Evidence map›Paper›PMID 19689354›Full record

ReviewCurrent protein & peptide science2009

Extracellular proteases as targets for drug development.

Mare Cudic, Gregg B Fields

Abstract readReview
In one paragraph

Review in Current protein & peptide science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 82 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Genetics in Cartilage Lesions: Basic Science and Therapy Approaches.International journal of molecular sciences · 2020
    Review
  8. CD147 promotes collective invasion through cathepsin B in hepatocellular carcinoma.Journal of experimental & clinical cancer research : CR · 2020
    Article
  9. Review
  10. Article
  11. Frontiers in immunology · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Structural Principles in the Development of Cyclic Peptidic Enzyme Inhibitors.International journal of biological sciences · 2017
    Review
  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

2 authors at 1 institution in 1 country.

Mare CudicDepartment of Biochemistry, University of Texas Health Science Center, 7703 Floyd Curl Drive, San Antonio, TX 78229, USA.
Gregg B Fields
The University of Texas Health Science Center at San Antonio · US

Funding

Mechanism &Inhibition of Collagenolytic ActivityR01CA098799 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI FIELDS, GREGG B · 2003 to 2017
$4.5M
TISSUE ENGINEERING USING PEPTIDE AMPHIPHILE BIOMIMETICSR01EB000289 · NIBIB · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI FIELDS, GREGG B · 2002 to 2008
$1.3M
NCI NIH HHS CA98799NCI NIH HHS R01 CA098799NIBIB NIH HHS EB000289NIBIB NIH HHS R01 EB000289NIMH NIH HHS MH078948
6 · The paper itself

Abstract

Proteases constitute one of the primary targets in drug discovery. In the present review, we focus on extracellular proteases (ECPs) because of their differential expression in many pathophysiological processes, including cancer, cardiovascular conditions, and inflammatory, pulmonary, and periodontal diseases. Many new ECP inhibitors are currently under clinical investigation and a significant increase in new therapies based on protease inhibition can be expected in the coming years. In addition to directly blocking the activity of a targeted protease, one can take advantage of differential expression in disease states to selectively deliver therapeutic or imaging agents. Recent studies in targeted drug development for the metalloproteases (matrix metalloproteinases, adamalysins, pappalysins, neprilysin, angiotensin-converting enzyme, metallocarboxypeptidases, and glutamate carboxypeptidase II), serine proteases (elastase, coagulation factors, tissue/urokinase plasminogen activator system, kallikreins, tryptase, dipeptidyl peptidase IV) and cysteine proteases (cathepsin B) are discussed herein.

Indexed as

Drug DiscoveryProtease InhibitorsAnimalsExtracellular SpaceHumansPeptide HydrolasesPeptide HydrolasesProtease Inhibitors

Identifiers

PMID19689354
PMCPMC4339022
OpenAlexW2074440833

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.