Evidence map›Paper›PMID 15770418›Full record

ReviewCellular and molecular life sciences : CMLS2005

Proteinaceous cysteine protease inhibitors.

G Dubin

Open access · bronzeAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.2field-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

32 citing papers in PubMed, 127 citations in OpenAlex.

  1. Review
  2. Article
  3. Refinement and curation of homologous groups facilitated by structure prediction.Protein science : a publication of the Protein Society · 2025
    Article
  4. Article
  5. Mechanisms Applied by Protein Inhibitors to Inhibit Cysteine Proteases.International journal of molecular sciences · 2021
    Review
  6. Cysteinyl cathepsins in cardiovascular diseases.Biochimica et biophysica acta. Proteins and proteomics · 2020
    Review
  7. Frontiers in bioengineering and biotechnology · 2020
    Article
  8. Expression of Cathepsin L and Its Intrinsic Inhibitors in Glomeruli of Rats With Puromycin Aminonucleoside Nephrosis.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2018
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Cysteine Protease Cathepsins in Atherosclerotic Cardiovascular Diseases.Journal of atherosclerosis and thrombosis · 2018
    Review
  14. Microbial inhibitors of cysteine proteases.Medical microbiology and immunology · 2016
    Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. 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

1 author at 1 institution in 1 country.

G DubinFaculty of Biotechnology, Jagiellonian University, ul. Gronostajowa 7, 30-387, Krakow, Poland. gdubin@mol.uj.edu.pl
Jagiellonian University · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Studies of proteinaceous cysteine protease inhibitors originated with the discovery of cystatins in the 1960s. Since that time, a rich and fascinating world of proteins that control and regulate a multitude of important physiological processes, ranging from the basics of protein turnover to development and brain function, has been uncovered. Failures in such important and complex systems inevitably lead to pathologies. Many threatening diseases such as cancer or neurological disorders, to mention only some, are attributed to deregulation of protease-inhibitor balance. Moreover, important aspects of infection pathology and host defense rely on proteolysis and protease inhibition. Recent advances in the field of protease inhibitors have drawn attention to the possible use of this collected knowledge to control related pathological processes. This review attempts to familiarize the reader with proteinaceous cysteine protease inhibitors by providing an overview of current knowledge. The work primarily highlights biological processes in which the inhibitors are involved and focuses on pathologies resulting from aberrant protease-inhibitor balance, pointing out emerging possibilities for their correction.

Indexed as

Cysteine Proteinase InhibitorsAmphibian ProteinsAnimalsBacterial ProteinsCalcium-Binding ProteinsCarrier ProteinsCystatinsFungal ProteinsHumansInhibitor of Apoptosis ProteinsInsulin-Like Growth Factor Binding ProteinsKininogensProteinsProtozoan ProteinsSerpinsViral ProteinsAmphibian ProteinsBacterial ProteinsCalcium-Binding ProteinscalpastatinCarrier Proteinschagasin, TrypanosomaClitocypin protein, Clitocybe nebularisCystatinsCysteine Proteinase InhibitorsequistatinFungal Proteinsinhibitor of apoptosis, NucleopolyhedrovirusInhibitor of Apoptosis ProteinsInsulin-Like Growth Factor Binding Proteinsinterleukin-1beta-converting enzyme inhibitorKininogensProteinsProtozoan Proteinssaxitoxin-binding protein, Rana catesbeianaSerpinsstaphostatin A, Staphylococcus epidermidisViral Proteins

Identifiers

PMID15770418
PMCPMC7079805
OpenAlexW2084104855

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.