Many untreatable neurodegenerative human disorders, like Parkinson’s, Alzheimer’s, and prion diseases, are associated with the aggregation of misfolded or natively unfolded proteins into amyloid fibrils. Cells have adapted two main sophisticated quality-control measures to protect against these protein aggregation processes: the molecular chaperones against the misfolded protein conformations that trigger the aggregation, and the ubiquitin-proteasome system to degrade those proteins that remain misfolded. Despite these natural defense mechanisms amyloidoses may very soon be the most prevalent and socially disruptive illness in the aging population. Currently available therapies against these diseases can neither arrest nor reverse their progression: only the symptoms can be managed. Most current efforts to develop new therapeutics are based on antibodies or synthetic molecules with sufficiently high affinity to compete against, and to inhibit the aggregation of proteins and/or to potentially dissolve their aggregates, once they are formed.
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I graduated in Chemistry (Hons.) from Banaras Hindu University (BHU), Varanasi, India in 2006. I have completed Master of Science in Bioinformatics from University of Allahabad, Allahabad, India in 2008. After completion of my master's degree I joined University of Bologna, Italy to complete my PhD in Cellular, Molecular and Industrial Biology.
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Taschenbuch. Condition: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -Many untreatable neurodegenerative human disorders, like Parkinson's, Alzheimer's, and prion diseases, are associated with the aggregation of misfolded or natively unfolded proteins into amyloid fibrils. Cells have adapted two main sophisticated quality-control measures to protect against these protein aggregation processes: the molecular chaperones against the misfolded protein conformations that trigger the aggregation, and the ubiquitin-proteasome system to degrade those proteins that remain misfolded. Despite these natural defense mechanisms amyloidoses may very soon be the most prevalent and socially disruptive illness in the aging population. Currently available therapies against these diseases can neither arrest nor reverse their progression: only the symptoms can be managed. Most current efforts to develop new therapeutics are based on antibodies or synthetic molecules with sufficiently high affinity to compete against, and to inhibit the aggregation of proteins and/or to potentially dissolve their aggregates, once they are formed. 124 pp. Englisch. Seller Inventory # 9783659592928
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Condition: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: Kumar DhruvI graduated in Chemistry (Hons.) from Banaras Hindu University (BHU), Varanasi, India in 2006. I have completed Master of Science in Bioinformatics from University of Allahabad, Allahabad, India in 2008. After completion o. Seller Inventory # 5167247
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Taschenbuch. Condition: Neu. This item is printed on demand - Print on Demand Titel. Neuware -Many untreatable neurodegenerative human disorders, like Parkinson's, Alzheimer's, and prion diseases, are associated with the aggregation of misfolded or natively unfolded proteins into amyloid fibrils. Cells have adapted two main sophisticated quality-control measures to protect against these protein aggregation processes: the molecular chaperones against the misfolded protein conformations that trigger the aggregation, and the ubiquitin-proteasome system to degrade those proteins that remain misfolded. Despite these natural defense mechanisms amyloidoses may very soon be the most prevalent and socially disruptive illness in the aging population. Currently available therapies against these diseases can neither arrest nor reverse their progression: only the symptoms can be managed. Most current efforts to develop new therapeutics are based on antibodies or synthetic molecules with sufficiently high affinity to compete against, and to inhibit the aggregation of proteins and/or to potentially dissolve their aggregates, once they are formed.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 124 pp. Englisch. Seller Inventory # 9783659592928
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Taschenbuch. Condition: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - Many untreatable neurodegenerative human disorders, like Parkinson's, Alzheimer's, and prion diseases, are associated with the aggregation of misfolded or natively unfolded proteins into amyloid fibrils. Cells have adapted two main sophisticated quality-control measures to protect against these protein aggregation processes: the molecular chaperones against the misfolded protein conformations that trigger the aggregation, and the ubiquitin-proteasome system to degrade those proteins that remain misfolded. Despite these natural defense mechanisms amyloidoses may very soon be the most prevalent and socially disruptive illness in the aging population. Currently available therapies against these diseases can neither arrest nor reverse their progression: only the symptoms can be managed. Most current efforts to develop new therapeutics are based on antibodies or synthetic molecules with sufficiently high affinity to compete against, and to inhibit the aggregation of proteins and/or to potentially dissolve their aggregates, once they are formed. Seller Inventory # 9783659592928
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Taschenbuch. Condition: Neu. Amyloidogenic Proceses Of Intrinsically Disordered Proteins | Understanding the aggregation process of intrinsically unstructured proteins related to neurodegenerative diseases | Dhruv Kumar (u. a.) | Taschenbuch | 124 S. | Englisch | 2014 | LAP LAMBERT Academic Publishing | EAN 9783659592928 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu. Seller Inventory # 105097420
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