ArticleProtein science : a publication of the Protein Society2013
Structure of an early native-like intermediate of β2-microglobulin amyloidogenesis.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Targeted Protein Modification with an Antibody-Based System.ACS central science · 2025Article
- Affibodies as valuable tool to prevent βBiology direct · 2025Article
- Structure of Nanobody Nb23.Molecules (Basel, Switzerland) · 2021Article
- Exploring cellular biochemistry with nanobodies.The Journal of biological chemistry · 2020Review
- A specific nanobody prevents amyloidogenesis of D76N βScientific reports · 2017Article
- Systemic amyloidosis: lessons from β2-microglobulin.The Journal of biological chemistry · 2015Review
- Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.Journal of the American Chemical Society · 2014Article
- A general protocol for the generation of Nanobodies for structural biology.Nature protocols · 2014Article
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Authors and funding
7 authors.
Funding
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Abstract
To investigate early intermediates of β2-microglobulin (β2m) amyloidogenesis, we solved the structure of β2m containing the amyloidogenic Pro32Gly mutation by X-ray crystallography. One nanobody (Nb24) that efficiently blocks fibril elongation was used as a chaperone to co-crystallize the Pro32Gly β2m monomer under physiological conditions. The complex of P32G β2m with Nb24 reveals a trans peptide bond at position 32 of this amyloidogenic variant, whereas Pro32 adopts the cis conformation in the wild-type monomer, indicating that the cis to trans isomerization at Pro32 plays a critical role in the early onset of β2m amyloid formation.
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