Evidence map›Paper›PMID 30925705›Full record

ArticleInternational journal of molecular sciences2019

Development of Chemical Tools to Monitor Human Kallikrein 13 (KLK13) Activity.

Natalia Gruba, Ewa Bielecka, Magdalena Wysocka, Anna Wojtysiak, Magdalena Brzezińska-Bodal, Kamila Sychowska, Magdalena Kalińska, Małgorzata Magoch, Aleksandra Pęcak, Katherine Falkowski and 11 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

9 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. 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

21 authors at 3 institutions in 4 countries.

Natalia GrubaFaculty of Chemistry, University of Gdansk, 80-308 Gdansk, Poland. natalia.gruba@ug.edu.pl.
Ewa BieleckaMalopolska Centre of Biotechnology, Jagiellonian University, 30-387 Krakow, Poland. ewa.bielecka@uj.edu.pl.ORCID 0000-0002-2631-6711
Magdalena WysockaFaculty of Chemistry, University of Gdansk, 80-308 Gdansk, Poland. magdalena.wysocka@ug.edu.pl.
Anna WojtysiakFaculty of Chemistry, University of Gdansk, 80-308 Gdansk, Poland. anna.wojtysiak@phdstud.ug.edu.pl.
Magdalena Brzezińska-BodalFaculty of Chemistry, University of Gdansk, 80-308 Gdansk, Poland. magdalena.brzezinska@phdstud.ug.edu.pl.
Kamila SychowskaFaculty of Chemistry, University of Gdansk, 80-308 Gdansk, Poland. kamila.sychowska@gmail.com.
Magdalena KalińskaFaculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, 30-387 Krakow, Poland. magda.kalinska@uj.edu.pl.
Małgorzata MagochMalopolska Centre of Biotechnology, Jagiellonian University, 30-387 Krakow, Poland. m.magoch@gmail.com.
Aleksandra PęcakMalopolska Centre of Biotechnology, Jagiellonian University, 30-387 Krakow, Poland. aleksandra.pecak@gmail.com.
Katherine FalkowskiMalopolska Centre of Biotechnology, Jagiellonian University, 30-387 Krakow, Poland. katherine.falkowski@doctoral.uj.edu.pl.ORCID 0000-0002-1470-256X
Magdalena WiśniewskaMalopolska Centre of Biotechnology, Jagiellonian University, 30-387 Krakow, Poland. wisienka.magdalena@gmail.com.ORCID 0000-0003-0107-926X
Laura SąsiadekMalopolska Centre of Biotechnology, Jagiellonian University, 30-387 Krakow, Poland. lmsasiadek@gmail.com.
Karolina PłazaFaculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, 30-387 Krakow, Poland. plaza.karolina@gmail.com.
Eileen KrollDepartment of Life Sciences and Chemistry, Jacobs University Bremen, 28759 Bremen, Germany. ek.eileenkroll@gmail.com.
Anastasija PejkovskaDepartment of Life Sciences and Chemistry, Jacobs University Bremen, 28759 Bremen, Germany. anja.pejkovska@gmail.com.ORCID 0000-0002-8727-544X
Maren RehdersDepartment of Life Sciences and Chemistry, Jacobs University Bremen, 28759 Bremen, Germany. m.rehders@jacobs-university.de.
Klaudia BrixDepartment of Life Sciences and Chemistry, Jacobs University Bremen, 28759 Bremen, Germany. k.brix@jacobs-university.de.
Grzegorz DubinMalopolska Centre of Biotechnology, Jagiellonian University, 30-387 Krakow, Poland. grzegorz.dubin@uj.edu.pl.ORCID 0000-0002-5535-5760
Tomasz KantykaMalopolska Centre of Biotechnology, Jagiellonian University, 30-387 Krakow, Poland. tomasz.kantyka@uj.edu.pl.ORCID 0000-0003-3023-2382
Jan PotempaFaculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, 30-387 Krakow, Poland. jan.potempa@uj.edu.pl.
Adam LesnerFaculty of Chemistry, University of Gdansk, 80-308 Gdansk, Poland. adam.lesner@ug.edu.pl.ORCID 0000-0001-8335-3431
Jagiellonian University · PLUniversity of Gdańsk · PLConstructor University · DE

Funding

Narodowe Centrum Nauki grant ID 211744, Ref. 2013/08/W/NZ1/00696Narodowe Centrum Nauki UMO-2013/08/W/NZ1/00696Narodowe Centrum Nauki UMO-2016/22/E/NZ5/00332
6 · The paper itself

Abstract

Kallikrein 13 (KLK13) was first identified as an enzyme that is downregulated in a subset of breast tumors. This serine protease has since been implicated in a number of pathological processes including ovarian, lung and gastric cancers. Here we report the design, synthesis and deconvolution of libraries of internally quenched fluorogenic peptide substrates to determine the specificity of substrate binding subsites of KLK13 in prime and non-prime regions (according to the Schechter and Berger convention). The substrate with the consensus sequential motive ABZ-Val-Arg-Phe-Arg-ANB-NH₂ demonstrated selectivity towards KLK13 and was successfully converted into an activity-based probe by the incorporation of a chloromethylketone warhead and biotin bait. The compounds described may serve as suitable tools to detect KLK13 activity in diverse biological samples, as exemplified by overexpression experiments and targeted labeling of KLK13 in cell lysates and saliva. In addition, we describe the development of selective activity-based probes targeting KLK13, to our knowledge the first tool to analyze the presence of the active enzyme in biological samples.

Indexed as

Amino Acid SequenceCell LineEnzyme AssaysHumansKallikreinsKineticsNeoplasmsPeptide LibraryPeptidesRecombinant ProteinsSubstrate SpecificityKallikreinsKLK13 protein, humanPeptide LibraryPeptidesRecombinant Proteinsactivity-based probecombinatorial chemistryfluorogenic substrateKLK13substrate specificity

Identifiers

PMID30925705
PMCPMC6479877
OpenAlexW2923051996

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.