Evidence map›Paper›PMID 30598439›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Role of domain interactions in the aggregation of full-length immunoglobulin light chains.

Enrico Rennella, Gareth J Morgan, Jeffery W Kelly, Lewis E Kay

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
–field-weighted citation impact
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

32 citing papers in PubMed.

  1. Article
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  3. Review
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  5. Article
  6. Review
  7. Article
  8. Article
  9. Kinetic evidence for multiple aggregation pathways in antibody light chain variable domains.Protein science : a publication of the Protein Society · 2024
    Article
  10. Role of complementarity-determining regions 1 and 3 in pathologic amyloid formation by human immunoglobulin κ1 light chains.Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis · 2023
    Article
  11. Review
  12. Article
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  15. Review
  16. Article
  17. Review
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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

4 authors.

Enrico RennellaDepartment of Molecular Genetics, The University of Toronto, Toronto, ON, Canada M5S 1A8; rennella@pound.med.utoronto.ca gjmorgan@bu.edu jkelly@scripps.edu kay@pound.med.utoronto.ca.
Gareth J MorganDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037; rennella@pound.med.utoronto.ca gjmorgan@bu.edu jkelly@scripps.edu kay@pound.med.utoronto.ca.ORCID 0000-0002-1275-2010
Jeffery W KellyDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037; rennella@pound.med.utoronto.ca gjmorgan@bu.edu jkelly@scripps.edu kay@pound.med.utoronto.ca.
Lewis E KayDepartment of Molecular Genetics, The University of Toronto, Toronto, ON, Canada M5S 1A8; rennella@pound.med.utoronto.ca gjmorgan@bu.edu jkelly@scripps.edu kay@pound.med.utoronto.ca.

Funding

Probing the Biochemical Mechanisms of Amyloid DiseaseR01DK046335 · NIDDK · SCRIPPS RESEARCH INSTITUTE, THE · PI KELLY, JEFFERY W · 1998 to 2025
$8.8M
Probing the biochemical mechanism of amyloid diseaseR37DK046335 · NIDDK · SCRIPPS RESEARCH INSTITUTE, THE · PI KELLY, JEFFERY W · 2006 to 2015
$5.9M
Canadian Institutes of Health ResearchNIDDK NIH HHS R01 DK046335NIDDK NIH HHS R37 DK046335
6 · The paper itself

Abstract

Amyloid light-chain (LC) amyloidosis is a protein misfolding disease in which the aggregation of an overexpressed antibody LC from a clonal plasma cell leads to organ toxicity and patient death if left untreated. While the overall dimeric architecture of LC molecules is established, with each LC composed of variable (V

Indexed as

Protein Aggregation, PathologicalDimerizationEscherichia coliHumansImmunoglobulin Light ChainsProtein DomainsImmunoglobulin Light Chainsantibody light-chain domainslight-chain amyloidosisprotein aggregationproteinopathysolution NMR spectroscopy

Identifiers

PMID30598439
PMCPMC6338840

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.