Evidence map›Paper›PMID 24900296›Full record

ArticleACS medicinal chemistry letters2011

Sulfonate-containing thiiranes as selective gelatinase inhibitors.

Sebastian A Testero, Mijoon Lee, Rachel T Staran, Mana Espahbodi, Leticia I Llarrull, Marta Toth, Shahriar Mobashery, Mayland Chang

Open access · greenAbstract read
In one paragraph

Article in ACS medicinal chemistry letters, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 20% 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

13 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Review
  3. Targeting MMP-9 in Diabetic Foot Ulcers.Pharmaceuticals (Basel, Switzerland) · 2019
    Review
  4. Article
  5. Acceleration of diabetic wound healing using a novel protease-anti-protease combination therapy.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Selective water-soluble gelatinase inhibitor prodrugs.Journal of medicinal chemistry · 2011
    Article
  12. Article
  13. Role of matrix metalloproteinases and therapeutic benefits of their inhibition in spinal cord injury.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2011
    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

8 authors at 1 institution in 1 country.

Sebastian A TesteroDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.
Mijoon LeeDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.
Rachel T StaranDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.
Mana EspahbodiDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.
Leticia I LlarrullDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.
Marta TothDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.
Shahriar MobasheryDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.
Mayland ChangDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.
University of Notre Dame · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Matrix metalloproteinases (MMPs) are important zinc-dependent endopeptidases. Two members of this family of enzymes called gelatinases (MMP-2 and MMP-9) have been implicated in a number of human diseases, including cancer, neurological and cardiovascular diseases, and inflammation, to name a few. We describe in this report the preparation and evaluation of two structural types of thiirane inhibitors that show selectivity toward gelatinases. The biphenyl series targets both gelatinases, whereas the monophenyl analogues exhibit potent inhibition of only MMP-2. The latter structural type also exhibits improved water solubility and metabolic stability, both traits desirable for progress of these molecules forward in gelatinase-dependent animal models of disease.

Indexed as

matrix metalloproteinasesSlow-binding gelatinase inhibitorsthiiranes

Identifiers

PMID24900296
PMCPMC4018095
OpenAlexW2089669123

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.