ArticleScientific reports2019
Metal ions and redox balance regulate distinct amyloid-like aggregation pathways of GAPR-1.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 16 citations in OpenAlex.
- Amyloid formation and depolymerization of tumor suppressor p16Nature communications · 2024Article
- Immunity functions of Arabidopsis pathogenesis-related 1 are coupled but not confined to its C-terminus processing and trafficking.Molecular plant pathology · 2022Article
- The less conserved metal-binding site in human CRISP1 remains sensitive to zinc ions to permit protein oligomerization.Scientific reports · 2021Article
- Zinc determines dynamical properties and aggregation kinetics of human insulin.Biophysical journal · 2021Article
- The skeletome of the red coral Corallium rubrum indicates an independent evolution of biomineralization process in octocorals.BMC ecology and evolution · 2021Article
- Regulation of Functional Protein Aggregation by Multiple Factors: Implications for the Amyloidogenic Behavior of the CAP Superfamily Proteins.International journal of molecular sciences · 2020Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Members of the CAP superfamily (Cysteine-rich secretory proteins, Antigen 5, and Pathogenesis-Related 1 proteins) are characterized by the presence of a structurally conserved CAP domain. The common structure-function relationship of this domain is still poorly understood. In this study, we unravel specific molecular mechanisms modulating the quaternary structure of the mammalian CAP protein GAPR-1 (Golgi-Associated plant Pathogenesis-Related protein 1). Copper ions are shown to induce a distinct amyloid-like aggregation pathway of GAPR-1 in the presence of heparin. This involves an immediate shift from native multimers to monomers which are prone to form amyloid-like fibrils. The Cu
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