Evidence map›Paper›PMID 29550974›Full record

ReviewCellular and molecular life sciences : CMLS2018

The pleiotropic roles of ADAM9 in the biology of solid tumors.

Victor O Oria, Paul Lopatta, Oliver Schilling

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed, 1 pooled it
2.8field-weighted citation impact, top 9% 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, 1 synthesis or guideline pooled it, 59 citations in OpenAlex.

  1. Pooled it
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  10. B4GALT5 inhibits CD8Journal for immunotherapy of cancer · 2025
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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

3 authors at 1 institution in 1 country.

Victor O OriaInstitute of Molecular Medicine and Cell Research, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
Paul LopattaInstitute of Molecular Medicine and Cell Research, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
Oliver SchillingInstitute of Molecular Medicine and Cell Research, Faculty of Medicine, University of Freiburg, Freiburg, Germany. oliver.schilling@mol-med.uni-freiburg.de.ORCID 0000-0001-7678-7653
University of Freiburg · DE

Funding

Deutsche Forschungsgemeinschaft (DE) EXC 294Deutsche Forschungsgemeinschaft (DE) GR 1748/6Deutsche Forschungsgemeinschaft (DE) GSC-4Deutsche Forschungsgemeinschaft (DE) INST 39/900-1Deutsche Forschungsgemeinschaft (DE) SCHI 871/11Deutsche Forschungsgemeinschaft (DE) SCHI 871/5Deutsche Forschungsgemeinschaft (DE) SCHI 871/6Deutsche Forschungsgemeinschaft (DE) SFB850-Project B8
6 · The paper itself

Abstract

A disintegrin and a metalloprotease (ADAM) 9 is a metzincin cell-surface protease involved in several biological processes such as myogenesis, fertilization, cell migration, inflammatory response, proliferation, and cell-cell interactions. ADAM9 has been found over-expressed in several solid tumors entities such as glioma, melanoma, prostate cancer, pancreatic ductal adenocarcinoma, gastric, breast, lung, and liver cancers. Immunohistochemical analyses highlight ADAM9 expression by actual cancer cells and associate its abundant presence with clinicopathological features such as shortened overall survival, poor tumor grade, de-differentiation, therapy resistance, and metastasis formation. In each of these tumors, ADAM9 may contribute to tumor biology via proteolytic or non-proteolytic mechanisms. For example, in liver cancer, ADAM9 has been found to shed MHC class I polypeptide-related sequence A, contributing towards the evasion of tumor immunity. ADAM9 may also contribute to tumor biology in non-proteolytic ways probably through interaction with different integrins. For example, in melanoma, the interaction between ADAM9 and β1 integrins facilitates tumor stroma cross talks, which then promotes invasion and metastasis via the activation of MMP1 and MMP2. In breast cancer, the interaction between β1 integrins on endothelial cells and ADAM9 on tumor cells facilitate tumor cell extravasation and invasion to distant sites. This review summarizes the present knowledge on ADAM9 in solid cancers, and the different mechanisms which it employ to drive tumor progression.

Indexed as

Gene Expression Regulation, NeoplasticADAM ProteinsCell CommunicationCell MovementDisease ProgressionHumansIntegrin beta1Membrane ProteinsNeoplasmsProtein BindingTumor MicroenvironmentADAM9 protein, humanADAM ProteinsIntegrin beta1Membrane ProteinsADAM9Non-proteolyticProteolyticSolid tumorsβ1 integrins

Identifiers

PMID29550974
PMCPMC11105608
OpenAlexW2789943000

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.