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  • Phosphorylation
  • American Association for the Advancement of Science (AAAS)  (6)
  • American Institute of Physics (AIP)
  • 1975-1979  (6)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (6)
  • American Institute of Physics (AIP)
  • Springer  (4)
Years
Year
  • 1
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1979-03-16
    Description: Addition of acetate to a stationary phase culture of Escherichia coli in glycerol mineral salts medium containing phosphorus-32-labeled orthophosphate results in rapid loss of isocitrate dehydrogenase activity and concomitant incorporation of phosphorus-32 into the enzyme. This is the first example of protein phosphorylation in a bacterium in which the endogenous substrate for the protein kinase has been identified.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Garnak, M -- Reeves, H C -- New York, N.Y. -- Science. 1979 Mar 16;203(4385):1111-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/34215" target="_blank"〉PubMed〈/a〉
    Keywords: Acetates/metabolism ; Escherichia coli/*enzymology ; Isocitrate Dehydrogenase/*metabolism ; NADP/metabolism ; Phosphorylation ; Protein Kinases/metabolism ; Serine/metabolism ; Threonine/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
    Publication Date: 1979-05-04
    Description: Of the proteins in mechanically disrupted chicken gizzard fibers (no functional sarcolemma) only the 20,000-dalton light chains of myosin underwent large Ca2+-and Sr2+-dependent changes in phosphorylation. Phosphorylation closely corresponded with the Ca2+- and Sr2+-activated tensions. Adenosine 5'-O (3'-thiotriphosphate) only in the presence of Ca2+ induced irreversible Ca2+-insensitive activation of tension and thiophosphorylation of the 20,000-dalton light chains, and blocked incorporation of 32P from [gamma-32P]adenosine triphosphate into the myosin light chains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoar, P E -- Kerrick, W G -- Cassidy, P S -- New York, N.Y. -- Science. 1979 May 4;204(4392):503-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/432654" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*pharmacology ; Chickens ; Gizzard/*physiology ; In Vitro Techniques ; Molecular Weight ; Muscle Contraction/*drug effects ; Muscle, Smooth/*physiology ; Myosins/*metabolism ; Phosphorylation ; Protein Kinases/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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  • 3
    Publication Date: 1979-09-28
    Description: Adenosine 3',5'-monophosphate (cyclic AMP) receptor protein of 56,000 daltons increases markedly in mammary tumors induced by 7,12-dimethylbenz[a]anthracene (DMBA) after incubation of tumor slices with cyclic AMP, benzamide, and arginine. Incubation of cytosol from these tumor slices with nuclei from unincubated tumors results in nuclear uptake of the 56,000-dalton cyclic AMP receptor and in phosphorylation of the 76,000-dalton nuclear protein. Binding of the 56,000-dalton receptor and phosphorylation of the 76,000-dalton protein also occur in DMBA tumor nuclei when protein kinase type II of bovine heart is used. The results suggest that cyclic AMP receptor is involved in the nuclear events of a hormone-dependent mammary tumor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cho-Chung, Y S -- Archibald, D -- Clair, T -- New York, N.Y. -- Science. 1979 Sep 28;205(4413):1390-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/224463" target="_blank"〉PubMed〈/a〉
    Keywords: 9,10-Dimethyl-1,2-benzanthracene ; Animals ; Cell Nucleus/metabolism ; Cell-Free System ; Chromosomal Proteins, Non-Histone/*metabolism ; Cyclic AMP/*metabolism ; Female ; Mammary Neoplasms, Experimental/*metabolism ; Neoplasm Proteins/metabolism ; Phosphorylation ; Protein Kinases/*metabolism ; Rats ; Receptors, Cyclic AMP/*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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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1979-05-11
    Description: 2-Deoxy-[14C]glucose metabolism was examined in brains of hypoxic, normotensive rats by autoradiography, which revealed alternating cortical columns of high and low metabolism. Activity in white matter was increased severalfold over that in adjacent gray matter. The columns were anatomically related to penetrating cortical arteries with areas between arteries demonstrating higher rates of metabolism. The results suggest the presence of interarterial tissue oxygen gradients that influence regional glucose metabolism. The relatively greater sensitivity of white matter metabolism to hypoxia may lead to an understanding of white matter damage in postanoxic leukoencephalopathy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pulsinelli, W A -- Duffy, T E -- New York, N.Y. -- Science. 1979 May 11;204(4393):626-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/432667" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anoxia/*metabolism/physiopathology ; Brain/*metabolism ; Cerebral Cortex/metabolism ; Cerebrovascular Circulation ; Deoxyglucose/metabolism ; Glucose/*metabolism ; Male ; Phosphorylation ; Rats
    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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  • 5
    Publication Date: 1979-01-05
    Description: Repetitive stimulation (100 pulses per second for 1 second) of the Schafer collateral-commissural system of the rat hippocampus induces long-term potentiation of synaptic strength and produces significant changes in the subsequent endogenous phosphorylation of a 40,000-dalton protein from synaptic plasma membranes. This effect is not observed after stimulation in calcium-deficient media or after simulation at the rate of one pulse per second for 100 seconds. These findings provide evidence that repetitive synaptic activation can alter the phosphorylation machinery of the synaptic region and suggest a biochemical process which may be involved in the production of neuronal plasticity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Browning, M -- Dunwiddie, T -- Bennett, W -- Gispen, W -- Lynch, G -- New York, N.Y. -- Science. 1979 Jan 5;203(4375):60-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/214855" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Electric Stimulation ; Hippocampus/*metabolism ; In Vitro Techniques ; Membrane Proteins/*metabolism ; Molecular Weight ; Phosphoproteins/*metabolism ; Phosphorylation ; Rats ; Synaptic Membranes/*metabolism ; *Synaptic Transmission ; Time Factors
    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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  • 6
    Publication Date: 1979-09-21
    Description: The bis-acridine ring system forms the basis for new biophysical probes of novel stereochemistry. Spectral data indicate that certain alkylene bridged bis-9-aminoacridines have a parallel plane conformation of predictable interplane distance. The parallel plane conformation is independent of solvent and thus is different from nucleic acid systems. This stable conformation allows these compounds to be used as sensitive "rulers" for describing binding site geometry in cholinergic enzymes and in the delineation of the mechanism of allosteric control in acetylcholinesterase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Himel, C M -- Taylor, J L -- Pape, C -- Millar, D B -- Christopher, J -- Kurlansik, L -- New York, N.Y. -- Science. 1979 Sep 21;205(4412):1277-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/472743" target="_blank"〉PubMed〈/a〉
    Keywords: *Acetylcholinesterase/metabolism ; *Acridines ; Binding Sites ; Kinetics ; Molecular Conformation ; Phosphorylation ; Protein Conformation ; Spectrophotometry, Ultraviolet
    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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