K. Sugimoto
Molecular Biology · 2001–2002
A researcher in the Science corpus: 2 papers; trusts 1 researcher and is trusted by 4 researchers here, as inferred from the citation graph.
Subfields
- Molecular Biology — 22 citations into it; #9,702 of 17,773 by trust here, #6,535 by citations
Whom K. Sugimoto trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
Who trusts K. Sugimoto overall
Papers from K. Sugimoto's perspective
Ordered by how strongly the researchers K. Sugimoto trusts endorse each paper. Same corpus, a different order for every researcher.
- The language of covalent histone modifications (Nature)
- Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain (Nature)
- Translating the Histone Code (Science)
- Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins (Nature)
- Rb targets histone H3 methylation and HP1 to promoters (Nature)
- Transitions in Distinct Histone H3 Methylation Patterns at the Heterochromatin Domain Boundaries (Science)
- 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)
- Role of Histone H3 Lysine 9 Methylation in Epigenetic Control of Heterochromatin Assembly (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)
- Correlation Between Histone Lysine Methylation and Developmental Changes at the Chicken β-Globin Locus (Science)
Their papers
- 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* (2001) — 795 citations
- G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis. (2002) — 1,277 citations