Evidence map›Paper›PMID 29187866›Full record

ArticleJournal of Cancer2017

Modification of proteolytic activity matrix analysis (PrAMA) to measure ADAM10 and ADAM17 sheddase activities in cell and tissue lysates.

Toshie Yoneyama, Michael Gorry, Miles A Miller, Autumn Gaither-Davis, Yan Lin, Marcia L Moss, Linda G Griffith, Douglas A Lauffenburger, Laura P Stabile, James G Herman and 1 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of Cancer, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 36% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

11 authors at 4 institutions in 1 country.

Toshie YoneyamaDepartment of Pathology, University of Pittsburgh Cancer Institute, Pittsburgh, PA.
Michael GorryDepartment of Pathology, University of Pittsburgh Cancer Institute, Pittsburgh, PA.
Miles A MillerCenter for Systems Biology, Massachusetts General Hospital and Harvard Medical School, Boston, MA.
Autumn Gaither-DavisDepartment of Medicine, University of Pittsburgh Cancer Institute, Pittsburgh, PA.
Yan LinDepartment of Biostatistics, University of Pittsburgh Cancer Institute, Pittsburgh, PA.
Marcia L MossBioZyme Inc, Apex, NC.
Linda G GriffithDepartment of Biologic Engineering, Massachusetts Institute of Technology.
Douglas A LauffenburgerDepartment of Biologic Engineering, Massachusetts Institute of Technology.
Laura P StabileDepartment of Pharmacology and Chemical Biology, University of Pittsburgh Cancer Institute, Pittsburgh, PA.
James G HermanDepartment of Medicine, University of Pittsburgh Cancer Institute, Pittsburgh, PA.
Nikola L VujanovicDepartment of Pathology, University of Pittsburgh Cancer Institute, Pittsburgh, PA.
UPMC Hillman Cancer Center · USBiolog (United States) · USBioZyme (United States) · USHarvard University · US

Funding

VECTOR CORE FACILITYP30CA047904 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Jessie Nedrow · 1988 to 2026
$158.0M
NCI NIH HHS P30 CA047904
6 · The paper itself

Abstract

Increases in expression of ADAM10 and ADAM17 genes and proteins have been evaluated, but not validated as cancer biomarkers. Specific enzyme activities better reflect enzyme cellular functions, and might be better biomarkers than enzyme genes or proteins. However, no high throughput assay is available to test this possibility. Recent studies have developed the high throughput real-time proteolytic activity matrix analysis (PrAMA) that integrates the enzymatic processing of multiple enzyme substrates with mathematical-modeling computation. The original PrAMA measures with significant accuracy the activities of individual metalloproteinases expressed on live cells. To make the biomarker assay usable in clinical practice, we modified PrAMA by testing enzymatic activities in cell and tissue lysates supplemented with broad-spectrum non-MP enzyme inhibitors, and by maximizing the assay specificity using systematic mathematical-modeling analyses. The modified PrAMA accurately measured the absence and decreases of ADAM10 sheddase activity (ADAM10sa) and ADAM17sa in

Indexed as

ADAM10ADAM17Cancer biomarkerCell lysateFluorogenic peptide substratesGene knockoutGene restorationGene silencelysateProtease inhibitorsProteolytic activity matrix analysisSheddase activityTissues

Identifiers

PMID29187866
PMCPMC5705993
OpenAlexW2766629977

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.