Evidence map›Paper›PMID 21648000›Full record

ReviewProtein science : a publication of the Protein Society2011

The role of calcium ions in the stability and instability of a thermolysin-like protease.

V G H Eijsink, B W Matthews, G Vriend

Open access · bronzeAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Thermostable Proteases fromMicroorganisms · 2025
    Review
  5. Protein sociology of ProA, Mip and other secreted virulence factors at theFrontiers in cellular and infection microbiology · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Architecture and function of metallopeptidase catalytic domains.Protein science : a publication of the Protein Society · 2014
    Review
  19. Structure of gentlyase, the neutral metalloprotease of Paenibacillus polymyxa.Acta crystallographica. Section D, Biological crystallography · 2013
    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 3 institutions in 3 countries.

V G H EijsinkDepartment of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, Ås, Norway.
B W Matthews
G Vriend
Norwegian University of Life Sciences · NORadboud University Medical Center · NLUniversity of Oregon · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thermolysin and other secreted broad-specificity proteases, such as subtilisin or alpha-lytic protease, are produced as pre-pro-proteins that stay at least partially unfolded while in the cytosol. After secretion, the pro-proteases fold to their active conformations in a process that includes the autolytic removal of the pro-peptide. We review the life cycle of the thermolysin-like protease from Bacillus stearothermophilus in light of the calcium dependent stability and instability of the N-terminal domain. The protease binds calcium ions in the regions that are involved in the autolytic maturation process. It is generally assumed that the calcium ions contribute to the extreme stability of the protease, but experimental evidence for TLP-ste indicates that at least one of the calcium ions plays a regulatory role. We hypothesize that this calcium ion plays an important role as a switch that modulates the protease between stable and unstable states as appropriate to the biological need.

Indexed as

Amino Acid SequenceCalciumGeobacillus stearothermophilusMetalloendopeptidasesModels, MolecularMolecular Sequence DataProtein FoldingProtein StabilityCalciumMetalloendopeptidasesmicrobial metalloproteinases

Identifiers

PMID21648000
PMCPMC3189520
OpenAlexW1989641248

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.