Evidence map›Paper›PMID 27048482›Full record

ReviewMedical microbiology and immunology2016

Microbial inhibitors of cysteine proteases.

Mateusz Kędzior, Rafał Seredyński, Jan Gutowicz

Abstract readReview
PubMed Publisher
In one paragraph

Review in Medical microbiology and immunology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Proteases in intestinal health and disease.Nature reviews. Gastroenterology & hepatology · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Fungal evasion ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Review
  10. Plants (Basel, Switzerland) · 2024
    Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Omp19 EnablesFrontiers in immunology · 2019
    Article
  16. 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

3 authors at 1 institution in 1 country.

Mateusz KędziorDepartment of Physical Chemistry of Microorganisms, Institute of Genetics and Microbiology, University of Wrocław, Przybyszewskiego 63/77, 51-148, Wrocław, Poland. mateusz.kedzior@uwr.edu.pl.
Rafał SeredyńskiDepartment of Physical Chemistry of Microorganisms, Institute of Genetics and Microbiology, University of Wrocław, Przybyszewskiego 63/77, 51-148, Wrocław, Poland.
Jan GutowiczDepartment of Physical Chemistry of Microorganisms, Institute of Genetics and Microbiology, University of Wrocław, Przybyszewskiego 63/77, 51-148, Wrocław, Poland.
University of Wrocław · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cysteine proteases are one of the major classes of proteolytic enzymes involved in a number of physiological and pathological processes in plants, animals and microorganisms. When their synthesis, activity and localization in mammalian cells are altered, they may contribute to the development of many diseases, including rheumatoid arthritis, osteoporosis and cancer. Therefore, cysteine proteases have become promising drug targets for the medical treatment of these disorders. Inhibitors of cysteine proteases are also produced by almost every group of living organisms, being responsible for the control of intracellular proteolytic activity. Microorganisms synthesize cysteine protease inhibitors not only to regulate the activity of endogenous, often virulent enzymes, but also to hinder the host's proteolytic defense system and evade its immune responses against infections. Present work describes known to date microbial inhibitors of cysteine proteases in terms of their structure, enzyme binding mechanism, specificity and pathophysiological roles. The overview of both proteinaceous and small-molecule inhibitors produced by all groups of microorganisms (bacteria, archaea, fungi, protists) and viruses is provided. Subsequently, possible applications of microbial inhibitors in science, medicine and biotechnology are also highlighted.

Indexed as

ArchaeaBacteriaCysteine ProteasesCysteine Proteinase InhibitorsFungiSubstrate SpecificityVirulence FactorsVirusesCysteine ProteasesCysteine Proteinase InhibitorsVirulence FactorsApplicationCysteine proteaseInhibitorMicrobial inhibitorMicroorganismVirus

Identifiers

PMID27048482
OpenAlexW2334024520

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.