Evidence map›Paper›PMID 21406063›Full record

ReviewThe Biochemical journal2011

Proteases as therapeutics.

Charles S Craik, Michael J Page, Edwin L Madison

Open access · greenAbstract readReview
In one paragraph

Review in The Biochemical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
5.8field-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

79 citing papers in PubMed, 238 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Latin American Natural Product Database (LANaPDB): An Update.Journal of chemical information and modeling · 2024
    Article
  17. Article
  18. Article
  19. Review
  20. Cold-Adapted Proteases: An Efficient and Energy-Saving Biocatalyst.International journal of molecular sciences · 2023
    Review

19 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

3 authors at 2 institutions in 1 country.

Charles S CraikDepartment of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, CA 94131, USA. craik@cgl.ucsf.edu
Michael J Page
Edwin L Madison
University of California, San Francisco · USCatalyst Biosciences (United States) · US

Funding

A Technological Platform for the Identification of Serine Proteases in CancerR01CA128765 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CRAIK, CHARLES SCOTT · 2009 to 2011
$1.1M
Extracellular Proteolysis as a Molecular Stratification Tool for CancerR21CA186077 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CRAIK, CHARLES SCOTT · 2014 to 2015
$370k
NCI NIH HHS R01 CA128765NCI NIH HHS R21 CA186077
6 · The paper itself

Abstract

Proteases are an expanding class of drugs that hold great promise. The U.S. FDA (Food and Drug Administration) has approved 12 protease therapies, and a number of next generation or completely new proteases are in clinical development. Although they are a well-recognized class of targets for inhibitors, proteases themselves have not typically been considered as a drug class despite their application in the clinic over the last several decades; initially as plasma fractions and later as purified products. Although the predominant use of proteases has been in treating cardiovascular disease, they are also emerging as useful agents in the treatment of sepsis, digestive disorders, inflammation, cystic fibrosis, retinal disorders, psoriasis and other diseases. In the present review, we outline the history of proteases as therapeutics, provide an overview of their current clinical application, and describe several approaches to improve and expand their clinical application. Undoubtedly, our ability to harness proteolysis for disease treatment will increase with our understanding of protease biology and the molecular mechanisms responsible. New technologies for rationally engineering proteases, as well as improved delivery options, will expand greatly the potential applications of these enzymes. The recognition that proteases are, in fact, an established class of safe and efficacious drugs will stimulate investigation of additional therapeutic applications for these enzymes. Proteases therefore have a bright future as a distinct therapeutic class with diverse clinical applications.

Indexed as

AnimalsCardiovascular DiseasesDrug Delivery SystemsGenetic TherapyHumansHydrolysisPeptide HydrolasesProtein EngineeringRecombinant ProteinsPeptide HydrolasesRecombinant Proteins

Identifiers

PMID21406063
PMCPMC4503466
OpenAlexW1980537409

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.