ReviewCurrent topics in medicinal chemistry2012
Amyloid formation in light chain amyloidosis.
Review in Current topics in medicinal chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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
31 citing papers in PubMed, 76 citations in OpenAlex.
- Phase 2 trial of daily, oral epigallocatechin gallate in patients with light-chain amyloidosis.International journal of hematology · 2017Trial
- Multiple Myeloma Concomitant with AL Amyloidosis: Histopathological Aspects of the Common Plasma Cell Spectrum.International journal of molecular sciences · 2026Article
- Nucleation of α-Synuclein Amyloid Fibrils Induced by Cross-Interaction with β-Hairpin Peptides Derived from Immunoglobulin Light Chains.International journal of molecular sciences · 2023Article
- Treatment of Alzheimer's Disease: Beyond Symptomatic Therapies.International journal of molecular sciences · 2023Review
- Stress-mediated aggregation of disease-associated proteins in amyloid bodies.Scientific reports · 2023Article
- Widespread amyloidogenicity potential of multiple myeloma patient-derived immunoglobulin light chains.BMC biology · 2023Article
- Dissection of the amyloid formation pathway in AL amyloidosis.Nature communications · 2021Article
- Genetic pathogenesis of immunoglobulin light chain amyloidosis: basic characteristics and clinical applications.Experimental hematology & oncology · 2021Review
- Search for AL amyloidosis risk factors using Mendelian randomization.Blood advances · 2021Article
- Article
- Pharmacologic targeting of plasma cell endoplasmic reticulum proteostasis to reduce amyloidogenic light chain secretion.Blood advances · 2021Article
- A kinetic coupling between protein unfolding and aggregation controls time-dependent solubility of the human myeloma antibody light chain.Protein science : a publication of the Protein Society · 2020Article
- Understanding Mesangial Pathobiology in AL-Amyloidosis and Monoclonal Ig Light Chain Deposition Disease.Kidney international reports · 2020Review
- Structural basis for the stabilization of amyloidogenic immunoglobulin light chains by hydantoins.Bioorganic & medicinal chemistry letters · 2020Article
- Fatal amyloid formation in a patient's antibody light chain is caused by a single point mutation.eLife · 2020Article
- Protein Misfolding during Pregnancy: New Approaches to Preeclampsia Diagnostics.International journal of molecular sciences · 2019Review
- Crystal structure of 6aJL2-R24G light chain variable domain: Does crystal packing explain amyloid fibril formation?Biochemistry and biophysics reports · 2019Article
- Stabilization of amyloidogenic immunoglobulin light chains by small molecules.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- AL amyloidosis with non-amyloid forming monoclonal immunoglobulin deposition; a case mimicking AHL amyloidosis.BMC nephrology · 2018Article
- Immunoglobulin light chain amyloid aggregation.Chemical communications (Cambridge, England) · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Light chain amyloidosis is one of the unique examples within amyloid diseases where the amyloidogenic precursor is a protein that escapes the quality control machinery and is secreted from the cells to be circulated in the bloodstream. The immunoglobulin light chains are produced by an abnormally proliferative monoclonal population of plasma cells that under normal conditions produce immunoglobulin molecules such as IgG, IgM or IgA. Once the light chains are in circulation, the proteins misfold and deposit as amyloid fibrils in numerous tissues and organs, causing organ failure and death. While there is a correlation between the thermodynamic stability of the protein and the kinetics of amyloid formation, we have recently found that this correlation applies within a thermodynamic range, and it is only a helpful correlation when comparing mutants from the same protein. Light chain amyloidosis poses unique challenges because each patient has a unique protein sequence as a result of the selection of a germline gene and the incorporation of somatic mutations. The exact location of the misfolding process is unknown as well as the full characterization of all of the toxic species populated during the amyloid formation process in light chain 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.