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Structural analysis of the complex of Keap1 with a prothymosin α peptide
scientific article
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title
Structural analysis of the complex of Keap1 with a prothymosin α peptide
(English)
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main subject
biophysics
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structural biology
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condensed matter physics
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author
Shigeyuki Yokoyama
object named as
Shigeyuki Yokoyama
series ordinal
3
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author name string
Balasundaram Padmanabhan
series ordinal
1
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Yoshihiro Nakamura
series ordinal
2
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publication date
1 April 2008
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published in
Acta Crystallographica Section F: Structural Biology Communications
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volume
64
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issue
Pt 4
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page(s)
233-8
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cites work
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Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling
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Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer
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Oxidative and electrophilic stresses activate Nrf2 through inhibition of ubiquitination activity of Keap1
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Distinct Cysteine Residues in Keap1 Are Required for Keap1-Dependent Ubiquitination of Nrf2 and for Stabilization of Nrf2 by Chemopreventive Agents and Oxidative Stress
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Molecular mechanism activating Nrf2-Keap1 pathway in regulation of adaptive response to electrophiles
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Identification of the interactive interface and phylogenic conservation of the Nrf2-Keap1 system.
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Processing of X-ray diffraction data collected in oscillation mode
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12 December 2020
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Identifiers
DOI
10.1107/S1744309108004995
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PMC publication ID
2374262
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PubMed publication ID
18391415
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