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  • 04. Solid Earth::04.08. Volcanology::04.08.07. Instruments and techniques
  • Chromatography
  • Environmental sensing
  • American Association for the Advancement of Science (AAAS)  (3)
  • American Chemical Society
  • American Institute of Physics (AIP)
  • Molecular Diversity Preservation International
  • 1985-1989  (2)
  • 1980-1984  (1)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (3)
  • American Chemical Society
  • American Institute of Physics (AIP)
  • Molecular Diversity Preservation International
  • Springer  (17)
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Years
Year
  • 1
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    Production of mammastatin, a tissue-specific growth inhibitor, by normal human mammary cells (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-06-30
    Description: The growth of human mammary cells may be regulated by a balance between growth stimulatory and growth inhibitory pathways. Polypeptides of 47 and 65 kilodaltons (mammastatin) were isolated from conditioned medium of normal human mammary cells. Monoclonal antibodies against mammastatin were generated that blocked its activity and were used for purification and further characterization of the protein. Mammastatin inhibited the growth of 5 transformed human mammary cell lines, but had no effect on the growth of 11 transformed human cell lines derived from nonmammary tissues. Mammastatin appeared to be a heat-labile protein distinct from transforming growth factor-beta (TGF-beta). By immunoperoxidase staining it was detected in cultured normal human mammary cells, but was decreased in transformed mammary cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ervin, P R Jr -- Kaminski, M S -- Cody, R L -- Wicha, M S -- New York, N.Y. -- Science. 1989 Jun 30;244(4912):1585-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, University of Michigan Cancer Center, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2662405" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal ; Breast/analysis/cytology/*metabolism ; Breast Neoplasms/metabolism/pathology ; Cell Division ; Cell Line, Transformed ; Chromatography ; Chromatography, Gel ; Electrophoresis, Polyacrylamide Gel ; Epithelium/metabolism ; Female ; Growth Inhibitors/*biosynthesis/isolation & purification/pharmacology ; Hot Temperature ; Humans ; Immunoassay ; Immunoenzyme Techniques ; Molecular Weight ; *Peptide Biosynthesis ; Peptides/isolation & purification/pharmacology ; Trypsin/pharmacology ; Tumor Cells, Cultured
    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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  • 2
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    Role of phosphatidylinositol kinase in PDGF receptor signal transduction (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-03-03
    Description: The molecules with which the platelet-derived growth factor (PDGF) receptor interacts to elicit the biochemical reactions responsible for cell proliferation have not been identified. Antisera directed against specific PDGF receptor peptides coprecipitated a phosphatidylinositol (PI) kinase and the PDGF receptor. Immunoprecipitates from PDGF-stimulated cells contained 10 to 50 times as much PI kinase as those from unstimulated cells. Mutation of the PDGF receptor by deletion of its kinase insert region resulted in a receptor markedly less effective than the wild type in eliciting cell proliferation and defective in PDGF-stimulated PI kinase, but still capable of PDGF-induced receptor autophosphorylation and phosphoinositide hydrolysis. These data show that the PDGF receptor is physically associated with a PDGF-sensitive PI kinase that is distinct from tyrosine kinase and is not required for PDGF-induced PI hydrolysis. The finding that the mutant PDGF receptor missing the kinase insert domain elicited known early biochemical responses to PDGF, but did not associate with or regulate PI kinase, suggests a novel role for the receptor-associated PI kinase in the transmission of mitogenic signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coughlin, S R -- Escobedo, J A -- Williams, L T -- HL 32898/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1989 Mar 3;243(4895):1191-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2466336" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Phosphatidylinositol 4-Kinase ; Animals ; Cell Line ; Chromatography ; Cricetinae ; Immunoassay ; Immunosorbent Techniques ; Mice ; Mice, Inbred BALB C ; Mutation ; Phosphatidylinositols/metabolism ; Phosphorylation ; Phosphotransferases/*metabolism ; Phosphotyrosine ; Platelet-Derived Growth Factor/pharmacology ; Protein-Tyrosine Kinases/metabolism ; Receptors, Cell Surface/genetics/*metabolism ; Receptors, Platelet-Derived Growth Factor ; *Signal Transduction ; Tyrosine/analogs & derivatives/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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  • 3
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    Contemporary methodology for protein structure determination (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-10-19
    Description: The techniques used for the characterization of protein and peptide structure have undergone great changes that have improved the speed, reliability, and applicability of the process. High-performance liquid chromatography and gel electrophoresis have made the purification of proteins and peptides a routine procedure, even when the compound of interest is a minor component of a complex biological mixture. The chemistry and instrumentation used in amino acid analysis and amino acid sequencing now permit the analysis of as little as 5 to 50 picomoles of samples. This represents an increase in sensitivity of more than a thousandfold over the last 10 years and has made possible the structural analysis of a wide variety of scarce but important compounds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hunkapiller, M W -- Strickler, J E -- Wilson, K J -- New York, N.Y. -- Science. 1984 Oct 19;226(4672):304-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6385254" target="_blank"〉PubMed〈/a〉
    Keywords: *Amino Acid Sequence ; Amino Acids/analysis ; Chemical Fractionation ; Chemistry Techniques, Analytical/*methods ; Chromatography ; Chromatography, High Pressure Liquid ; Chromatography, Ion Exchange ; Electrophoresis, Polyacrylamide Gel ; Isoelectric Focusing ; Peptide Hydrolases ; Peptides/analysis ; Proteins/*analysis/isolation & purification
    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)
    Location Call Number Expected Availability
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    PAPER CURRENT
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