English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Tools annual

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Presents the access of premium content as premium feature

Premium Content

Global: Zendy Plus annual

Global: Zendy Free Plan

Significance GFP and other related fluorescent proteins (FPs) are widely used in biological sciences. We discovered that FPs have an intrinsic high binding propensity for the core of amyloid fibrils. We have demonstrated this using over 10 different amyloid fibrils, characterized the binding interface, probed binding interface via mutagenesis, and performed a number of controls to show that binding is specific to amyloid structures and not to other nonamyloid fibrillar structures or soluble proteins with extended β-structure. This previously unrecognized functionality of FPs has two major implications: 1) It provides a tool to study amyloid structures, and 2) It suggests that caution should be taken when FPs are used as a fusion to visualize the cellular localization of proteins of interest.

Sequence-independent recognition of the amyloid structural motif by GFP protein family