ArticleBioscience reports2019
Zinc binding regulates amyloid-like aggregation of GAPR-1.
Article in Bioscience reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 21 citations in OpenAlex.
- Article
- Histopathological characterization of skin and muscle lesions induced by lionfish (The journal of venomous animals and toxins including tropical diseases · 2025Article
- 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
- Cysteine-Rich Secretory Proteins (CRISP) are Key Players in Mammalian Fertilization and Fertility.Frontiers in cell and developmental biology · 2021Review
- Regulation of Functional Protein Aggregation by Multiple Factors: Implications for the Amyloidogenic Behavior of the CAP Superfamily Proteins.International journal of molecular sciences · 2020Review
- Metal ions and redox balance regulate distinct amyloid-like aggregation pathways of GAPR-1.Scientific reports · 2019Article
- Cofactor-mediated amyloidogenesis.Bioscience reports · 2019Article
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Authors and funding
8 authors at 2 institutions in 3 countries.
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 CAP domain that is defined by four sequence motifs and a highly conserved tertiary structure. A common structure-function relationship for this domain is hitherto unknown. A characteristic of several CAP proteins is their formation of amyloid-like structures in the presence of lipids. Here we investigate the structural modulation of Golgi-Associated plant Pathogenesis Related protein 1 (GAPR-1) by known interactors of the CAP domain, preceding amyloid-like aggregation. Using isothermal titration calorimetry (ITC), we demonstrate that GAPR-1 binds zinc ions. Zn
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.