Evidence map›Paper›PMID 36823438›Full record

ArticleCommunications biology2023

A constant domain mutation in a patient-derived antibody light chain reveals principles of AL amyloidosis.

Georg J Rottenaicher, Ramona M Absmeier, Laura Meier, Martin Zacharias, Johannes Buchner

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

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  6. 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

5 authors at 2 institutions in 1 country.

Georg J RottenaicherCenter for Functional Protein Assemblies, Technical University Munich, Ernst-Otto-Fischer-Str. 8, 85748, Garching, Germany.
Ramona M AbsmeierCenter for Functional Protein Assemblies, Technical University Munich, Ernst-Otto-Fischer-Str. 8, 85748, Garching, Germany.ORCID 0000-0002-9267-8358
Laura MeierCenter for Functional Protein Assemblies, Technical University Munich, Ernst-Otto-Fischer-Str. 8, 85748, Garching, Germany.
Martin ZachariasCenter for Functional Protein Assemblies, Technical University Munich, Ernst-Otto-Fischer-Str. 8, 85748, Garching, Germany.ORCID 0000-0001-5163-2663
Johannes BuchnerCenter for Functional Protein Assemblies, Technical University Munich, Ernst-Otto-Fischer-Str. 8, 85748, Garching, Germany. johannes.buchner@tum.de.ORCID 0000-0003-1282-7737
Fischer (Germany) · DETechnical University of Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Light chain (AL) amyloidosis is a debilitating disease in which mutant antibody light chains (LC), secreted by aberrant plasma cell clones, misfold and form insoluble fibrils, which can be deposited in various organs. In the majority of cases, the fibrillar deposits consist of LC variable domains (V

Indexed as

Immunoglobulin Light-chain AmyloidosisAmyloidAmyloidogenic ProteinsHumansImmunoglobulin Light ChainsMutationAmyloidAmyloidogenic ProteinsImmunoglobulin Light Chains

Identifiers

PMID36823438
PMCPMC9950467
OpenAlexW4321600816

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.