Biasing the native α-synuclein conformational ensemble towards compact states abolishes aggregation and neurotoxicity

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Biasing the native α-synuclein conformational ensemble towards compact states abolishes aggregation and neurotoxicity is …
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scholarly articleQ13442814

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P356DOI10.1016/J.REDOX.2019.101135
P932PMC publication ID6375061
P698PubMed publication ID30769283

P50authorSalvador VenturaQ41047849
Carlo SantambrogioQ64683010
Tiago Fleming OuteiroQ79139390
P2093author name stringJordi Pujols
Rita Grandori
Anita Carija
Francisca Pinheiro
Susanna Navarro
Diana Fernandes Lázaro
Inês C Brás
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The effects of the novel A53E alpha-synuclein mutation on its oligomerization and aggregation.Q42355152
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Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicityQ46858479
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Compact conformations of α-synuclein induced by alcohols and copperQ57267827
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Modulation of α-synuclein aggregation by dopamine in the presence of MPTP and its metaboliteQ83630151
P4510describes a project that usesImageJQ1659584
P407language of work or nameEnglishQ1860
P921main subjectdisulfide bondQ423252
neurotoxicityQ3338704
toxic encephalopathyQ7830379
SynucleinQ24767155
P304page(s)101135
P577publication date2019-02-05
P1433published inRedox BiologyQ27724751
P859sponsorCollaborative Research Centre (CRC) 1286: "Quantitative Synaptologie"Q87186232
P1476titleBiasing the native α-synuclein conformational ensemble towards compact states abolishes aggregation and neurotoxicity
P478volume22

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cites work (P2860)
Q91762151Inducing α-synuclein compaction: a new strategy for inhibiting α-synuclein aggregation?
Q96303508Tuning Functional Amyloid Formation Through Disulfide Engineering
Q92535141ZPD-2, a Small Compound That Inhibits α-Synuclein Amyloid Aggregation and Its Seeded Polymerization

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