Evidence map›Paper›PMID 20539873›Full record

ReviewMolecular bioSystems2010

Allosteric regulation of protease activity by small molecules.

Aimee Shen

Open access · greenAbstract readReview
In one paragraph

Review in Molecular bioSystems, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.0field-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

26 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Allosterically switchable network orientsProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Inhibitory antibodies identify unique sites of therapeutic vulnerability in rhinovirus and other enteroviruses.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  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

1 author at 1 institution in 1 country.

Aimee ShenDepartment of Pathology, Stanford School of Medicine, Stanford, California 94305, USA. ashen2@stanford.edu
Stanford Medicine · US

Funding

Chemically Interrogating Clostridium difficile Glucosylating Toxin ActivationK99GM092934 · NIGMS · STANFORD UNIVERSITY · PI SHEN, AIMEE · 2010 to 2010
$82k
NIGMS NIH HHS K99 GM092934
6 · The paper itself

Abstract

Proteases regulate a plethora of biological processes. Because they irreversibly cleave peptide bonds, the activity of proteases is strictly controlled. While there are many ways to regulate protease activity, an emergent mechanism is the modulation of protease function by small molecules acting at allosteric sites. This mode of regulation holds the potential to allow for the specific and temporal control of a given biological process using small molecules. These compounds also serve as useful tools for studying protein dynamics and function. This review highlights recent advances in identifying and characterizing natural and synthetic small molecule allosteric regulators of proteases and discusses their utility in studies of protease function, drug discovery and protein engineering.

Indexed as

Allosteric RegulationAllosteric SiteAnimalsBacterial ToxinsEnzyme ActivationHumansLigandsModels, BiologicalModels, MolecularMolecular WeightPeptide HydrolasesSmall Molecule LibrariesBacterial ToxinsLigandsPeptide HydrolasesSmall Molecule Libraries

Identifiers

PMID20539873
PMCPMC4356121
OpenAlexW2034970659

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.