The DOI matches its Crossref record; 69 of the 69 references it cites were found in a registry or an index.
Exposure to hydrogen peroxide induces oxidation and activation of AMP-activated protein kinase
Open accessAbstract
Although metabolic conditions associated with an increased AMP/ATP ratio are primary factors in the activation of 5'-adenosine monophosphate-activated protein kinase (AMPK), a number of recent studies have shown that increased intracellular levels of reactive oxygen species can stimulate AMPK activity, even without a decrease in cellular levels of ATP. We found that exposure of recombinant AMPKαβγ complex or HEK 293 cells to H(2)O(2) was associated with increased kinase activity and also resulted in oxidative modification of AMPK, including S-glutathionylation of the AMPKα and AMPKβ subunits. In experiments using C-terminal truncation mutants of AMPKα (amino acids 1-312), we found that mutation of cysteine 299 to alanine diminished the ability of H(2)O(2) to induce kinase activation, and mutation of cysteine 304 to alanine totally abrogated the enhancing effect of H(2)O(2) on kinase activity. Similar to the results obtained with H(2)O(2)-treated HEK 293 cells, activation and S-glutathionylation of the AMPKα subunit were present in the lungs of acatalasemic mice or mice treated with the catalase inhibitor aminotriazole, conditions in which intracellular steady state levels of H(2)O(2) are increased. These results demonstrate that physiologically relevant concentrations of H(2)O(2) can activate AMPK through oxidative modification of the AMPKα subunit. The present findings also imply that AMPK activation, in addition to being a response to alterations in intracellular metabolic pathways, is directly influenced by cellular redox status.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Recent lines of evidence have demonstrated AMPK responsiveness to imbalanced redox status, thus bringing new insights into the networks of redox-stimulated signals upstream of AMPK (Table 1) [42,43,44,45,46,47,48,49,50,51].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [48]
In the citing paper
“Exogenous or glucose oxidase-generated hydrogen peroxide induced direct S-glutathionylation on the AMPKα subunit at Cys299 and Cys304, which contributes to AMPK activation [48].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [48]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
Yun, H., Lee, M., Kim, S. S., & Ha, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412994200 · Cited by 147
RetractedReduction in the incidence of type 2 diabetes with lifestyle intervention or metformin
(2002) · New England Journal of Medicine · doi:10.1056/nejmoa012512 · Cited by 19,011
Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855
Mechanisms Underlying Acute Protection From Cardiac Ischemia-Reperfusion Injury
Murphy, E., & Steenbergen, C. (2008) · Physiological Reviews · doi:10.1152/physrev.00024.2007 · Cited by 1,504
Hawley, S. A., Davison, M., Woods, A., Davies, S. P., Beri, R. K., Carling, D., & Hardie, D. G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.44.27879 · Cited by 1,264
AMP-Activated Protein Kinase in Metabolic Control and Insulin Signaling
Towler, M. C., & Hardie, D. G. (2007) · Circulation Research · doi:10.1161/01.res.0000256090.42690.05 · Cited by 1,262
Schulz, T. J., Zarse, K., Voigt, A., Urban, N., Birringer, M., & Ristow, M. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.08.011 · Cited by 1,209
AMP-activated protein kinase signaling in metabolic regulation
Long, Y. C. (2006) · Journal of Clinical Investigation · doi:10.1172/jci29044 · Cited by 1,125
Shibata, R., Sato, K., Pimentel, D. R., Takemura, Y., Kihara, S., Ohashi, K., Funahashi, T., Ouchi, N., & Walsh, K. (2005) · Nature Medicine · doi:10.1038/nm1295 · Cited by 982
Management of cellular energy by the AMP‐activated protein kinase system
Hardie, D. G., Scott, J. W., Pan, D. A., & Hudson, E. R. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00560-x · Cited by 868
AMP-Activated Protein Kinase – Development of the Energy Sensor Concept
Hardie, D. G., Hawley, S. A., & Scott, J. W. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.108944 · Cited by 813
Use of Cells Expressing γ Subunit Variants to Identify Diverse Mechanisms of AMPK Activation
Hawley, S. A., Ross, F. A., Chevtzoff, C., Green, K. A., Evans, A., Fogarty, S., Towler, M. C., Brown, L. J., Ogunbayo, O. A., Evans, A. M., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.04.001 · Cited by 773
Scott, J. W., Hawley, S. A., Green, K. A., Anis, M., Stewart, G., Scullion, G. A., Norman, D. G., & Hardie, D. G. (2004) · Journal of Clinical Investigation · doi:10.1172/jci19874 · Cited by 754
Russell, R. R., Li, J., Coven, D. L., Pypaert, M., Zechner, C., Palmeri, M., Giordano, F. J., Mu, J., Birnbaum, M. J., & Young, L. H. (2004) · Journal of Clinical Investigation · doi:10.1172/jci19297 · Cited by 738
Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle
Winder, W. W., Holmes, B. F., Rubink, D. S., Jensen, E. B., Chen, M., & Holloszy, J. O. (2000) · Journal of Applied Physiology · doi:10.1152/jappl.2000.88.6.2219 · Cited by 709
Metformin in non-alcoholic steatohepatitis.
