Evidence map›Paper›PMID 28754951›Full record

ArticleScientific reports2017

Mass spectrometry-based determination of Kallikrein-related peptidase 7 (KLK7) cleavage preferences and subsite dependency.

Lakmali Munasinghage Silva, Thomas Stoll, Thomas Kryza, Carson Ryan Stephens, Marcus Lachlan Hastie, Helen Frances Irving-Rodgers, Ying Dong, Jeffrey John Gorman, Judith Ann Clements

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

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

3 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. 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 at 4 institutions in 1 country.

Lakmali Munasinghage SilvaQueensland University of Technology (QUT), Institute of Health and Biomedical Innovation (IHBI) and School of Biomedical Sciences at the Translational Research Institute, 37 Kent Street, Woolloongabba, Queensland, 4102, Australia.
Thomas StollQIMR Berghofer Medical Research Institute, 300 Herston Road, Herston, Queensland, 4006, Australia.
Thomas KryzaQueensland University of Technology (QUT), Institute of Health and Biomedical Innovation (IHBI) and School of Biomedical Sciences at the Translational Research Institute, 37 Kent Street, Woolloongabba, Queensland, 4102, Australia.
Carson Ryan StephensQueensland University of Technology (QUT), Institute of Health and Biomedical Innovation (IHBI) and School of Biomedical Sciences at the Translational Research Institute, 37 Kent Street, Woolloongabba, Queensland, 4102, Australia.
Marcus Lachlan HastieQIMR Berghofer Medical Research Institute, 300 Herston Road, Herston, Queensland, 4006, Australia.
Helen Frances Irving-RodgersSchool of Medical Science, Griffith University Gold Coast Campus, Parklands Drive, Southport, Queensland, 4215, Australia.
Ying DongQueensland University of Technology (QUT), Institute of Health and Biomedical Innovation (IHBI) and School of Biomedical Sciences at the Translational Research Institute, 37 Kent Street, Woolloongabba, Queensland, 4102, Australia.
Jeffrey John GormanQIMR Berghofer Medical Research Institute, 300 Herston Road, Herston, Queensland, 4006, Australia.
Judith Ann ClementsQueensland University of Technology (QUT), Institute of Health and Biomedical Innovation (IHBI) and School of Biomedical Sciences at the Translational Research Institute, 37 Kent Street, Woolloongabba, Queensland, 4102, Australia. j.clements@qut.edu.au.
Translational Research Institute · AUQIMR Berghofer Medical Research Institute · AUGriffith University · AUQueensland University of Technology · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cleavage preferences of Kallikrein-related peptidase 7 (KLK7) have previously been delineated using synthetic peptide libraries of fixed length, or single protein chains and have suggested that KLK7 exerts a chymotryptic-like cleavage preference. Due to the short length of the peptides utilised, only a limited number of subsites have however been assessed. To determine the subsite preferences of KLK7 in a global setting, we used a mass spectrometry (MS)-based in-depth proteomics approach that utilises human proteome-derived peptide libraries of varying length, termed Proteomic Identification of protease Cleavage Sites (PICS). Consistent with previous findings, KLK7 was found to exert chymotryptic-like cleavage preferences. KLK7 subsite preferences were also characterised in the P2-P2' region, demonstrating a preference for hydrophobic residues in the non-prime and hydrophilic residues in the prime subsites. Interestingly, single catalytic triad mutant KLK7 (mKLK7; S195A) also showed residual catalytic activity (k

Indexed as

Amino Acid SubstitutionCatalytic DomainHEK293 CellsHumansKallikreinsMass SpectrometryPichiaProteolysisProteomeSubstrate SpecificityKallikreinsKLK7 protein, humanProteome

Identifiers

PMID28754951
PMCPMC5533777
OpenAlexW2739278322

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.