Evidence map›Paper›PMID 9032441›Full record

ArticleThe Biochemical journal1997

PACE4: a subtilisin-like endoprotease with unique properties.

R E Mains, C A Berard, J B Denault, A Zhou, R C Johnson, R Leduc

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

16 citing papers in PubMed, 59 citations in OpenAlex.

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  13. Mutational analysis of predicted interactions between the catalytic and P domains of prohormone convertase 3 (PC3/PC1).Proceedings of the National Academy of Sciences of the United States of America · 2003
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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.

R E MainsDepartment of Neuroscience, The Johns Hopkins University School of Medicine, Baltimore, MD 21205-2185, U.S.A.
C A Berard
J B Denault
A Zhou
R C Johnson
R Leduc
Université de Sherbrooke · CA

Funding

UNDERSTANDING NO SIGNALING RESULTING IN NEUROPROTECTION.P50DA000266 · NIDA · JOHNS HOPKINS UNIVERSITY · PI WORLEY, PAUL F · 1985 to 2017
$45.2M
NIDA NIH HHS DA- 000266NIDA NIH HHS P50 DA000266PHS HHS 0GP-0171374
6 · The paper itself

Abstract

PACE4 is one of the neuroendocrine-specific mammalian subtilisin-related endoproteases believed to function in the secretory pathway. The biosynthesis and secretion of PACE4 have been studied using transfected neuroendocrine and fibroblast cell lines. as well as primary pituitary cultures. ProPACE4 (approx. 106 kDa) is cleaved intracellularly before secretion of PACE4 (approx. 97 kDa); the N-terminal propeptide cleavage is accelerated in a truncated form of PACE4 lacking the Cys-rich C-terminal region (PACE4s). Neither PACE4 nor PACE4s is stored in regulated neuroendocrine secretory granules, whereas pro-opiomelanocortin-derived peptides and prohormone convertase I enter the regulated secretory pathway efficiently. The relatively slow cleavage of the proregion of proPACE4 in primary anterior pituitary cells, followed by rapid secretion of PACE4, is similar to the results for proPACE4 in transfected cell lines. The enzyme activity of PACE4 is distinct from furin and prohormone convertases, both in the marked sensitivity of PACE4 to inhibition by leupeptin and the relative insensitivity of PACE4 to inhibition by Ca2+ chelators and dithiothreitol; PACE4 is not inhibited by the alpha1-antitrypsin Portland variant that is very potent at inhibiting furin. The unique biosynthetic and enzymic patterns seen for PACE4 suggest a role for this neuroendocrine-specific subtilisin-like endoprotease outside the pathway for peptide biosynthesis.

Indexed as

beta-Endorphinbeta-LipotropinBlotting, WesternCells, CulturedCloning, MolecularDNA, ComplementaryElectrophoresis, Polyacrylamide GelEndonucleasesEnzyme InhibitorsFurinGene ExpressionHumansImmunohistochemistryPituitary GlandProprotein ConvertasesProtein Processing, Post-Translationalbeta-Endorphinbeta-LipotropinDNA, ComplementaryEndonucleasesEnzyme InhibitorsFurinPCSK6 protein, humanProprotein ConvertasesSerine EndopeptidasesSubtilisins

Identifiers

PMID9032441
PMCPMC1218110
OpenAlexW1490680197

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.