Evidence map›Paper›PMID 28110559›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2017

Comparing hydrazine-derived reactive groups as inhibitors of quinone-dependent amine oxidases.

Ashley A Burke, Elizabeth S Severson, Shreya Mool, Maria J Solares Bucaro, Frederick T Greenaway, Charles E Jakobsche

Open access · goldAbstract readComparative Study
In one paragraph

Article in Journal of enzyme inhibition and medicinal chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.2field-weighted citation impact, top 45% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Article
  3. An in situ activity assay for lysyl oxidases.Communications biology · 2021
    Article
  4. 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

6 authors at 1 institution in 1 country.

Ashley A Burkea Carlson School of Chemistry and Biochemistry, Clark University , Worcester , MA , USA.
Elizabeth S Seversona Carlson School of Chemistry and Biochemistry, Clark University , Worcester , MA , USA.
Shreya Moola Carlson School of Chemistry and Biochemistry, Clark University , Worcester , MA , USA.
Maria J Solares Bucaroa Carlson School of Chemistry and Biochemistry, Clark University , Worcester , MA , USA.
Frederick T Greenawaya Carlson School of Chemistry and Biochemistry, Clark University , Worcester , MA , USA.
Charles E Jakobschea Carlson School of Chemistry and Biochemistry, Clark University , Worcester , MA , USA.
Clark University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysyl oxidase has emerged as an important enzyme in cancer metastasis. Its activity has been reported to become upregulated in several types of cancer, and blocking its activity has been shown to limit the metastatic potential of various cancers. The small-molecules phenylhydrazine and β-aminopropionitrile are known to inhibit lysyl oxidase; however, issues of stability, toxicity, and poorly defined mechanisms limit their potential use in medical applications. The experiments presented herein evaluate three other families of hydrazine-derived compounds - hydrazides, alkyl hydrazines, and semicarbazides - as irreversible inhibitors of lysyl oxidase including determining the kinetic parameters and comparing the inhibition selectivities for lysyl oxidase against the topaquinone-containing diamine oxidase from lentil seedlings. The results suggest that the hydrazide group may be a useful core functionality that can be developed into potent and selective inhibitors of lysyl oxidase and eventually find application in cancer metastasis research.

Indexed as

HydrazinesOxidoreductasesQuinonesHydrazinesOxidoreductasesQuinonesenzyme kineticshydrazineirreversible inhibitionLysyl oxidase

Identifiers

PMID28110559
PMCPMC6009937
OpenAlexW2581334425

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.