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  • LUNAR AND PLANETARY EXPLORATION  (15)
  • Humans  (6)
  • insulin receptor  (3)
  • 1985-1989  (12)
  • 1980-1984  (8)
  • 1975-1979  (4)
  • 1
    Electronic Resource
    Electronic Resource
    Interaction of the insulin receptor kinase with serine/threonine kinases in vitro (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 28 (1985), S. 171-182 
    Details
    ISSN: 0730-2312
    Keywords: insulin receptor ; tyrosine phosphorylation ; serine kinases ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Insulin causes rapid phosphorylation of the β subunit (Mr = 95,000) of its receptor in broken cell preparations. This occurs on tyrosine residues and is due to activation of a protein kinase which is contained in the receptor itself. In the intact cell, insulin also stimulates the phosphorylation of the receptor and other cellular proteins on serine and threonine residues. In an attempt to find a protein that might link the receptor tyrosine kinase to these serine/threonine phosphorylation reactions, we have studied the interaction of a partially purified preparation of insulin receptor with purified preparations of serine/threoine kinases known to phosphorylate glycogen synthase. No insulin-dependent phosphorylation was ob served when casein kinases I and II, phosphorylase kinase, or glycogen synthase kinase 3 was incubated in vitro with the insulin receptor. These kinases also failed to phosphorylate the receptor. By contrast, the insulin receptor kinase catalyzed the phosphorylation of the calmodulin-dependent kinase and addition of insulin in vitro resulted in a 40% increase in this phosphorylation. In the presence of calmodulin-dependent kinase and the insulin receptor kinase, insulin also stimulated the phosphorylation of calmodulin. Phosphoamino acid analysis showed an increase of phosphotyrosine content in both calmodulin and calmodulindependent protein kinase. These data suggest that the insulin receptor kinase may interact directly and specifically with the calmodulin-dependent kinase and calmodulin. Further studies will be required to determine if these phosphorylations modify the action of these regulatory proteins.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240280209
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Phosphorylation of the solubilized insulin receptor by the gene product of the Rous sarcoma virus, pp60src (1984)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 26 (1984), S. 169-179 
    Details
    ISSN: 0730-2312
    Keywords: insulin receptor ; tyrosine kinase ; pp60src ; phosphorylation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Both the insulin receptor and the gene product of the Rous sarcoma virus, pp60src, are protein kinases which phosphorylate themselves and other proteins on tyrosinc residues. Addition of the solubilized insulin receptor to purified pp60src increased the phosphorylation of the β-subunit of the insulin receptor. Phosphorylation of the insulin receptor by pp60src occurred both in the absence and presence of insulin but did not alter the insulin dose response for autophosphorylation of the receptor. Increasing concentrations of pp60src increased the phosphorylation of the receptor and at high concentrations equaled the maximal effect produced by insulin. Our observations suggest a possible mechanism by which the metabolically regulated insulin receptor tyrosine kinase could be altered by other tyrosine kinases such as that associated with pp60src. Further studies will be required to determine if the insulin receptor is phosphorylated by pp60src in Rous sarcoma virus-infected cells.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240260305
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  • 3
    Electronic Resource
    Electronic Resource
    Phosphorylation of glycolytic and gluconeogenic enzymes by the insulin receptor kinase (1987)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 33 (1987), S. 15-26 
    Details
    ISSN: 0730-2312
    Keywords: phosphorylation ; insulin receptor ; tyrosine kinase ; phosphofructokinase ; glycolysis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Various glycolytic and gluconeogenic enzymes were tested as substrates for the insulin receptor kinase. Phosphofructokinase and phosphoglycerate mutase were found to be the best substrates. Phosphorylation of these enzymes was rapid, stimulated 2- to 6-fold by 10-7 M insulin and occurred exclusively on tyrosine residues. Enolase, fructose 1,6-bisphosphatase, lactate dehydrogenases in decreasing order, were also subject to insulin-stimulated phosphorylation but to a smaller extent than that for phpsphofructokinase or phosphoglycerate mutase.The phosphorylation of phosphofructokinase was studied most extensively since phosphofructokinase is known to catalyze a rate-limiting step in glycolosis. The apparent Km of the insulin receptor for phosphofructokinase was 0.1 μM, which is within the physiologic range of concentration of this enzyme in most cells. Tyrosine phosphorylation of phosphofructokinase paralleled autophosphorylation of the β-subunit of the insulin receptor with respect to time course, insulin dose response (half maximal effect between 10-9 and 10-8 M insulin), and cation requirement (Mn2+ 〉 Mg2+ 〉 〉 Ca2+). Further study will be required to determine whether the tyrosine phosphorylation of phosphofructokinase plays a role in insulin-stimulated increases in glycolytic flux.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240330103
