Title : Lung cancer-associated JmjC domain protein mdig suppresses formation of tri-methyl lysine 9 of histone H3.

Pub. Date : 2009 Jul 1

PMID : 19502796






5 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 Lung cancer-associated JmjC domain protein mdig suppresses formation of tri-methyl lysine 9 of histone H3. trimethyllysine ribosomal oxygenase 2 Homo sapiens
2 Gene silencing or overexpression of mdig revealed that mdig is involved in demethylation of tri-methyl lysine 9 on histone H3, leading to an increase in ribosomal RNA expression. trimethyllysine ribosomal oxygenase 2 Homo sapiens
3 Gene silencing or overexpression of mdig revealed that mdig is involved in demethylation of tri-methyl lysine 9 on histone H3, leading to an increase in ribosomal RNA expression. trimethyllysine ribosomal oxygenase 2 Homo sapiens
4 The pronounced expression of mdig in lung cancer tissues but not normal lung tissues, thus, suggests that mdig possesses oncogenic property through antagonizing tri-methyl lysine 9 on histone H3 and promoting ribosomal RNA synthesis. trimethyllysine ribosomal oxygenase 2 Homo sapiens
5 The pronounced expression of mdig in lung cancer tissues but not normal lung tissues, thus, suggests that mdig possesses oncogenic property through antagonizing tri-methyl lysine 9 on histone H3 and promoting ribosomal RNA synthesis. trimethyllysine ribosomal oxygenase 2 Homo sapiens