Evidence map›Paper›PMID 31463913›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2020

Cell-Based Interaction Analysis of ADAMTS Proteases and ADAMTS-Like Proteins with Fibrillin Microfibrils.

Dirk Hubmacher

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Alternative splicing of the metalloprotease ADAMTS17 spacer regulates secretion and modulates autoproteolytic activity.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
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

1 author.

Dirk HubmacherOrthopaedic Research Laboratories, Leni & Peter W. May Department of Orthopaedics, Icahn School of Medicine at Mount Sinai, New York, NY, USA. dirk.hubmacher@mssm.edu.

Funding

Regulation of Skeletal Growth by Soft Tissue Extracellular MatrixR01AR070748 · NIAMS · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI HUBMACHER, DIRK · 2017 to 2021
$1.9M
NIAMS NIH HHS R01 AR070748
6 · The paper itself

Abstract

The extracellular matrix (ECM) is a composite biomaterial that serves as an anchor for cells and provides guidance cues for cell migration, proliferation, and differentiation. However, many details of the hierarchical ECM assembly process and the role of individual protein-protein interactions are not well understood. Here, I describe a cell-culture-based method that allows for determination of the ECM localization of recombinant ADAMTS proteases and ADAMTS-like (L) proteins in relationship to fibrillin microfibrils deposited by human dermal fibroblasts. The method can be readily adapted to study the localization of ECM components other than ADAMTS and ADAMTSL proteins to fibrillin microfibrils and other ECM networks.

Indexed as

ADAMTS ProteinsCells, CulturedCoculture TechniquesExtracellular MatrixFibrillinsFibroblastsHEK293 CellsHumansMicrofibrilsRecombinant ProteinsSkinADAMTS ProteinsFibrillinsRecombinant ProteinsADAMTS-like proteinsADAMTS proteasesCoculture assayExtracellular matrixFibrillin microfibrilsImmuno-colocalizationRecombinant protein

Identifiers

PMID31463913
PMCPMC6910243

What OpenQuestion holds

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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.