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- W1571410949 abstract "Protein misfolding has long been recognized as a primary cause of systemic amyloidosis and, increasingly, template-mediated misfolding of native host proteins is now also considered to be central pathogenetic events in some neurodegenerative diseases. Alzheimer's disease, naturally occurring transmissible spongiform encephalopathies (TSEs) and experimental disorders caused by misfolded prion protein (PrP) generated in vitro all share an imbalance of protein synthesis, aggregation and clearance that leads to protein aggregation, prompting some to suggest that Alzheimer's disease is caused by a prion-like mechanism. In TSEs, the host-coded, glycosyl-phosphoinositol (GPI) membrane-anchored prion protein (PrPc) is misfolded into disease-associated, putatively infectious aggregates known as prions. In Alzheimer's disease the membrane-spanning Alzheimer's precursor protein (APP) is progressively cleaved within the plasmalemma to form Aβ peptide fragments that can form pathogenic extracellular aggregates while microtubule-associated tau proteins may also aggregate within neurones. Oligomeric Aβ peptides and full-length misfolded PrP show a common potential to convert native protein and aggregate on plasma membranes before subsequent release to form amyloid fibrils in the extracellular space. However, the nature, membrane topography and processing of the precursor and propagated proteins in prion and Alzheimer's disease all differ, and each group of diseases has distinctive spectra of additional pathological changes and clinical signs suggesting that fundamentally different disease mechanisms are involved." @default.
- W1571410949 created "2016-06-24" @default.
- W1571410949 creator A5023524926 @default.
- W1571410949 date "2013-03-11" @default.
- W1571410949 modified "2023-10-03" @default.
- W1571410949 title "Review: Membrane-associated misfolded protein propagation in natural transmissible spongiform encephalopathies (TSEs), synthetic prion diseases and Alzheimer's disease" @default.
- W1571410949 cites W1493986974 @default.
- W1571410949 cites W1570261319 @default.
- W1571410949 cites W1584834830 @default.
- W1571410949 cites W1601041713 @default.
- W1571410949 cites W1601881612 @default.
- W1571410949 cites W1602910611 @default.
- W1571410949 cites W1963997990 @default.
- W1571410949 cites W1965674141 @default.
- W1571410949 cites W1966745534 @default.
- W1571410949 cites W1967464880 @default.
- W1571410949 cites W1972242036 @default.
- W1571410949 cites W1979044678 @default.
- W1571410949 cites W1979421187 @default.
- W1571410949 cites W1979816273 @default.
- W1571410949 cites W1980156175 @default.
- W1571410949 cites W1980750700 @default.
- W1571410949 cites W1982148242 @default.
- W1571410949 cites W1983292653 @default.
- W1571410949 cites W1992084965 @default.
- W1571410949 cites W1992675300 @default.
- W1571410949 cites W1994142447 @default.
- W1571410949 cites W1994183414 @default.
- W1571410949 cites W1995227965 @default.
- W1571410949 cites W1997907787 @default.
- W1571410949 cites W1998949210 @default.
- W1571410949 cites W2002320632 @default.
- W1571410949 cites W2003424080 @default.
- W1571410949 cites W2004185979 @default.
- W1571410949 cites W2008098790 @default.
- W1571410949 cites W2009207248 @default.
- W1571410949 cites W2013158957 @default.
- W1571410949 cites W2015075898 @default.
- W1571410949 cites W2015329538 @default.
- W1571410949 cites W2017199541 @default.
- W1571410949 cites W2021034011 @default.
- W1571410949 cites W2022388059 @default.
- W1571410949 cites W2023529808 @default.
- W1571410949 cites W2027937601 @default.
- W1571410949 cites W2034504118 @default.
- W1571410949 cites W2037927479 @default.
- W1571410949 cites W2046388027 @default.
- W1571410949 cites W2048881833 @default.
- W1571410949 cites W2053399545 @default.
- W1571410949 cites W2055346376 @default.
- W1571410949 cites W2060941647 @default.
- W1571410949 cites W2062840301 @default.
- W1571410949 cites W2065995979 @default.
- W1571410949 cites W2067540111 @default.
- W1571410949 cites W2068003070 @default.
- W1571410949 cites W2074199271 @default.
- W1571410949 cites W2077009055 @default.
- W1571410949 cites W2079843273 @default.
- W1571410949 cites W2081598046 @default.
- W1571410949 cites W2081660290 @default.
- W1571410949 cites W2083120573 @default.
- W1571410949 cites W2096206310 @default.
- W1571410949 cites W2096410114 @default.
- W1571410949 cites W2098022922 @default.
- W1571410949 cites W2099093150 @default.
- W1571410949 cites W2099340107 @default.
- W1571410949 cites W2100842400 @default.
- W1571410949 cites W2101534570 @default.
- W1571410949 cites W2110458251 @default.
- W1571410949 cites W2124577407 @default.
- W1571410949 cites W2125507585 @default.
- W1571410949 cites W2125522501 @default.
- W1571410949 cites W2129951633 @default.
- W1571410949 cites W2130157010 @default.
- W1571410949 cites W2130240156 @default.
- W1571410949 cites W2133007412 @default.
- W1571410949 cites W2134693070 @default.
- W1571410949 cites W2137802088 @default.
- W1571410949 cites W2138390885 @default.
- W1571410949 cites W2143238511 @default.
- W1571410949 cites W2146246590 @default.
- W1571410949 cites W2146597523 @default.
- W1571410949 cites W2147406941 @default.
- W1571410949 cites W2147589584 @default.
- W1571410949 cites W2149005426 @default.
- W1571410949 cites W2152719134 @default.
- W1571410949 cites W2158707059 @default.
- W1571410949 cites W2165147575 @default.
- W1571410949 cites W2165152085 @default.
- W1571410949 cites W2166409332 @default.
- W1571410949 cites W2167115031 @default.
- W1571410949 cites W2167884034 @default.
- W1571410949 cites W2169849112 @default.
- W1571410949 cites W2171495114 @default.
- W1571410949 cites W2325854321 @default.
- W1571410949 doi "https://doi.org/10.1111/nan.12004" @default.
- W1571410949 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23171056" @default.
- W1571410949 hasPublicationYear "2013" @default.