Evidence map›Paper›PMID 10077646›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Molecular cloning and characterization of prostase, an androgen-regulated serine protease with prostate-restricted expression.

P S Nelson, L Gan, C Ferguson, P Moss, R Gelinas, L Hood, K Wang

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
17.7field-weighted citation impact, top 1% 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

34 citing papers in PubMed, 218 citations in OpenAlex.

  1. Article
  2. KLK4T2 Is a Hormonally Regulated Transcript from theInternational journal of molecular sciences · 2021
    Article
  3. Review
  4. Crystal structure of the inhibitor-free form of the serine protease kallikrein-4.Acta crystallographica. Section F, Structural biology communications · 2019
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Protein-mediated enamel mineralization.Frontiers in bioscience (Landmark edition) · 2012
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

7 authors at 1 institution in 1 country.

P S NelsonDepartment of Molecular Biotechnology, University of Washington, Seattle, WA 98195, USA. psnels@u.washington.edu
L Gan
C Ferguson
P Moss
R Gelinas
L Hood
K Wang
University of Washington · US

Funding

MOLECULAR ALTERATIONS IN PROSTATE CANCER PROGRESSIONK08CA075173 · NCI · UNIVERSITY OF WASHINGTON · PI NELSON, PETER S · 1998 to 2002
$267k
NCI NIH HHS K08 CA75173-01A1
6 · The paper itself

Abstract

The identification of genes with selective expression in specific organs or cell types provides an entry point for understanding biological processes that occur uniquely within a particular tissue. Using a subtraction approach designed to identify genes preferentially expressed in specific tissues, we have identified prostase, a human serine protease with prostate-restricted expression. The prostase cDNA encodes a putative 254-aa polypeptide with a conserved serine protease catalytic triad and an amino-terminal pre-propeptide sequence, indicating a potential secretory function. The genomic sequence comprises five exons and four introns and contains multiple copies of a chromosome 19q-specific minisatellite repeat. Northern analysis indicates that prostase mRNA is expressed in hormonally responsive normal and neoplastic prostate epithelial tissues, but not in prostate stromal constituents. Prostase shares 35% amino acid identity with prostate-specific antigen (PSA) and 78% identity with the porcine enamel matrix serine proteinase 1, an enzyme involved in enamel matrix degradation and with a putative role in the disruption of intercellular junctions. Radiation-hybrid-panel mapping localized prostase to chromosome 19q13, a region containing several other serine proteases, including protease M, pancreatic/renal kallikrein hK1, and the prostate-specific kallikreins hK2 and hK3 (PSA). The sequence homology between prostase and other well-characterized serine proteases suggests several potential functional roles for the prostase protein that include the degradation of extracellular matrix and the activation of PSA and other proteases.

Indexed as

Gene Expression Regulation, EnzymologicAmino Acid SequenceAndrogensBase SequenceCloning, MolecularHumansMaleMolecular Sequence DataOrgan SpecificityProstateSequence AlignmentSequence Analysis, DNASerine EndopeptidasesAndrogensSerine Endopeptidases

Identifiers

PMID10077646
PMCPMC15904
OpenAlexW1966110638

What OpenQuestion holds

Texttitle and abstract
measurements read2
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.