Evidence map›Paper›PMID 34914017›Full record

ArticleJournal of molecular modeling2021

Specific interactions between the alkaline protease of P. aeruginosa and its natural peptide inhibitor: ab initio molecular simulations.

Ryosuke Saito, Kyohei Imai, Shohei Yamamoto, Takuya Ezawa, Satoshi Sugiyama, Linn Samira Mari Evenseth, Ingebrigt Sylte, Noriyuki Kurita

Open access · greenAbstract read
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In one paragraph

Article in Journal of molecular modeling, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 80% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

8 authors at 2 institutions in 2 countries.

Ryosuke SaitoDepartment of Computer Science and Engineering, Toyohashi University of Technology, Toyohashi, 441-8580, Japan.
Kyohei ImaiDepartment of Computer Science and Engineering, Toyohashi University of Technology, Toyohashi, 441-8580, Japan.
Shohei YamamotoDepartment of Computer Science and Engineering, Toyohashi University of Technology, Toyohashi, 441-8580, Japan.
Takuya EzawaDepartment of Computer Science and Engineering, Toyohashi University of Technology, Toyohashi, 441-8580, Japan.
Satoshi SugiyamaDepartment of Computer Science and Engineering, Toyohashi University of Technology, Toyohashi, 441-8580, Japan.
Linn Samira Mari EvensethDepartment of Medical Biology, Faculty of Health Sciences, UiT The Arctic University of Norway, NO-9037, Tromsø, Norway.
Ingebrigt SylteDepartment of Medical Biology, Faculty of Health Sciences, UiT The Arctic University of Norway, NO-9037, Tromsø, Norway.
Noriyuki KuritaDepartment of Computer Science and Engineering, Toyohashi University of Technology, Toyohashi, 441-8580, Japan. kurita@cs.tut.ac.jp.
Toyohashi University of Technology · JPUiT The Arctic University of Norway · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alkaline protease aeruginolysin (APR) is an important virulence factor in the evasion of the immune system by Pseudomonas aeruginosa (P. aeruginosa). The P. aeruginosa genome also encodes the highly potent and specific APR peptide inhibitor (APRin). However, the structural reason for the significant inhibition has not been revealed. Using ab initio molecular simulations, we here investigated the specific interactions between APR and APRin to elucidate which amino acid residues of APRin and APR contribute strongest to the inhibition. Since APR has a Zn

Indexed as

Models, MolecularAmino AcidsBacterial ProteinsBinding SitesBiological ProductsEndopeptidasesKineticsMolecular ConformationMolecular StructurePeptidesProtease InhibitorsProtein BindingPseudomonas aeruginosaalkaline proteaseAmino AcidsBacterial ProteinsBiological ProductsEndopeptidasesPeptidesProtease InhibitorsDrug designFragment molecular orbitalMetalloproteaseMolecular simulationProtein–protein interactionsProtonation

Identifiers

PMID34914017
OpenAlexW4226019493

What OpenQuestion holds

Textmetadata
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.