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    A secreted disulfide catalyst controls extracellular matrix composition and function (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-05-25
    Description: Disulfide bond formation in secretory proteins occurs primarily in the endoplasmic reticulum (ER), where multiple enzyme families catalyze cysteine cross-linking. Quiescin sulfhydryl oxidase 1 (QSOX1) is an atypical disulfide catalyst, localized to the Golgi apparatus or secreted from cells. We examined the physiological function for extracellular catalysis of de novo disulfide bond formation by QSOX1. QSOX1 activity was required for incorporation of laminin into the extracellular matrix (ECM) synthesized by fibroblasts, and ECM produced without QSOX1 was defective in supporting cell-matrix adhesion. We developed an inhibitory monoclonal antibody against QSOX1 that could modulate ECM properties and undermine cell migration.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ilani, Tal -- Alon, Assaf -- Grossman, Iris -- Horowitz, Ben -- Kartvelishvily, Elena -- Cohen, Sidney R -- Fass, Deborah -- New York, N.Y. -- Science. 2013 Jul 5;341(6141):74-6. doi: 10.1126/science.1238279. Epub 2013 May 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel. tal.ilani@weizmann.ac.il〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23704371" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal ; Cell Adhesion ; Cell Line, Tumor ; Cell Movement ; Cells, Cultured ; Cysteine/metabolism ; Disulfides/metabolism ; Extracellular Matrix/enzymology/*physiology/ultrastructure ; Fibroblasts/enzymology/ultrastructure ; Humans ; Laminin/metabolism ; Oxidoreductases Acting on Sulfur Group Donors/antagonists & ; inhibitors/*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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  • 2
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    Spinal fluid differences in experimental allergic encephalomyelitis and multiple sclerosis (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-01-20
    Description: The spinal fluid of sheep with experimental allergic encephalomyelitis contains myelin basic protein (6 to 18 nanograms per milliliter) bound to antibody as well as excess free antibody. This bound myelin basic protein appeared concurrently with the onset of the disease and remained elevated until death. In contrast, in active multiple sclerosis, the spinal fluid contains free myelin basic protein and there are no detectable levels of antibody. The results indicate that the antibodies enter the spinal fluid from the serum by passive diffusion. This mechanism may also explain the presence of viral antibodies in the spinal fluid of multiple sclerosis patients.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gutstein, H S -- Cohen, S R -- New York, N.Y. -- Science. 1978 Jan 20;199(4326):301-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/619457" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigen-Antibody Complex ; Autoantibodies/*cerebrospinal fluid ; Encephalomyelitis, Autoimmune, Experimental/*cerebrospinal fluid/immunology ; Humans ; Multiple Sclerosis/*cerebrospinal fluid/immunology ; Myelin Proteins/*cerebrospinal fluid/immunology ; Sheep
    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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