T. Ohta
Molecular Biology · Genes & Development · 2002–2008
A researcher in the Science corpus: 5 papers; trusts 1 researcher and is trusted by 2 researchers here, as inferred from the citation graph.
Subfields
- Molecular Biology — 64 citations into it; #13,599 of 17,773 by trust here, #3,333 by citations
Whom T. Ohta trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
Who trusts T. Ohta overall
Papers from T. Ohta's perspective
Ordered by how strongly the researchers T. Ohta trusts endorse each paper. Same corpus, a different order for every researcher.
- Oxidative Stress Sensor Keap1 Functions as an Adaptor for Cul3-Based E3 Ligase To Regulate Proteasomal Degradation of Nrf2 (Molecular and Cellular Biology)
- Keap1-null mutation leads to postnatal lethality due to constitutive Nrf2 activation (Nature Genetics)
- The language of covalent histone modifications (Nature)
- Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer. (Molecules and Cells)
- Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway. (Annual Review of Pharmacology and Toxicology)
- Targeting HIF-1 for cancer therapy (Nature Reviews. Cancer)
- Translating the Histone Code (Science)
- Comparative protein structure modeling of genes and genomes.
- 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)
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
- Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer. (2006) — 744 citations
- Cancer related mutations in NRF2 impair its recognition by Keap1-Cul3 E3 ligase and promote malignancy (2008) — 761 citations
- Loss of Keap1 function activates Nrf2 and provides advantages for lung cancer cell growth. (2008) — 625 citations
- Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9. (2005) — 853 citations