Evidence map›Paper›PMID 34002692›Full record

ArticleeLife2021

Polymerization of misfolded Z alpha-1 antitrypsin protein lowers CX3CR1 expression in human PBMCs.

Srinu Tumpara, Matthias Ballmaier, Sabine Wrenger, Mandy König, Matthias Lehmann, Ralf Lichtinghagen, Beatriz Martinez-Delgado, Elena Korenbaum, David DeLuca, Nils Jedicke and 5 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

5 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
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

15 authors at 5 institutions in 3 countries.

Srinu TumparaDepartment of Respiratory Medicine, Hannover Medical School, Biomedical Research in Endstage and Obstructive Lung Disease Hannover (BREATH), Member of the German Center for Lung Research (DZL), Hannover, Germany.ORCID 0000-0003-0363-3914
Matthias BallmaierCell Sorting Core Facility Hannover Medical School, Hannover, Germany.ORCID 0000-0002-1352-5995
Sabine WrengerDepartment of Respiratory Medicine, Hannover Medical School, Biomedical Research in Endstage and Obstructive Lung Disease Hannover (BREATH), Member of the German Center for Lung Research (DZL), Hannover, Germany.ORCID 0000-0002-9733-6162
Mandy König8sens.biognostic GmbH, Berlin, Germany.
Matthias Lehmann8sens.biognostic GmbH, Berlin, Germany.
Ralf LichtinghagenInstitute of Clinical Chemistry, Hannover Medical School, Hannover, Germany.
Beatriz Martinez-DelgadoDepartment of Molecular Genetics, Institute of Health Carlos III, Center for Biomedical Research in the Network of Rare Diseases (CIBERER), Majadahonda, Spain.ORCID 0000-0001-6834-350X
Elena KorenbaumInstitute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany.
David DeLucaDepartment of Respiratory Medicine, Hannover Medical School, Biomedical Research in Endstage and Obstructive Lung Disease Hannover (BREATH), Member of the German Center for Lung Research (DZL), Hannover, Germany.ORCID 0000-0002-0141-9116
Nils JedickeDepartment of Gastroenterology, Hepatology and Endocrinology, Hannover Medical School, Hannover, Germany.
Tobias WelteDepartment of Respiratory Medicine, Hannover Medical School, Biomedical Research in Endstage and Obstructive Lung Disease Hannover (BREATH), Member of the German Center for Lung Research (DZL), Hannover, Germany.
Malin FrommeMedical Clinic III, Gastroenterology, Metabolic Diseases and Intensive Care, University Hospital RWTH Aachen, Aachen, Germany.
Pavel StrnadMedical Clinic III, Gastroenterology, Metabolic Diseases and Intensive Care, University Hospital RWTH Aachen, Aachen, Germany.
Jan StolkDepartment of Pulmonology, Leiden University Medical Center, Member of European Reference Network LUNG, section Alpha-1-antitrypsin Deficiency, Leiden, Netherlands.
Sabina JanciauskieneDepartment of Respiratory Medicine, Hannover Medical School, Biomedical Research in Endstage and Obstructive Lung Disease Hannover (BREATH), Member of the German Center for Lung Research (DZL), Hannover, Germany.ORCID 0000-0001-7687-5258
Medizinische Hochschule Hannover · DELeiden University Medical Center · NLPathodiagnostik Berlin · DERWTH Aachen University · DEInstituto de Salud Carlos III · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Expression levels of CX3CR1 (C-X3-C motif chemokine receptor 1) on immune cells have significant importance in maintaining tissue homeostasis under physiological and pathological conditions. The factors implicated in the regulation of CX3CR1 and its specific ligand CX3CL1 (fractalkine) expression remain largely unknown. Recent studies provide evidence that host's misfolded proteins occurring in the forms of polymers or amyloid fibrils can regulate CX3CR1 expression. Herein, a novel example demonstrates that polymers of human ZZ alpha-1 antitrypsin (Z-AAT) protein, resulting from its conformational misfolding due to the Z (Glu342Lys) mutation in

Indexed as

MutationPolymersAdultalpha 1-AntitrypsinChemokine CX3CL1CX3C Chemokine Receptor 1FemaleHumansLeukocytes, MononuclearMaleMiddle AgedProtein ConformationRNA, Messengeralpha 1-AntitrypsinChemokine CX3CL1CX3C Chemokine Receptor 1CX3CL1 protein, humanCX3CR1 protein, humanPolymersRNA, MessengerSERPINA1 protein, humanalpha-1-antitrypsincell biologyCX3CR1/CX3CL1 axishumaninflammationmedicinePBMCspolymersprotein misfolding

Identifiers

PMID34002692
PMCPMC8205483
OpenAlexW3161962671

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.