Conformational Change of Amyloid-β 40 in Association with Binding to GM1-Glycan Cluster

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 2045-2322

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: Conformational Change of Amyloid-β 40 in Association with Binding to GM1-Glycan Cluster ; volume:9 ; number:1 ; day:2 ; month:5 ; year:2019 ; pages:1-11 ; date:12.2019
Scientific reports ; 9, Heft 1 (2.5.2019), 1-11, 12.2019

Creator: Tachi, Yuhei
Okamoto, Yuko
Okumura, Hisashi

Contributor: SpringerLink (Online service)

DOI: 10.1038/s41598-019-43117-6

URN: urn:nbn:de:101:1-2019052000092501538533

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

Last update: 14.08.2025, 11:01 AM CEST

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Tachi, Yuhei
Okamoto, Yuko
Okumura, Hisashi
SpringerLink (Online service)

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Evidence of amyloid-β cerebral amyloid angiopathy transmission through neurosurgery

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Conformational Analysis and Application in Diagnostic of Glycosylphosphatidylinositol Glycan Derivatives

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Selective amyloid-β lowering agents

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Conformational Heterogeneity of the HIV Envelope Glycan Shield

Evidence of amyloid-β cerebral amyloid angiopathy transmission through neurosurgery

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Conformational Change of Amyloid-β 40 in Association with Binding to GM1-Glycan Cluster

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Other Objects (12)

Origins of amyloid-β

Selective amyloid-β lowering agents

Development of conformation specific Amyloid-β [Amyloid-beta] antibodies

Conformational Heterogeneity of the HIV Envelope Glycan Shield

Evidence of amyloid-β cerebral amyloid angiopathy transmission through neurosurgery

The modulating effect of soluble amyloid-β dimers on amyloid-β aggregation in vivo and in vitro

Copper mediated amyloid-β binding to Transthyretin

Corynoxine isomers decrease levels of amyloid-β peptide and amyloid-β precursor protein by promoting autophagy and lysosome biogenesis

Amyloid-β 1–24 C-terminal truncated fragment promotes amyloid-β 1–42 aggregate formation in the healthy brain

Conformational alteration in glycan induces phospholipase Cβ1 activation and angiogenesis

Conformational Analysis and Application in Diagnostic of Glycosylphosphatidylinositol Glycan Derivatives

Rationally Designed Peptoid Inhibitors of Amyloid‐β Oligomerization

Origins of amyloid-β

Selective amyloid-β lowering agents

Development of conformation specific Amyloid-β [Amyloid-beta] antibodies

Conformational Heterogeneity of the HIV Envelope Glycan Shield

Evidence of amyloid-β cerebral amyloid angiopathy transmission through neurosurgery

The modulating effect of soluble amyloid-β dimers on amyloid-β aggregation in vivo and in vitro

Copper mediated amyloid-β binding to Transthyretin

Corynoxine isomers decrease levels of amyloid-β peptide and amyloid-β precursor protein by promoting autophagy and lysosome biogenesis

Amyloid-β 1–24 C-terminal truncated fragment promotes amyloid-β 1–42 aggregate formation in the healthy brain

Conformational alteration in glycan induces phospholipase Cβ1 activation and angiogenesis

Conformational Analysis and Application in Diagnostic of Glycosylphosphatidylinositol Glycan Derivatives

Rationally Designed Peptoid Inhibitors of Amyloid‐β Oligomerization

Origins of amyloid-β

Selective amyloid-β lowering agents

Development of conformation specific Amyloid-β [Amyloid-beta] antibodies

Conformational Heterogeneity of the HIV Envelope Glycan Shield

Evidence of amyloid-β cerebral amyloid angiopathy transmission through neurosurgery

The modulating effect of soluble amyloid-β dimers on amyloid-β aggregation in vivo and in vitro

Copper mediated amyloid-β binding to Transthyretin

Corynoxine isomers decrease levels of amyloid-β peptide and amyloid-β precursor protein by promoting autophagy and lysosome biogenesis

Amyloid-β 1–24 C-terminal truncated fragment promotes amyloid-β 1–42 aggregate formation in the healthy brain

Conformational alteration in glycan induces phospholipase Cβ1 activation and angiogenesis

Conformational Analysis and Application in Diagnostic of Glycosylphosphatidylinositol Glycan Derivatives

Rationally Designed Peptoid Inhibitors of Amyloid‐β Oligomerization

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