Evidence map›Paper›PMID 34276683›Full record

ArticleFrontiers in immunology2021

Serum Amyloid A1 Induces Classically Activated Macrophages: A Role for Enhanced Fibril Formation.

Ann-Kathrin Gaiser, Shanna Bauer, Stephanie Ruez, Karlheinz Holzmann, Marcus Fändrich, Tatiana Syrovets, Thomas Simmet

Open access · goldAbstract read
In one paragraph

Article in Frontiers in immunology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

20 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Serum amyloid A in HFpEF and cardiometabolic diseases.Basic research in cardiology · 2026
    Review
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  19. Frontiers in immunology · 2022
    Article
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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

7 authors at 1 institution in 1 country.

Ann-Kathrin GaiserInstitute of Pharmacology of Natural Products and Clinical Pharmacology, Ulm University, Ulm, Germany.
Shanna BauerInstitute of Pharmacology of Natural Products and Clinical Pharmacology, Ulm University, Ulm, Germany.
Stephanie RuezInstitute of Protein Biochemistry, Ulm University, Ulm, Germany.
Karlheinz HolzmannGenomics Core Facility, Medical Faculty, Ulm University, Ulm, Germany.
Marcus FändrichInstitute of Protein Biochemistry, Ulm University, Ulm, Germany.
Tatiana SyrovetsInstitute of Pharmacology of Natural Products and Clinical Pharmacology, Ulm University, Ulm, Germany.
Thomas SimmetInstitute of Pharmacology of Natural Products and Clinical Pharmacology, Ulm University, Ulm, Germany.
Universität Ulm · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AA amyloidosis belongs to the group of amyloid diseases which can follow chronic inflammatory conditions of various origin. The disease is characterized by the deposition of insoluble amyloid fibrils formed by serum amyloid A1 (SAA1) leading eventually to organ failure. Macrophages are intimately involved in the fibrillogenesis as well as in the clearance of amyloid fibrils.

Indexed as

AnimalsCells, CulturedCytokinesGene Expression RegulationMacrophage ActivationMacrophagesMiceRecombinant ProteinsSerum Amyloid A ProteinCytokinesRecombinant ProteinsSaa2 protein, mouseSerum Amyloid A Proteinamyloidosisinflammationinnate immunityM1 subsetmacrophage polarizationserum amyloid A

Identifiers

PMID34276683
PMCPMC8278318
OpenAlexW3175711451

What OpenQuestion holds

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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.