PGAM5, a Bcl-XL-interacting protein, is a novel substrate for the redox-regulated Keap1-dependent ubiquitin ligase complex

Points of control in inflammation

Nathan, C. (2002) · Nature · doi:10.1038/nature01320 · Cited by 2,738 · see citing works

Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2

Kobayashi, A., Kang, M.-I., Okawa, H., Ohtsuji, M., Zenke, Y., Chiba, T., Igarashi, K., & Yamamoto, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.16.7130-7139.2004 · Cited by 2,224 · see citing works

Pathways of Oxidative Damage

Imlay, J. A. (2003) · Annual Review of Microbiology · doi:10.1146/annurev.micro.57.030502.090938 · Cited by 2,206 · see citing works

Function and regulation of cullin–RING ubiquitin ligases

Petroski, M. D., & Deshaies, R. J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1547 · Cited by 2,148 · see citing works

TIGAR, a p53-Inducible Regulator of Glycolysis and Apoptosis

Bensaad, K., Tsuruta, A., Selak, M. A., Vidal, M. N. C., Nakano, K., Bartrons, R., Gottlieb, E., & Vousden, K. H. (2006) · Cell · doi:10.1016/j.cell.2006.05.036 · Cited by 2,019 · see citing works

Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants

Dinkova-Kostova, A. T., Holtzclaw, W. D., Cole, R. N., Itoh, K., Wakabayashi, N., Katoh, Y., Yamamoto, M., & Talalay, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172398899 · Cited by 1,947 · see citing works

Oxidative Damage Is the Earliest Event in Alzheimer Disease

Nunomura, A., Perry, G., Aliev, G., Hirai, K., Takeda, A., Balraj, E. K., Jones, P. K., Ghanbari, H., Wataya, T., Shimohama, S., et al. (2001) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/60.8.759 · Cited by 1,885 · see citing works

Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics

Letai, A., Bassik, M. C., Walensky, L. D., Sorcinelli, M. D., Weiler, S., & Korsmeyer, S. J. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00127-7 · Cited by 1,677 · see citing works

Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress

Zhang, D. D., & Hannink, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.22.8137-8151.2003 · Cited by 1,480 · see citing works

Keap1 Is a Redox-Regulated Substrate Adaptor Protein for a Cul3-Dependent Ubiquitin Ligase Complex

Zhang, D. D., Lo, S., Cross, J. V., Templeton, D. J., & Hannink, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.24.10941-10953.2004 · Cited by 1,262 · see citing works

Untitled work

(2002) · PubMed · Cited by 1,190 · see citing works

Protection against electrophile and oxidant stress by induction of the phase 2 response: Fate of cysteines of the Keap1 sensor modified by inducers

Wakabayashi, N., Dinkova-Kostova, A. T., Holtzclaw, W. D., Kang, M.-I., Kobayashi, A., Yamamoto, M., Kensler, T. W., & Talalay, P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307301101 · Cited by 986 · see citing works

The Keap1-BTB Protein Is an Adaptor That Bridges Nrf2 to a Cul3-Based E3 Ligase: Oxidative Stress Sensing by a Cul3-Keap1 Ligase

Cullinan, S. B., Gordan, J. D., Jin, J., Harper, J. W., & Diehl, J. A. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.19.8477-8486.2004 · Cited by 986 · see citing works

The SCFbeta -TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in Ikappa Balpha and beta -catenin and stimulates Ikappa Balpha ubiquitination in vitroPreprint

Winston, J. T., Strack, P. R., Beer‐Romero, P., Chu, C. Y., Elledge, S. J., & Harper, J. W. (1999) · Genes & Development · doi:10.1101/gad.13.3.270 · Cited by 949 · see citing works

Oxidative and Electrophilic Stresses Activate Nrf2 through Inhibition of Ubiquitination Activity of Keap1

Kobayashi, A., Kang, M.-I., Watai, Y., Tong, K. I., Shibata, T., Uchida, K., & Yamamoto, M. P. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.26.1.221-229.2006 · Cited by 933 · see citing works

Rbx1, a Component of the VHL Tumor Suppressor Complex and SCF Ubiquitin Ligase

Kamura, T., Koepp, D. M., Conrad, M. N., Skowyra, D., Moreland, R. J., Iliopoulos, O., Lane, W. S., Kaelin, W. G., Elledge, S. J., Conaway, R. C., et al. (1999) · Science · doi:10.1126/science.284.5414.657 · Cited by 786 · see citing works

Identification of the NF-E2-related Factor-2-dependent Genes Conferring Protection against Oxidative Stress in Primary Cortical Astrocytes Using Oligonucleotide Microarray Analysis

Lee, J., Calkins, M. J., Chan, K., Kan, Y. W., & Johnson, J. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211558200 · Cited by 783 · see citing works

Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer

Padmanabhan, B., Tong, K. I., Ohta, T., Nakamura, Y., Scharlock, M., Ohtsuji, M., Kang, M.-I., Kobayashi, A., Yokoyama, S., & Yamamoto, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.013 · Cited by 735 · see citing works

Modulation of Gene Expression by Cancer Chemopreventive Dithiolethiones through the Keap1-Nrf2 Pathway

Kwak, M.-K., Wakabayashi, N., Itoh, K., Motohashi, H., Yamamoto, M. P., & Kensler, T. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211898200 · Cited by 661 · see citing works

The contribution of endogenous sources of DNA damage to the multiple mutations in cancer

Jackson, A. L., & Loeb, L. A. (2001) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(01)00091-4 · Cited by 630 · see citing works

