ReviewJournal of molecular histology2004
Role of subtilisin-like convertases in cadherin processing or the conundrum to stall cadherin function by convertase inhibitors in cancer therapy.
Review in Journal of molecular histology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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.
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.
Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Potent inhibitors of furin and furin-like proprotein convertases containing decarboxylated P1 arginine mimetics.Journal of medicinal chemistry · 2010Article
- Intercellular junction assembly, dynamics, and homeostasis.Cold Spring Harbor perspectives in biology · 2010Review
- PC2/CPE-mediated pro-protein processing in tumor cells and its differentiated cells or tissues.Molecular and cellular endocrinology · 2009Article
- Peptide processing and biology in human disease.Current opinion in endocrinology, diabetes, and obesity · 2009Review
- Pro-protein convertase-2/carboxypeptidase-E mediated neuropeptide processing of RGC-5 cell after in vitro ischemia.Neuroscience bulletin · 2009Article
- Potential opportunity in the development of new therapeutic agents based on endogenous and exogenous inhibitors of the proprotein convertases.Medicinal research reviews · 2007Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cadherins are a family of intercellular adhesion receptors. Produced as inactive precursors, they become functional adhesion molecules after proteolytic cleavage by subtilisin-like pro-protein convertases (PCs). Owing to their activation and assembly into multiprotein adhesion complexes at sites of cell contacts, adhesion-competent cadherins are prerequisite for tissue integrity. In recent years evidence has accumulated that intercellular junctions not only provide mechanical linkage, but in addition are potent modulators of signalling cascades. This infers a biological role to intercellular adhesion complexes that is significantly more complex and powerful. Currently, the broad implications of disturbances in somatic tissue adhesion components are only just beginning to emerge. Prominent examples of adhesion defects include autoimmune diseases, or tumour invasion and metastasis and malignant transformation. This review reports on our current knowledge of cadherin function and their maturation by pro-protein convertases, and puts special emphasis on the consequences of pro-protein convertase inhibition for epithelial tissue homeostasis.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.