Marchesini, G., Bianchi, G., Tomassetti, S., Zoli, M., & Melchionda, N. (2001) · The Lancet · doi:10.1016/s0140-6736(01)06042-1 · Cited by 682
Metformin reverses fatty liver disease in obese, leptin-deficient mice.
Lin, H. Z., Yang, S. Q., Chuckaree, C., Kuhajda, F., Ronnet, G., & Diehl, A. M. (2000) · Nature Medicine · doi:10.1038/79697 · Cited by 673
The regulation of AMP-activated protein kinase by phosphorylation
STEIN, S. C., Woods, A., Jones, N. A., DAVISON, M. D., & Carling, D. (2000) · Biochemical Journal · doi:10.1042/bj3450437 · Cited by 605
Kudo, N., Barr, A., Barr, R. L., Desai, S. S., & Lopaschuk, G. D. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.29.17513 · Cited by 565
AMPK: A Key Sensor of Fuel and Energy Status in Skeletal Muscle
Hardie, D. G., & Sakamoto, K. (2006) · Physiology · doi:10.1152/physiol.00044.2005 · Cited by 536
Molecular Mechanisms and Clinical Implications of Reversible Protein S -Glutathionylation
Mieyal, J. J., Gallogly, M. M., Qanungo, S., Sabens, E. A., & Shelton, M. D. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2089 · Cited by 523
S-glutathionylation in protein redox regulation
Dalle‐Donne, I., Rossi, R., Giustarini, D., Colombo, R., & Milzani, A. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.06.014 · Cited by 506
DAVIES, S. P., Carling, D., & Hardie, D. G. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb15185.x · Cited by 431
Shelton, M. D., Chock, P., & Mieyal, J. J. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.348 · Cited by 425
Gundewar, S., Calvert, J. W., Jha, S. K., Toedt‐Pingel, I., Ji, S. Y., Nunez, D. J., Ramachandran, A., Anaya-Cisneros, M., Tian, R., & Lefer, D. J. (2008) · Circulation Research · doi:10.1161/circresaha.108.190918 · Cited by 425
Functional Domains of the α1 Catalytic Subunit of the AMP-activated Protein Kinase
Crute, B. E., Seefeld, K. J., Gamble, J., Kemp, B. E., & Witters, L. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.52.35347 · Cited by 370
Irrcher, I., Ljubicic, V., & Hood, D. A. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00267.2007 · Cited by 356
Emerling, B. M., Weinberg, F., Snyder, C., Burgess, Z., Mutlu, G. M., Viollet, B., Budinger, G. R. S., & Chandel, N. S. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.02.019 · Cited by 330
Zhao, X., Zmijewski, J. W., Lorne, E., Liu, G., Park, Y.-J., Tsuruta, Y., & Abraham, E. H. (2008) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.90210.2008 · Cited by 303
Self-citationThe Regulation of AMP-Activated Protein Kinase by H2O2
Choi, S.-L., Kim, S.-J., Lee, K.-T., Kim, J., Mu, J., Birnbaum, M. J., Soo Kim, S., & Ha, J. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5544 · Cited by 294
S‐Glutathionylation: from redox regulation of protein functions to human diseases
Giustarini, D., Rossi, R., Milzani, A., Colombo, R., & Dalle‐Donne, I. (2004) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2004.tb00275.x · Cited by 281
Kim, J.-R., Yoon, H. W., Kwon, K., Lee, S.-R., & Rhee, S. G. (2000) · Analytical Biochemistry · doi:10.1006/abio.2000.4623 · Cited by 273
Nucleotide Release Provides a Mechanism for Airway Surface Liquid Homeostasis
Lazarowski, E. R., Tarran, R., Grubb, B. R., van Heusden, C. A., Okada, S. F., & Boucher, R. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405367200 · Cited by 234
Self-citationYing, J., Clavreul, N., Sethuraman, M., Adachi, T. K., & Cohen, R. A. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.07.014 · Cited by 218
