Epigallocatechin gallate (EGCG) reduces the intensity of pancreatic amyloid fibrils in human islet amyloid polypeptide (hIAPP) transgenic mice

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 2045-2322

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: Epigallocatechin gallate (EGCG) reduces the intensity of pancreatic amyloid fibrils in human islet amyloid polypeptide (hIAPP) transgenic mice ; volume:8 ; number:1 ; day:18 ; month:1 ; year:2018 ; pages:1-12 ; date:12.2018
Scientific reports ; 8, Heft 1 (18.1.2018), 1-12, 12.2018

Creator: Franko, Andras

Contributor: Rodriguez Camargo, Diana C.
Böddrich, Annett
Garg, Divita
Rodriguez Camargo, Andres
Rathkolb, Birgit
Janik, Dirk
Aichler, Michaela
Feuchtinger, Annette
Neff, Frauke
Fuchs, Helmut
Wanker, Erich
Reif, Bernd
Häring, Hans-Ulrich
Peter, Andreas
Hrabé de Angelis, Martin
SpringerLink (Online service)

DOI: 10.1038/s41598-017-18807-8

URN: urn:nbn:de:1111-2018041217637

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 10:51 AM CEST

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Associated

Franko, Andras
Rodriguez Camargo, Diana C.
Böddrich, Annett
Garg, Divita
Rodriguez Camargo, Andres
Rathkolb, Birgit
Janik, Dirk
Aichler, Michaela
Feuchtinger, Annette
Neff, Frauke
Fuchs, Helmut
Wanker, Erich
Reif, Bernd
Häring, Hans-Ulrich
Peter, Andreas
Hrabé de Angelis, Martin
SpringerLink (Online service)

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Epigallocatechin gallate (EGCG) reduces the intensity of pancreatic amyloid fibrils in human islet amyloid polypeptide (hIAPP) transgenic mice

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Other Objects (12)

The role of SORLA in islet amyloid polypeptide transport and islet amyloid deposition

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Amyloid-like fibrils labeled with magnetic nanoparticles

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Formation of soluble amyloid oligomers and amyloid fibrils by the multifunctional protein vitronectin

Explanation for the mechanical strength of amyloid fibrils

Plant Protein Amyloid Fibrils for Multifunctional Sustainable Materials

Cryo-EM observation of the amyloid key structure of polymorphic TDP-43 amyloid fibrils

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Amyloid-beta antibody binding to cerebral amyloid angiopathy fibrils and risk for amyloid-related imaging abnormalities

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Explanation for the mechanical strength of amyloid fibrils

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Estimating the division of amyloid fibrils

Structural polymorphism of pathological AA amyloid fibrils

Amyloid-like fibrils labeled with magnetic nanoparticles

Amyloid-beta antibody binding to cerebral amyloid angiopathy fibrils and risk for amyloid-related imaging abnormalities

Formation of soluble amyloid oligomers and amyloid fibrils by the multifunctional protein vitronectin

Explanation for the mechanical strength of amyloid fibrils

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