Liam Baird
Molecular Biology · 2011–2020
A researcher in the Science corpus: 2 papers; trusts 19 researchers and is trusted by 1 researcher here, as inferred from the citation graph.
Subfields
- Molecular Biology — 106 citations into it; #17,452 of 17,773 by trust here, #14,833 by citations
- Cell Biology — 14 citations into it
- Health, Toxicology and Mutagenesis — 8 citations into it
Whom Liam Baird trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
- K. Itoh
- Masayuki Yamamoto
- A. Dinkova-Kostova
- Michael T. McMahon
- Donna D. Zhang
- N. Wakabayashi
- K. I. Tong
- A. Kobayashi
- T. Ohta
- T. Kensler
Who trusts Liam Baird overall
Papers from Liam Baird's perspective
Ordered by how strongly the researchers Liam Baird 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)
- Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants (Proceedings of the National Academy of Sciences of the United States of America)
- BTB Protein Keap1 Targets Antioxidant Transcription Factor Nrf2 for Ubiquitination by the Cullin 3-Roc1 Ligase (Molecular and Cellular Biology)
- Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex (Nature)
- Keap1 regulates both cytoplasmic‐nuclear shuttling and degradation of Nrf2 in response to electrophiles (Genes to Cells)
- Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway. (Annual Review of Pharmacology and Toxicology)
- Keap1-null mutation leads to postnatal lethality due to constitutive Nrf2 activation (Nature Genetics)
- Distinct Cysteine Residues in Keap1 Are Required for Keap1-Dependent Ubiquitination of Nrf2 and for Stabilization of Nrf2 by Chemopreventive Agents and Oxidative Stress (Molecular and Cellular Biology)
- Cancer related mutations in NRF2 impair its recognition by Keap1-Cul3 E3 ligase and promote malignancy (Proceedings of the National Academy of Sciences of the United States of America)
- Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer. (Molecules and Cells)
Their papers
- The cytoprotective role of the Keap1–Nrf2 pathway (2011) — 995 citations
- The Molecular Mechanisms Regulating the KEAP1-NRF2 Pathway (2020) — 1,188 citations