Role of reactive oxygen species in contraction‐mediated glucose transport in mouse skeletal muscle
Sandström, M., Zhang, S., Bruton, J. D., Silva, J., Reid, M. B., Westerblad, H., & Katz, A. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.110601 · Cited by 213
Structural insight into the autoinhibition mechanism of AMP-activated protein kinase
Chen, L., Jiao, Z., Zheng, L., Zhang, Y., Xie, S.-T., Wang, Z., & Wu, J. (2009) · Nature · doi:10.1038/nature08075 · Cited by 200
Wrona, M., Patel, K., & Wardman, P. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.10.022 · Cited by 195
Evans, A. M., Mustard, K. J. W., Wyatt, C. N., Peers, C., Dipp, M., Kumar, P., Kinnear, N. P., & Hardie, D. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510040200 · Cited by 191
AMPKα1 regulates the antioxidant status of vascular endothelial cells
Colombo, S. L., & Moncada, S. (2009) · Biochemical Journal · doi:10.1042/bj20090613 · Cited by 175
Mitochondrial Respiratory Complex I Regulates Neutrophil Activation and Severity of Lung Injury
Żmijewski, J. W., Lorne, E., Zhao, X., Tsuruta, Y., Sha, Y., Liu, G., Siegal, G. P., & Abraham, E. H. (2008) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200710-1602oc · Cited by 167
Self-citationCoordinated release of nucleotides and mucin from human airway epithelial Calu‐3 cells
Kreda, S. M., Okada, S. F., van Heusden, C. A., O’Neal, W. K., Gabriel, S. E., Abdullah, L. H., Davis, C. W., Boucher, R. C., & Lazarowski, E. R. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2007.139840 · Cited by 166
Self-citationRegulation of Signal Transduction Through Protein Cysteine Oxidation
Cross, J. V., & Templeton, D. J. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1819 · Cited by 162
Posttranslational Modifications of the 5′-AMP-activated Protein Kinase β1 Subunit
Mitchelhill, K. I., Michell, B. J., House, C. M., Stapleton, D., Dyck, J. R. B., Gamble, J., Ullrich, C., Witters, L. A., & Kemp, B. E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.39.24475 · Cited by 158
Schulz, E., Dopheide, J. F., Schuhmacher, S., Thomas, S. R., Chen, K., Daiber, A., Wenzel, P., Münzel, T. F., & Keaney, J. F. (2008) · Circulation · doi:10.1161/circulationaha.108.784289 · Cited by 150
Żmijewski, J. W., Moellering, D. R., Goffe, C. L., Landar, A. L., Ramachandran, A., & Darley-Usmar, V. M. (2005) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00015.2005 · Cited by 149
Methodology for the measurement of mucociliary function in the mouse by scintigraphy
Foster, W. M., Walters, D. M., Longphre, M. V., Macri, K., & Miller, L. M. (2001) · Journal of Applied Physiology · doi:10.1152/jappl.2001.90.3.1111 · Cited by 141
Toyoda, T., Hayashi, T., Miyamoto, L., Yonemitsu, S., Nakano, M., Tanaka, S., Ebihara, K., Masuzaki, H., Hosoda, K., Inoue, G., et al. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00487.2003 · Cited by 139
Sukhodub, A., Jovanović, S., Du, Q., Budas, G. R., Clelland, A. K., Shen, M., Sakamoto, K., Tian, R., & Jovanović, A. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20862 · Cited by 136
Iseli, T. J., Walter, M., van Denderen, B. J. W., Katsis, F., Witters, L. A., Kemp, B. E., Michell, B. J., & Stapleton, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412993200 · Cited by 134
Role of AMP-activated protein kinase in healthy and diseased hearts
Dolinsky, V. W., & Dyck, J. R. B. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00329.2006 · Cited by 134
