Search Results - (Author, Cooperation:P. M. Edwards)

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  1. 1
    Staff View
    Publication Date:
    2014-10-03
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Published by:
    http://www.nature.com/

    Latest Papers from Table of Contents or Articles in Press
  2. 2
    Schrama, L. H. ; Frankena, H. ; Edwards, P. M. ; Schotman, P.

    Oxford, UK : Blackwell Publishing Ltd
    Published 1984
    Staff View
    ISSN:
    1471-4159
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Medicine
    Notes:
    Gel electrophoretic separation of proteins phosphorylated in a postmitochondrial supernatant fraction of brain in the presence of spermine or adrenocorticotropin (ACTH) indicated modulation in only one region (30 kD) of the gel. The 30-kD (pp30) protein together with enzyme activity catalyzing its phosphorylation and sensitivity of the phosphorylation to spermine and ACTH were retained in a free polyribosomal fraction of this extract. ACTH(11–24) inhibited phosphorylation at all the spermine or Mg2+ concentrations tested. Structure-activity studies revealed that the inhibitory activity within ACTH(l–24) resides in the sequences ACTH(11–24), (5–18,17Lys,18Lys)-NH2, (15–24), (7–16)-NH2, and (1–16)-NH2 and can also be found in certain polylysine fragments. Phosphorylation under conditions suitable for measuring protein synthesis revealed only one phosphoprotein (pp30), sensitive to both ACTH(15–24) and spermine. The possibility of a relationship between modulation of pp30 phosphorylation and modulation of brain cell-free protein synthesis is discussed in relation to the effects of ACTH, spermine, and Mg2+ .
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1111/j.1471-4159.1984.tb06097.x

    Articles: DFG German National Licenses
  3. 3
    Schrama, L. H. ; Frankena, H. ; Edwards, P. M. ; Schotman, P.
    Springer
    Published 1984
    Staff View
    ISSN:
    1573-6903
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Medicine
    Notes:
    Abstract The incorporation of [γ-32P]ATP into proteins of rat brain polyribosomes was studied in vitro. The effects of cyclic nucleotides, calcium, hemin, ACTH, GTP, and spermine were examined. The incorporation of phosphate into proteins increased with time and phosphatase activity was very low; thus, the extent of phosphorylation was predominantly a reflection of protein kinase activity. Phosphorylation of proteins was not sensitive to Ca2+ in the presence or absence of either calmodulin or phosphatidylserine. Phosphorylation was also unaffected by cyclic nucleotides in the absence of exogenous enzymes. However, addition of a cMAP-dependent protein kinase together with cAMP resulted in a stimulation of the incorporation of phosphate into 4 phosphoproteins (pp70, pp58, pp43, and pp32); phosphorylation of pp32 was completely dependent on the addition of the kinase. ACTH (1–24), (11–24), and spermine inhibited the endogenous phosphorylation of one protein band (pp30). The phosphorylation of this 30 kD band was also selectively increased by hemin (5 μM). Higher concentrations of hemin exerted an inhibitory effect on the majority of the phosphoproteins. Protein phosphatase activity was not influenced by ACTH or spermine. The specific inhibition of pp30 phosphorylation by ACTH or spermine is most probably explained by an interaction with a cyclic nucleotide- and Ca2+-independent protein kinase.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/BF00973039

    Articles: DFG German National Licenses
  4. 4
    King, M. L. ; Edwards, P. M.
    Springer
    Published 1989
    Staff View
    ISSN:
    1435-8921
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Economics
    Notes:
    Abstract This paper considers testing for structural change of unknown form in the linear regression model as a problem of testing for goodness-of-fit. Transformations of recursive (or other LUS) residuals that reduce the problem to one of testing independently distributed uniform variables are presented. Exact empirical distribution function tests can then be applied without having to estimate unknown Parameters. The tests are illustrated by their application to a money demand model.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/BF01980591

    Articles: DFG German National Licenses