ArticleFEBS letters2014
Hot spots in apolipoprotein A-II misfolding and amyloidosis in mice and men.
Article in FEBS letters, 2014. 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Recent Advances in Non-Invasive Blood Markers for Intraductal Papillary Mucinous Neoplasm Grading.Oncology research · 2026Review
- Apolipoprotein A-II, a Player in Multiple Processes and Diseases.Biomedicines · 2022Review
- Dynamic protein structures in normal function and pathologic misfolding in systemic amyloidosis.Biophysical chemistry · 2022Review
- Knockout of receptor for advanced glycation end-products attenuates age-related renal lesions.Aging cell · 2019Article
- Characterization of ApoJ-reconstituted high-density lipoprotein (rHDL) nanodisc for the potential treatment of cerebral β-amyloidosis.Scientific reports · 2017Article
- Hereditary Renal Amyloidosis Associated With a Novel Apolipoprotein A-II Variant.Kidney international reports · 2017Article
- Triglyceride increase in the core of high-density lipoproteins augments apolipoprotein dissociation from the surface: Potential implications for treatment of apolipoprotein deposition diseases.Biochimica et biophysica acta. Molecular basis of disease · 2017Article
- Amyloid-Forming Properties of Human Apolipoproteins: Sequence Analyses and Structural Insights.Advances in experimental medicine and biology · 2015Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
ApoA-II is the second-major protein of high-density lipoproteins. C-terminal extension in human apoA-II or point substitutions in murine apoA-II cause amyloidosis. The molecular mechanism of apolipoprotein misfolding, from the native predominantly α-helical conformation to cross-β-sheet in amyloid, is unknown. We used 12 sequence-based prediction algorithms to identify two ten-residue segments in apoA-II that probably initiate β-aggregation. Previous studies of apoA-II fragments experimentally verify this prediction. Together, experimental and bioinformatics studies explain why the C-terminal extension in human apoA-II causes amyloidosis and why, unlike murine apoA-II, human apoA-II normally does not cause amyloidosis despite its unusually high sequence propensity for β-aggregation.
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Registered trials
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