Evidence map›Paper›PMID 34067041›Full record

ReviewInternational journal of molecular sciences2021

ADAM10 Site-Dependent Biology: Keeping Control of a Pervasive Protease.

Francesca Tosetti, Massimo Alessio, Alessandro Poggi, Maria Raffaella Zocchi

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

19 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. A Valuable Target for Therapy: The Metalloproteinase ADAM10.Current protein & peptide science · 2025
    Review
  11. Review
  12. Article
  13. Article
  14. A Bioengineering Strategy to Control ADAM10 Activity in Living Cells.International journal of molecular sciences · 2023
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. 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

4 authors at 2 institutions in 1 country.

Francesca TosettiMolecular Oncology and Angiogenesis Unit, IRCCS Ospedale Policlinico S. Martino Largo R. Benzi 10, 16132 Genoa, Italy.ORCID 0000-0001-8772-4834
Massimo AlessioProteome Biochemistry, IRCCS San Raffaele Scientific Institute, 20132 Milan, Italy.
Alessandro PoggiMolecular Oncology and Angiogenesis Unit, IRCCS Ospedale Policlinico S. Martino Largo R. Benzi 10, 16132 Genoa, Italy.ORCID 0000-0002-1860-430X
Maria Raffaella ZocchiDivision of Immunology, Transplants and Infectious Diseases, IRCCS San Raffaele Scientific Institute, 20132 Milan, Italy.
Ospedale Policlinico San Martino · ITVita-Salute San Raffaele University · IT

Funding

Associazione Italiana per la Ricerca sul Cancro IG-21648the 5x1000 2015 and 5x1000 2016 from the Italian Ministry of Health no number
6 · The paper itself

Abstract

Enzymes, once considered static molecular machines acting in defined spatial patterns and sites of action, move to different intra- and extracellular locations, changing their function. This topological regulation revealed a close cross-talk between proteases and signaling events involving post-translational modifications, membrane tyrosine kinase receptors and G-protein coupled receptors, motor proteins shuttling cargos in intracellular vesicles, and small-molecule messengers. Here, we highlight recent advances in our knowledge of regulation and function of A Disintegrin And Metalloproteinase (ADAM) endopeptidases at specific subcellular sites, or in multimolecular complexes, with a special focus on ADAM10, and tumor necrosis factor-α convertase (TACE/ADAM17), since these two enzymes belong to the same family, share selected substrates and bioactivity. We will discuss some examples of ADAM10 activity modulated by changing partners and subcellular compartmentalization, with the underlying hypothesis that restraining protease activity by spatial segregation is a complex and powerful regulatory tool.

Indexed as

ADAM10 ProteinAnimalsHumansModels, BiologicalProtein Processing, Post-TranslationalProtein TransportSignal TransductionSubstrate SpecificityADAM10 ProteinADAMADCcancerexosomesimmunomodulationmetalloproteinasessignalingsubcellular traffickingvesicles

Identifiers

PMID34067041
PMCPMC8124674
OpenAlexW3158319821

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.