Structure of a β-TrCP1-Skp1-β-Catenin Complex

Wu, G., Xu, G., Schulman, B. A., Jeffrey, P. D., Harper, J. W., & Pavletich, N. P. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00234-x · Cited by 612 · see citing works

Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling

Lo, S., Li, X., Henzl, M. T., Beamer, L. J., & Hannink, M. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601243 · Cited by 604 · see citing works

Structural Basis for Phosphodependent Substrate Selection and Orientation by the SCFCdc4 Ubiquitin Ligase

Orlicky, S. M., Tang, X., Willems, A. R., Tyers, M., & Sicheri, F. (2003) · Cell · doi:10.1016/s0092-8674(03)00034-5 · Cited by 510 · see citing works

Modifying specific cysteines of the electrophile-sensing human Keap1 protein is insufficient to disrupt binding to the Nrf2 domain Neh2

Eggler, A. L., Liu, G., Pezzuto, J. M., van Breemen, R. B., & Mesecar, A. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502402102 · Cited by 459 · see citing works

Development of Protacs to Target Cancer-promoting Proteins for Ubiquitination and Degradation

Sakamoto, K. M., Kim, K. B., Verma, R., Ransick, A., Stein, B., Crews, C. M., & Deshaies, R. J. (2003) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t300009-mcp200 · Cited by 425 · see citing works

Identification of Sensor Cysteines in Human Keap1 Modified by the Cancer Chemopreventive Agent Sulforaphane

Hong, F., Freeman, M. L., & Liebler, D. C. (2005) · Chemical Research in Toxicology · doi:10.1021/tx0502138 · Cited by 404 · see citing works

Identification of the interactive interface and phylogenic conservation of the Nrf2‐Keap1 system

Kobayashi, M., Itoh, K., Suzuki, T., Osanai, H., Nishikawa, K., Katoh, Y., Takagi, Y., & Yamamoto, M. P. (2002) · Genes to Cells · doi:10.1046/j.1365-2443.2002.00561.x · Cited by 340 · see citing works

Specific Patterns of Electrophile Adduction Trigger Keap1 Ubiquitination and Nrf2 Activation

Hong, F., Sekhar, K. R., Freeman, M. L., & Liebler, D. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503346200 · Cited by 316 · see citing works

DNA and Free Radicals

Aruoma, O. I., Halliwell, B. B., & DPhil, B. H. (1993) · Medical Entomology and Zoology · Cited by 283 · see citing works

The Processivity of Multiubiquitination by the APC Determines the Order of Substrate Degradation

Rapé, M., Reddy, S., & Kirschner, M. W. (2006) · Cell · doi:10.1016/j.cell.2005.10.032 · Cited by 280 · see citing works

Crystal Structure of the Kelch Domain of Human Keap1

Li, X., Zhang, D. D., Hannink, M., & Beamer, L. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410073200 · Cited by 249 · see citing works

Nuclear Oncoprotein Prothymosin α Is a Partner of Keap1: Implications for Expression of Oxidative Stress-Protecting Genes

Karapetian, R. N., Evstafieva, A. G., Abaeva, I. S., Chichkova, N. V., Filonov, G. S., Rubtsov, Y. P., Sukhacheva, E. A., Melnikov, S. V., Schneider, U., Wanker, E. E., et al. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.3.1089-1099.2005 · Cited by 173 · see citing works

Regulation of ZAP-70 Activation and TCR Signaling by Two Related Proteins, Sts-1 and Sts-2

Carpino, N., Turner, S., Mekala, D. J., Takahashi, Y., Zang, H., Geiger, T. L., Doherty, P. C., & Ihle, J. N. (2004) · Immunity · doi:10.1016/s1074-7613(03)00351-0 · Cited by 169 · see citing works

Bcl‐xL sequesters its C‐terminal membrane anchor in soluble, cytosolic homodimers

Jeong, S., Gaume, B. R., Lee, Y.-J., Hsu, Y., Ryu, S., Yoon, S., & Youle, R. J. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600225 · Cited by 162 · see citing works

Comparison of (−)-Epigallocatechin-3-Gallate Elicited Liver and Small Intestine Gene Expression Profiles Between C57BL/6J Mice and C57BL/6J/Nrf2 (−/−) Mice

Shen, G., Xu, C., Hu, R., Jain, M. R., Nair, S., Lin, W., Yang, C. S., Chan, J. Y., & Kong, A.-N. T. (2005) · Pharmaceutical Research · doi:10.1007/s11095-005-7546-8 · Cited by 159 · see citing works

Nrf1 Is Targeted to the Endoplasmic Reticulum Membrane by an N-terminal Transmembrane Domain

Wang, W., & Chan, J. Y. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602802200 · Cited by 158 · see citing works

Suppressors of T-cell Receptor Signaling Sts-1 and Sts-2 Bind to Cbl and Inhibit Endocytosis of Receptor Tyrosine Kinases

Kowanetz, K., Crosetto, N., Haglund, K., Schmidt, M. H. H., Heldin, C.-H., & Dikic, I. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403759200 · Cited by 147 · see citing works

Structure, function, and evolution of phosphoglycerate mutases: comparison with fructose-2,6-bisphosphatase, acid phosphatase, and alkaline phosphatase

Jedrzejas, M. J. (2000) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(00)00007-9 · Cited by 145 · see citing works

Coronary atherosclerosis and somatic mutations: an overview of the contributive factors for oxidative DNA damage

Andreassi, M. G. (2002) · Mutation Research/Reviews in Mutation Research · doi:10.1016/s1383-5742(02)00089-3 · Cited by 138 · see citing works

