Evidence map›Paper›PMID 31085586›Full record

ArticleThe Journal of biological chemistry2019

A disintegrin-like and metalloproteinase domain with thrombospondin type 1 motif 9 (ADAMTS9) regulates fibronectin fibrillogenesis and turnover.

Lauren W Wang, Sumeda Nandadasa, Douglas S Annis, Joanne Dubail, Deane F Mosher, Belinda B Willard, Suneel S Apte

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

12 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Metalloproteases in gonad formation and ovulation.General and comparative endocrinology · 2021
    Review
  5. Article
  6. Review
  7. Article
  8. Regulation of ADAMTS Proteases.Frontiers in molecular biosciences · 2021
    Review
  9. Review
  10. Article
  11. Characterization of Burn Eschar Pericytes.Journal of clinical medicine · 2020
    Article
  12. 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

7 authors at 3 institutions in 1 country.

Lauren W WangFrom the Department of Biomedical Engineering and.
Sumeda NandadasaFrom the Department of Biomedical Engineering and.
Douglas S Annisthe Departments of Biomolecular Chemistry and Medicine, University of Wisconsin, Madison, Wisconsin 53706.
Joanne DubailFrom the Department of Biomedical Engineering and.ORCID 0000-0001-9124-9765
Deane F Mosherthe Departments of Biomolecular Chemistry and Medicine, University of Wisconsin, Madison, Wisconsin 53706.
Belinda B Willardthe Proteomics and Metabolomics Core, Cleveland Clinic Lerner Research Institute, Cleveland, Ohio 44195 and.
Suneel S ApteFrom the Department of Biomedical Engineering and aptes@ccf.org.
University of Wisconsin–Madison · USAlbuquerque Public Schools · USCleveland Clinic · US

Funding

Extracellular matrix remodeling in ocular anterior segment developmentR01EY024943 · NEI · CLEVELAND CLINIC LERNER COM-CWRU · PI APTE, SUNEEL S · 2015 to 2017
$1.1M
LTQ-Orbitrap Velos instrumentS10RR031537 · NCRR · CLEVELAND CLINIC LERNER COM-CWRU · PI WILLARD, BELINDA BELLE · 2011 to 2011
$600k
NCRR NIH HHS S10 RR031537NEI NIH HHS R01 EY024943
6 · The paper itself

Abstract

The secreted metalloprotease ADAMTS9 has dual roles in extracellular matrix (ECM) turnover and biogenesis of the primary cilium during mouse embryogenesis. Its gene locus is associated with several human traits and disorders, but ADAMTS9 has few known interacting partners or confirmed substrates. Here, using a yeast two-hybrid screen for proteins interacting with its C-terminal Gon1 domain, we identified three putative ADAMTS9-binding regions in the ECM glycoprotein fibronectin. Using solid-phase binding assays and surface plasmon resonance experiments with purified proteins, we demonstrate that ADAMTS9 and fibronectin interact. ADAMTS9 constructs, including those lacking Gon1, co-localized with fibronectin fibrils formed by cultured fibroblasts lacking fibrillin-1, which co-localizes with fibronectin and binds several ADAMTSs. We observed no fibrillar ADAMTS9 staining after blockade of fibroblast fibronectin fibrillogenesis with a peptide based on the functional upstream domain of a

Indexed as

Protein AggregatesADAMTS9 ProteinAnimalsCells, CulturedEmbryo, MammalianFibroblastsFibronectinsHumansMiceProteolysisRetinal Pigment EpitheliumTwo-Hybrid System TechniquesADAMTS9 ProteinADAMTS9 protein, humanFibronectinsProtein AggregatesADAM metallopeptidase with thrombospondin type 1 motif (ADAMTS)ADAMTSECMextracellular matrixfibrilfibrillogenesisfibronectinmass spectrometry (MS)metalloproteaseprimary ciliumproteolysisproteolytic enzyme

Identifiers

PMID31085586
PMCPMC6597835
OpenAlexW2945341589

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.