ArticleJournal of lipid research2013
Thermodynamic and structural destabilization of apoE3 by hereditary mutations associated with the development of lipoprotein glomerulopathy.
Article in Journal of lipid research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 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
19 citing papers in PubMed, 38 citations in OpenAlex.
- Lipoprotein glomerulopathy with a novel apolipoprotein E variant, APOE Kanto (Asp 151dup).CEN case reports · 2025Article
- A case report of youth-onset lipoprotein glomerulopathy with APOE Chicago mutation.BMC nephrology · 2024Article
- Isoform-specific modification of apolipoprotein E by 4-hydroxynonenal: protective role of apolipoprotein E3 against oxidative species.The FEBS journal · 2023Article
- Lipoprotein Glomerulopathy, First Case Report from Canada.International journal of nephrology and renovascular disease · 2022Article
- An Updated Review and Meta Analysis of Lipoprotein Glomerulopathy.Frontiers in medicine · 2022Review
- Lipoprotein glomerulopathy associated with the Osaka/Kurashiki APOE variant: two cases identified in Latin America.Diagnostic pathology · 2021Article
- Lipoprotein glomerulopathy induced by ApoE Kyoto mutation in ApoE-deficient mice.Journal of translational medicine · 2021Article
- Clinical and genetic analysis of lipoprotein glomerulopathy patients caused by APOE mutations.Molecular genetics & genomic medicine · 2020Article
- Thermodynamic destabilization and aggregation propensity as the mechanism behind the association of apoE3 mutants and lipoprotein glomerulopathy.Journal of lipid research · 2018Article
- The Novel Apolipoprotein E Mutation ApoE Chengdu (c.518T＞C, p.L173P) in a Chinese Patient with Lipoprotein Glomerulopathy.Journal of atherosclerosis and thrombosis · 2018Article
- Complement Factor H and Apolipoprotein E Participate in Regulation of Inflammation in THP-1 Macrophages.Frontiers in immunology · 2018Article
- The ability of apolipoprotein E fragments to promote intraneuronal accumulation of amyloid beta peptide 42 is both isoform and size-specific.Scientific reports · 2016Article
- Fluorescence study of domain structure and lipid interaction of human apolipoproteins E3 and E4.Biochimica et biophysica acta · 2014Article
- Molecular basis for increased risk for late-onset Alzheimer disease due to the naturally occurring L28P mutation in apolipoprotein E4.The Journal of biological chemistry · 2014Article
- A possible structural basis behind the pathogenic role of apolipoprotein E hereditary mutations associated with lipoprotein glomerulopathy.Clinical and experimental nephrology · 2014Review
- Topics in lipoprotein glomerulopathy: an overview.Clinical and experimental nephrology · 2014Review
- Pathogenesis, histopathologic findings and treatment modalities of lipoprotein glomerulopathy: A review.Jornal brasileiro de nefrologiaReview
- Membranous Nephropathy-Like Apolipoprotein E Deposition Disease with Apolipoprotein E Toyonaka (Ser197Cys) and a Homozygous Apolipoprotein E2/2.Case reports in nephrology and dialysisArticle
- A Case of Lipoprotein Glomerulopathy with apoE Chicago and apoE (Glu3Lys) Treated with Fenofibrate.Case reports in nephrology and dialysisArticle
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipoprotein glomerulopathy (LPG) is a dominant inherited kidney disorder characterized by lipoprotein thrombi in glomerular capillaries. Single-amino-acid mutations in apoE have been associated with the development of the disease, although the mechanism is unknown. In an effort to gain mechanistic insight linking the presence of such mutations and the development of LPG, we evaluated the effects of three of the most common apoE3 variants associated with this disease, namely R145P(Sendai), R147P(Chicago), and R158P(Osaka or Kurashiki), on the structural and conformational integrity of the protein. All three variants were found to have significantly reduced helical content, to expose a larger portion of hydrophobic surface to the solvent, and to be significantly thermodynamically destabilized, often lacking functionally relevant unfolding intermediates. Furthermore, all variants were aggregation prone and had enhanced sensitivity to protease digestion. Finally, although the variants were able to form discoidal lipoprotein particles, discrete subpopulations of poorly formed or aberrant particles were evident. Furthermore, these lipoprotein particles were thermodynamically destabilized and aggregation prone. Overall, our data suggest that these mutations induce a generalized unfolding of the N-terminal domain of apoE3 toward a molten-globule-like structure. ApoE3 N-terminal domain unfolding due to mutation may constitute a common mechanism underlying the protein's association with the pathogenesis of LPG.
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.