Antioxidant and cytoprotective responses to redox stress

Mathers, J. E., Fraser, J. A., McMahon, M. J., Saunders, R. D. C., Hayes, J. D., & McLellan, L. I. (2004) · Biochemical Society Symposia · doi:10.1042/bss0710157 · Cited by 134 · see citing works

CAND1-Mediated Substrate Adaptor Recycling Is Required for Efficient Repression of Nrf2 by Keap1

Lo, S., & Hannink, M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.4.1235-1244.2006 · Cited by 99 · see citing works

In Vitro Selection and Characterization of Bcl-XL-binding Proteins from a Mix of Tissue-specific mRNA Display Libraries

Hammond, P. W., Alpin, J., Rise, C. E., Wright, M. C., & Kreider, B. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011641200 · Cited by 94 · see citing works

Evolution of the Phosphoglycerate mutase Processed Gene in Human and Chimpanzee Revealing the Origin of a New Primate Gene

Betrán, E., Wang, W., Li, J., & Long, M. (2002) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a004124 · Cited by 77 · see citing works

Identification, cDNA Cloning, and Targeted Deletion of p70, a Novel, Ubiquitously Expressed SH3 Domain-Containing Protein

Carpino, N., Kobayashi, R., Zang, H., Takahashi, Y., Jou, S.-T., Feng, J., Nakajima, H., & Ihle, J. N. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.21.7491-7500.2002 · Cited by 75 · see citing works

Fetal Alz-50 Clone 1 Interacts with the Human Orthologue of the Kelch-like Ech-Associated Protein

Strachan, G. D., Morgan, K. L., Otis, L. L., Caltagarone, J., Gittis, A. H., Bowser, R. P., & Jordan‐Sciutto, K. L. (2004) · Biochemistry · doi:10.1021/bi0494166 · Cited by 34 · see citing works

Dimethylarsinic acid effects on DNA damage and oxidative stress related biochemical parameters in B6C3F1 mice

Ahmad, S., Anderson, W. L., & Kitchin, K. T. (1999) · Cancer Letters · doi:10.1016/s0304-3835(99)00022-1 · Cited by 30 · see citing works

Expression of the fetal Alz-50 clone 1 protein induces apoptotic cell death

Strachan, G. D., Ostrow, L. A., & Jordan‐Sciutto, K. L. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.08.127 · Cited by 17 · see citing works

Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease

Ngo, V., & Duennwald, M. L. (2022) · Antioxidants · doi:10.3390/antiox11122345 · Cited by 1,130 · see citing works

The cytoprotective role of the Keap1–Nrf2 pathway

Baird, L., & Dinkova‐Kostova, A. T. (2011) · Archives of Toxicology · doi:10.1007/s00204-011-0674-5 · Cited by 1,029 · see citing works

The Mitochondrial Phosphatase PGAM5 Functions at the Convergence Point of Multiple Necrotic Death Pathways

Wang, Z., Jiang, H., Chen, S., Du, F., & Wang, X. (2012) · Cell · doi:10.1016/j.cell.2011.11.030 · Cited by 949 · see citing works

NRF2 and KEAP1 mutations: permanent activation of an adaptive response in cancer

Hayes, J. D., & McMahon, M. J. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2008.12.008 · Cited by 870 · see citing works

Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease

Tebay, L. E., Robertson, H., Durant, S. T., Vitale, S. R., Penning, T. M., Dinkova-Kostova, A. T., & Hayes, J. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.021 · Cited by 837 · see citing works

The Keap1–Nrf2–ARE Pathway As a Potential Preventive and Therapeutic Target: An Update

Lu, M., Ji, J., Jiang, Z., & You, Q. (2016) · Medicinal Research Reviews · doi:10.1002/med.21396 · Cited by 801 · see citing works

Stress-activated cap’n’collar transcription factors in aging and human disease

Sykiotis, G. P., & Bohmann, D. (2010) · Science Signaling · doi:10.1126/scisignal.3112re3 · Cited by 776 · see citing works

Molecular mechanisms of Nrf2‐mediated antioxidant response

Li, W., & Kong, A. T. (2008) · Molecular Carcinogenesis · doi:10.1002/mc.20465 · Cited by 786 · see citing works

A Regulatory Signaling Loop Comprising the PGAM5 Phosphatase and CK2 Controls Receptor-Mediated Mitophagy

Chen, G., Han, Z., Feng, D., Chen, Y., Chen, L., Wu, H., Huang, L., Zhou, C., Cai, X., Fu, C., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.034 · Cited by 600 · see citing works

Cancer Chemoprevention Mechanisms Mediated Through the Keap1–Nrf2 Pathway

Hayes, J. D., McMahon, M. J., Chowdhry, S., & Dinkova‐Kostova, A. T. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3221 · Cited by 540 · see citing works

Oxeiptosis, a ROS-induced caspase-independent apoptosis-like cell-death pathway

Holze, C., Michaudel, C., Mackowiak, C., Haas, D. A., Benda, C., Hubel, P., Pennemann, F. L., Schnepf, D., Wettmarshausen, J., Braun, M., et al. (2017) · Nature Immunology · doi:10.1038/s41590-017-0013-y · Cited by 459 · see citing works

Nrf2 and Keap1 Abnormalities in Non–Small Cell Lung Carcinoma and Association with Clinicopathologic Features

Solis, L. M., Behrens, C., Dong, W., Suraokar, M. B., Ozburn, N. C., Moran, C. A., Corvalán, A. H., Biswal, S. S., Swisher, S. G., Bekele, B. N., et al. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-09-3352 · Cited by 430 · see citing works

