Evidence map›Paper›PMID 37520549›Full record

ReviewFrontiers in immunology2023

Role of the mechanisms for antibody repertoire diversification in monoclonal light chain deposition disorders: when a friend becomes foe.

Luis Del Pozo-Yauner, Guillermo A Herrera, Julio I Perez Carreon, Elba A Turbat-Herrera, Francisco J Rodriguez-Alvarez, Robin A Ruiz Zamora

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in immunology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
5.3field-weighted citation impact, top 4% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 23 citations in OpenAlex.

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  9. An updated AL-base reveals ranked enrichment of immunoglobulin light chain variable genes in AL amyloidosis.Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Luis Del Pozo-YaunerDepartment of Pathology, University of South Alabama-College of Medicine, Mobile, AL, United States.
Guillermo A HerreraDepartment of Pathology, University of South Alabama-College of Medicine, Mobile, AL, United States.
Julio I Perez CarreonInstituto Nacional de Medicina Genomica (INMEGEN), Ciudad de México, Mexico.
Elba A Turbat-HerreraDepartment of Pathology, University of South Alabama-College of Medicine, Mobile, AL, United States.
Francisco J Rodriguez-AlvarezInstituto Nacional de Medicina Genomica (INMEGEN), Ciudad de México, Mexico.
Robin A Ruiz ZamoraInstituto Nacional de Medicina Genomica (INMEGEN), Ciudad de México, Mexico.
National Institute of Genomic Medicine · MXUniversity of South Alabama · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The adaptive immune system of jawed vertebrates generates a highly diverse repertoire of antibodies to meet the antigenic challenges of a constantly evolving biological ecosystem. Most of the diversity is generated by two mechanisms: V(D)J gene recombination and somatic hypermutation (SHM). SHM introduces changes in the variable domain of antibodies, mostly in the regions that form the paratope, yielding antibodies with higher antigen binding affinity. However, antigen recognition is only possible if the antibody folds into a stable functional conformation. Therefore, a key force determining the survival of B cell clones undergoing somatic hypermutation is the ability of the mutated heavy and light chains to efficiently fold and assemble into a functional antibody. The antibody is the structural context where the selection of the somatic mutations occurs, and where both the heavy and light chains benefit from protective mechanisms that counteract the potentially deleterious impact of the changes. However, in patients with monoclonal gammopathies, the proliferating plasma cell clone may overproduce the light chain, which is then secreted into the bloodstream. This places the light chain out of the protective context provided by the quaternary structure of the antibody, increasing the risk of misfolding and aggregation due to destabilizing somatic mutations. Light chain-derived (AL) amyloidosis, light chain deposition disease (LCDD), Fanconi syndrome, and myeloma (cast) nephropathy are a diverse group of diseases derived from the pathologic aggregation of light chains, in which somatic mutations are recognized to play a role. In this review, we address the mechanisms by which somatic mutations promote the misfolding and pathological aggregation of the light chains, with an emphasis on AL amyloidosis. We also analyze the contribution of the variable domain (V

Indexed as

Multiple MyelomaParaproteinemiasAnimalsB-LymphocytesEcosystemFriendsHumansamyloidantibodiesimmune systemlight chain (AL) amyloidosisprotein aggregationsomatic hypermutationV(D)J rearrangement

Identifiers

PMID37520549
PMCPMC10374031
OpenAlexW4384154655

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

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.