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MMRN2 gene

Known as: FLJ13465, EndoGlyx-1, MULTIMERIN 2 
National Institutes of Health

Related topics

Related topics

1 relation
Multimerin-1, human

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Review
2020
Review
2020
Role of extra cellular proteins in gastric cancer progression and metastasis: an update
Background Gastric cancer (GC) is one of the most common cancers in the world with a high ratio of mortality. Regarding the late… 
2020
2020
Expression patterns and the prognostic value of the EMILIN/Multimerin family members in low-grade glioma
Managing low-grade gliomas (LGG) remains a major medical challenge due to the infiltrating nature of the tumor and failure of… 
2018
2018
Association of specific gene mutations derived from machine learning with survival in lung adenocarcinoma
Lung cancer is the second most common cancer in the United States and the leading cause of mortality in cancer patients… 
Highly Cited
2018
Highly Cited
2018
CD93 promotes β1 integrin activation and fibronectin fibrillogenesis during tumor angiogenesis
Tumor angiogenesis occurs through regulation of genes that orchestrate endothelial sprouting and vessel maturation, including… 
Highly Cited
2017
Highly Cited
2017
The angiostatic molecule Multimerin 2 is processed by MMP-9 to allow sprouting angiogenesis.
2017
2017
Dissecting the CD93-Multimerin 2 interaction involved in cell adhesion and migration of the activated endothelium.
2017
2017
Multimerin-2 is a ligand for group 14 family C-type lectins CLEC14A, CD93 and CD248 spanning the endothelial pericyte interface
The C-type lectin domain containing group 14 family members CLEC14A and CD93 are proteins expressed by endothelium and are… 
Highly Cited
2012
Highly Cited
2012
MULTIMERIN2 impairs tumor angiogenesis and growth by interfering with VEGF-A/VEGFR2 pathway
MULTIMERIN2 (MMRN2), also known as Endoglyx-1, is an extracellular matrix glycoprotein whose function has so far remained elusive… 
1994
1994
Identification of a high molecular weight endothelial cell surface glycoprotein, endoGlyx-1, in normal and tumor blood vessels.
BACKGROUND The vascular endothelium participates in diverse physiologic and pathologic processes, ranging from blood clotting to… 
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