KEAP1 E3 Ligase-Mediated Downregulation of NF-κB Signaling by Targeting IKKβ

Lee, D.-F., Kuo, H.-P., Liu, M., Chou, C.-K., Xia, W., Du, Y., Shen, J., Chen, C.-T., Huo, L., Hsu, M.-C., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.07.025 · Cited by 399 · see citing works

Canonical and non-canonical mechanisms of Nrf2 activation

Silva‐Islas, C. A., & Maldonado, P. D. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.06.013 · Cited by 393 · see citing works

PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria

Lo, S.-C., & Hannink, M. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.02.014 · Cited by 300 · see citing works

The Nrf2-antioxidant response element pathway: a target for regulating energy metabolism

Vomhof‐DeKrey, E. E., & Picklo, M. J. (2012) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2012.03.005 · Cited by 283 · see citing works

Parkin and mitophagy in cancer

Bernardini, J. P., Lazarou, M., & Dewson, G. (2016) · Oncogene · doi:10.1038/onc.2016.302 · Cited by 282 · see citing works

Beyond repression of Nrf2: An update on Keap1

Kopacz, A., Klóska, D., Forman, H. J., Józkowicz, A., & Grochot‐Przeczek, A. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.03.023 · Cited by 262 · see citing works

Physical and functional interaction of sequestosome 1 with Keap1 regulates the Keap1-Nrf2 cell defense pathway

Copple, I. M., Lister, A., Obeng, A. D., Kitteringham, N. R., Jenkins, R. E., Layfield, R., Foster, B. J., Goldring, C. E., & Park, B. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.096545 · Cited by 260 · see citing works

Update on the Kelch-like (KLHL) gene family

Dhanoa, B. S., Cogliati, T., Satish, A. G., Bruford, E. A., & Friedman, J. S. (2013) · Human Genomics · doi:10.1186/1479-7364-7-13 · Cited by 260 · see citing works

The Crosstalk between Nrf2 and Inflammasomes

Hennig, P., Garstkiewicz, M., Grossi, S., Filippo, M. D., French, L. E., & Beer, H. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020562 · Cited by 256 · see citing works

Suppression of NF-κB signaling by KEAP1 regulation of IKKβ activity through autophagic degradation and inhibition of phosphorylation

Kim, J.-E., You, D., Lee, C., Ahn, C., Seong, J. Y., & Hwang, J. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.06.004 · Cited by 223 · see citing works

The histidine phosphatase superfamily: structure and function

Rigden, D. J. (2007) · Biochemical Journal · doi:10.1042/bj20071097 · Cited by 217 · see citing works

Molecular cross-talk between the NRF2/KEAP1 signaling pathway, autophagy, and apoptosis

Stępkowski, T. M., & Kruszewski, M. K. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.01.033 · Cited by 212 · see citing works

Depletion of RIPK3 or MLKL blocks TNF-driven necroptosis and switches towards a delayed RIPK1 kinase-dependent apoptosis

Remijsen, Q., Goossens, V., Grootjans, S., den Haute, C. V., Vanlangenakker, N., Dondelinger, Y., Roelandt, R., Bruggeman, I., Gonçalves, A. C., Bertrand, M. J. M., et al. (2014) · Cell Death and Disease · doi:10.1038/cddis.2013.531 · Cited by 203 · see citing works

The KEAP1–NRF2 System as a Molecular Target of Cancer Treatment

Taguchi, K., & Yamamoto, M. (2020) · Cancers · doi:10.3390/cancers13010046 · Cited by 195 · see citing works

Phosphoglycerate mutase 5 exacerbates cardiac ischemia-reperfusion injury through disrupting mitochondrial quality control

Zhu, H., Tan, Y., Du, W., Li, Y., Toan, S., Mui, D., Tian, F., & Zhou, H. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101777 · Cited by 188 · see citing works

Mitophagy and Oxidative Stress: The Role of Aging

Gaetano, A. D., Gibellini, L., Zanini, G., Nasi, M., Cossarizza, A., & Pinti, M. (2021) · Antioxidants · doi:10.3390/antiox10050794 · Cited by 188 · see citing works

The BCL2L1 and PGAM5 axis defines hypoxia-induced receptor-mediated mitophagy

Wu, H., Xue, D., Chen, G., Han, Z., Huang, L., Zhu, C., Wang, X., Jin, H., Wang, J., Zhu, Y., et al. (2014) · Autophagy · doi:10.4161/auto.29568 · Cited by 183 · see citing works

Comparison of Secondary Structure Formation Using 10 Different Force Fields in Microsecond Molecular Dynamics Simulations

Cino, E. A., Choy, W., & Karttunen, M. (2012) · Journal of Chemical Theory and Computation · doi:10.1021/ct300323g · Cited by 184 · see citing works

Necroptosis: an alternative cell death program defending against cancer

Chen, D., Yu, J., & Zhang, L. (2016) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2016.03.003 · Cited by 182 · see citing works

NRF2 Induction Supporting Breast Cancer Cell Survival Is Enabled by Oxidative Stress–Induced DPP3–KEAP1 Interaction

Lu, K., Alcivar, A. L., Ma, J., Foo, T. K., Zywea, S., Mahdi, A., Huo, Y., Kensler, T. W., Gatza, M. L., & Xia, B. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-2204 · Cited by 178 · see citing works

p62 at the Interface of Autophagy, Oxidative Stress Signaling, and Cancer

Nezis, I. P., & Stenmark, H. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4394 · Cited by 176 · see citing works

Increased Nrf2 Activation in Livers from Keap1-Knockdown Mice Increases Expression of Cytoprotective Genes that Detoxify Electrophiles more than those that Detoxify Reactive Oxygen Species

Reisman, S. A., Yeager, R. L., Yamamoto, M. P., & Klaassen, C. D. (2009) · Toxicological Sciences · doi:10.1093/toxsci/kfn267 · Cited by 174 · see citing works

The Keap1–Nrf2 Cell Defense Pathway – A Promising Therapeutic Target?

