A novel molecular diagnostic of glioblastomas: detection of an extracellular fragment of protein tyrosine phosphatase mu - Test2 - elhamkhani - TriplyDB

A novel molecular diagnostic of glioblastomas: detection of an extracellular fragment of protein tyrosine phosphatase mu

A novel molecular diagnostic of glioblastomas: detection of an extracellular fragment of protein tyrosine phosphatase mu

http://www.wikidata.org/entity/Q24608210

about

Tumour suppressor function of protein tyrosine phosphatase receptor-T Dinosaurs and ancient civilizations: reflections on the treatment of cancer Cancer cells cut homophilic cell adhesion molecules and run Identification of phospholipase C gamma1 as a protein tyrosine phosphatase mu substrate that regulates cell migration Tumor-derived extracellular fragments of receptor protein tyrosine phosphatases (RPTPs) as cancer molecular diagnostic tools Regulation of development and cancer by the R2B subfamily of RPTPs and the implications of proteolysis Investigation of serum proteome alterations in human glioblastoma multiforme.The interconnectedness of cancer cell signaling.Cadherin-11, a marker of the mesenchymal phenotype, regulates glioblastoma cell migration and survival in vivo.Protein tyrosine phosphatase mu regulates glioblastoma cell growth and survival in vivo.Molecular Imaging of Tumors Using a Quantitative T 1 Mapping Technique via Magnetic Resonance Imaging A protease storm cleaves a cell-cell adhesion molecule in cancer: multiple proteases converge to regulate PTPmu in glioma cells Cryo-image analysis of tumor cell migration, invasion, and dispersal in a mouse xenograft model of human glioblastoma multiforme.Synthesis and evaluation of a peptide targeted small molecular Gd-DOTA monoamide conjugate for MR molecular imaging of prostate cancer.Molecular Magnetic Resonance Imaging of Tumors with a PTPµ Targeted Contrast Agent.Fluorescent-Guided Surgical Resection of Glioma with Targeted Molecular Imaging Agents: A Literature Review.The malignant social network: cell-cell adhesion and communication in cancer stem cells Genetic alterations of protein tyrosine phosphatases in human cancers.Novel cryo-imaging of the glioma tumor microenvironment reveals migration and dispersal pathways in vivid three-dimensional detail.Overcoming intratumor heterogeneity of polygenic cancer drug resistance with improved biomarker integration MR molecular imaging of prostate cancer with a small molecular CLT1 peptide targeted contrast agent.Single cell molecular recognition of migrating and invading tumor cells using a targeted fluorescent probe to receptor PTPmu.Quantitative Molecular Imaging with a Single Gd-Based Contrast Agent Reveals Specific Tumor Binding and Retention in Vivo.

P2860

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P2860

A novel molecular diagnostic of glioblastomas: detection of an extracellular fragment of protein tyrosine phosphatase mu

http://www.wikidata.org/entity/Q24608210

description

2010 nî lūn-bûn

@nan

2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի ապրիլին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

@zh-hk

2010年論文

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2010年論文

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2010年论文

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name

A novel molecular diagnostic o ...... rotein tyrosine phosphatase mu

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A novel molecular diagnostic o ...... rotein tyrosine phosphatase mu

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A novel molecular diagnostic o ...... rotein tyrosine phosphatase mu

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type

label

A novel molecular diagnostic o ...... rotein tyrosine phosphatase mu

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A novel molecular diagnostic o ...... rotein tyrosine phosphatase mu

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A novel molecular diagnostic o ...... rotein tyrosine phosphatase mu

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prefLabel

A novel molecular diagnostic o ...... rotein tyrosine phosphatase mu

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A novel molecular diagnostic o ...... rotein tyrosine phosphatase mu

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A novel molecular diagnostic o ...... rotein tyrosine phosphatase mu

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A novel molecular diagnostic o ...... rotein tyrosine phosphatase mu

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Adam M Burgoyne

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Andrew E Sloan

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David T Lodowski

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James P Basilion

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Jennifer L Cutter

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Robert H Miller

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Shenandoah Robinson

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Susann M Brady-Kalnay

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Theresa J Gates

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P2860

Impaired flow-induced dilation in mesenteric resistance arteries from receptor protein tyrosine phosphatase-mu-deficient mice

The conserved immunoglobulin domain controls the subcellular localization of the homophilic adhesion receptor protein-tyrosine phosphatase mu

Cell-cell adhesion mediated by a receptor-like protein tyrosine phosphatase

Large-scale structural analysis of the classical human protein tyrosine phosphatome

Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion

Furin-, ADAM 10-, and gamma-secretase-mediated cleavage of a receptor tyrosine phosphatase and regulation of beta-catenin's transcriptional activity

Expression of the receptor-linked protein tyrosine phosphatase LAR: proteolytic cleavage and shedding of the CAM-like extracellular region

PTPmu suppresses glioma cell migration and dispersal

Proteolytic cleavage of protein tyrosine phosphatase mu regulates glioblastoma cell migration

Homophilic binding of PTP mu, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation

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305-316

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scholarly article

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10.1593/NEO.91940

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4

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12

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Susan M Burden-Gulley

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2010-04-01T00:00:00Z

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42834143

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20360941

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2847738

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