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  • 1
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    Increased vascularization in mice overexpressing angiopoietin-1 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-17
    Description: The angiopoietins and members of the vascular endothelial growth factor (VEGF) family are the only growth factors thought to be largely specific for vascular endothelial cells. Targeted gene inactivation studies in mice have shown that VEGF is necessary for the early stages of vascular development and that angiopoietin-1 is required for the later stages of vascular remodeling. Here it is shown that transgenic overexpression of angiopoietin-1 in the skin of mice produces larger, more numerous, and more highly branched vessels. These results raise the possibility that angiopoietins can be used, alone or in combination with VEGF, to promote therapeutic angiogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Suri, C -- McClain, J -- Thurston, G -- McDonald, D M -- Zhou, H -- Oldmixon, E H -- Sato, T N -- Yancopoulos, G D -- HL-24136/HL/NHLBI NIH HHS/ -- HL-59157/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 16;282(5388):468-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals, 777 Old Saw Mill River Road, Tarrytown, NY 10591, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9774272" target="_blank"〉PubMed〈/a〉
    Keywords: Angiopoietin-1 ; Animals ; Capillaries/anatomy & histology/ultrastructure ; Endothelial Growth Factors/genetics/physiology ; Endothelium, Vascular/ultrastructure ; Gene Expression ; Keratinocytes/metabolism ; Lymphokines/genetics/physiology ; Membrane Glycoproteins/genetics/*physiology ; Mice ; Mice, Transgenic ; *Neovascularization, Physiologic ; Skin/*blood supply/metabolism ; Transgenes ; Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factors ; Venules/anatomy & histology/ultrastructure
    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
    Electronic Resource
    Electronic Resource
    Two proposed general configurations for bacterial cell wall peptidoglycans shown by space-filling molecular models (1974)
    New York : Wiley-Blackwell
    Biopolymers 13 (1974), S. 2037-2060 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Bacterial cell wall peptidoglycans are built from unbranched β-(1 → 4)-linked glycan chains composed of alternately repeating units of N-acetylglucosamine and N-acetylmuramic acid residues, with peptide side chains attached to the muramic acid residues. The glycan chains are interconnected by peptide bonds formed between the peptide side chains. Through the use of three-dimensional molecular models, two configurations of the glycan strands and the peptide side chains are described, which by their constancy of form reflect the fundamental constancies of the covalent structures. Each of these two models will accommodate any chemical modification that has been observed in bacteria without change in the configuration of the peptide backbone. Some alterations in the chemical structure, which have been sought in bacteria, but not found, would not be tolerated by the models. In these models, glycan strands are parallel, with their lengths and widths predominantly in the plane of the cell wall. The cross-bridging portions of the peptide side chains are at right angles to the glycan strand, in a separate, parallel plane. A compact model is presented in which the peptide side chain is closely appressed to the glycan strand and is stabilized by three hydrogen bonds per disaccharide-peptide subunit. In a second model, the peptide side chain is raised away from the glycan strand in an entirely extended configuration. The compact and extended forms are interconvertible. The thickness of a sheet of peptidoglycan would be from 10.6 to 11.1 Å for the compact model, and 19.1 Å for the extended model.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1974.360131008
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