Copple, I. M. (2012) · Advances in pharmacology · doi:10.1016/b978-0-12-398339-8.00002-1 · Cited by 172 · see citing works

Monitoring Keap1–Nrf2 interactions in single live cells

Baird, L., Swift, S., Llères, D., & Dinkova‐Kostova, A. T. (2014) · Biotechnology Advances · doi:10.1016/j.biotechadv.2014.03.004 · Cited by 171 · see citing works

The Role of NRF2/KEAP1 Signaling Pathway in Cancer Metabolism

Song, M.-Y., Lee, D.-Y., Chun, K., & Kim, E. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094376 · Cited by 166 · see citing works

Genetic deficiency of the mitochondrial protein PGAM5 causes a Parkinson’s-like movement disorder

Lü, W., Karuppagounder, S. S., Springer, D., Allen, M. D., Zheng, L., Chao, B. N., Zhang, Y., Dawson, V. L., Dawson, T. M., & Lenardo, M. J. (2014) · Nature Communications · doi:10.1038/ncomms5930 · Cited by 161 · see citing works

Redox homeostasis, oxidative stress and mitophagy

Garza-Lombó, C., Pappa, A., Panayiotidis, M. I., & Franco, R. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.01.002 · Cited by 161 · see citing works

PGAM5: A crucial role in mitochondrial dynamics and programmed cell death

Cheng, M., Lin, N., Dong, D., Ma, J., Su, J., & Sun, L. (2020) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2020.151144 · Cited by 159 · see citing works

Mitochondrial Protein PGAM5 Regulates Mitophagic Protection against Cell Necroptosis

Lü, W., Sun, J., Yoon, J. S., Zhang, Y., Zheng, L., Murphy, E., Mattson, M. P., & Lenardo, M. J. (2016) · PLoS ONE · doi:10.1371/journal.pone.0147792 · Cited by 155 · see citing works

The Role of the Antioxidant Response in Mitochondrial Dysfunction in Degenerative Diseases: Cross-Talk between Antioxidant Defense, Autophagy, and Apoptosis

Huang, M., Chiang, S., Kalinowski, D. S., Bae, D.-H., Sahni, S., & Richardson, D. R. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/6392763 · Cited by 154 · see citing works

Keap1/Cullin3 Modulates p62/SQSTM1 Activity via UBA Domain Ubiquitination

Lee, Y., Chou, T., Pittman, S. K., Keith, A. L., Razani, B., & Weihl, C. C. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.03.030 · Cited by 154 · see citing works

Dynamic PGAM5 multimers dephosphorylate BCL-xL or FUNDC1 to regulate mitochondrial and cellular fate

Ma, K., Zhang, Z., Chang, R., Cheng, H., Mu, C., Zhao, T., Chen, L., Zhang, C., Luo, Q., Lin, J., et al. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0396-4 · Cited by 150 · see citing works

Expanding the arsenal of E3 ubiquitin ligases for proximity-induced protein degradation

Kannt, A., & Đikić, I. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.007 · Cited by 148 · see citing works

Mitochondrial phosphoglycerate mutase 5 uses alternate catalytic activity as a protein serine/threonine phosphatase to activate ASK1

Takeda, K., Komuro, Y., Hayakawa, T., Oguchi, H., Ishida, Y., Murakami, S., Noguchi, T., Kinoshita, H., Sekine, Y., Iemura, S.-I., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901823106 · Cited by 147 · see citing works

Effects of Resveratrol on the Mechanisms of Antioxidants and Estrogen in Alzheimer’s Disease

Kong, D., Yan, Y., He, X., Yang, H., Liang, B., Wang, J., He, Y., Ding, Y., & Yu, H. (2019) · BioMed Research International · doi:10.1155/2019/8983752 · Cited by 132 · see citing works

The Marburg Virus VP24 Protein Interacts with Keap1 to Activate the Cytoprotective Antioxidant Response Pathway

Edwards, M. R., Johnson, B., Mire, C. E., Xü, W., Shabman, R. S., Speller, L. N., Leung, D. W., Geisbert, T. W., Amarasinghe, G. K., & Basler, C. F. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.01.043 · Cited by 119 · see citing works

The Mitochondrial Phosphatase PGAM5 Is Dispensable for Necroptosis but Promotes Inflammasome Activation in Macrophages

Moriwaki, K., Farias Luz, N., Balaji, S., De Rosa, M. J., O’Donnell, C. L., Gough, P. J., Bertin, J., Welsh, R. M., & Chan, F. K.-M. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1501662 · Cited by 116 · see citing works

Keap1: One stone kills three birds Nrf2, IKKβ and Bcl-2/Bcl-xL

Tian, H., Zhang, B., Di, J., Jiang, G., Chen, F., Li, H., Li, L., Pei, D., & Zheng, J. (2012) · Cancer Letters · doi:10.1016/j.canlet.2012.06.007 · Cited by 110 · see citing works

Regulation ofKEAP1expression by promoter methylation in malignant gliomas and association with patient’s outcome

