Evidence map›Paper›PMID 16079176›Full record

ArticleMolecular biology of the cell2005

Selective modulation of integrin-mediated cell migration by distinct ADAM family members.

Jing Huang, Lance C Bridges, Judith M White

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

36 citing papers in PubMed, 93 citations in OpenAlex.

  1. ADAM19: biological characteristics and implications in disease pathology and clinical applications.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026
    Review
  2. Expression ofInternational journal of molecular sciences · 2026
    Article
  3. Article
  4. Article
  5. Hypoxia-inducible factor-dependent ADAM12 expression mediates breast cancer invasion and metastasis.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. Review
  7. Article
  8. Multiple non-catalytic ADAMs are novel integrin α4 ligands.Molecular and cellular biochemistry · 2018
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
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  19. Article
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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.

Jing HuangDepartment of Cell Biology, School of Medicine, University of Virginia Health System, Charlottesville, VA 22908, USA.
Lance C Bridges
Judith M White
University of Virginia Health System · US

Funding

MOLECULAR MECHANISMS OF CELL/CELL FUSION PROTEINSR01GM048739 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI WHITE, JUDITH M. · 1993 to 2004
$1.6M
NIGMS NIH HHS GM-48739NIGMS NIH HHS R01 GM048739
6 · The paper itself

Abstract

A disintegrin and a metalloprotease (ADAM) family members have been implicated in many biological processes. Although it is recognized that recombinant ADAM disintegrin domains can interact with integrins, little is known about ADAM-integrin interactions in cellular context. Here, we tested whether ADAMs can selectively regulate integrin-mediated cell migration. ADAMs were expressed in Chinese hamster ovary cells that express defined integrins (alpha4beta1, alpha5beta1, or both), and cell migration on full-length fibronectin or on its alpha4beta1 or alpha5beta1 binding fragments was studied. We found that ADAMs inhibit integrin-mediated cell migration in patterns dictated by the integrin binding profiles of their isolated disintegrin domains. ADAM12 inhibited cell migration mediated by the alpha4beta1 but not the alpha5beta1 integrin. ADAM17 had the reciprocal effect; it inhibited alpha5beta1- but not alpha4beta1-mediated cell migration. ADAM19 and ADAM33 inhibited migration mediated by both alpha4beta1 and alpha5beta1 integrins. A point mutation in the ADAM12 disintegrin loop partially reduced the inhibitory effect of ADAM12 on cell migration on the alpha4beta1 binding fragment of fibronectin, whereas mutations that block metalloprotease activity had no effect. Our results indicate that distinct ADAMs can modulate cell migration mediated by specific integrins in a pattern dictated, at least in part, by their disintegrin domains.

Indexed as

ADAM12 ProteinADAM17 ProteinADAM ProteinsAnimalsCell AdhesionCell MovementCHO CellsCricetinaeCricetulusFibronectinsIntegrin alpha4beta1Integrin alpha5beta1Point MutationADAM12 ProteinAdam12 protein, mouseADAM17 ProteinAdam17 protein, mouseAdam33 protein, mouseADAM ProteinsFibronectinsIntegrin alpha4beta1Integrin alpha5beta1

Identifiers

PMID16079176
PMCPMC1237097
OpenAlexW2130806310

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.