Keap1 is a forked-stem dimer structure with two large spheres enclosing the intervening, double glycine repeat, and C-terminal domains

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Keap1 is a forked-stem dimer structure with two large spheres enclosing the intervening, double glycine repeat, and C-terminal domains is …
instance of (P31):
scholarly articleQ13442814

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P819ADS bibcode2010PNAS..107.2842O
P356DOI10.1073/PNAS.0914036107
P932PMC publication ID2840362
P698PubMed publication ID20133743
P5875ResearchGate publication ID41408595

P50authorKazuhiro MioQ56501628
Chikara SatoQ58883334
P2093author name stringToshihiko Ogura
Masayuki Yamamoto
Kit I Tong
Yuusuke Maruyama
Hirofumi Kurokawa
P2860cites workFunctional polymorphisms in the transcription factor NRF2 in humans increase the risk of acute lung injuryQ40154556
Hepatocyte-specific deletion of the keap1 gene activates Nrf2 and confers potent resistance against acute drug toxicity.Q46808839
The Sodium Channel Has Four Domains Surrounding a Central PoreQ47686490
A fully automatic 3D reconstruction method using simulated annealing enables accurate posterioric angular assignment of protein projectionsQ51934118
An automatic particle pickup method using a neural network applicable to low-contrast electron micrographs.Q52039243
Dimerization of substrate adaptors can facilitate cullin-mediated ubiquitylation of proteins by a "tethering" mechanism: a two-site interaction model for the Nrf2-Keap1 complexQ53616483
Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signalingQ24298930
BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligaseQ24558689
Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complexQ24559743
Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2Q24563807
Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domainQ24609907
Physiological significance of reactive cysteine residues of Keap1 in determining Nrf2 activityQ24655442
Crystal structure of the BTB domain from the LRF/ZBTB7 transcriptional regulatorQ27640942
Different Electrostatic Potentials Define ETGE and DLG Motifs as Hinge and Latch in Oxidative Stress ResponseQ27647812
A new generation of the IMAGIC image processing systemQ28131751
The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasmQ28216217
Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidantsQ28218883
An Nrf2/Small Maf Heterodimer Mediates the Induction of Phase II Detoxifying Enzyme Genes through Antioxidant Response ElementsQ28244853
Crystal structure of the Kelch domain of human Keap1Q28287182
Dysfunctional KEAP1-NRF2 interaction in non-small-cell lung cancerQ28469051
Keap1 recruits Neh2 through binding to ETGE and DLG motifs: characterization of the two-site molecular recognition modelQ28910182
Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in nrf2 transcription factor-deficient miceQ29615438
Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancerQ29616499
The Keap1-BTB protein is an adaptor that bridges Nrf2 to a Cul3-based E3 ligase: oxidative stress sensing by a Cul3-Keap1 ligaseQ29616502
Protection against electrophile and oxidant stress by induction of the phase 2 response: fate of cysteines of the Keap1 sensor modified by inducersQ29616503
Keap1-null mutation leads to postnatal lethality due to constitutive Nrf2 activationQ29618051
Auto-accumulation method using simulated annealing enables fully automatic particle pickup completely free from a matching template or learning dataQ30923909
Topology representing network enables highly accurate classification of protein images taken by cryo electron-microscope without masking.Q31015634
Automatic particle pickup method using a neural network has high accuracy by applying an initial weight derived from eigenimages: a new reference free method for single-particle analysis.Q33201007
Single-particle electron cryo-microscopy: towards atomic resolution.Q33936480
Nrf2 is essential for the chemopreventive efficacy of oltipraz against urinary bladder carcinogenesisQ33981477
Chemoprotection against cancer by induction of phase 2 enzymesQ34160772
The BACK domain in BTB-kelch proteins.Q35950674
Evolutionary conserved N-terminal domain of Nrf2 is essential for the Keap1-mediated degradation of the protein by proteasomeQ35974394
Nrf2-Keap1 regulation of cellular defense mechanisms against electrophiles and reactive oxygen speciesQ36556032
Genetic or pharmacologic amplification of nrf2 signaling inhibits acute inflammatory liver injury in miceQ36732083
Oxidative stress and antioxidants in the pathogenesis of pulmonary fibrosis: a potential role for Nrf2.Q36999941
The Nrf2-Keap1 defence pathway: role in protection against drug-induced toxicityQ37033412
Nrf2 signaling: an adaptive response pathway for protection against environmental toxic insultsQ37046924
The transcription factor Nrf2 is a therapeutic target against brain inflammationQ39970287
Loss of Keap1 function activates Nrf2 and provides advantages for lung cancer cell growth.Q40006300
P433issue7
P407language of work or nameEnglishQ1860
P921main subjectKelch-like ECH-associated protein 1Q21979992
P304page(s)2842-2847
P577publication date2010-01-27
P1433published inProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
P1476titleKeap1 is a forked-stem dimer structure with two large spheres enclosing the intervening, double glycine repeat, and C-terminal domains
P478volume107

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