Evidence map›Paper›PMID 39604162›Full record

ArticleProtein science : a publication of the Protein Society2024

Enzymatic, structural, and biophysical characterization of a single-domain antibody (VHH) selectively and tightly inhibiting neutrophil elastase and exhibiting favorable developability properties.

Paola Redeghieri, Joël Moray, Frédéric Kerff, Sophie Gohy, Teresinha Leal, Serge Muyldermans, Rita Vanbever, Francisco Javier Morales-Yánez, Mireille Dumoulin

Abstract read
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In one paragraph

Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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

9 authors.

Paola RedeghieriNano-Antibodies to Explore Protein Structure and Functions (NEPTUNS), Centre for Protein Engineering, InBios, Department of Life Sciences, University of Liège, Liège, Belgium.
Joël MorayNano-Antibodies to Explore Protein Structure and Functions (NEPTUNS), Centre for Protein Engineering, InBios, Department of Life Sciences, University of Liège, Liège, Belgium.
Frédéric KerffBiological Macromolecule Crystallography, Centre for Protein Engineering, InBios, Department of Life Sciences, University of Liège, Liège, Belgium.
Sophie GohyDepartment of Pneumology, ENT and Dermatology, Institute of Experimental and Clinical Research (IREC), Université Catholique de Louvain, Brussels, Belgium.
Teresinha LealLouvain Center for Toxicology and Applied Pharmacology (LTAP), Institute of Experimental and Clinical Research (IREC), Université Catholique de Louvain, Brussels, Belgium.
Serge MuyldermansLaboratory of Cellular and Molecular Immunology, Vrije Universiteit Brussel, Brussels, Belgium.
Rita VanbeverLouvain Drug Research Institute (LDRI), Université Catholique de Louvain, Brussels, Belgium.ORCID 0000-0002-0784-8771
Francisco Javier Morales-YánezNano-Antibodies to Explore Protein Structure and Functions (NEPTUNS), Centre for Protein Engineering, InBios, Department of Life Sciences, University of Liège, Liège, Belgium.
Mireille DumoulinNano-Antibodies to Explore Protein Structure and Functions (NEPTUNS), Centre for Protein Engineering, InBios, Department of Life Sciences, University of Liège, Liège, Belgium.

Funding

Fonds De La Recherche Scientifique - FNRSWalinnov project (Nanoneutra) from the Walloon Region 1710173
6 · The paper itself

Abstract

Human neutrophil elastase (hNE), a serine protease released by neutrophils during inflammation, plays a major role in the pathophysiology of several conditions especially in inflammatory lung diseases. Its inhibition constitutes, therefore, a promising therapeutic strategy to combat these diseases. In this work, we characterized the in vitro properties of a VHH (i.e., the antigen binding domain of camelid heavy chain-only antibodies), referred to as NbE201. This VHH is able to inhibit tightly, selectively and competitively both human and murine elastases with the inhibition constants (K

Indexed as

Leukocyte ElastaseSingle-Domain Antibodiesalpha 1-AntitrypsinAnimalsCrystallography, X-RayHumansMiceModels, Molecularalpha 1-AntitrypsinELANE protein, humanLeukocyte ElastaseSingle-Domain Antibodiescamelid antibody fragmentschemical stabilitycompetitive inhibitory VHHdevelopabilityelastase inhibitionneutrophilic inflammatory diseasesserine proteasestability towards oxidationthermal stabilitythermodynamic stabilityVHHs

Identifiers

PMID39604162
PMCPMC11602439

What OpenQuestion holds

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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.