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  • 4
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    Molecular defects in insulin action (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-07-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kahn, C R -- Goldstein, B J -- New York, N.Y. -- Science. 1989 Jul 7;245(4913):13.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2662406" target="_blank"〉PubMed〈/a〉
    Keywords: Diabetes Mellitus/*physiopathology ; Humans ; Insulin/*physiology ; Insulin Resistance
    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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  • 5
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    Contact-mediated bone resorption by human monocytes in vitro (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-03-03
    Description: Human circulating monocytes in tissue culture are capable of resorbing devitalized adult and fetal bone. An important component of this process is the adhesion of the cells to the mineralized substrate and the localized removal of matrix from beneath the attached cells. The process appears to involve both release of lysosomal enzymes onto the substrate and intracellular accumulation (transport) of resorbed matrix.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kahn, A J -- Stewart, C C -- Teitelbaum, S L -- New York, N.Y. -- Science. 1978 Mar 3;199(4332):988-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/622581" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone Matrix/cytology/metabolism/physiology ; *Bone Resorption ; Bone and Bones/embryology/metabolism ; Calcium Radioisotopes ; Cell Adhesion ; Culture Techniques ; Humans ; Monocytes/cytology/metabolism/*physiology ; Rats
    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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  • 6
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    Radioimmunoassay of the insulin receptor: a new probe of receptor structure and function (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-02-09
    Description: A sensitive and specific radioimmunoassay for the insulin receptor has been developed employing receptor autoantibodies from the serum of a patient with insulin-resistant diabetes. The assay detects insulin binding sites at concentrations as low as 0.1 nanomolar; distinguishes between receptors originating from human placental membranes, human lymphoblastoid cells, and mouse liver membranes; and measures the receptor independently of its binding function. Down-regulation, or loss of binding after exposure to insulin, is associated with loss of immunoreactive receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harrison, L C -- Flier, J -- Itin, A -- Kahn, C R -- Roth, J -- New York, N.Y. -- Science. 1979 Feb 9;203(4380):544-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/83675" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigen-Antibody Reactions ; Binding Sites ; Binding Sites, Antibody ; Epitopes ; Female ; Humans ; Liver/analysis ; Lymphocytes/analysis ; Mice ; Placenta/analysis ; Pregnancy ; Radioimmunoassay/methods ; Receptor, Insulin/analysis/*immunology ; Solubility
    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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  • 7
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    Insulin stimulates the phosphorylation of the 95,000-dalton subunit of its own receptor (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-01-08
    Description: Cultured human lymphocytes and rat hepatoma cells were labeled with [32P]orthophosphate and the insulin receptor subunits identified by immunoprecipitation and sodium dodecyl sulfate-gel electrophoreses. In both cell types the 95,000-dalton (beta) subunit of the insulin receptor was selectively phosphorylated. Phosphorylation was specifically stimulated by insulin in a dose-dependent fashion after 1 and 15 minutes of hormone treatment, whereas human growth hormone was without effect. This phosphorylation may be a very early event in insulin action.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kasuga, M -- Karlsson, F A -- Kahn, C R -- New York, N.Y. -- Science. 1982 Jan 8;215(4529):185-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7031900" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Growth Hormone/pharmacology ; Humans ; Insulin/*pharmacology ; Liver Neoplasms, Experimental/metabolism ; Lymphocytes ; Macromolecular Substances ; Molecular Weight ; Phosphorylation ; Rats ; Receptor, Insulin/*metabolism
