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  • 1
    Publication Date: 2000-01-05
    Description: The mitogen-activated protein (MAP) kinase cascade is inactivated at the level of MAP kinase by members of the MAP kinase phosphatase (MKP) family, including MKP-1. MKP-1 was a labile protein in CCL39 hamster fibroblasts; its degradation was attenuated by inhibitors of the ubiquitin-directed proteasome complex. MKP-1 was a target in vivo and in vitro for p42(MAPK) or p44(MAPK), which phosphorylates MKP-1 on two carboxyl-terminal serine residues, Serine 359 and Serine 364. This phosphorylation did not modify MKP-1's intrinsic ability to dephosphorylate p44(MAPK) but led to stabilization of the protein. These results illustrate the importance of regulated protein degradation in the control of mitogenic signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brondello, J M -- Pouyssegur, J -- McKenzie, F R -- GM26939/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Dec 24;286(5449):2514-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Signaling, Developmental Biology and Cancer Research, CNRS UMR 6543, Centre A. Lacassagne, 33 Avenue de Valombrose, Nice 06189, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10617468" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood ; *Cell Cycle Proteins ; Cell Division ; Cell Line ; Cricetinae ; Culture Media ; Cysteine Endopeptidases/metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; Dual Specificity Phosphatase 1 ; Estradiol/pharmacology ; Humans ; Immediate-Early Proteins/chemistry/*metabolism ; Leucine/analogs & derivatives/pharmacology ; Leupeptins/pharmacology ; MAP Kinase Signaling System ; Mitogen-Activated Protein Kinase 1/*metabolism ; Mitogen-Activated Protein Kinase 3 ; Mitogen-Activated Protein Kinases/*metabolism ; Multienzyme Complexes/metabolism ; Mutation ; Nitrophenols/metabolism ; Organophosphorus Compounds/metabolism ; *Phosphoprotein Phosphatases ; Phosphorylation ; Proteasome Endopeptidase Complex ; Protein Phosphatase 1 ; Protein Tyrosine Phosphatases/chemistry/*metabolism ; Ubiquitins/metabolism
    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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  • 2
    ISSN: 1365-2494
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Effects of timing and rate of N fertilizer application on concentrations of P, K, S, Ca, Mg, Na, Cl, Mn, Fe, Cu and Zn in herbage from perennial ryegrass/white clover pastures were studied at two sites in south-western Victoria, Australia. Nitrogen fertilizer (0, 15, 25, 30, 45 and 60 kg ha–1) was applied as urea in mid-April, early May, mid-May, early June and mid-June 1996 to pastures grazed by dairy cows. At Site 1, N fertilizer resulted in a linear increase in P, K, S, Mg and Cl concentrations in herbage and a linear decrease in Ca concentration. For all times of application, concentrations of P, K, Ca, Mg and Cl in herbage increased by 0·0048, 0·08, −0·010, 0·0013 and 0·053 g kg–1 dry matter (DM) per kg N applied respectively. For S concentration, maximum responses occurred in mid-May (0·012 g kg–1 DM per kg N applied). At Site 2, N fertilizer resulted in a linear increase in P, S and Na concentrations in herbage, a linear decrease in Ca concentration and a curvilinear increase in K and Cl concentration. The maximum responses for P, S and K concentrations in herbage occurred for the N application in mid-June and were 0·015, 0·008 and 0·47 g kg–1 DM per kg N applied respectively. For Cl concentration, the maximum response occurred for the N application in early June and was 0·225 g kg–1 DM per kg N applied. Overall, applications of N fertilizer up to 60 kg ha–1 did not alter herbage mineral concentration to levels that might affect pasture growth or animal health.
    Type of Medium: Electronic Resource
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