Evidence map›Paper›PMID 21235433›Full record

ReviewAnti-cancer agents in medicinal chemistry2011

Tumor-derived extracellular fragments of receptor protein tyrosine phosphatases (RPTPs) as cancer molecular diagnostic tools.

Sonya E L Craig, Susann M Brady-Kalnay

Abstract readReview
In one paragraph

Review in Anti-cancer agents in medicinal chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

13 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. LAR Receptor Tyrosine Phosphatase Family in Healthy and Diseased Brain.Frontiers in cell and developmental biology · 2021
    Review
  5. PTPmu-targeted nanoparticles label invasive pediatric and adult glioblastoma.Nanomedicine : nanotechnology, biology, and medicine · 2020
    Article
  6. Surfen-mediated blockade of extratumoral chondroitin sulfate glycosaminoglycans inhibits glioblastoma invasion.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. 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

2 authors at 2 institutions in 1 country.

Sonya E L CraigDepartment of Molecular Biology and Microbiology, Case Western Reserve University, Cleveland, OH 44106-4960, USA.
Susann M Brady-Kalnay
Case Comprehensive Cancer CenterCase Western Reserve University · US

Funding

TUMOR METABOLISM PROGRAMP30CA043703 · NCI · CASE WESTERN RESERVE UNIVERSITY · PI MARK R CHANCE · 1987 to 2026
$142.3M
Detecting invading glioma cells through in vivo molecular imaging of the cell surR01NS063971 · NINDS · CASE WESTERN RESERVE UNIVERSITY · PI BRADY-KALNAY, SUSANN M · 2009 to 2013
$1.9M
PTP mu Supresses Brain Tumor Cell Migration and DispersalR01NS051520 · NINDS · CASE WESTERN RESERVE UNIVERSITY · PI BRADY-KALNAY, SUSANN M · 2006 to 2010
$1.8M
NCI NIH HHS P30 CA043703NCI NIH HHS P30-CA043703NINDS NIH HHS R01 NS051520NINDS NIH HHS R01-NS051520NINDS NIH HHS R01 NS063971NINDS NIH HHS R01-NS063971
6 · The paper itself

Abstract

Receptor protein tyrosine phosphatase (RPTPs) are involved in many cellular processes, including the regulation of adhesion, migration and cellular signaling. Many RPTPs are putative tumor suppressors because of the transcriptional and translational changes observed in their expression during tumorigenesis. Recently, RPTPs were shown to be post-translationally regulated during tumorigenesis by proteolysis in a manner similar to proteolysis of the Notch receptor. There is accumulating evidence that proteolysis of RPTPs influence their cellular function and that RPTP fragments may function as oncogenes. By exploiting what is known about RPTP ligand binding domains and crystal structures of ligand-RPTP interfaces, we describe novel molecular diagnostics that have been or can be developed to identify tumor margins and target tumor tissues.

Indexed as

Molecular Diagnostic TechniquesHumansLigandsNeoplasmsReceptor-Like Protein Tyrosine Phosphatases, Class 2LigandsReceptor-Like Protein Tyrosine Phosphatases, Class 2

Identifiers

PMID21235433
PMCPMC3337336
OpenAlexW2333646725

What OpenQuestion holds

Textmetadata
LicenceTDM
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.