    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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  • 8
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    Monocyte chemotaxis: stimulation by specific exosite region in thrombin (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-05-13
    Description: Human alpha-thrombin is a potent chemoattractant for human monocytes, with optimum activity occurring at about 10 nanomoles per liter. A variety of thrombins that were chemically modified to alter procoagulant or esterolytic functions showed a similar optimum activity, but complexes of prothrombin or alpha-thrombin with either antithrombin III or hirudin did not. These findings indicate that the regions in thrombin responsible for monocyte chemotaxis are proximate to those involved in certain protein recognition interactions of alpha-thrombin (for example, hirudin binding) but are distinct from the catalytic site and from certain exosites required for clotting.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bar-Shavit, R -- Kahn, A -- Wilner, G D -- Fenton, J W 2nd -- DE-04629/DE/NIDCR NIH HHS/ -- HL-13160/HL/NHLBI NIH HHS/ -- HL-14147/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1983 May 13;220(4598):728-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6836310" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Chemotaxis, Leukocyte/*drug effects ; Hirudins/pharmacology ; Humans ; Monocytes/*drug effects ; Prothrombin/pharmacology ; Thrombin/*pharmacology
    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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  • 9
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    Human aging: usual and successful (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-07-10
    Description: Research in aging has emphasized average age-related losses and neglected the substantial heterogeneity of older persons. The effects of the aging process itself have been exaggerated, and the modifying effects of diet, exercise, personal habits, and psychosocial factors underestimated. Within the category of normal aging, a distinction can be made between usual aging, in which extrinsic factors heighten the effects of aging alone, and successful aging, in which extrinsic factors play a neutral or positive role. Research on the risks associated with usual aging and strategies to modify them should help elucidate how a transition from usual to successful aging can be facilitated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rowe, J W -- Kahn, R L -- New York, N.Y. -- Science. 1987 Jul 10;237(4811):143-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3299702" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Aged, 80 and over ; *Aging/metabolism/physiology/psychology ; Carbohydrate Metabolism ; Cognition ; Cross-Sectional Studies ; Grief ; Health Promotion ; Health Services for the Aged ; Humans ; Longitudinal Studies ; Osteoporosis/physiopathology ; Patient Acceptance of Health Care ; Reference Values ; Social Support ; Volition
    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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  • 10
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    The Evolution of CO2 on Mars (1985)
    In:  CASI
    Details
    Publication Date: 2014-10-08
    Description: The consequences of the hypothesis that the evolution of CO2 is directly linked to the occurrence of at least transitory pockets of moisture were exposed. The current conditions preclude the existence of open bodies of liquid water and the formation of moisture in disequilibrium is not excluded by any known constraints. The water evaporation rate is inversely proportional to PCO2, and the existence of a limiting value (P*) for which liquid water can form in the Mars environment is postulated. The evolution of PCO2 is controlled largely by relatively rapid aqueous chemistry forming carbon-containing sedimentary rocks, perhaps during early history in open water, but more recently in transitory pockets of moisture in the soil. Once the total atmospheric pressure is reduced to near P*, the occurrence of transitory moisture is inhibited, and atmospheric CO2 is no longer depleted by an efficient mechanism. The role of the carbonate reservoir in the current overall carbon budget on Mars, according to this scheme, is illustrated.
    Keywords: LUNAR AND PLANETARY EXPLORATION
    Type: NASA, Washington Repts. of Planetary Geol. and Geophys. Program; p 232-234
    Format: text
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    NASA TECHNICAL REPORTS
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