Muscarella, L. A., Barbano, R., D’Angelo, V., Copetti, M., Coco, M., Balsamo, T., la Torre, A., Notarangelo, A., Troiano, M., Parisi, S., et al. (2011) · Epigenetics · doi:10.4161/epi.6.3.14408 · Cited by 108 · see citing works

Subunit 6 of the COP9 signalosome promotes tumorigenesis in mice through stabilization of MDM2 and is upregulated in human cancers

Zhao, R., Yeung, S. J., Chen, J., Iwakuma, T., Su, C., Chen, B., Qu, C., Zhang, F., Chen, Y., Lin, Y., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44111 · Cited by 106 · see citing works

Identification of PGAM5 as a Mammalian Protein Histidine Phosphatase that Plays a Central Role to Negatively Regulate CD4 + T Cells

Panda, S., Srivastava, S., Zhai, L., Vaeth, M., Fuhs, S. R., Hunter, T. R., & Skolnik, E. Y. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.06.021 · Cited by 104 · see citing works

Kelch-like ECH-associated protein 1 (KEAP1) differentially regulates nuclear factor erythroid-2–related factors 1 and 2 (NRF1 and NRF2)

Tian, W., de la Vega, M. R., Schmidlin, C. J., Ooi, A., & Zhang, D. D. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000428 · Cited by 101 · see citing works

Activation of KEAP1/NRF2/P62 signaling alleviates high phosphate-induced calcification of vascular smooth muscle cells by suppressing reactive oxygen species production

Wei, R., Enaka, M., & Muragaki, Y. (2019) · Scientific Reports · doi:10.1038/s41598-019-46824-2 · Cited by 98 · see citing works

Increased cell migration and plasticity in Nrf2-deficient cancer cell lines

Rachakonda, G., Sekhar, K. R., Jowhar, D., Samson, P. C., Wikswo, J. P., Beauchamp, R. D., Datta, P. K., & Freeman, M. L. (2010) · Oncogene · doi:10.1038/onc.2010.118 · Cited by 93 · see citing works

The Loss of PGAM5 Suppresses the Mitochondrial Degeneration Caused by Inactivation of PINK1 in Drosophila

Imai, Y., Kanao, T., Sawada, T., Kobayashi, Y., Moriwaki, Y., Ishida, Y., Takeda, K., Ichijo, H., Lu, B., & Takahashi, R. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001229 · Cited by 93 · see citing works

Negative Regulation of the Keap1-Nrf2 Pathway by a p62/Sqstm1 Splicing Variant

Kageyama, S., Saito, T., Obata, M., Koide, R.-H., Ichimura, Y., & Komatsu, M. (2018) · Molecular and Cellular Biology · doi:10.1128/mcb.00642-17 · Cited by 95 · see citing works

A novel role of KEAP1/PGAM5 complex: ROS sensor for inducing mitophagy

Zeb, A., Choubey, V., Gupta, R., Kuum, M., Safiulina, D., Vaarmann, A., Gogichaishvili, N., Liiv, M., Ilves, I., Tämm, K., et al. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102186 · Cited by 92 · see citing works

The spatiotemporal regulation of the Keap1–Nrf2 pathway and its importance in cellular bioenergetics

Dinkova‐Kostova, A. T., Baird, L., Holmström, K. M., Meyer, C. J., & Abramov, A. Y. (2015) · Biochemical Society Transactions · doi:10.1042/bst20150003 · Cited by 86 · see citing works

Hyperactivity of the transcription factor Nrf2 causes metabolic reprogramming in mouse esophagus

Fu, J., Xiong, Z., Huang, C. D., Li, J., Yang, W., Han, Y., Paiboonrungruan, C., Major, M. B., Chen, K., Kang, X., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005963 · Cited by 85 · see citing works

Nordihydroguaiaretic Acid: From Herbal Medicine to Clinical Development for Cancer and Chronic Diseases

Manda, G., Rojo, A. I., Martínez‐Klimova, E., Pedraza‐Chaverrí, J., & Cuadrado, A. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00151 · Cited by 86 · see citing works

Identification and Characterization of MCM3 as a Kelch-like ECH-associated Protein 1 (KEAP1) Substrate

Mulvaney, K. M., Matson, J. P., Siesser, P. F., Tamir, T. Y., Goldfarb, D., Jacobs, T. M., Cloer, E. W., Harrison, J. S., Vaziri, C., Cook, J. G., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.729418 · Cited by 82 · see citing works

Frequency Modulated Translocational Oscillations of Nrf2 Mediate the Antioxidant Response Element Cytoprotective Transcriptional Response

Xue, M., Momiji, H., Rabbani, N., Barker, G. C., Bretschneider, T., Shmygol, A., Rand, D. A. J., & Thornalley, P. J. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5962 · Cited by 83 · see citing works

Impaired antioxidant KEAP1-NRF2 system in amyotrophic lateral sclerosis: NRF2 activation as a potential therapeutic strategy

Bono, S., Feligioni, M., & Corbo, M. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00479-8 · Cited by 83 · see citing works

Insights into the intracellular localization, protein associations and artemisinin resistance properties of Plasmodium falciparum K13

Gnädig, N. F., Stokes, B. H., Edwards, R. L., Kalantarov, G., Heimsch, K. C., Kuderjavy, M., Crane, A., Lee, M., Straimer, J., Becker, K., et al. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008482 · Cited by 81 · see citing works

Functional analysis of Cullin 3 E3 ligases in tumorigenesis

Cheng, J., Guo, J., Wang, Z. P., North, B. J., Tao, K., Dai, X., & Wei, W. (2017) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2017.11.001 · Cited by 80 · see citing works

