The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Succination of Proteins by Fumarate: Mechanism of Inactivation of Glyceraldehyde‐3‐Phosphate Dehydrogenase in Diabetes
Open accessAbstract
S ‐(2‐succinyl)cysteine (2SC) is a chemical modification of proteins formed by a Michael addition reaction between the Krebs cycle intermediate, fumarate, and thiol groups in protein—a process known as succination of protein. Succination causes irreversible inactivation of glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH) in vitro . GAPDH was immunoprecipitated from muscle of diabetic rats, then analyzed by ultra‐performance liquid chromatography–electrospray ionization–mass spectroscopy. Succination of GAPDH was increased in muscle of diabetic rats, and the extent of succination correlated strongly with the decrease in specific activity of the enzyme. We propose that 2SC is a biomarker of mitochondrial and oxidative stress in diabetes and that succination of GAPDH and other thiol proteins may provide the chemical link between glucotoxicity and the pathogenesis of diabetic complications.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“This chemical modification of proteins at the catalytic cysteine residues regulates protein functions (46).”
From Alzheimer's Disease–Associated Amyloid-β Precursor Protein Prevents Aging Stress–Induced Mitophagy and Fumarate Depletion to Improve Antitumor Immunity (2025) · cites this paper as [46]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Succination is a post-translational modification resulting from increased fumarate levels (46).”
From Alzheimer's Disease–Associated Amyloid-β Precursor Protein Prevents Aging Stress–Induced Mitophagy and Fumarate Depletion to Improve Antitumor Immunity (2025) · cites this paper as [46]
In the citing paper
“More recently, Kornberg and colleagues (2018) suggested that a potential consequence of elevated fumarate levels is to negatively regulate glycolysis via succination of the active site cysteine residue (C152) in GAPDH99,100.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [99]
In the citing paper
“Importantly, inhibition of aerobic glycolysis by the specific GAPDH inhibitor heptelidic acid (HA) and 2-deoxyglucose (2-DG) recapitulated the immunomodulatory effects of DMF in vitro, while in vivo administration of HA inhibited the development of experimental autoimmune encephalomyelitis (EAE), a murine model of MS99.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [99]
In the citing paper
“Intriguingly, endogenous fumarate was also found to succinate GAPDH in both mouse and human macrophages, suggesting that elevated fumarate levels may act as an endogenous anti-inflammatory signal to limit inflammation, however, the precise role of fumarate accumulation remains an open question to be explored.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [99]
In the citing paper
“Two pro-inflammatory T cell subsets implicated in the pathogenesis of MS, namely TH1 and TH17 cells, rely heavily on aerobic glycolysis and treatment with DMF or MMF inhibited their development in vitro, as previously reported99,101,102, 49.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [99]
In the citing paper
“Two pro-inflammatory T cell subsets implicated in the pathogenesis of MS, namely TH1 and TH17 cells, rely heavily on aerobic glycolysis and treatment with DMF or MMF inhibited their development in vitro, as previously reported99,101,102, 49.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [99]
In the citing paper
“This suggestion arose from the observation that the cell-permeable fumaric esters, DMF and MMF, modify and irreversibly inhibit GAPDH enzymatic activity and aerobic glycolysis in peripheral blood mononuclear cells (PBMCs) from mice and MS patients treated with DMF99.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [99]
In the citing paper
“Importantly, inhibition of aerobic glycolysis by the specific GAPDH inhibitor heptelidic acid (HA) and 2-deoxyglucose (2-DG) recapitulated the immunomodulatory effects of DMF in vitro, while in vivo administration of HA inhibited the development of experimental autoimmune encephalomyelitis (EAE), a murine model of MS99.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [99]
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
The Pathobiology of Diabetic Complications
Brownlee, M. (2005) · Diabetes · doi:10.2337/diabetes.54.6.1615 · Cited by 5,339
Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage
Nishikawa, T., Edelstein, D., Du, X. L., Yamagishi, S.-I., Matsumura, T., Kaneda, Y., Yorek, M. A., Beebe, D., Oates, P. J., Hammes, H.-P., et al. (2000) · Nature · doi:10.1038/35008121 · Cited by 4,277
