The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm
about
sameAs
Molecular basis of electrophilic and oxidative defense: promises and perils of Nrf2Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signalingEctodermal-neural cortex 1 down-regulates Nrf2 at the translational levelBTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligaseKeap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex.Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2Nuclear transport, oxidative stress, and neurodegenerationCysteine-based regulation of the CUL3 adaptor protein Keap1Direct interaction between Nrf2 and p21(Cip1/WAF1) upregulates the Nrf2-mediated antioxidant responseNrf2 is a direct PERK substrate and effector of PERK-dependent cell survivalPhysiological significance of reactive cysteine residues of Keap1 in determining Nrf2 activityMolecular phylogeny of the kelch-repeat superfamily reveals an expansion of BTB/kelch proteins in animalsThe Role of Cyclo(His-Pro) in NeurodegenerationRedox Modulating NRF2: A Potential Mediator of Cancer Stem Cell ResistanceThe Nrf2-ARE pathway: a valuable therapeutic target for the treatment of neurodegenerative diseasesConcerted action of Nrf2-ARE pathway, MRN complex, HMGB1 and inflammatory cytokines - implication in modification of radiation damageRedox control of microglial function: molecular mechanisms and functional significanceStructural analysis of the complex of Keap1 with a prothymosin α peptideStructure of the BTB domain of Keap1 and its interaction with the triterpenoid antagonist CDDOKelch proteins: emerging roles in skeletal muscle development and diseases.Discovery of direct inhibitors of Keap1-Nrf2 protein-protein interaction as potential therapeutic and preventive agentsTumor cell survival pathways activated by photodynamic therapy: a molecular basis for pharmacological inhibition strategiesThe BTB-kelch protein LZTR-1 is a novel Golgi protein that is degraded upon induction of apoptosisDelayed mechanism for induction of gamma-glutamylcysteine synthetase heavy subunit mRNA stability by oxidative stress involving p38 mitogen-activated protein kinase signalingMechanistic studies of the Nrf2-Keap1 signaling pathwayFetal Alz-50 clone 1 interacts with the human orthologue of the Kelch-like Ech-associated proteinReactive oxygen production induced by the gut microbiota: pharmacotherapeutic implicationsPGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondriaStress-activated cap'n'collar transcription factors in aging and human diseaseSmall molecule modulators of Keap1-Nrf2-ARE pathway as potential preventive and therapeutic agentsDietary chemoprevention strategies for induction of phase II xenobiotic-metabolizing enzymes in lung carcinogenesis: A reviewAntiapoptotic Effects of EGb 761Regulation of Nrf2-an updateBasic principles and emerging concepts in the redox control of transcription factorsNrf2 signaling and cell survivalEmerging roles of Nrf2 and phase II antioxidant enzymes in neuroprotection4-Hydroxynonenal induces rat gamma-glutamyl transpeptidase through mitogen-activated protein kinase-mediated electrophile response element/nuclear factor erythroid 2-related factor 2 signalingScaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genesMacrophage Migration Inhibitory Factor as an Emerging Drug Target to Regulate Antioxidant Response Element SystemKeap1 recruits Neh2 through binding to ETGE and DLG motifs: characterization of the two-site molecular recognition model
P2860
Q23919668-AEA694CF-6405-445E-892D-561837233FD5Q24298930-0497C6AB-CCA6-47F6-9AFA-3CB7C6F4BA5CQ24323175-188F3A0E-E5DD-426D-8622-8E7436FB1CF1Q24558689-78FFD3EE-529A-481C-B020-F797989C094DQ24559743-7B625729-B013-4273-BAF6-F1400E058783Q24563807-AF82D85D-550D-4D47-A96A-864F8191BBA9Q24624357-0A1FE3E5-A346-46C9-B026-F1289805E950Q24629359-8252C39E-8CF6-4246-A21B-51EC11F2FE21Q24646029-70939054-F4E7-4800-8FA3-F9C886AC3E0FQ24653078-FFF909F4-A6CC-4096-B217-6A51D92F41DBQ24655442-496C5546-12EE-4579-B07D-9CD5A8304180Q24804994-CDF01DBC-775D-4BC2-BE18-F823387A93D6Q26741190-5D948202-999B-4464-BFC0-3C9788C49E2BQ26774916-06D636F0-6258-4A64-B9E5-FD9995A209A8Q26822972-30D8A19A-1893-4788-851D-C21040CCA327Q26995211-6550F117-60F0-405C-AF29-6BB9BD984A6CQ27000279-755CAC34-C65E-4145-B9EE-EFE35251E8C2Q27650252-6ACC6D2E-DA4E-40B5-B607-303C58182D3AQ27684072-78E51D4D-019F-4C68-ADAA-AEF96FF36C25Q27687474-8B8146AD-73E1-4F36-95B5-A6E8FF7507ECQ28085561-C266B320-48D0-4194-8279-1767BC8BB9EFQ28085631-D768D8E3-DD17-46BF-BF27-AF1AD7ECD30BQ28116515-E85DBE76-89F1-4D4E-B1C7-86F64A239F0DQ28255526-B7C08457-9424-4F96-A3D4-C29B6D8F560EQ28277182-CF01D18B-1572-41EF-AB1F-5A655E075C75Q28283167-F50B2586-3FC1-4E40-8CE5-049E7ED3EB91Q28384349-1E604840-2D1F-4793-87AA-364788951343Q28384526-8AEE35DF-CE47-49B5-B0BE-9E27AABDEE85Q28384783-26608149-706F-4772-A4A3-36D203D70CB8Q28386244-F86C12A7-D4EC-4204-BB1B-38EF960EABABQ28386665-D19DAC1B-7359-4326-8C11-E4E11E432DECQ28387384-78F74FD2-F06E-4F64-9ACE-1D90149714A5Q28388589-1306D0FF-F258-463D-B74F-325B85F76DB2Q28391506-BB3FF2F1-CAD0-4551-A04F-C52D3791E2AEQ28394210-C2C70ED9-2B23-4804-BC56-FE6EE732E5D2Q28396785-4E393D3B-2A54-49C9-BEF3-02F9A3044385Q28574082-CFBA6160-E8D4-4369-A607-6F8239781AAFQ28593237-7F4E87C5-F731-46C4-857E-970408EF7BE7Q28817936-E5CBD980-89A7-4993-872A-82CA4FE7CCE4Q28910182-3D9D2861-62C8-4973-83E7-25409B78327D
P2860
The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm
description
2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2002
@ast
im September 2002 veröffentlichter wissenschaftlicher Artikel
@de
scientific article (publication date: 27 September 2002)
@en
vedecký článok (publikovaný 2002/09/27)
@sk
vědecký článek publikovaný v roce 2002
@cs
wetenschappelijk artikel (gepubliceerd op 2002/09/27)
@nl
наукова стаття, опублікована у вересні 2002
@uk
name
The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm
@ast
The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm
@en
The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm
@nl
type
label
The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm
@ast
The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm
@en
The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm
@nl
prefLabel
The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm
@ast
The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm
@en
The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm
@nl
P2860
P3181
P356
P1476
The Keap1 BTB/POZ dimerization function is required to sequester Nrf2 in cytoplasm
@en
P2093
Laurie M Zipper
R Timothy Mulcahy
P2860
P304
P3181
P356
10.1074/JBC.M206530200
P407
P577
2002-09-27T00:00:00Z