Evidence map›Paper›PMID 35269582›Full record

ReviewInternational journal of molecular sciences2022

A Review of Alpha-1 Antitrypsin Binding Partners for Immune Regulation and Potential Therapeutic Application.

Michael E O'Brien, Grace Murray, Debananda Gogoi, Azeez Yusuf, Cormac McCarthy, Mark R Wormald, Michelle Casey, Claudie Gabillard-Lefort, Noel G McElvaney, Emer P Reeves

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
6.6field-weighted citation impact, top 2% 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

54 citing papers in PubMed, 76 citations in OpenAlex.

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  13. An endogenous human peptide derived from αNaunyn-Schmiedeberg's archives of pharmacology · 2026
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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

10 authors at 2 institutions in 2 countries.

Michael E O'BrienIrish Centre for Genetic Lung Disease, Department of Medicine, RCSI University of Medicine and Health Sciences, Beaumont Hospital, D02 YN77 Dublin, Ireland.
Grace MurrayIrish Centre for Genetic Lung Disease, Department of Medicine, RCSI University of Medicine and Health Sciences, Beaumont Hospital, D02 YN77 Dublin, Ireland.
Debananda GogoiIrish Centre for Genetic Lung Disease, Department of Medicine, RCSI University of Medicine and Health Sciences, Beaumont Hospital, D02 YN77 Dublin, Ireland.
Azeez YusufIrish Centre for Genetic Lung Disease, Department of Medicine, RCSI University of Medicine and Health Sciences, Beaumont Hospital, D02 YN77 Dublin, Ireland.ORCID 0000-0001-5241-6620
Cormac McCarthyIrish Centre for Genetic Lung Disease, Department of Medicine, RCSI University of Medicine and Health Sciences, Beaumont Hospital, D02 YN77 Dublin, Ireland.ORCID 0000-0003-2896-5210
Mark R WormaldDepartment of Biochemistry, Oxford Glycobiology Institute, University of Oxford, Oxford OX1 3QU, UK.
Michelle CaseyIrish Centre for Genetic Lung Disease, Department of Medicine, RCSI University of Medicine and Health Sciences, Beaumont Hospital, D02 YN77 Dublin, Ireland.
Claudie Gabillard-LefortIrish Centre for Genetic Lung Disease, Department of Medicine, RCSI University of Medicine and Health Sciences, Beaumont Hospital, D02 YN77 Dublin, Ireland.
Noel G McElvaneyIrish Centre for Genetic Lung Disease, Department of Medicine, RCSI University of Medicine and Health Sciences, Beaumont Hospital, D02 YN77 Dublin, Ireland.
Emer P ReevesIrish Centre for Genetic Lung Disease, Department of Medicine, RCSI University of Medicine and Health Sciences, Beaumont Hospital, D02 YN77 Dublin, Ireland.ORCID 0000-0002-1922-0447
Beaumont Hospital · IEUniversity of Oxford · GB

Funding

US Alpha-1 Foundation Grant # 615848
6 · The paper itself

Abstract

Alpha-1 antitrypsin (AAT) is the canonical serine protease inhibitor of neutrophil-derived proteases and can modulate innate immune mechanisms through its anti-inflammatory activities mediated by a broad spectrum of protein, cytokine, and cell surface interactions. AAT contains a reactive methionine residue that is critical for its protease-specific binding capacity, whereby AAT entraps the protease on cleavage of its reactive centre loop, neutralises its activity by key changes in its tertiary structure, and permits removal of the AAT-protease complex from the circulation. Recently, however, the immunomodulatory role of AAT has come increasingly to the fore with several prominent studies focused on lipid or protein-protein interactions that are predominantly mediated through electrostatic, glycan, or hydrophobic potential binding sites. The aim of this review was to investigate the spectrum of AAT molecular interactions, with newer studies supporting a potential therapeutic paradigm for AAT augmentation therapy in disorders in which a chronic immune response is strongly linked.

Indexed as

alpha 1-Antitrypsinalpha 1-Antitrypsin DeficiencyApolipoproteinsBinding SitesCaspasesComplement System ProteinsCOVID-19CytokinesGlycosylationHumansMutationProtein BindingProtein DomainsSARS-CoV-2alpha 1-AntitrypsinApolipoproteinsCaspasesComplement System ProteinsCytokinesalpha-1 antitrypsinalpha-1 antitrypsin deficiencycomplement C3coronavirus disease 2019 (COVID-19)cytokinesinterleukin-6proteases

Identifiers

PMID35269582
PMCPMC8910375
OpenAlexW4212904005

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.