A Common Mechanism of Cellular Death Induced by Bactericidal Antibiotics
Kohanski, M. A., Dwyer, D. J., Hayete, B., Lawrence, C. A., & Collins, J. J. (2007) · Cell · doi:10.1016/j.cell.2007.06.049 · Cited by 2,982
Du, X., Matsumura, T., Edelstein, D., Rossetti, L., Zsengellér, Z. K., Szabó, C., & Brownlee, M. (2003) · Journal of Clinical Investigation · doi:10.1172/jci18127 · Cited by 843
The Hyperglycemia-induced Inflammatory Response in Adipocytes
Lin, Y., Berg, A. H., Iyengar, P., Lam, T. K. T., Giacca, A., Combs, T. P., Rajala, M. W., Du, X., Rollman, B., Li, W., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411863200 · Cited by 507
Alderson, N. L., Wang, Y., Blatnik, M., Frizzell, N., Walla, M. D., Lyons, T. J., Alt, N., Carson, J. A., Nagai, R., Thorpe, S. R., et al. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2006.03.005 · Cited by 202
Self-citationInactivation of Glyceraldehyde-3-Phosphate Dehydrogenase by Fumarate in Diabetes
Blatnik, M., Frizzell, N., Thorpe, S. R., & Baynes, J. (2007) · Diabetes · doi:10.2337/db07-0838 · Cited by 141
Self-citationSuccination of Protein Thiols during Adipocyte Maturation
Nagai, R., Brock, J. W. C., Blatnik, M., Baatz, J. E., Bethard, J. R., Walla, M. D., Thorpe, S. R., Baynes, J., & Frizzell, N. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703551200 · Cited by 122
Self-citationA mechanistic view of mitochondrial death decision pores
Belizário, J. E., Alves, J. V., Occhiucci, J. M., Garay-Malpartida, M., & Sesso, A. (2007) · Brazilian Journal of Medical and Biological Research · doi:10.1590/s0100-879x2006005000109 · Cited by 89
Proteomic Analysis of the Site Specificity of Glycation and Carboxymethylation of Ribonuclease
Brock, J. W. C., Hinton, D. J. S., Cotham, W. E., Metz, T., Thorpe, S. R., Baynes, J., & Ames, J. M. (2003) · Journal of Proteome Research · doi:10.1021/pr0340173 · Cited by 82
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Mitochondrial TCA cycle metabolites control physiology and disease
Martínez-Reyes, I., & Chandel, N. S. (2020) · Nature Communications · doi:10.1038/s41467-019-13668-3 · Cited by 2,813
Adam, J., Hatipoglu, E., O'Flaherty, L., Ternette, N., Sahgal, N., Lockstone, H., Baban, D., Nye, E., Stamp, G. W., Wolhuter, K., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.09.006 · Cited by 585
Ooi, A., Wong, J.-C., Petillo, D., Roossien, D., Perrier-Trudova, V., Whitten, D., Min, B. W. H., Tan, M.-H., Zhang, Z., Yang, X. J., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.08.024 · Cited by 401
Coupling Krebs cycle metabolites to signalling in immunity and cancer
Ryan, D. G., Murphy, M. P., Frezza, C., Prag, H. A., Chouchani, E. T., O’Neill, L. A., & Mills, E. L. (2018) · Nature Metabolism · doi:10.1038/s42255-018-0014-7 · Cited by 398
Sirover, M. A. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.05.010 · Cited by 333
Redox regulation of mitochondrial function with emphasis on cysteine oxidation reactions
Mailloux, R. J., Jin, X., & Willmore, W. G. (2013) · Redox Biology · doi:10.1016/j.redox.2013.12.011 · Cited by 321
Fumarate Is Cardioprotective via Activation of the Nrf2 Antioxidant Pathway
Ashrafian, H., Czibik, G., Bellahcene, M., Aksentijević, D., Smith, A. C., Mitchell, S. J., Dodd, M. S., Kirwan, J., Byrne, J. J., Ludwig, C., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.01.017 · Cited by 302
Oncometabolites in renal cancer
Yong, C., Stewart, G. D., & Frezza, C. (2019) · Nature Reviews Nephrology · doi:10.1038/s41581-019-0210-z · Cited by 216
Oncometabolites: Unconventional triggers of oncogenic signalling cascades
Sciacovelli, M., & Frezza, C. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.025 · Cited by 184
Features and regulation of non-enzymatic post-translational modifications
Harmel, R. K., & Fiedler, D. (2018) · Nature Chemical Biology · doi:10.1038/nchembio.2575 · Cited by 171
Inhibition of Mitochondrial Aconitase by Succination in Fumarate Hydratase Deficiency
Ternette, N., Yang, M., Laroyia, M., Kitagawa, M., O’Flaherty, L., Wolhulter, K., Igarashi, K., Saito, K., Kato, K., Fischer, R., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.02.013 · Cited by 158
Fumarate hydratase in cancer: A multifaceted tumour suppressor
Schmidt, C., Sciacovelli, M., & Frezza, C. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.05.002 · Cited by 166
Targeting GPX4 in human cancer: Implications of ferroptosis induction for tackling cancer resilience
Lee, J., & Roh, J. (2023) · Cancer Letters · doi:10.1016/j.canlet.2023.216119 · Cited by 152
Cui, C., Yang, F., & Li, Q. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.901565 · Cited by 145
Hyperglycemic Stress and Carbon Stress in Diabetic Glucotoxicity
