ReviewThe Journal of biological chemistry2015
Systemic amyloidosis: lessons from β2-microglobulin.
Review in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 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
41 citing papers in PubMed.
- Effects of different hemodialysis modalities combined with low-calcium dialysate on mineral metabolism and vascular calcification in maintenance hemodialysis patients with chronic kidney disease.Journal of applied biomedicine · 2024Trial
- Affibodies as valuable tool to prevent βBiology direct · 2025Article
- A Review of Mobile Device Interventions for Continuous Nursing of Patients Undergoing Maintenance Haemodialysis.Journal of multidisciplinary healthcare · 2024Review
- Human wild-type and D76N βFASEB bioAdvances · 2023Article
- Disease-relevant βNature communications · 2023Article
- Macromolecular crowding and supersaturation protect hemodialysis patients from the onset of dialysis-related amyloidosis.Nature communications · 2022Article
- Micro- and Nanoplastics' Effects on Protein Folding and Amyloidosis.International journal of molecular sciences · 2022Review
- Anti-amyloidogenic property of gold nanoparticle decorated quercetin polymer nanorods in pH and temperature induced aggregation of lysozyme.RSC advances · 2022Article
- Supersaturation-Dependent Formation of Amyloid Fibrils.Molecules (Basel, Switzerland) · 2022Review
- Amyloid Formation by Globular Proteins: The Need to Narrow the Gap BetweenFrontiers in molecular biosciences · 2022Review
- Pathogenic D76N Variant of βBiology · 2021Article
- In Vitro and In Vivo Effects of SerpinA1 on the Modulation of Transthyretin Proteolysis.International journal of molecular sciences · 2021Article
- Predicting stable binding modes from simulated dimers of the D76N mutant ofComputational and structural biotechnology journal · 2021Article
- Article
- Effect of Oxidation on Quality of Chiba Tofu Produced by Soy Isolate Protein When Subjected to Storage.Foods (Basel, Switzerland) · 2020Article
- Quantification of amyloid fibril polymorphism by nano-morphometry reveals the individuality of filament assembly.Communications chemistry · 2020Article
- Sequence-independent recognition of the amyloid structural motif by GFP protein family.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Conformational Stability and Dynamics in Crystals Recapitulate Protein Behavior in Solution.Biophysical journal · 2020Article
- Insight into the Folding and Dimerization Mechanisms of the N-Terminal Domain from Human TDP-43.International journal of molecular sciences · 2020Article
- The role of the IThe Journal of biological chemistry · 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
2 authors.
Funding
Abstract
β2-Microglobulin is responsible for systemic amyloidosis affecting patients undergoing long-term hemodialysis. Its genetic variant D76N causes a very rare form of familial systemic amyloidosis. These two types of amyloidoses differ significantly in terms of the tissue localization of deposits and for major pathological features. Considering how the amyloidogenesis of the β2-microglobulin mechanism has been scrutinized in depth for the last three decades, the comparative analysis of molecular and pathological properties of wild type β2-microglobulin and of the D76N variant offers a unique opportunity to critically reconsider the current understanding of the relation between the protein's structural properties and its pathologic behavior.
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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.