Evidence map›Paper›PMID 33579029›Full record

ReviewMolecules (Basel, Switzerland)2021

Strategies to Target ADAM17 in Disease: From its Discovery to the iRhom Revolution.

Matteo Calligaris, Doretta Cuffaro, Simone Bonelli, Donatella Pia Spanò, Armando Rossello, Elisa Nuti, Simone Dario Scilabra

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
7.4field-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

78 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Proteases in intestinal health and disease.Nature reviews. Gastroenterology & hepatology · 2026
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Ménétrier disease: A clinical review.World journal of gastroenterology · 2025
    Review
  20. Article

18 more citing papers are in PubMed but not listed here.

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

7 authors at 3 institutions in 1 country.

Matteo CalligarisProteomics Group of Fondazione Ri.MED, Research Department IRCCS ISMETT (Istituto Mediterraneo per i Trapianti e Terapie ad Alta Specializzazione), via E. Tricomi 5, 90145 Palermo, Italy.
Doretta CuffaroDepartment of Pharmacy, University of Pisa, Via Bonanno 6, 56126 Pisa, Italy.
Simone BonelliProteomics Group of Fondazione Ri.MED, Research Department IRCCS ISMETT (Istituto Mediterraneo per i Trapianti e Terapie ad Alta Specializzazione), via E. Tricomi 5, 90145 Palermo, Italy.
Donatella Pia SpanòSTEBICEF (Dipartimento di Scienze e Tecnologie Biologiche Chimiche e Farmaceutiche), Università degli Studi di Palermo, Viale delle Scienze Ed. 16, 90128 Palermo, Italy.
Armando RosselloDepartment of Pharmacy, University of Pisa, Via Bonanno 6, 56126 Pisa, Italy.
Elisa NutiDepartment of Pharmacy, University of Pisa, Via Bonanno 6, 56126 Pisa, Italy.
Simone Dario ScilabraProteomics Group of Fondazione Ri.MED, Research Department IRCCS ISMETT (Istituto Mediterraneo per i Trapianti e Terapie ad Alta Specializzazione), via E. Tricomi 5, 90145 Palermo, Italy.
University of Pisa · ITRi.MED · ITUniversity of Palermo · IT

Funding

Fondazione CON IL SUD 2018-PDR-00799
6 · The paper itself

Abstract

For decades, disintegrin and metalloproteinase 17 (ADAM17) has been the object of deep investigation. Since its discovery as the tumor necrosis factor convertase, it has been considered a major drug target, especially in the context of inflammatory diseases and cancer. Nevertheless, the development of drugs targeting ADAM17 has been harder than expected. This has generally been due to its multifunctionality, with over 80 different transmembrane proteins other than tumor necrosis factor α (TNF) being released by ADAM17, and its structural similarity to other metalloproteinases. This review provides an overview of the different roles of ADAM17 in disease and the effects of its ablation in a number of in vivo models of pathological conditions. Furthermore, here, we comprehensively encompass the approaches that have been developed to accomplish ADAM17 selective inhibition, from the newest non-zinc-binding ADAM17 synthetic inhibitors to the exploitation of iRhom2 to specifically target ADAM17 in immune cells.

Indexed as

ADAM17 ProteinAnimalsAnti-Inflammatory AgentsAntineoplastic AgentsHumansInflammationIntracellular Signaling Peptides and ProteinsNeoplasmsADAM17 ProteinAnti-Inflammatory AgentsAntineoplastic AgentsIntracellular Signaling Peptides and ProteinsADAM17ectodomain sheddingEGFRiRhomsmetalloproteinasesTIMPsTNF

Identifiers

PMID33579029
PMCPMC7916773
OpenAlexW3127610985

What OpenQuestion 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 OpenQuestion graph.