Evidence map›Paper›PMID 27898009›Full record

ReviewInternational journal of molecular sciences2016

Effects of Glycosylation on the Enzymatic Activity and Mechanisms of Proteases.

Peter Goettig

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

48 citing papers in PubMed, 124 citations in OpenAlex.

  1. Iterative evolution ofSynthetic and systems biotechnology · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Proteases in intestinal health and disease.Nature reviews. Gastroenterology & hepatology · 2026
    Review
  7. Drug Discovery Strategies for Kallikrein-Related Peptidases.International journal of molecular sciences · 2025
    Review
  8. Journal of proteome research · 2025
    Article
  9. Article
  10. Review
  11. Implications of Mucin-TypeMolecules (Basel, Switzerland) · 2025
    Review
  12. Review
  13. Substrate O-glycosylation actively regulates extracellular proteolysis.Protein science : a publication of the Protein Society · 2024
    Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  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.

Peter GoettigStructural Biology Group, Faculty of Molecular Biology, University of Salzburg, Billrothstrasse 11, 5020 Salzburg, Austria. peter.goettig@sbg.ac.at.
University of Salzburg · AT

Funding

Austrian Science Fund FWF P 25003
6 · The paper itself

Abstract

Posttranslational modifications are an important feature of most proteases in higher organisms, such as the conversion of inactive zymogens into active proteases. To date, little information is available on the role of glycosylation and functional implications for secreted proteases. Besides a stabilizing effect and protection against proteolysis, several proteases show a significant influence of glycosylation on the catalytic activity. Glycans can alter the substrate recognition, the specificity and binding affinity, as well as the turnover rates. However, there is currently no known general pattern, since glycosylation can have both stimulating and inhibiting effects on activity. Thus, a comparative analysis of individual cases with sufficient enzyme kinetic and structural data is a first approach to describe mechanistic principles that govern the effects of glycosylation on the function of proteases. The understanding of glycan functions becomes highly significant in proteomic and glycomic studies, which demonstrated that cancer-associated proteases, such as kallikrein-related peptidase 3, exhibit strongly altered glycosylation patterns in pathological cases. Such findings can contribute to a variety of future biomedical applications.

Indexed as

GlycoproteinsGlycosylationKineticsPeptide HydrolasesPolysaccharidesProteomicsSubstrate SpecificityGlycoproteinsPeptide HydrolasesPolysaccharidescore glycanenzyme kineticsflexible loopsMichaelis constantN-glycosylationO-glycosylationsecreted proteasesequonsubstrate recognitionturnover number

Identifiers

PMID27898009
PMCPMC5187769
OpenAlexW2554188434

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.