Evidence map›Paper›PMID 32151314›Full record

ArticleeLife2020

Fatal amyloid formation in a patient's antibody light chain is caused by a single point mutation.

Pamina Kazman, Marie-Theres Vielberg, María Daniela Pulido Cendales, Lioba Hunziger, Benedikt Weber, Ute Hegenbart, Martin Zacharias, Rolf Köhler, Stefan Schönland, Michael Groll and 1 more

Open access · goldAbstract readCase Reports
In one paragraph

Article in eLife, 2020. 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
2.8field-weighted citation impact, top 9% 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

32 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
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  8. Review
  9. The molecular landscape of AL amyloidosis.British journal of haematology · 2025
    Review
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  14. Review
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  18. Cu(II) Binding Increases the Soluble Toxicity of Amyloidogenic Light Chains.International journal of molecular sciences · 2022
    Article
  19. Review
  20. Review
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

11 authors at 2 institutions in 1 country.

Pamina KazmanCenter for Integrated Protein Science Munich at the Department Chemie, Technische Universität München, Garching, Germany.ORCID 0000-0003-2369-9726
Marie-Theres VielbergCenter for Integrated Protein Science Munich at the Department Chemie, Technische Universität München, Garching, Germany.
María Daniela Pulido CendalesCenter for Integrated Protein Science Munich at the Department Physik, Technische Universität München, Garching, Germany.
Lioba HunzigerCenter for Integrated Protein Science Munich at the Department Chemie, Technische Universität München, Garching, Germany.
Benedikt WeberCenter for Integrated Protein Science Munich at the Department Chemie, Technische Universität München, Garching, Germany.
Ute HegenbartMedical Department V, Amyloidosis Center, University of Heidelberg, Heidelberg, Germany.
Martin ZachariasCenter for Integrated Protein Science Munich at the Department Physik, Technische Universität München, Garching, Germany.
Rolf KöhlerInstitute of Human Genetics, University of Heidelberg, Heidelberg, Germany.
Stefan SchönlandMedical Department V, Amyloidosis Center, University of Heidelberg, Heidelberg, Germany.
Michael GrollCenter for Integrated Protein Science Munich at the Department Chemie, Technische Universität München, Garching, Germany.
Johannes BuchnerCenter for Integrated Protein Science Munich at the Department Chemie, Technische Universität München, Garching, Germany.ORCID 0000-0003-1282-7737
Center for Integrated Protein Science Munich · DEHeidelberg University · DE

Funding

Deutsche Forschungsgemeinschaft FOR 2969
6 · The paper itself

Abstract

In systemic light chain amyloidosis, an overexpressed antibody light chain (LC) forms fibrils which deposit in organs and cause their failure. While it is well-established that mutations in the LC's V

Indexed as

Genetic Predisposition to DiseaseAmino Acid SequenceAmyloidosisFatal OutcomeFemaleHumansImmunoglobulin Light ChainsMiddle AgedModels, MolecularMutationPlaque, AmyloidProtein ConformationProtein FoldingImmunoglobulin Light ChainsAL amyloidosisantibody light chainbiochemistrychemical biologyE. colihydrophobic interactionsprotein dynamicsprotein stability

Identifiers

PMID32151314
PMCPMC7064341
OpenAlexW3011907048

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.