Transthyretin Aggregation Pathway toward the Formation of Distinct Cytotoxic Oligomers

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 2045-2322

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: Transthyretin Aggregation Pathway toward the Formation of Distinct Cytotoxic Oligomers ; volume:9 ; number:1 ; day:10 ; month:1 ; year:2019 ; pages:1-10 ; date:12.2019
Scientific reports ; 9, Heft 1 (10.1.2019), 1-10, 12.2019

Creator: Dasari, Anvesh K. R.
Hughes, Robert M.
Wi, Sungsool
Hung, Ivan
Gan, Zhehong
Kelly, Jeffrey W.
Lim, Kwang Hun

Contributor: SpringerLink (Online service)

DOI: 10.1038/s41598-018-37230-1

URN: urn:nbn:de:101:1-2019020921144704192756

Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 10:45 AM CEST

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Dasari, Anvesh K. R.
Hughes, Robert M.
Wi, Sungsool
Hung, Ivan
Gan, Zhehong
Kelly, Jeffrey W.
Lim, Kwang Hun
SpringerLink (Online service)

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Transthyretin Aggregation Pathway toward the Formation of Distinct Cytotoxic Oligomers

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Other Objects (12)

Molecular properties and diagnostic potential of monoclonal antibodies targeting cytotoxic α-synuclein oligomers

Antibacterial isoamphipathic oligomers highlight the importance of multimeric lipid aggregation for antibacterial potency

Critical aggregation concentration for the formation of early Amyloid-β (1–42) oligomers

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Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases

Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes

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Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes

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Critical aggregation concentration for the formation of early Amyloid-β (1–42) oligomers

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Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases

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