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