Evidence map›Paper›PMID 25698643›Full record

ReviewNature reviews. Drug discovery2015

Unleashing the therapeutic potential of human kallikrein-related serine proteases.

Ioannis Prassas, Azza Eissa, Gennadiy Poda, Eleftherios P Diamandis

Erratum issuedAbstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Drug discovery, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
16.6field-weighted citation impact, top 1% 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

111 citing papers in PubMed, 234 citations in OpenAlex.

  1. Article
  2. Fragment-Based Discovery of KLK6 and KLK7 Inhibitors.Journal of chemical information and modeling · 2026
    Article
  3. Article
  4. Human Kallikrein 2: A Novel Lineage-Specific Surface Target in Prostate Cancer.Clinical cancer research : an official journal of the American Association for Cancer Research · 2025
    Article
  5. Article
  6. Pharmacophore-driven antibody discovery on the yeast surface.bioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Cnidarian toxins: omics approaches and recombinant proteins.The journal of venomous animals and toxins including tropical diseases · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Deletion of Kallikrein-related peptidases (microPublication biology · 2024
    Article
  19. Article
  20. Article

51 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors at 3 institutions in 1 country.

Ioannis Prassas1] Department of Pathology and Laboratory Medicine, Mount Sinai Hospital, Toronto, M5G 1X5, Canada. [2] Department of Clinical Biochemistry, University Health Network, Toronto, M5G 2C4, Canada. [3].
Azza Eissa1] Department of Pathology and Laboratory Medicine, Mount Sinai Hospital, Toronto, M5G 1X5, Canada. [2] Department of Clinical Biochemistry, University Health Network, Toronto, M5G 2C4, Canada. [3].
Gennadiy Poda1] Drug Discovery Program, Ontario Institute for Cancer Research, Toronto, M5G 0A3, Canada. [2] Leslie Dan Faculty of Pharmacy, University of Toronto, Toronto, M5S 3M2, Canada.
Eleftherios P Diamandis1] Department of Pathology and Laboratory Medicine, Mount Sinai Hospital, Toronto, M5G 1X5, Canada. [2] Department of Clinical Biochemistry, University Health Network, Toronto, M5G 2C4, Canada.
Mount Sinai Hospital · CAOntario Institute for Cancer Research · CAUniversity Health Network · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tissue kallikreins are a family of fifteen secreted serine proteases encoded by the largest protease gene cluster in the human genome. In the past decade, substantial progress has been made in characterizing the natural substrates, endogenous inhibitors and in vivo functions of kallikreins, and studies have delineated important pathophysiological roles for these proteases in a variety of tissues. Thus, kallikreins are now considered attractive targets for the development of novel therapeutics for airway, cardiovascular, tooth, brain, skin and neoplastic diseases. In this Review, we discuss recent advances in our understanding of the physiological functions and pathological implications of kallikrein proteases, and highlight progress in the identification of kallikrein inhibitors, which together are bringing us closer to therapeutically targeting kallikreins in selected disease settings.

Indexed as

AnimalsHumansModels, MolecularSerine ProteasesSerine Proteinase InhibitorsTissue KallikreinsSerine ProteasesSerine Proteinase InhibitorsTissue Kallikreins

Identifiers

PMID25698643
OpenAlexW2004101774

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.