ArticleCurrent protein & peptide science2009
Light chain amyloidosis - current findings and future prospects.
Article in Current protein & peptide science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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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.
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Who cites it
24 citing papers in PubMed, 42 citations in OpenAlex.
- Tracking reduction-induced molecular changes in pathological free light chains by SV-AUC.European biophysics journal : EBJ · 2025Article
- The molecular landscape of AL amyloidosis.British journal of haematology · 2025Review
- Amyloidogenic light chains impair plasma cell survival.Haematologica · 2023Article
- Dissection of the amyloid formation pathway in AL amyloidosis.Nature communications · 2021Article
- Light chain amyloidosis induced inflammatory changes in cardiomyocytes and adipose-derived mesenchymal stromal cells.Leukemia · 2020Article
- Fatal amyloid formation in a patient's antibody light chain is caused by a single point mutation.eLife · 2020Article
- Identification of two principal amyloid-driving segments in variable domains of Ig light chains in systemic light-chain amyloidosis.The Journal of biological chemistry · 2018Article
- Integrative Transcriptomic and microRNAomic Profiling Reveals Immune Mechanism for the Resilience to Soybean Meal Stress in Fish Gut and Liver.Frontiers in physiology · 2018Article
- Mesenchymal stromal cells protect human cardiomyocytes from amyloid fibril damage.Cytotherapy · 2017Article
- Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study.Scientific reports · 2017Article
- Solid-state NMR chemical shift assignments for AL-09 VBiomolecular NMR assignments · 2017Article
- Immunoglobulin Light Chains Form an Extensive and Highly Ordered Fibril Involving the N- and C-Termini.ACS omega · 2017Article
- Cell Damage in Light Chain Amyloidosis: FIBRIL INTERNALIZATION, TOXICITY AND CELL-MEDIATED SEEDING.The Journal of biological chemistry · 2016Article
- Mutations can cause light chains to be too stable or too unstable to form amyloid fibrils.Protein science : a publication of the Protein Society · 2015Article
- Formation of amyloid fibers by monomeric light chain variable domains.The Journal of biological chemistry · 2014Article
- IgG Fab fragments forming bivalent complexes by a conformational mechanism that is reversible by osmolytes.The Journal of biological chemistry · 2012Article
- Tyrosine residues mediate fibril formation in a dynamic light chain dimer interface.The Journal of biological chemistry · 2012Article
- How to manage primary amyloidosis.Leukemia · 2012Article
- Amyloid formation in light chain amyloidosis.Current topics in medicinal chemistry · 2012Review
- Glycosaminoglycans promote fibril formation by amyloidogenic immunoglobulin light chains through a transient interaction.Biophysical chemistry · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Systemic light chain amyloidosis (AL) is one of several protein misfolding diseases and is characterized by extracellular deposition of immunoglobulin light chains in the form of amyloid fibrils [1]. Immunoglobulin (Ig) proteins consist of two light chains (LCs) and two heavy chains (HCs) that ordinarily form a heterotetramer which is secreted by a plasma cell. In AL, however, a monoclonal plasma cell population produces an abundance of a pathogenic LC protein. In this case, not all of the LCs pair with the HCs, and free LCs are secreted into circulation. The LC-HC dimer is very stable, and losing this interaction may result in an unstable LC protein [2]. Additionally, somatic mutations are thought to cause amyloidogenic proteins to be less stable compared to non-amyloidogenic proteins [3-5], leading to protein misfolding and amyloid fibril formation. The amyloid fibrils cause tissue damage and cell death, leading to patient death within 12-18 months if left untreated [6]. Current therapies are harsh and not curative, including chemotherapy and autologous stem cell transplants. Studies of protein pathogenesis and fibril formation mechanisms may lead to better therapies with an improved outlook for patient survival. Much has been done to determine the molecular factors that make a particular LC protein amyloidogenic and to elucidate the mechanism of amyloid fibril formation. Anthony Fink's work, particularly with discerning the role of intermediates in the fibril formation pathway, has made a remarkable impact in the field of amyloidosis research. This review provides a general overview of the current state of AL research and also attempts to capture the most recent ideas and knowledge generated from the Fink laboratory.
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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.