KEAP1 Is a Redox Sensitive Target That Arbitrates the Opposing Radiosensitive Effects of Parthenolide in Normal and Cancer Cells

Xu, Y., Fang, F., Miriyala, S., Crooks, P. A., Oberley, T. D., Chaiswing, L., Noel, T. J., Holley, A. K., Zhao, Y., Kiningham, K. K., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-4297 · Cited by 79 · see citing works

The Conserved SKN-1/Nrf2 Stress Response Pathway Regulates Synaptic Function in Caenorhabditis elegans

Staab, T. A., Griffen, T. C., Corcoran, C., Evgrafov, O. V., Knowles, J. A., & Sieburth, D. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003354 · Cited by 75 · see citing works

Mitochondrial Mechanisms of Necroptosis in Liver Diseases

Xue, C., Gu, X., Li, G., Bao, Z., & Li, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010066 · Cited by 70 · see citing works

PARL: The mitochondrial rhomboid protease

Spinazzi, M., & Strooper, B. D. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.07.034 · Cited by 68 · see citing works

Type I interferon enhances necroptosis of <i>Salmonella</i> Typhimurium–infected macrophages by impairing antioxidative stress responses

Hos, N. J., Ganesan, R., Gutiérrez, S., Hos, D., Klimek, J., Abdullah, Z., Krönke, M., & Robinson, N. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201701107 · Cited by 64 · see citing works

Emerging Substrate Proteins of Kelch-like ECH Associated Protein 1 (Keap1) and Potential Challenges for the Development of Small-Molecule Inhibitors of the Keap1-Nuclear Factor Erythroid 2‑Related Factor 2 (Nrf2) Protein–Protein Interaction

Zhang, Y., Shi, Z., Zhou, Y., Xiao, Q., Wang, H., & Peng, Y. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01865 · Cited by 67 · see citing works

Role of Natural and Synthetic Compounds in Modulating NRF2/KEAP1 Signaling Pathway in Prostate Cancer

Tossetta, G., Fantone, S., Marzioni, D., & Roberta Mazzucchelli, A. (2023) · Cancers · doi:10.3390/cancers15113037 · Cited by 66 · see citing works

p62-Dependent Phase Separation of Patient-Derived KEAP1 Mutations and NRF2

Cloer, E. W., Siesser, P. F., Cousins, E. M., Goldfarb, D., Mowrey, D. D., Harrison, J. S., Weir, S., Dokholyan, N. V., & Major, M. B. (2018) · Molecular and Cellular Biology · doi:10.1128/mcb.00644-17 · Cited by 65 · see citing works

The see-saw of Keap1-Nrf2 pathway in cancer

Pandey, P., Singh, A. K., Singh, M., Tewari, M., Shukla, H. S., & Gambhir, I. S. (2017) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2017.02.006 · Cited by 65 · see citing works

Oxeiptosis: a novel pathway of melanocytes death in response to oxidative stress in vitiligo

Kang, P., Chen, J., Zhang, W., Guo, N., Yi, X., Cui, T., Chen, J., Yang, Y., Wang, Y., Du, P., et al. (2022) · Cell Death Discovery · doi:10.1038/s41420-022-00863-3 · Cited by 64 · see citing works

Phototropism: Mechanism and Outcomes

Pedmale, U. V., Celaya, R. B., & Emmanuel Liscum, A. (2010) · The Arabidopsis Book · doi:10.1199/tab.0125 · Cited by 63 · see citing works

Curcumin analog A13 alleviates oxidative stress by activating Nrf2/ARE pathway and ameliorates fibrosis in the myocardium of high-fat-diet and streptozotocin-induced diabetic rats

Xiang, L.-T., Zhang, Q., Chen, C., Wu, G., Lin, Z., Li, J., Gu, Q., & Chen, G. (2020) · Diabetology & Metabolic Syndrome · doi:10.1186/s13098-019-0485-z · Cited by 63 · see citing works

Hepatocyte-specific Keap1 deletion reduces liver steatosis but not inflammation during non-alcoholic steatohepatitis development

Ramadori, P., Drescher, H., Erschfeld, S., Schumacher, F., Berger, C., Fragoulis, A., Schenkel, J., Kensler, T. W., Wruck, C. J., Trautwein, C., et al. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.12.014 · Cited by 61 · see citing works

Innate immune evasion by filoviruses

Basler, C. F. (2015) · Virology · doi:10.1016/j.virol.2015.03.030 · Cited by 59 · see citing works

Necrosis-like death can engage multiple pro-apoptotic Bcl-2 protein family members

Tischner, D., Manzl, C., Soratroi, C., Villunger, A., & Krumschnabel, G. (2012) · APOPTOSIS · doi:10.1007/s10495-012-0756-8 · Cited by 59 · see citing works

Metabolic control of signalling pathways and metabolic auto‐regulation

Lorendeau, D., Christen, S., Rinaldi, G., & Fendt, S. (2015) · Biology of the Cell · doi:10.1111/boc.201500015 · Cited by 59 · see citing works

The Phosphorylation-Dependent Regulation of Mitochondrial Proteins in Stress Responses

Kanamaru, Y., Sekine, S., Ichijo, H., & Takeda, K. (2012) · Journal of Signal Transduction · doi:10.1155/2012/931215 · Cited by 56 · see citing works

