Evidence map›Paper›PMID 25613106›Full record

ArticleBiochemistry2015

Ligand recognition specificity of leukocyte integrin αMβ2 (Mac-1, CD11b/CD18) and its functional consequences.

Nataly P Podolnikova, Andriy V Podolnikov, Thomas A Haas, Valeryi K Lishko, Tatiana P Ugarova

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

55 citing papers in PubMed, 82 citations in OpenAlex.

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  15. CD11b agonists offer a novel approach for treating lupus nephritis.Translational research : the journal of laboratory and clinical medicine · 2022
    Review
  16. Review
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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 2 countries.

Nataly P PodolnikovaCenter for Metabolic and Vascular Biology, School of Life Sciences, Arizona State University , Tempe, Arizona 85287, United States.
Andriy V Podolnikov
Thomas A Haas
Valeryi K Lishko
Tatiana P Ugarova
Arizona State University · USUniversity of Saskatchewan · CA

Funding

The role of beta 2 integrins in macrophage fusionR01HL063199 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI Tatiana P Ugarova · 1999 to 2026
$8.6M
NHLBI NIH HHS HL 63199NHLBI NIH HHS R01 HL063199
6 · The paper itself

Abstract

The broad recognition specificity exhibited by integrin α(M)β2 (Mac-1, CD11b/CD18) has allowed this adhesion receptor to play innumerable roles in leukocyte biology, yet we know little about how and why α(M)β2 binds its multiple ligands. Within α(M)β2, the α(M)I-domain is responsible for integrin's multiligand binding properties. To identify its recognition motif, we screened peptide libraries spanning sequences of many known protein ligands for α(M)I-domain binding and also selected the α(M)I-domain recognition sequences by phage display. Analyses of >1400 binding and nonbinding peptides derived from peptide libraries showed that a key feature of the α(M)I-domain recognition motif is a small core consisting of basic amino acids flanked by hydrophobic residues. Furthermore, the peptides selected by phage display conformed to a similar pattern. Identification of the recognition motif allowed the construction of an algorithm that reliably predicts the α(M)I-domain binding sites in the α(M)β2 ligands. The recognition specificity of the α(M)I-domain resembles that of some chaperones, which allows it to bind segments exposed in unfolded proteins. The disclosure of the α(M)β2 binding preferences allowed the prediction that cationic host defense peptides, which are strikingly enriched in the α(M)I-domain recognition motifs, represent a new class of α(M)β2 ligands. This prediction has been tested by examining the interaction of α(M)β2 with the human cathelicidin peptide LL-37. LL-37 induced a potent α(M)β2-dependent cell migratory response and caused activation of α(M)β2 on neutrophils. The newly revealed recognition specificity of α(M)β2 toward unfolded protein segments and cationic proteins and peptides suggests that α(M)β2 may serve as a previously proposed "alarmin" receptor with important roles in innate host defense.

Indexed as

Amino Acid SequenceBinding SitesHumansLigandsMacrophage-1 AntigenMolecular Sequence DataProtein ConformationLigandsMacrophage-1 Antigen

Identifiers

PMID25613106
PMCPMC4532391
OpenAlexW2335432651

What OpenQuestion holds

Textmetadata
LicenceTDM
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.