Evidence map›Paper›PMID 8341687›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1993

cDNA structure of the mouse and rat subtilisin/kexin-like PC5: a candidate proprotein convertase expressed in endocrine and nonendocrine cells.

J Lusson, D Vieau, J Hamelin, R Day, M Chrétien, N G Seidah

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
9.0field-weighted citation impact, top 2% 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

57 citing papers in PubMed, 223 citations in OpenAlex.

  1. Review
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  6. Validation of the manufacturing process used to produce long-acting recombinant factor IX Fc fusion protein.Haemophilia : the official journal of the World Federation of Hemophilia · 2014
    Article
  7. Review
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  9. Proprotein convertases play an important role in regulating PKGI endoproteolytic cleavage and nuclear transport.American journal of physiology. Lung cellular and molecular physiology · 2013
    Article
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  11. Review
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  19. In vivo functions of the proprotein convertase PC5/6 during mouse development: Gdf11 is a likely substrate.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  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

6 authors at 1 institution in 1 country.

J LussonJ. A. DeSève Laboratorie of Biochemical Neuroendocrinology, Clinical Research Institute of Montreal, PQ, Canada.
D Vieau
J Hamelin
R Day
M Chrétien
N G Seidah
Montreal Clinical Research Institute · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

By using reverse transcriptase/PCR and oligonucleotide sequences derived from conserved segments (including the conserved RRGDL sequence) of the known proprotein convertases (PCs) PC1, PC2, furin, and PC4, we identified a subtilisin/kexin-like PC called PC5 in both mouse and rat tissues. The composite structure (2.85 kb) was deduced from the analysis of the reverse transcription/PCR products combined with the sequence from a clone isolated from a cDNA library made from corticotropin-activated mouse adrenocortical Y1 cells. The deduced cDNA structures of mouse PC5 and rat PC5 showed that the closest homologue is PACE4. Furthermore, like furin, Drosophila melanogaster (d) dfurin2, and PACE4, PC5 shows the presence of a C-terminal Cys-rich domain containing either 5 (PC5 and PACE4) or 10 (dfurin2) repeats of the consensus motif Cys-Xaa2-Cys-Xaa3-Cys-Xaa(5-7)-Cys-Xaa2-Cys-Xaa (8-15)-Cys-Xaa3-Cys-Xaa(9-16). The richest sources of rat PC5 mRNA (3.8 kb) are the adrenal and gut, but it can also be detected in many endocrine and nonendocrine tissues. Corticotropin-stimulated adrenocortical Y1 cells showed an increased expression of PC5 mRNA, suggesting an upregulation by cAMP. In situ hybridization of rat brain sections demonstrated a unique distribution of PC5 compared to PC1, PC2, and furin.

Indexed as

Proprotein ConvertasesProtein Processing, Post-TranslationalSaccharomyces cerevisiae ProteinsAdrenal GlandsAmino Acid SequenceAnimalsBase SequenceBrain ChemistryIn Situ HybridizationMiceMolecular Sequence DataProprotein Convertase 5Protein PrecursorsRatsRNA, MessengerSequence Analysis, DNAKEX2 protein, S cerevisiaePcsk6 protein, mousePcsk6 protein, ratpropeptide convertase 5, mousepropeptide convertase 5, ratProprotein Convertase 5Proprotein ConvertasesProtein PrecursorsRNA, MessengerSaccharomyces cerevisiae ProteinsSerine EndopeptidasesSubtilisins

Identifiers

PMID8341687
PMCPMC46998
OpenAlexW1980284138

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.