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• W2029105864 endingPage "14736" @default.
• W2029105864 startingPage "14724" @default.
• W2029105864 abstract "There is evidence that alterations in the normal physiological activity of PrPC contribute to prion-induced neurotoxicity. This mechanism has been difficult to investigate, however, because the normal function of PrPC has remained obscure, and there are no assays available to measure it. We recently reported that cells expressing PrP deleted for residues 105–125 exhibit spontaneous ionic currents and hypersensitivity to certain classes of cationic drugs. Here, we utilize cell culture assays based on these two phenomena to test how changes in PrP sequence and/or cellular localization affect the functional activity of the protein. We report that the toxic activity of Δ105–125 PrP requires localization to the plasma membrane and depends on the presence of a polybasic amino acid segment at the N terminus of PrP. Several different deletions spanning the central region as well as three disease-associated point mutations also confer toxic activity on PrP. The sequence domains identified in our study are also critical for PrPSc formation, suggesting that common structural features may govern both the functional activity of PrPC and its conversion to PrPSc. There is evidence that alterations in the normal physiological activity of PrPC contribute to prion-induced neurotoxicity. This mechanism has been difficult to investigate, however, because the normal function of PrPC has remained obscure, and there are no assays available to measure it. We recently reported that cells expressing PrP deleted for residues 105–125 exhibit spontaneous ionic currents and hypersensitivity to certain classes of cationic drugs. Here, we utilize cell culture assays based on these two phenomena to test how changes in PrP sequence and/or cellular localization affect the functional activity of the protein. We report that the toxic activity of Δ105–125 PrP requires localization to the plasma membrane and depends on the presence of a polybasic amino acid segment at the N terminus of PrP. Several different deletions spanning the central region as well as three disease-associated point mutations also confer toxic activity on PrP. The sequence domains identified in our study are also critical for PrPSc formation, suggesting that common structural features may govern both the functional activity of PrPC and its conversion to PrPSc." @default.
• W2029105864 created "2016-06-24" @default.
• W2029105864 creator A5002859044 @default.
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• W2029105864 creator A5090309926 @default.
• W2029105864 date "2011-04-01" @default.
• W2029105864 modified "2023-10-06" @default.
• W2029105864 title "An N-terminal Polybasic Domain and Cell Surface Localization Are Required for Mutant Prion Protein Toxicity" @default.
• W2029105864 cites W1520668014 @default.
• W2029105864 cites W1534728973 @default.
• W2029105864 cites W1591864042 @default.
• W2029105864 cites W1845629226 @default.
• W2029105864 cites W1964241324 @default.
• W2029105864 cites W1966382960 @default.
• W2029105864 cites W1972577522 @default.
• W2029105864 cites W1977972671 @default.
• W2029105864 cites W1978195237 @default.
• W2029105864 cites W1984973536 @default.
• W2029105864 cites W1987268193 @default.
• W2029105864 cites W1990833847 @default.
• W2029105864 cites W1998038512 @default.
• W2029105864 cites W2000966016 @default.
• W2029105864 cites W2004190654 @default.
• W2029105864 cites W2005768267 @default.
• W2029105864 cites W2008004502 @default.
• W2029105864 cites W2016170408 @default.
• W2029105864 cites W2021287373 @default.
• W2029105864 cites W2021664587 @default.
• W2029105864 cites W2021719065 @default.
• W2029105864 cites W2022300284 @default.
• W2029105864 cites W2022392367 @default.
• W2029105864 cites W2024478381 @default.
• W2029105864 cites W2024954984 @default.
• W2029105864 cites W2025546736 @default.
• W2029105864 cites W2030103154 @default.
• W2029105864 cites W2032338659 @default.
• W2029105864 cites W2042978244 @default.
• W2029105864 cites W2044666532 @default.
• W2029105864 cites W2046241482 @default.
• W2029105864 cites W2047690397 @default.
• W2029105864 cites W2052976709 @default.
• W2029105864 cites W2053636966 @default.
• W2029105864 cites W2053782362 @default.
• W2029105864 cites W2058602000 @default.
• W2029105864 cites W2063553621 @default.
• W2029105864 cites W2063880942 @default.
• W2029105864 cites W2065060909 @default.
• W2029105864 cites W2065471991 @default.
• W2029105864 cites W2068309669 @default.
• W2029105864 cites W2070160124 @default.
• W2029105864 cites W2071509261 @default.
• W2029105864 cites W2073308771 @default.
• W2029105864 cites W2073472657 @default.
• W2029105864 cites W2077404304 @default.
• W2029105864 cites W2081333099 @default.
• W2029105864 cites W2082872027 @default.
• W2029105864 cites W2093864265 @default.
• W2029105864 cites W2096966552 @default.
• W2029105864 cites W2099437683 @default.
• W2029105864 cites W2099756588 @default.
• W2029105864 cites W2099970570 @default.
• W2029105864 cites W2102427988 @default.
• W2029105864 cites W2109401365 @default.
• W2029105864 cites W2113792335 @default.
• W2029105864 cites W2116647726 @default.
• W2029105864 cites W2118510702 @default.
• W2029105864 cites W2119616506 @default.
• W2029105864 cites W2128057594 @default.
• W2029105864 cites W2147276565 @default.
• W2029105864 cites W2149247478 @default.
• W2029105864 cites W2150362155 @default.
• W2029105864 cites W2151541409 @default.
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• W2029105864 cites W2171526610 @default.
• W2029105864 cites W2181649940 @default.
• W2029105864 cites W2324660492 @default.
• W2029105864 cites W4250761851 @default.
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• W2029105864 doi "https://doi.org/10.1074/jbc.m110.214973" @default.
• W2029105864 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3077669" @default.
• W2029105864 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21385869" @default.
• W2029105864 hasPublicationYear "2011" @default.
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