Evidence map›Paper›PMID 19300906›Full record

ReviewCellular and molecular life sciences : CMLS2009

Processing of peptide and hormone precursors at the dibasic cleavage sites.

Mohamed Rholam, Christine Fahy

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

35 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Article
  7. ScrepYard: An online resource for disulfide-stabilized tandem repeat peptides.Protein science : a publication of the Protein Society · 2023
    Article
  8. Review
  9. Article
  10. Antimicrobial Peptides as Anti-Infective Agents in Pre-Post-Antibiotic Era?International journal of molecular sciences · 2019
    Review
  11. Review
  12. Article
  13. Biosynthesis of human myeloperoxidase.Archives of biochemistry and biophysics · 2018
    Review
  14. Review
  15. PTHrP(12-48) Modulates the Bone Marrow Microenvironment and Suppresses Human Osteoclast Differentiation and Lifespan.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. 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

2 authors at 1 institution in 1 country.

Mohamed RholamInterfaces, Traitements, Organisation et Dynamique des Systrèmes, Université Paris Diderot (Paris 7), CNRS UMR 7086, Bâtiment Lavoisier, 15 rue Jean-Antoine de Baïf, 75205, Paris Cedex 13, France. mohamed.rholam@univ-paris-diderot.fr
Christine Fahy
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many functionally important cellular peptides and proteins, including hormones, neuropeptides, and growth factors, are synthesized as inactive precursor polypeptides, which require post-translational proteolytic processing to become biologically active polypeptides. This is achieved by the action of a relatively small number of proteases that belong to a family of seven subtilisin-like proprotein convertases (PCs) including furin. In view of this, this review focuses on the importance of privileged secondary structures and of given amino acid residues around basic cleavage sites in substrate recognition by these endoproteases. In addition to their participation in normal cell functions, PCs are crucial for the initiation and progress of many important diseases. Hence, these proteases constitute potential drug targets in medicine. Accordingly, this review also discusses the approaches used to shed light on the cleavage preference and the substrate specificity of the PCs, a prerequisite to select which PCs are promising drug targets in each disease.

Indexed as

Amino Acid SequenceAnimalsHormonesHumansModels, MolecularMolecular Sequence DataNeuropeptidesProprotein ConvertasesProtein PrecursorsProtein Processing, Post-TranslationalProtein Structure, SecondaryHormonesNeuropeptidesProprotein ConvertasesProtein Precursors

Identifiers

PMID19300906
PMCPMC11115611
OpenAlexW2054809740

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.