Evidence map›Paper›PMID 15166260›Full record

ReviewJournal of clinical pathology2004

Membrane associated proteases and their inhibitors in tumour angiogenesis.

A Noel, C Maillard, N Rocks, M Jost, V Chabottaux, N E Sounni, E Maquoi, D Cataldo, J M Foidart

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of clinical pathology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

37 citing papers in PubMed, 110 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. The critical role of dysregulated FOXM1-PLAUR signaling in human colon cancer progression and metastasis.Clinical cancer research : an official journal of the American Association for Cancer Research · 2013
    Article
  13. Article
  14. Perlecan modulates VEGF signaling and is essential for vascularization in endochondral bone formation.Matrix biology : journal of the International Society for Matrix Biology · 2012
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Epithelial-to-mesenchymal transitions and circulating tumor cells.Journal of mammary gland biology and neoplasia · 2010
    Review
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

9 authors at 1 institution in 1 country.

A NoelLaboratory of Tumour and Development Biology, University of Liège, Sart Tilman, B-4000 Liège, Belgium. noel@ulg.ac.be
C Maillard
N Rocks
M Jost
V Chabottaux
N E Sounni
E Maquoi
D Cataldo
J M Foidart
University of Liège · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell surface proteolysis is an important mechanism for generating biologically active proteins that mediate a range of cellular functions and contribute to biological processes such as angiogenesis. Although most studies have focused on the plasminogen system and matrix metalloproteinases (MMPs), recently there has been an increase in the identification of membrane associated proteases, including serine proteases, ADAMs, and membrane-type MMPs (MT-MMPs). Normally, protease activity is tightly controlled by tissue inhibitors of MMPs (TIMPs) and plasminogen activator inhibitors (PAIs). The balance between active proteases and inhibitors is thought to determine the occurrence of proteolysis in vivo. High concentrations of proteolytic system components correlate with poor prognosis in many cancers. Paradoxically, high (not low) PAI-1 or TIMP concentrations predict poor survival in patients with various cancers. Recent observations indicate a much more complex role for protease inhibitors in tumour progression and angiogenesis than initially expected. As knowledge in the field of protease biology has improved, the unforeseen complexities of cell associated enzymes and their interaction with physiological inhibitors have emerged, often revealing unexpected mechanisms of action.

Indexed as

Cell MembraneEndopeptidasesHumansMatrix MetalloproteinasesNeoplasmsNeovascularization, PathologicProtease InhibitorsSerine EndopeptidasesTissue Inhibitor of MetalloproteinasesEndopeptidasesMatrix MetalloproteinasesProtease InhibitorsSerine EndopeptidasesTissue Inhibitor of Metalloproteinases

Identifiers

PMID15166260
PMCPMC1770325
OpenAlexW2008685071

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.