HOXA9 methylation by PRMT5 is essential for endothelial cell expression of leukocyte adhesion molecules (Q24303362)

endothelial cell activation

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author name string

Smarajit Bandyopadhyay

1

0 references

Daniel P Harris

2

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Gregory N Adams

3

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Gregory E Lause

4

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Anne McHugh

5

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Emily G Tillmaand

6

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Angela Money

7

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Belinda Willard

8

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Paul L Fox

9

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Paul E Dicorleto

Molecular and Cellular Biology

10

0 references

language of work or name

English

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publication date

April 2012

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published in

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volume

32

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issue

7

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page(s)

1202-13

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describes a project that uses

ImageJ

1 reference

Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC3302442/fullTextXML

based on heuristic

inferred from PubMed Central ID database lookup

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HOXA9 participates in the transcriptional activation of E-selectin in endothelial cells

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Histone deacetylase activity is essential for the expression of HoxA9 and for endothelial commitment of progenitor cells

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Protein kinase C-mediated phosphorylation of the leukemia-associated HOXA9 protein impairs its DNA binding ability and induces myeloid differentiation.

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Endothelial cells express a novel, tumor necrosis factor-alpha-regulated variant of HOXA9.

27 September 2017

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