Mikiko Fukuda
Molecular Biology · 2002–2005
A researcher in the Science corpus: 2 papers; trusts 1 researcher and is trusted by 0 researchers here, as inferred from the citation graph.
Subfields
- Molecular Biology — 35 citations into it
Whom Mikiko Fukuda trusts
Their strongest outbound trust, strongest first, inferred from their citations.
- C. D. Allis (in Molecular Biology)
Papers from Mikiko Fukuda's perspective
Ordered by how strongly the researchers Mikiko Fukuda trusts endorse each paper. Same corpus, a different order for every researcher.
- The language of covalent histone modifications (Nature)
- Translating the Histone Code (Science)
- Rb targets histone H3 methylation and HP1 to promoters (Nature)
- Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain (Nature)
- Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins (Nature)
- Transitions in Distinct Histone H3 Methylation Patterns at the Heterochromatin Domain Boundaries (Science)
- SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins. (Genes & Development)
- The many faces of histone lysine methylation. (Current Opinion in Cell Biology)
- Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component (Nature Genetics)
- SET Domain-containing Protein, G9a, Is a Novel Lysine-preferring Mammalian Histone Methyltransferase with Hyperactivity and Specific Selectivity to Lysines 9 and 27 of Histone H3* (Journal of Biological Chemistry)
Their papers
- G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis. (2002) — 1,277 citations
- Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9. (2005) — 853 citations