2016
DOI: 10.1002/jmr.2587
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Force spectroscopy reveals the presence of structurally modified dimers in transthyretin amyloid annular oligomers

Abstract: Toxicity in amyloidogenic protein misfolding disorders is thought to involve intermediate states of aggregation associated with the formation of amyloid fibrils. Despite their relevance, the heterogeneity and transience of these oligomers have placed great barriers in our understanding of their structural properties. Among amyloid intermediates, annular oligomers or annular protofibrils have raised considerable interest because they may contribute to a mechanism of cellular toxicity via membrane permeation. He… Show more

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Cited by 7 publications
(10 citation statements)
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“…In addition, FP i of βC and βE segments shifts from ‘C 5 strand’ to ‘C 7eq strand’ propensity. These changes destabilize the outer β sheet of transthyretin βC↓βB↑βE↓βF↑; (b) Putative amyloidogenic monomers of transthyretin generated by step-by-step dismantling and rearrangement of transthyretin β sandwich consistent with the destabilizing FP i shifts and the solid state NMR [ 162 164 ], spin-labelling [ 165 , 166 ], immunoreactivity [ 167 ] and H/D exchange (HXMS) [ 168 , 169 ] studies; (c) The pathway of acid-induced unfolding and aggregation of transthyretin [ 38 ], and the topology of annular octamers [ 170 172 ] and protofibrils [ 169 ].…”
Section: Resultsmentioning
confidence: 71%
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“…In addition, FP i of βC and βE segments shifts from ‘C 5 strand’ to ‘C 7eq strand’ propensity. These changes destabilize the outer β sheet of transthyretin βC↓βB↑βE↓βF↑; (b) Putative amyloidogenic monomers of transthyretin generated by step-by-step dismantling and rearrangement of transthyretin β sandwich consistent with the destabilizing FP i shifts and the solid state NMR [ 162 164 ], spin-labelling [ 165 , 166 ], immunoreactivity [ 167 ] and H/D exchange (HXMS) [ 168 , 169 ] studies; (c) The pathway of acid-induced unfolding and aggregation of transthyretin [ 38 ], and the topology of annular octamers [ 170 172 ] and protofibrils [ 169 ].…”
Section: Resultsmentioning
confidence: 71%
“…Fig 7 ). (D) Acid-induced unfolding and aggregation of transthyretin [ 38 , 162 172 ]: (a) The superposed FP i plots for transthyretin at pH >7 and pH 4, and the DSSP assignments for the native monomer (homotetramer subunit, β sandwich fold). The red and purple outlines mark the strand and turn segments most affected by the reduction of pH: FP i of the V30-F33 segment (βB strand) shifts from ‘C 5 strand’ to ‘helix’ propensity, and the two ‘turn’ segments (D-E≡D* and E-F≡E*) are destabilized.…”
Section: Resultsmentioning
confidence: 99%
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“…A virtual issue appeared in the Journal of Molecular Recognition in 2017 . Nine research articles composed this special issue . At the end of the conference, it was announced that the next one will be organized in Kraków, in 2017.…”
Section: Afmbiomed Conferencesmentioning
confidence: 99%
“…[48][49][50][51][52][53][54][55][56][57] The last change that was made during the 75 Nine research articles composed this special issue. [76][77][78][79][80][81][82][83][84] At the end of the conference, it was announced that the next one will…”
Section: Afmbiomed Conferencesmentioning
confidence: 99%