Fibril‐Type Textile Electrodes Enabling Extremely High Areal Capacity through Pseudocapacitive Electroplating onto Chalcogenide Nanoparticle‐Encapsulated Fibrils (Adv. Sci. 33/2022)
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Fibril‐Type Textile Electrodes Enabling Extremely High Areal Capacity through Pseudocapacitive Electroplating onto Chalcogenide Nanoparticle‐Encapsulated Fibrils (Adv. Sci. 33/2022) ; volume:9 ; number:33 ; year:2022 ; extent:1
Advanced science ; 9, Heft 33 (2022) (gesamt 1)
- Creator
- DOI
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10.1002/advs.202270209
- URN
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urn:nbn:de:101:1-2022112414340207112265
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:34 AM CEST
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Chang, Woojae
- Nam, Donghyeon
- Lee, Seokmin
- Ko, Younji
- Kwon, Cheong Hoon
- Ko, Yongmin
- Cho, Jinhan
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Fibril‐Type Textile Electrodes Enabling Extremely High Areal Capacity through Pseudocapacitive Electroplating onto Chalcogenide Nanoparticle‐Encapsulated Fibrils
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Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers
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Functionalization of α-synuclein fibrils
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Modelling fibril formation on membrane surfaces
Fibril‐Type Textile Electrodes Enabling Extremely High Areal Capacity through Pseudocapacitive Electroplating onto Chalcogenide Nanoparticle‐Encapsulated Fibrils
Protofibril–Fibril Interactions Inhibit Amyloid Fibril Assembly by Obstructing Secondary Nucleation
Effects of oligomer toxicity, fibril toxicity and fibril spreading in synucleinopathies
Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers
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Roadmap on chalcogenide photonics
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Functionalization of α-synuclein fibrils
Distinct position-specific sequence features of hexa-peptides that form amyloid-fibrils: application to discriminate between amyloid fibril and amorphous β-aggregate forming peptide sequences