ArticleBiochemistry2014
Amyloid triangles, squares, and loops of apolipoprotein C-III.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Tryptophan Probes of TDP-43 C-Terminal Domain Amyloid Formation.The journal of physical chemistry. B · 2021Article
- A dual apolipoprotein C-II mimetic-apolipoprotein C-III antagonist peptide lowers plasma triglycerides.Science translational medicine · 2020Article
- Bax expression is optimal at low oxygen tension and constant agitation.Protein expression and purification · 2020Article
- Hidden Aggregation Hot-Spots on Human Apolipoprotein E: A Structural Study.International journal of molecular sciences · 2019Article
- Raman fingerprints of amyloid structures.Chemical communications (Cambridge, England) · 2018Article
- Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.Chemical Society reviews · 2017Review
- Article
- D25V apolipoprotein C-III variant causes dominant hereditary systemic amyloidosis and confers cardiovascular protective lipoprotein profile.Nature communications · 2016Article
- Tryptophan probes reveal residue-specific phospholipid interactions of apolipoprotein C-III.Biochimica et biophysica acta · 2015Article
- Amyloid-Forming Properties of Human Apolipoproteins: Sequence Analyses and Structural Insights.Advances in experimental medicine and biology · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
While a significant component of atherosclerotic plaques has been characterized as amyloid, the specific proteins remain to be fully identified. Probable amyloidogenic proteins are apolipoproteins (Apos), which are vital for the formation and function of lipoproteins. ApoCIII is an abundant protein implicated in atherosclerosis, and we show it forms a ribbonlike looped amyloid, strikingly similar to that previously reported for ApoAI and ApoCII. Triangles and squares with a width of ~50 nm were also observed, which may be a novel form of amyloid or related to previously reported amyloid rings.
Indexed as
Identifiers
What OpenQuestion holds
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.