Conserved α-Helix Acts as Autoinhibitory Sequence in AMP-activated Protein Kinase α Subunits
Pang, T., Xiong, B., Li, J.-Y., Qiu, B., Jin, G.-Z., Shen, J., & Li, J. X. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605790200 · Cited by 118
Horie, T., Ono, K., Nagao, K., Nishi, H., Kinoshita, M., Kawamura, T., Wada, H., Shimatsu, A., Kita, T., & Hasegawa, K. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.21353 · Cited by 118
Dual Mechanisms Regulating AMPK Kinase Action in the Ischemic Heart
Baron, S. J., Li, J., Russell, R. R., Neumann, D., Miller, E. J., Tuerk, R. D., Wallimann, T., Hurley, R. L., Witters, L. A., & Young, L. H. (2005) · Circulation Research · doi:10.1161/01.res.0000155723.53868.d2 · Cited by 108
Antiinflammatory Effects of Hydrogen Peroxide in Neutrophil Activation and Acute Lung Injury
Zmijewski, J. W., Lorne, E., Zhao, X., Tsuruta, Y., Sha, Y., Liu, G., & Abraham, E. H. (2009) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200806-851oc · Cited by 96
Self-citationWatanabe, N., Zmijewski, J. W., Takabe, W., Umezu‐Goto, M., Goffe, C. L., Sekine, A., Landar, A. L., Watanabe, A., Aoki, J., Arai, H., et al. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.050648 · Cited by 95
Self-citationLamberts, R. R., Onderwater, G., Hamdani, N., Vreden, M. J. A., Steenhuisen, J., Eringa, E. C., Loer, S. A., Stienen, G. J. M., & Bouwman, R. A. (2009) · Circulation · doi:10.1161/circulationaha.108.828426 · Cited by 93
Zhang, M., Dong, Y., Xu, J., Xie, Z., Wu, Y., Song, P., Guzman, M., Wu, J., & Zou, M.-H. (2008) · Circulation Research · doi:10.1161/circresaha.107.163253 · Cited by 82
AMP-activated protein kinase conducts the ischemic stress response orchestra
Young, L. H. (2008) · Circulation · doi:10.1161/circulationaha.107.713115 · Cited by 82
Involvement of Vitronectin in Lipopolysaccaride-Induced Acute Lung Injury
Tsuruta, Y., Park, Y.-J., Siegal, G. P., Liu, G., & Abraham, E. H. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.10.7079 · Cited by 73
Self-citationS-Glutathionylation of the Rpn2 Regulatory Subunit Inhibits 26 S Proteasomal Function
Zmijewski, J. W., Banerjee, S., & Abraham, E. H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.028902 · Cited by 67
Self-citationParticipation of mitochondrial respiratory complex III in neutrophil activation and lung injury
Zmijewski, J. W., Lorne, E., Banerjee, S., & Abraham, E. H. (2009) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.90522.2008 · Cited by 66
Self-citationŻmijewski, J. W., Zhao, X., Xu, Z., & Abraham, E. H. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00618.2006 · Cited by 64
Self-citationShin, E., Schram, K., Zheng, X., & Sweeney, G. (2009) · Journal of Cellular Physiology · doi:10.1002/jcp.21883 · Cited by 60
Strassheim, D., Asehnoune, K., Park, J., Kim, J. Y., He, Q., Richter, D., Mitra, S., Arcaroli, J. J., Kuhn, K., & Abraham, E. H. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00296.2003 · Cited by 54
Self-citationSensitive and real-time determination of H2O2 release from intact peroxisomes
Mueller, S., Weber, A., Fritz, R., Mütze, S., Rost, D., Walczak, H., Völkl, A., & Stremmel, W. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3630483 · Cited by 51
CD14 is an essential mediator of LPS-induced airway disease
Brass, D. M., Hollingsworth, J. W., McElvania, E., Garantziotis, S., Hossain, I., & Schwartz, D. A. (2007) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00282.2006 · Cited by 45
