ArticlePloS one2015
Transthyretin Amyloidosis: Chaperone Concentration Changes and Increased Proteolysis in the Pathway to Disease.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed, 35 citations in OpenAlex.
- Transthyretin at the crossroads of neurodegeneration: a silent guardian in Parkinson's disease.Metabolic brain disease · 2026Review
- Plasma Proteome Profiling Reveals Inflammation Markers and Tafamidis Effects in V30M Transthyretin Polyneuropathy.International journal of molecular sciences · 2025Article
- Exercise training decreases the load and changes the content of circulating SDS-resistant protein aggregates in patients with heart failure with reduced ejection fraction.Molecular and cellular biochemistry · 2024Article
- Familial occurrences of cardiac wild-type transthyretin amyloidosis: a case series.European heart journal. Case reports · 2024Article
- Molecular mechanisms and emerging therapies in wild-type transthyretin amyloid cardiomyopathy.Heart failure reviews · 2024Review
- Targeted sequencing of selected functional genes in patients with wild-type transthyretin amyloidosis.BMC research notes · 2023Article
- Transthyretin Stabilizers and Seeding Inhibitors as Therapies for Amyloid Transthyretin Cardiomyopathy.Pharmaceutics · 2023Review
- The Role of Proteolysis in Amyloidosis.International journal of molecular sciences · 2022Review
- The Journey of Human Transthyretin: Synthesis, Structure Stability, and Catabolism.Biomedicines · 2022Review
- The yeast molecular chaperone, Hsp104, influences transthyretin aggregate formation.Frontiers in molecular neuroscience · 2022Article
- In Vitro and In Vivo Effects of SerpinA1 on the Modulation of Transthyretin Proteolysis.International journal of molecular sciences · 2021Article
- Review
- Change in the plasma proteome associated with canine cognitive dysfunction syndrome (CCDS) in Thailand.BMC veterinary research · 2021Article
- A serine protease secreted from Bacillus subtilis cleaves human plasma transthyretin to generate an amyloidogenic fragment.Communications biology · 2020Article
- Diagnosis and treatment of cardiac amyloidosis: an interdisciplinary consensus statement.Wiener klinische Wochenschrift · 2020Article
- Modulation of the Mechanisms Driving Transthyretin Amyloidosis.Frontiers in molecular neuroscience · 2020Review
- Increased Risk of Multiple Outpatient Surgeries in African-American Carriers ofJournal of clinical medicine · 2019Article
- Transthyretin Amyloid Fibril Disrupting Activities of Extracts and Fractions fromMolecules (Basel, Switzerland) · 2019Article
- Systemic amyloidoses and proteomics: The state of the art.EuPA open proteomics · 2016Article
- ApoA1, ApoJ and ApoE Plasma Levels and Genotype Frequencies in Cerebral Amyloid Angiopathy.Neuromolecular medicine · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transthyretin amyloidosis is a conformational pathology characterized by the extracellular formation of amyloid deposits and the progressive impairment of the peripheral nervous system. Point mutations in this tetrameric plasma protein decrease its stability and are linked to disease onset and progression. Since non-mutated transthyretin also forms amyloid in systemic senile amyloidosis and some mutation bearers are asymptomatic throughout their lives, non-genetic factors must also be involved in transthyretin amyloidosis. We discovered, using a differential proteomics approach, that extracellular chaperones such as fibrinogen, clusterin, haptoglobin, alpha-1-anti-trypsin and 2-macroglobulin are overrepresented in transthyretin amyloidosis. Our data shows that a complex network of extracellular chaperones are over represented in human plasma and we speculate that they act synergistically to cope with amyloid prone proteins. Proteostasis may thus be as important as point mutations in transthyretin amyloidosis.
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.