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• W2157339888 endingPage "165" @default.
• W2157339888 startingPage "148" @default.
• W2157339888 abstract "Aggregation of amyloid-β (Aβ) peptide, a 39- to 43-residue fragment of the amyloid precursor protein, is associated with Alzheimer's disease, the most common form of dementia in the elderly population. Several experimental studies have tried to characterize the atomic details of amyloid fibrils, which are the final product of Aβ aggregation. Much less is known about species forming during the early stages of aggregation, in particular about the monomeric state of the Aβ peptide that may be viewed as the product of the very first step in the hypothesized amyloid cascade. Here, the equilibrium ensembles of monomeric Aβ alloforms Aβ(1-40) and Aβ(1-42) are investigated by Monte Carlo simulations using an atomistic force field and implicit solvent model that have been shown previously to correctly reproduce the ensemble properties of other intrinsically disordered polypeptides. Our simulation results indicate that at physiological temperatures, both alloforms of Aβ assume a largely collapsed globular structure. Conformations feature a fluid hydrophobic core formed, on average, by contacts both within and between the two segments comprising residues 12-21 and 24-40/42, respectively. Furthermore, the 11 N-terminal residues are completely unstructured, and all charged side chains, in particular those of Glu22 and Asp23, remain exposed to solvent. Taken together, these observations indicate a micelle-like† architecture at the monomer level whose implications for oligomerization, as well as fibril formation and elongation, are discussed. We establish quantitatively the intrinsic disorder of Aβ and find the propensity to form regular secondary structure to be low but sequence specific. In the presence of a global and unspecific bias for backbone conformations to populate the β-basin, the β-sheet propensity along the sequence is consistent with the arrangement of the monomer within the fibril, as derived from solid-state NMR data. These observations indicate that the primary sequence partially encodes fibril structure, but that fibril elongation must be thought of as a templated assembly step." @default.
• W2157339888 created "2016-06-24" @default.
• W2157339888 creator A5024363437 @default.
• W2157339888 creator A5035048768 @default.
• W2157339888 date "2010-10-01" @default.
• W2157339888 modified "2023-10-16" @default.
• W2157339888 title "Micelle-Like Architecture of the Monomer Ensemble of Alzheimer’s Amyloid-β Peptide in Aqueous Solution and Its Implications for Aβ Aggregation" @default.
• W2157339888 cites W1575285231 @default.
• W2157339888 cites W1595368494 @default.
• W2157339888 cites W1603138791 @default.
• W2157339888 cites W1677883125 @default.
• W2157339888 cites W1964758432 @default.
• W2157339888 cites W1964976698 @default.
• W2157339888 cites W1966195914 @default.
• W2157339888 cites W1970022221 @default.
• W2157339888 cites W1970434234 @default.
• W2157339888 cites W1972535964 @default.
• W2157339888 cites W1973134139 @default.
• W2157339888 cites W1975769486 @default.
• W2157339888 cites W1976210162 @default.
• W2157339888 cites W1978314140 @default.
• W2157339888 cites W1979509752 @default.
• W2157339888 cites W1981458288 @default.
• W2157339888 cites W1981735680 @default.
• W2157339888 cites W1984964811 @default.
• W2157339888 cites W1987686455 @default.
• W2157339888 cites W1992631275 @default.
• W2157339888 cites W1994081387 @default.
• W2157339888 cites W1994459636 @default.
• W2157339888 cites W1995394213 @default.
• W2157339888 cites W1998249326 @default.
• W2157339888 cites W1999650655 @default.
• W2157339888 cites W2006679891 @default.
• W2157339888 cites W2008151389 @default.
• W2157339888 cites W2008708467 @default.
• W2157339888 cites W2011056613 @default.
• W2157339888 cites W2012561243 @default.
• W2157339888 cites W2013145865 @default.
• W2157339888 cites W2015640782 @default.
• W2157339888 cites W2016819659 @default.
• W2157339888 cites W2022793853 @default.
• W2157339888 cites W2022863531 @default.
• W2157339888 cites W2028204954 @default.
• W2157339888 cites W2029667189 @default.
• W2157339888 cites W2031218856 @default.
• W2157339888 cites W2033992991 @default.
• W2157339888 cites W2035963355 @default.
• W2157339888 cites W2037751823 @default.
• W2157339888 cites W2039011144 @default.
• W2157339888 cites W2039667582 @default.
• W2157339888 cites W2042742422 @default.
• W2157339888 cites W2042978261 @default.
• W2157339888 cites W2043308634 @default.
• W2157339888 cites W2044862505 @default.
• W2157339888 cites W2051792081 @default.
• W2157339888 cites W2056544504 @default.
• W2157339888 cites W2063679630 @default.
• W2157339888 cites W2067214887 @default.
• W2157339888 cites W2068515908 @default.
• W2157339888 cites W2069231617 @default.
• W2157339888 cites W2071953900 @default.
• W2157339888 cites W2073394015 @default.
• W2157339888 cites W2073623394 @default.
• W2157339888 cites W2075066347 @default.
• W2157339888 cites W2075068625 @default.
• W2157339888 cites W2075702662 @default.
• W2157339888 cites W2078933468 @default.
• W2157339888 cites W2084187244 @default.
• W2157339888 cites W2087947213 @default.
• W2157339888 cites W2091916149 @default.
• W2157339888 cites W2095215796 @default.
• W2157339888 cites W2096759266 @default.
• W2157339888 cites W2103440561 @default.
• W2157339888 cites W2112154906 @default.
• W2157339888 cites W2114078421 @default.
• W2157339888 cites W2118241214 @default.
• W2157339888 cites W2118280241 @default.
• W2157339888 cites W2122294662 @default.
• W2157339888 cites W2123976234 @default.
• W2157339888 cites W2133833315 @default.
• W2157339888 cites W2136686218 @default.
• W2157339888 cites W2137587206 @default.
• W2157339888 cites W2139561304 @default.
• W2157339888 cites W2162741488 @default.
• W2157339888 cites W2166848357 @default.
• W2157339888 cites W2168025729 @default.
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• W2157339888 doi "https://doi.org/10.1016/j.jmb.2010.08.003" @default.
• W2157339888 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20709081" @default.
• W2157339888 hasPublicationYear "2010" @default.
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