Sensitive and real-time determination of H2O2 release from intact peroxisomes
Mueller, S., Weber, A., Fritz, R., et al. (2002) · Biochemical Journal · doi:10.1042/bj3630483 · Cited by 32
Modulation of SCFβ-TrCP-dependent IκBα Ubiquitination by Hydrogen Peroxide
Banerjee, S., Zmijewski, J. W., Lorne, E., Liu, G., Sha, Y., & Abraham, E. H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.060822 · Cited by 24
Self-citationAnalysis of Protein Redox Modification by Hypoxia
Choi, K., Park, S., Baek, S., Dey‐Rao, R., Park, Y., Zhang, H., Ip, C. C. Y., Park, E., Kim, Y. H., & Park, J. H. (2006) · Preparative Biochemistry & Biotechnology · doi:10.1080/10826060500388520 · Cited by 11
Flagged first, then by citations
Cited by
Sorted by citations
AMPK: a nutrient and energy sensor that maintains energy homeostasis
Hardie, D. G., Ross, F. A., & Hawley, S. A. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3311 · Cited by 4,602
Oxidative stress and autophagy: The clash between damage and metabolic needs
Filomeni, G., De Zio, D., & Cecconi, F. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.150 · Cited by 2,195
Reactive Oxygen Species in Metabolic and Inflammatory Signaling
Forrester, S. J., Kikuchi, D. S., Hernandes, M. S., Xu, Q., & Griendling, K. K. (2018) · Circulation Research · doi:10.1161/circresaha.117.311401 · Cited by 2,081
AMPK: Mechanisms of Cellular Energy Sensing and Restoration of Metabolic Balance
Garcia, D., & Shaw, R. J. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.05.032 · Cited by 2,061
Role of oxidative stress in the pathogenesis of nonalcoholic fatty liver disease
Chen, Z., Tian, R., She, Z., Cai, J., & Li, H. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.02.025 · Cited by 1,340
Metadata
- Authors
- Zmijewski, J. W., Banerjee, S., Bae, H., Friggeri, A., Lazarowski, E. R., & Abraham, E.
- Affiliations
- University of Alabama at Birmingham (US)
- University of North Carolina at Chapel Hill (US)
- Corresponding author
- Zmijewski, Jaroslaw W.
- Abraham, Edward
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2010-10
- Volume
- 285
- Issue
- 43
- Pages
- 33154-33164
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2963401
- OpenAlex
- W2073966685
- Cited by
- 441
- References
- 68
- Citations by year
- 2026: 21 · 2025: 35 · 2024: 30 · 2023: 22 · 2022: 41 · 2021: 40 · 2020: 45 · 2019: 28 · 2018: 27 · 2017: 27 · 2016: 26 · 2015: 30 · 2014: 22 · 2013: 22 · 2012: 15
- FWCI
- 6.12
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Carolina Digital Repository (University of North Carolina at Chapel Hill) (submittedVersion)
- UNC Libraries
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (HL-62221, P01HL034322, HL 76206, R01HL076206, R01HL062221)
- National Institute of General Medical Sciences (R01GM087748, GM87748)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- AMPK, hydrogen peroxide, oxidative modification, S-glutathionylation, reactive oxygen species, cysteine residues, redox state, catalase inhibition, 3-amino-1,2,4-triazole, AMP/ATP ratio, kinase activation
- MeSH terms
- Adenosine Monophosphate, Adenosine Triphosphate, Amitrole, Animals, Catalase, Cell Line, Enzyme Induction, Enzyme Inhibitors, Glutathione, Humans, Hydrogen Peroxide, Mutation, Oxidation-Reduction, Protein Processing, Post-Translational, Oxidants, Catalytic Domain, Acatalasia, Mice, AMP-Activated Protein Kinases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
