ArticleThe Journal of biological chemistry2020
A transient amphipathic helix in the prodomain of PCSK9 facilitates binding to low-density lipoprotein particles.
Article in The Journal of biological chemistry, 2020. 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, 25 citations in OpenAlex.
- Role of Hyperlipidemia-RelatedMolecular syndromology · 2026Article
- The CspC:CspA heterodimer transduces germinant and co-germinant signals during Clostridioides difficile spore germination.PLoS biology · 2026Article
- First LDLRAP1 and Recurrent LDLR Mutations in Tunisian Families With Familial Hypercholesterolemia.Journal of cellular and molecular medicine · 2026Article
- Article
- PCSK9 genetic variants and risk of vascular and non-vascular diseases in Chinese and UK populations.European journal of preventive cardiology · 2024Article
- A proteomic approach for investigating the pleiotropic effects of statins in the atherosclerosis risk in communities (ARIC) study.Journal of proteomics · 2023Article
- Editorial: Women in lipid and fatty acid research: 2022.Frontiers in physiology · 2023Article
- Pathogenic gain-of-function mutations in the prodomain and C-terminal domain of PCSK9 inhibit LDL binding.Frontiers in physiology · 2022Article
- PCSK9 Activity Is Potentiated Through HDL Binding.Circulation research · 2021Article
- In Silico Insights into Protein-protein Interaction Disruptive Mutations in the PCSK9-LDLR complex.International journal of molecular sciences · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Proprotein convertase subtilisin/kexin type-9 (PCSK9) is a ligand of low-density lipoprotein (LDL) receptor (LDLR) that promotes LDLR degradation in late endosomes/lysosomes. In human plasma, 30-40% of PCSK9 is bound to LDL particles; however, the physiological significance of this interaction remains unknown. LDL binding
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.