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N. Camp, Richard James, D. Dawson, Feng Yan, J. Davison, Scott Houck, Xiaobo Tang, N. Zheng, M. Major, R. Moon (2012)
Wilms Tumor Gene on X Chromosome (WTX) Inhibits Degradation of NRF2 Protein through Competitive Binding to KEAP1 Protein*The Journal of Biological Chemistry, 287
Laurie Zipper, R. Mulcahy (2002)
The Keap1 BTB/POZ Dimerization Function Is Required to Sequester Nrf2 in Cytoplasm*The Journal of Biological Chemistry, 277
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Structural analysis of the complex of Keap1 with a prothymosin alpha peptide.Acta crystallographica. Section F, Structural biology and crystallization communications, 64 Pt 4
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Residues with traceable assigned resonances are colored based on their combined absolute proton and nitrogen
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Molecular mechanism activating Nrf2-Keap1 pathway in regulation of adaptive response to electrophiles.Free radical biology & medicine, 36 10
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S. Lo, Xuchu Li, M. Henzl, L. Beamer, M. Hannink (2006)
Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signalingThe EMBO Journal, 25
G. Strachan, Kathleen Morgan, L. Otis, John Caltagarone, A. Gittis, R. Bowser, K. Jordan-Sciutto (2004)
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The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1Nature Cell Biology, 12
K. Tong, Y. Katoh, H. Kusunoki, K. Itoh, Toshiyuki Tanaka, Masayuki Yamamoto (2006)
Keap1 Recruits Neh2 through Binding to ETGE and DLG Motifs: Characterization of the Two-Site Molecular Recognition ModelMolecular and Cellular Biology, 26
K. Tong, B. Padmanabhan, A. Kobayashi, Chengwei Shang, Yosuke Hirotsu, S. Yokoyama, Masayuki Yamamoto (2007)
Different Electrostatic Potentials Define ETGE and DLG Motifs as Hinge and Latch in Oxidative Stress ResponseMolecular and Cellular Biology, 27
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The Computer Aided Resonance Assignment Tutorial
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Wilms Tumor Suppressor WTX Negatively Regulates WNT/ß-Catenin SignalingScience, 316
Jianglin Ma, H. Cai, Tongde Wu, B. Sobhian, Yanying Huo, Allen Alcivar, Monal Mehta, K. Cheung, S. Ganesan, A. Kong, Donna Zhang, B. Xia (2012)
PALB2 Interacts with KEAP1 To Promote NRF2 Nuclear Accumulation and FunctionMolecular and Cellular Biology, 32
Michael Major, N. Camp, J. Berndt, X. Yi, S. Goldenberg, Charlotte Hubbert, T. Biechele, A. Gingras, N. Zheng, M. MacCoss, S. Angers, R. Moon (2007)
Wilms tumor suppressor WTX negatively regulates WNT/beta-catenin signaling.Science, 316 5827
J. Marsh, Vinay Singh, Z. Jia, J. Forman-Kay (2006)
Sensitivity of secondary structure propensities to sequence differences between α‐ and γ‐synuclein: Implications for fibrillationProtein Science, 15
B. Padmanabhan, K. Tong, T. Ohta, Y. Nakamura, Maria Scharlock, Makiko Ohtsuji, Moon-Il Kang, A. Kobayashi, S. Yokoyama, Masayuki Yamamoto (2006)
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S. Lo, Xuchu Li, M. Henzl, L. Beamer, M. Hannink (2006)
Structure of the Keap 1 : Nrf 2 interface provides mechanistic insight into Nrf 2 signaling
Kelch-like ECH-associated Protein 1 (Keap1) is a multi-domain protein that functions as an inhibitor of the transcription factor nuclear factor E2-related factor 2 (Nrf2) in the cellular response to oxidative stress. Under normal conditions, Keap1 binds to Nrf2 via its C-terminal Kelch domain and the interaction ultimately leads to the ubiquitin-dependent degradation of Nrf2. It has been proposed that designing molecules to selectively disrupt the Keap1–Nrf2 interaction can be a potential therapeutic approach for enhancing the expression of cytoprotective genes. Here, we reported the 1H, 13C, and 15N backbone chemical shift assignments of the Kelch domain of mouse Keap1. Further, unlabeled Nrf2 peptide containing the Kelch-binding motif was added to the 15N-labeled Kelch sample. 1H–15N HSQC spectra of the protein in the absence and presence of an equimolar concentration of the Nrf2 peptide were presented. A significant number of resonance signals were shifted upon addition of the peptide, confirming the protein–peptide interaction. The results here will not just facilitate the further studies of the binding between Keap1 and Nrf2, it will also be valuable for probing interactions between the Kelch domain and small molecules, as well as a growing list of protein targets that have been identified recently.
Biomolecular NMR Assignments – Springer Journals
Published: Jun 12, 2012
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