Evidence map›Paper›PMID 20507279›Full record

ReviewThe Biochemical journal2010

The cutting edge: membrane-anchored serine protease activities in the pericellular microenvironment.

Toni M Antalis, Marguerite S Buzza, Kathryn M Hodge, John D Hooper, Sarah Netzel-Arnett

Abstract readReview
In one paragraph

Review in The Biochemical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
–field-weighted citation impact, top 96% 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

76 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
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  9. Article
  10. Treatment of ovarian cancer with modified anthrax toxin.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
  12. Article
  13. Article
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  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

16 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Toni M AntalisCenter for Vascular and Inflammatory Diseases and Department of Physiology, University of Maryland School of Medicine, Baltimore, MD 21201, USA. tantalis@som.umaryland.edu
Marguerite S Buzza
Kathryn M Hodge
John D Hooper
Sarah Netzel-Arnett
Queensland University of Technology · AU

Funding

UNIVERSITY OF MARYLAND GREENEBAUM CANCER CENTERSUPPORT GRANTP30CA134274 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI FEYRUZ VIRGILIA RASSOOL · 2008 to 2026
$51.0M
New Function for the Serpin PAI-2 as a Regulator of pRbR01CA098369 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI ANTALIS, TONI M. · 2003 to 2007
$1.5M
Vascular Remodeling by Membrane Serine ProteasesR01HL084387 · NHLBI · UNIVERSITY OF MARYLAND BALTIMORE · PI ANTALIS, TONI M · 2007 to 2010
$1.5M
Protease Pathways in the Gastrointestinal TractR01DK081376 · NIDDK · UNIVERSITY OF MARYLAND BALTIMORE · PI ANTALIS, TONI M · 2009 to 2010
$675k
NEW FUNCTION SERPIN PAI 2 AS A REGULAR OF RBR56CA098369 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI ANTALIS, TONI M · 2009 to 2009
$316k
NCI NIH HHS CA098369NCI NIH HHS P30 CA134274NCI NIH HHS R01 CA098369NCI NIH HHS R56 CA098369NHLBI NIH HHS HL084387NHLBI NIH HHS R01 HL084387NIDDK NIH HHS DK081376NIDDK NIH HHS R01 DK081376
6 · The paper itself

Abstract

The serine proteases of the trypsin-like (S1) family play critical roles in many key biological processes including digestion, blood coagulation, and immunity. Members of this family contain N- or C-terminal domains that serve to tether the serine protease catalytic domain directly to the plasma membrane. These membrane-anchored serine proteases are proving to be key components of the cell machinery for activation of precursor molecules in the pericellular microenvironment, playing vital functions in the maintenance of homoeostasis. Substrates activated by membrane-anchored serine proteases include peptide hormones, growth and differentiation factors, receptors, enzymes, adhesion molecules and viral coat proteins. In addition, new insights into our understanding of the physiological functions of these proteases and their involvement in human pathology have come from animal models and patient studies. The present review discusses emerging evidence for the diversity of this fascinating group of membrane serine proteases as potent modifiers of the pericellular microenvironment through proteolytic processing of diverse substrates. We also discuss the functional consequences of the activities of these proteases on mammalian physiology and disease.

Indexed as

AnimalsCell MembraneHumansSerine ProteasesSubstrate SpecificitySerine Proteases

Identifiers

PMID20507279
PMCPMC3680374
OpenAlexW1501052315

What OpenQuestion holds

Textmetadata
LicenceTDM
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.