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Cited by 251

The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

Aspects on human amyloid forms and their fibril polypeptides

Open access
Westermark, Per·2005·The FEBS Journal

Abstract

Amyloid is an in vivo fibrillar substance containing a fibril protein and several additional molecules. Presently, 25 proteins have been reported as main fibril components. Why just a few proteins form amyloid in vivo is still insufficiently understood. Many fibril proteins appear as fragments of larger precursors and for some types it is not clear whether fragmentation comes before or after fibrillation. The self‐assembly by amyloid proteins can be speeded up by seeding with preformed fibrils. In mice, systemic amyloidoses are transmissible by a seeding mechanism. Whether this prion‐like mechanism occurs in humans is not known, but can definitely not be ruled out.

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Crossref · 10.1111/j.1742-4658.2005.05024.x

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Metadata

Authors
Westermark, P.
Venue
The FEBS Journal
Publisher
Wiley
Published
2005-11-16
Volume
272
Issue
23
Pages
5942-5949
ISSN
  • 1742-464X (ISSN-L)
  • 1742-4658
OpenAlex
W2140559080
Cited by
251
References
4
FWCI
8.64
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Aspects on human amyloid forms and their fibril polypeptides. https://app.cochat.ai/papers/10.1111/j.1742-4658.2005.05024.x
The paper
Westermark, P. (2005). Aspects on human amyloid forms and their fibril polypeptides. The FEBS Journal. https://doi.org/10.1111/j.1742-4658.2005.05024.x

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.