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  • 1
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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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    Biological fabrication of cellulose fibers with tailored properties (2017)
    American Association for the Advancement of Science (AAAS)
    In: Science
    Details
    Publication Date: 2017-09-15
    Description: Cotton is a promising basis for wearable smart textiles. Current approaches that rely on fiber coatings suffer from function loss during wear. We present an approach that allows biological incorporation of exogenous molecules into cotton fibers to tailor the material’s functionality. In vitro model cultures of upland cotton ( Gossypium hirsutum ) are incubated with 6-carboxyfluorescein–glucose and dysprosium–1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid–glucose, where the glucose moiety acts as a carrier capable of traveling from the vascular connection to the outermost cell layer of the ovule epidermis, becoming incorporated into the cellulose fibers. This yields fibers with unnatural properties such as fluorescence or magnetism. Combining biological systems with the appropriate molecular design offers numerous possibilities to grow functional composite materials and implements a material-farming concept.
    Keywords: Materials Science
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Geosciences , 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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    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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  • 4
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    Secondary nucleation and elongation occur at different sites on Alzheimers amyloid-{beta} aggregates (2019)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2019
    Description: 〈p〉The aggregates of the Aβ peptide associated with Alzheimer’s disease are able to both grow in size as well as generate, through secondary nucleation, new small oligomeric species, that are major cytotoxins associated with neuronal death. Despite the importance of these amyloid fibril-dependent processes, their structural and molecular underpinnings have remained challenging to elucidate. Here, we consider two molecular chaperones: the Brichos domain, which suppresses specifically secondary nucleation processes, and clusterin which our results show is capable of inhibiting, specifically, the elongation of Aβ fibrils at remarkably low substoichiometric ratios. Microfluidic diffusional sizing measurements demonstrate that this inhibition originates from interactions of clusterin with fibril ends with high affinity. Kinetic experiments in the presence of both molecular chaperones reveal that their inhibitory effects are additive and noncooperative, thereby indicating that the reactive sites associated with the formation of new aggregates and the growth of existing aggregates are distinct.〈/p〉
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
    Published by American Association for the Advancement of Science (AAAS)
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