Evidence map›Paper›PMID 26408415›Full record

ReviewBiochimie2016

Kallikreins - The melting pot of activity and function.

Magdalena Kalinska, Ulf Meyer-Hoffert, Tomasz Kantyka, Jan Potempa

Open access · greenAbstract readReview
In one paragraph

Review in Biochimie, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

54 citing papers in PubMed, 118 citations in OpenAlex.

  1. Article
  2. Article
  3. Drug Discovery Strategies for Kallikrein-Related Peptidases.International journal of molecular sciences · 2025
    Review
  4. Review
  5. Article
  6. The Evolution of Functional Amyloids and Their Impact on Host-Microbe Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Eosinophilic esophagitis: Immune mechanisms and therapeutic targets.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2022
    Review
  18. Review
  19. Article
  20. Review
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

4 authors at 2 institutions in 3 countries.

Magdalena KalinskaDepartment of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Krakow, Poland. Electronic address: magda.kalinska@uj.edu.pl.
Ulf Meyer-HoffertDepartment of Dermatology, University Hospital Schleswig-Holstein, Campus Kiel, Kiel, Germany. Electronic address: umeyerhoffert@dermatology.uni-kiel.de.
Tomasz KantykaMalopolska Center of Biotechnology, Jagiellonian University, Krakow, Poland. Electronic address: tomasz.kantyka@uj.edu.pl.
Jan PotempaDepartment of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Krakow, Poland; University of Louisville School of Densitry, Oral Health and Systemic Disease, Louisville, USA. Electronic address: jan.potempa@uj.edu.pl.
Jagiellonian University · PLUniversity Hospital Schleswig-Holstein · DE

Funding

BACTERIAL PROTEINASES IN PERIODONTAL DISEASER01DE009761 · NIDCR · UNIVERSITY OF LOUISVILLE · PI POTEMPA, JAN S · 1991 to 2012
$3.8M
NIDCR NIH HHS DE 09761NIDCR NIH HHS R01 DE009761
6 · The paper itself

Abstract

The human tissue kallikrein and kallikrein-related peptidases (KLKs), encoded by the largest contiguous cluster of protease genes in the human genome, are secreted serine proteases with diverse expression patterns and physiological roles. Because of the broad spectrum of processes that are modulated by kallikreins, these proteases are the subject of extensive investigations. This review brings together basic information about the biochemical properties affecting enzymatic activity, with highlights on post-translational modifications, especially glycosylation. Additionally, we present the current state of knowledge regarding the physiological functions of KLKs in major human organs and outline recent discoveries pertinent to the involvement of kallikreins in cell signaling and in viral infections. Despite the current depth of knowledge of these enzymes, many questions regarding the roles of kallikreins in health and disease remain unanswered.

Indexed as

Protein Processing, Post-TranslationalChromosomes, Human, Pair 19GlycosylationHumansKallikreinsModels, MolecularMultigene FamilyProtein Structure, SecondaryProtein Structure, TertiaryKallikreinsEGFEnzymatic activityGlycosylationKallikreinPSASerine proteases

Identifiers

PMID26408415
PMCPMC4747678
OpenAlexW1793418802

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.