Mazes of Nrf2 regulation

Зенков, Н. К., Kozhin, P. M., Владимирович, Ч. А., Мартинович, Г. Г., Кандалинцева, Н. В., & Брониславовна, М. Е. (2017) · Biochemistry (Moscow) · doi:10.1134/s0006297917050030 · Cited by 56 · see citing works

Insight into the Intermolecular Recognition Mechanism between Keap1 and IKKβ Combining Homology Modelling, Protein-Protein Docking, Molecular Dynamics Simulations and Virtual Alanine Mutation

Jiang, Z., Chu, H., Xi, M., Yang, T., Jia, J.-M., Huang, J., Guo, X., Zhang, X., You, Q., & Sun, H.-P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075076 · Cited by 52 · see citing works

The Cul3/Klhdc5 E3 Ligase Regulates p60/Katanin and Is Required for Normal Mitosis in Mammalian Cells

Cummings, C. M., Bentley, C. A., Perdue, S. A., Baas, P. W., & Singer, J. D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809374200 · Cited by 52 · see citing works

Amelioration of inflammatory myopathies by glucagon‐like peptide‐1 receptor agonist via suppressing muscle fibre necroptosis

Kamiya, M., Mizoguchi, F., & Yasuda, S. (2022) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.13025 · Cited by 49 · see citing works

Targeting oxeiptosis-mediated tumor suppression: a novel approach to treat colorectal cancers by sanguinarine

Pallichankandy, S., Thayyullathil, F., Cheratta, A. R., Subburayan, K., Alakkal, A., Sultana, M., Drou, N., Arshad, M. A., Tariq, S., & Galadari, S. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01376-3 · Cited by 52 · see citing works

Post-translational modifications of Keap1: the state of the art

Song, Y., Qu, Y., Mao, C., Zhang, R., Jiang, D., & Sun, X. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1332049 · Cited by 49 · see citing works

Cotargeting histone deacetylases and oncogenic BRAF synergistically kills human melanoma cells by necrosis independently of RIPK1 and RIPK3

Lai, F., Guo, S., Jin, L., Jiang, C. C., Wang, C. Y., Croft, A. J., Chi, M. N., Tseng, H.-Y., Farrelly, M. L., Atmadibrata, B., et al. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.192 · Cited by 49 · see citing works

Redox Control of Protein–DNA Interactions: From Molecular Mechanisms to Significance in Signal Transduction, Gene Expression, and DNA Replication

Shlomai, J. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.3029 · Cited by 47 · see citing works

PGAM5 is an MFN2 phosphatase that plays an essential role in the regulation of mitochondrial dynamics

Nag, S., Szederkenyi, K., Gorbenko, O., Tyrrell, H., Yip, C. M., & McQuibban, G. A. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112895 · Cited by 48 · see citing works

Degradation of Keap1 activates BH3-only proteins Bim and PUMA during hepatocyte lipoapoptosis

Cazanave, S. C., Wang, X., Zhou, H., Rahmani, M., Grant, S., Durrant, D., Klaassen, C. D., Yamamoto, M. P., & Sanyal, A. J. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.49 · Cited by 48 · see citing works

AMP-activated protein kinase protects against necroptosis via regulation of Keap1-PGAM5 complex

Wang, Y.-S., Yu, P., Wang, Y., Zhang, J., Hang, W., Yin, Z.-X., Liu, G., Chen, J., Werle, K. D., Quan, C., et al. (2018) · International Journal of Cardiology · doi:10.1016/j.ijcard.2018.01.036 · Cited by 48 · see citing works

High PGAM5 expression induces chemoresistance by enhancing Bcl-xL-mediated anti-apoptotic signaling and predicts poor prognosis in hepatocellular carcinoma patients

Cheng, J., Qian, D., Ding, X., Song, T., Cai, M., Xie, D., Wang, Y., Zhao, J., Liu, Z., Wu, Z., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-1017-8 · Cited by 48 · see citing works

Functional role of PGAM5 multimeric assemblies and their polymerization into filaments

Ruiz, K., Thaker, T. M., Agnew, C., Miller-Vedam, L. E., Trenker, R., Herrera, C., Ingaramo, M., Toso, D. B., Frost, A. S., & Jura, N. (2019) · Nature Communications · doi:10.1038/s41467-019-08393-w · Cited by 48 · see citing works

Photoproximity Profiling of Protein–Protein Interactions in Cells

McCutcheon, D. C., Lee, G., Carlos, A. J., Montgomery, J. E., & Moellering, R. E. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b06528 · Cited by 47 · see citing works

PGAM5, a Bcl-X L-interacting Protein, Is a Novel Substrate for the Redox-regulated Keap1-dependent

Complex, U. L., Lo, S.-C., & Hannink, M. (2013)

Keap1 Is a Redox-Regulated Substrate Adaptor Protein for a Cul3-Dependent Ubiquitin Ligase Complex

Zhang, D. D., Lo, S., Cross, J. V., Templeton, D. J., & Hannink, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.24.10941-10953.2004 · Cited by 1,262 · see citing works

Ubiquitination of Keap1, a BTB-Kelch Substrate Adaptor Protein for Cul3, Targets Keap1 for Degradation by a Proteasome-independent Pathway

Zhang, D. D., Lo, S., Sun, Z., Habib, G. M., Lieberman, M. W., & Hannink, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501279200 · Cited by 299 · see citing works

Proteosome-independent degradation of Keap1 1 Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteosome-independent pathway

Zhang, D. D., Lo, S.-C., Sun, Z., Habib, G. M., Lieberman, M. W., & Hannink, M. (2015)

PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria

Lo, S.-C., & Hannink, M. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.02.014 · Cited by 300 · see citing works