Evidence map›Paper›PMID 31593799›Full record

ReviewCancer letters2019

ADAM proteases: Emerging role and targeting of the non-catalytic domains.

Nayanendu Saha, Dorothea Robev, Juha P Himanen, Dimitar B Nikolov

Open access · greenAbstract readReview
In one paragraph

Review in Cancer letters, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.3field-weighted citation impact, top 6% 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

43 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Fully human monoclonal antibody targeting activated ADAM10 on colorectal cancer cells.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2023
    Article
  19. Article
  20. ADAM10-a "multitasker" in sepsis: focus on its posttranslational target.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2023
    Review
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 1 institution in 1 country.

Nayanendu SahaSloan-Kettering Institute for Cancer Research, 1275 York Avenue, New York, NY, 10065, USA. Electronic address: sahan@mskcc.org.
Dorothea RobevSloan-Kettering Institute for Cancer Research, 1275 York Avenue, New York, NY, 10065, USA.
Juha P HimanenSloan-Kettering Institute for Cancer Research, 1275 York Avenue, New York, NY, 10065, USA.
Dimitar B NikolovSloan-Kettering Institute for Cancer Research, 1275 York Avenue, New York, NY, 10065, USA.
Kettering University · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SELWYN M VICKERS · 1985 to 2026
$347.4M
STRUCTURAL STUDY OF EPH RECEPTORS AND EPHRINSR01NS038486 · NINDS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI NIKOLOV, DIMITAR B · 1999 to 2018
$5.9M
Targeting EphA2 in GlioblastomaR01NS096956 · NINDS · CASE WESTERN RESERVE UNIVERSITY · PI WANG, BINGCHENG · 2016 to 2021
$2.6M
Function-blocking anti-ADAM protease antibodies for inhibition of tumorigenesisR21CA185930 · NCI · SLOAN-KETTERING INST CAN RESEARCH · PI NIKOLOV, DIMITAR B · 2015 to 2016
$421k
Trends and Disparities in Bladder Cancer TreatmentR21CA185931 · NCI · KAISER FOUNDATION RESEARCH INSTITUTE · PI DANFORTH, KIM N · 2014 to 2015
$402k
NCI NIH HHS P30 CA008748NCI NIH HHS R21 CA185930NCI NIH HHS R21 CA185931NINDS NIH HHS R01 NS038486NINDS NIH HHS R01 NS096956
6 · The paper itself

Abstract

ADAM proteases are multi domain transmembrane metalloproteases that cleave a range of cell surface proteins and activate signaling pathways implicated in tumor progression, including those mediated by Notch, EFGR, and the Eph receptors. Consequently, they have emerged as key therapeutic targets in the efforts to inhibit tumor initiation and progression. To that end, two main approaches have been taken to develop ADAM antagonists: (i) small molecule inhibitors, and (ii) monoclonal antibodies. In this mini-review we describe the distinct features of ADAM proteases, particularly of ADAM10 and ADAM17, their domain organization, conformational rearrangements, regulation, as well as their emerging importance as therapeutic targets in cancer. Further, we highlight an anti-ADAM10 monoclonal antibody that we have recently developed, which has shown significant promise in inhibiting Notch signaling and deterring growth of solid tumors in pre-clinical settings.

Indexed as

ADAM10 ProteinADAM17 ProteinADAM ProteinsAnimalsAntineoplastic Agents, ImmunologicalCatalytic DomainGene Expression Regulation, NeoplasticHumansNeoplasmsProtein ConformationProtein DomainsADAM10 ProteinADAM17 ProteinADAM17 protein, humanADAM ProteinsAntineoplastic Agents, ImmunologicalADAM10ADAM17IntegrinsNotch signalingTherapeutic antibody

Identifiers

PMID31593799
PMCPMC7485987
OpenAlexW2978946150

What OpenQuestion holds

Textmetadata
LicenceTDM
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.