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Liam Baird

Researcher at Tohoku University

Publications -  23
Citations -  2989

Liam Baird is an academic researcher from Tohoku University. The author has contributed to research in topics: KEAP1 & Transcription factor. The author has an hindex of 15, co-authored 21 publications receiving 2106 citations. Previous affiliations of Liam Baird include University of Dundee.

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The cytoprotective role of the Keap1–Nrf2 pathway

TL;DR: Cross-talks with other signalling pathways broadens the role of the Keap1–Nrf2 pathway in determining the fate of the cell, impacting fundamental biological processes such as proliferation, apoptosis, angiogenesis and metastasis.
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The Molecular Mechanisms Regulating the KEAP1-NRF2 Pathway.

TL;DR: The integration of the KEAP1-NRF2 system into multiple cellular signaling and metabolic pathways places NRF2 activation as a critical regulatory node in many disease phenotypes and suggests that the pharmaceutical modulation of NRF 2’s cytoprotective activity will be beneficial for human health in a broad range of noncommunicable diseases.
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Nrf2 impacts cellular bioenergetics by controlling substrate availability for mitochondrial respiration

TL;DR: A novel role is demonstrated for Nrf2 in directly regulating mitochondrial bioenergetics in murine neurons and embryonic fibroblasts through modulating the availability of substrates for mitochondrial respiration and the importance of efficient energy metabolism in NRF2-mediated cytoprotection.
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Regulatory flexibility in the Nrf2-mediated stress response is conferred by conformational cycling of the Keap1-Nrf2 protein complex

TL;DR: A quantitative Förster resonance energy transfer-based methodology using multiphoton fluorescence lifetime imaging microscopy was developed and found that under homeostatic conditions, the interaction between Keap1 and Nrf2 follows a cycle in which the complex sequentially adopts two distinct conformations.
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Characterizations of Three Major Cysteine Sensors of Keap1 in Stress Response

TL;DR: It is demonstrated that Keap1 utilizes multiple cysteine residues specifically and/or collaboratively as sensors for the detection of a wide range of environmental stresses.