Evidence map›Paper›PMID 19410608›Full record

ArticleBiochimica et biophysica acta2009

Tumor suppressive effect of lysyl oxidase proenzyme.

Sara Contente, Tze-Jou Annie Yeh, Robert M Friedman

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

7 citing papers in PubMed, 16 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Lysyl oxidase is associated with the epithelial-mesenchymal transition of gastric cancer cells in hypoxia.Gastric cancer : official journal of the International Gastric Cancer Association and the Japanese Gastric Cancer Association · 2016
    Article
  6. Human copper-dependent amine oxidases.Archives of biochemistry and biophysics · 2014
    Review
  7. 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

3 authors at 1 institution in 1 country.

Sara ContenteDepartment of Pathology, United States Military Cancer Institute, Uniformed Services University of the Health Sciences, Bethesda, Maryland, USA. scontente@usuhs.mil
Tze-Jou Annie Yeh
Robert M Friedman
Uniformed Services University of the Health Sciences · US

Funding

INHIBITION OF HUMAN ONCOGENE EXPRESSION BY INTERFERONR01CA037351 · NCI · U.S. UNIFORMED SERVICES UNIV OF HLTH SCI · PI FRIEDMAN, ROBERT M · 1985 to 2003
$699k
NCI NIH HHS R01 CA037351
6 · The paper itself

Abstract

Lysyl oxidase acts as both a matrix modifying enzyme and an oncogene suppressor. It is synthesized as a 50-kDa proenzyme, secreted, and processed into an approximately 30 kDa mature, active enzyme and an 18-kDa propeptide. The tumor suppressive effect of lysyl oxidase appears to be exerted within the cell, so the subcellular localization of protein forms was investigated. Propeptide-specific antibody detected 50-kDa proenzyme in cytoplasmic and nuclear extracts of non-transformed mouse fibroblasts, but free 18-kDa propeptide was not detected in any extract. Antibody to epitope near the N-terminus of mature lysyl oxidase detected the proenzyme product in non-transformed cells, and a 30-kDa cytoplasmic protein in both non-transformed and transformed cells. RNA interference reduced the expression of lysyl oxidase mRNA and 50-kDa proenzyme in non-transformed cells, but had no effect on 30-kDa protein, indicating that although this protein displays a lysyl oxidase epitope, it is not derived from lysyl oxidase message. The absence of both free 18-kDa propeptide and mature lysyl oxidase within non-transformed cells suggests that cellular reversion after restoration of lysyl oxidase gene expression is mediated by the 50-kDa proenzyme within cells.

Indexed as

AnimalsCell Line, TransformedEmbryo, MammalianEnzyme PrecursorsFibroblastsImmunoblottingMiceNIH 3T3 CellsPeptide FragmentsProtein BiosynthesisProtein-Lysine 6-OxidaseTranscription, GeneticTumor Suppressor ProteinsEnzyme PrecursorsPeptide FragmentsProtein-Lysine 6-OxidaseTumor Suppressor Proteins

Identifiers

PMID19410608
PMCPMC10197974
OpenAlexW2045055844

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.