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PTPmu suppresses glioma cell migration and dispersal
scientific article
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instance of
scholarly article
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title
PTPmu suppresses glioma cell migration and dispersal
(English)
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main subject
cell migration
1 reference
based on heuristic
inferred from title
author name string
Adam M Burgoyne
series ordinal
1
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Juan M Palomo
series ordinal
2
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Polly J Phillips-Mason
series ordinal
3
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Susan M Burden-Gulley
series ordinal
4
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Denice L Major
series ordinal
5
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Anita Zaremba
series ordinal
6
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Shenandoah Robinson
series ordinal
7
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Andrew E Sloan
series ordinal
8
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Michael A Vogelbaum
series ordinal
9
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Robert H Miller
series ordinal
10
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Susann M Brady-Kalnay
series ordinal
11
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language of work or name
English
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publication date
December 2009
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published in
Neuro-Oncology
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volume
11
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issue
6
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page(s)
767-78
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describes a project that uses
ImageJ
1 reference
stated in
Europe PubMed Central
retrieved
11 June 2022
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/PMC2802397/fullTextXML
based on heuristic
inferred from PubMed Central ID database lookup
cites work
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The receptor protein-tyrosine phosphatase PTPmu interacts with IQGAP1
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PTPmu signaling via PKCdelta is instructive for retinal ganglion cell guidance
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The PTPmu protein-tyrosine phosphatase binds and recruits the scaffolding protein RACK1 to cell-cell contacts
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PTPmu regulates N-cadherin-dependent neurite outgrowth
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Dynamic interaction of PTPmu with multiple cadherins in vivo
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Homophilic binding of PTP mu, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation
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Cell-cell adhesion mediated by a receptor-like protein tyrosine phosphatase
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Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding
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Cell surface expression of receptor protein tyrosine phosphatase RPTP mu is regulated by cell-cell contact
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Rho GTPases regulate PTPmu-mediated nasal neurite outgrowth and temporal repulsion of retinal ganglion cell neurons
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Receptor protein tyrosine phosphatases regulate neural development and axon guidance
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PTP mu-dependent growth cone rearrangement is regulated by Cdc42
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Protein kinase C delta (PKCdelta) is required for protein tyrosine phosphatase mu (PTPmu)-dependent neurite outgrowth
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A novel protein-tyrosine phosphatase related to the homotypically adhering kappa and mu receptors
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Purification and characterization of the human protein tyrosine phosphatase, PTP mu, from a baculovirus expression system
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Malignant gliomas in adults
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7 April 2017
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7 April 2017
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Phosphoprotein enriched in astrocytes-15 kDa expression inhibits astrocyte migration by a protein kinase C delta-dependent mechanism
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LRRC4 controls in vitro invasion of glioblastoma cells through inhibiting RPTP-zeta expression
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28 September 2017
RNA interference targeting protein tyrosine phosphatase zeta/receptor-type protein tyrosine phosphatase beta suppresses glioblastoma growth in vitro and in vivo
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28 September 2017
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28 September 2017
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28 September 2017
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28 September 2017
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28 September 2017
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28 September 2017
Cost of Migration: Invasion of Malignant Gliomas and Implications for Treatment
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28 September 2017
Anti-invasive effect of an anti-matrix metalloproteinase agent in a murine brain slice model using the serial monitoring of green fluorescent protein-labeled glioma cells
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28 September 2017
Protein kinase Calpha and protein kinase Cdelta play opposite roles in the proliferation and apoptosis of glioma cells
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28 September 2017
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28 September 2017
Structural alterations of the epidermal growth factor receptor gene in human gliomas
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28 September 2017
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Fixation of mammalian cells for flow cytometric evaluation of DNA content and nuclear immunofluorescence
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Control of astrocyte migration in the developing cerebral cortex
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28 November 2018
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Purification and characterization of the human protein tyrosine phosphatase, PTP?, from a baculovirus expression system
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reference URL
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based on heuristic
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Identifiers
DOI
10.1215/15228517-2009-019
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3758215
OpenCitations bibliographic resource ID
3758215
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3758215
PMCID
2802397
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3758215
PubMed ID
19304959
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3758215
ResearchGate publication ID
24218381
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