Luo, X., Wu, J., Jing, S., & Yan, L. (2016) · Aging and Disease · doi:10.14336/ad.2015.0702 · Cited by 145
Haythorne, E., Lloyd, M., Walsby-Tickle, J., Tarasov, A. I., Sandbrink, J. B., Portillo, I., Terrón-Expósito, R., Sachse, G., Cyranka, M., Rohm, M., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34095-x · Cited by 118
Fumarate hydratase (FH) and cancer: a paradigm of oncometabolism
Valcárcel-Jiménez, L., & Frezza, C. (2023) · British Journal of Cancer · doi:10.1038/s41416-023-02412-w · Cited by 117
Lückel, C., Picard, F. S. R., Raifer, H., Carrascosa, L. C., Guralnik, A., Zhang, Y., Klein, M., Bittner, S., Steffen, F., Moos, S., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13731-z · Cited by 106
Emerging Role of the Inflammasome and Pyroptosis in Hypertension
Miguel, C. D., Pelegrı́n, P., Baroja‐Mazo, A., & Cuevas, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031064 · Cited by 105
Cardiac anaplerosis in health and disease: food for thought
Rosiers, C. D., Labarthe, F., Lloyd, S. G., & Chatham, J. C. (2011) · Cardiovascular Research · doi:10.1093/cvr/cvr055 · Cited by 94
Post-translational modifications and their implications in cancer
Dutta, H., & Jain, N. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1240115 · Cited by 96
Rare insights into cancer biology
Adam, J., Yang, M., Soga, T., & Pollard, P. J. (2013) · Oncogene · doi:10.1038/onc.2013.222 · Cited by 90
Bénit, P., Letouzé, É., Rak, M., Aubry, L., Burnichon, N., Favier, J., Gimenez‐Roqueplo, A., & Rustin, P. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.03.013 · Cited by 89
Merkley, E. D., Metz, T., Smith, R. D., Baynes, J., & Frizzell, N. (2013) · Mass Spectrometry Reviews · doi:10.1002/mas.21382 · Cited by 86
Self-citationAdvances in hereditary leiomyomatosis and renal cell carcinoma (HLRCC) research
Ooi, A. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.10.016 · Cited by 85
Diabetes Induces Lysine Acetylation of Intermediary Metabolism Enzymes in the Kidney
Kosanam, H., Thai, K., Zhang, Y., Advani, A., Connelly, K. A., Diamandis, E. P., & Gilbert, R. E. (2014) · Diabetes · doi:10.2337/db12-1770 · Cited by 72
GAPDH: Biological Properties and Diversity
Seidler, N. W. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-4716-6 · Cited by 74
Zheng, H., Wu, J., Jin, Z. H., & Yan, L. (2016) · Biochemistry Insights · doi:10.4137/bci.s36141 · Cited by 73
Enhancing Top-Down Proteomics of Brain Tissue with FAIMS
Fulcher, J. M., Makaju, A., Moore, R. J., Zhou, M., Bennett, D. A., De Jager, P. L., Qian, W.-J., Paša-Tolić, L., & Petyuk, V. A. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00049 · Cited by 68
Fumaric acid diesters deprive cultured primary astrocytes rapidly of glutathione
Schmidt, M., & Dringen, R. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2010.01.006 · Cited by 66
Metabolic implications of hypoxia and pseudohypoxia in pheochromocytoma and paraganglioma
Kľučková, K., & Tennant, D. A. (2018) · Cell and Tissue Research · doi:10.1007/s00441-018-2801-6 · Cited by 68
Rahmadi, A., Steiner, N., & Münch, G. W. (2011) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.2011.079 · Cited by 63
Mitochondrial redox and TCA cycle metabolite signaling in the heart
Vujić, A., Koo, A., Prag, H. A., & Krieg, T. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.02.041 · Cited by 62
Ginsenoside Rc ameliorated atherosclerosis via regulating gut microbiota and fecal metabolites
Xie, B., Zu, X., Wang, Z., Xu, X., Liu, G., & Liu, R. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.990476 · Cited by 64
Succination of proteins in diabetes
Frizzell, N., Lima, M., & Baynes, J. (2010) · Free Radical Research · doi:10.3109/10715762.2010.524643 · Cited by 59
Self-citationSDHA gain-of-function engages inflammatory mitochondrial retrograde signaling via KEAP1–Nrf2
Burgener-Gasser, A.-V., Bantug, G. R., Meyer, B. J., Higgins, R., Ghosh, A., Bignucolo, O., Ma, E. H., Loeliger, J., Unterstab, G., Geigges, M., et al. (2019) · Nature Immunology · doi:10.1038/s41590-019-0482-2 · Cited by 57
Pyroptosis and Redox Balance in Kidney Diseases
Cuevas, S., & Pelegrı́n, P. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8243 · Cited by 55
Ferroptosis: Mechanism and connections with cutaneous diseases
Liu, L., Lian, N., Shi, L., Hao, Z., & Chen, K. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1079548 · Cited by 52
Functional implications of fumarate-induced cysteine succination
Guberović, I., & Frezza, C. (2024) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2024.05.003 · Cited by 52
Zhou, Z., Ibekwe, E., & Chornenkyy, Y. (2018) · Antioxidants · doi:10.3390/antiox7010016 · Cited by 44
Johnson, T. I., Costa, A. S. H., Ferguson, A. N., & Frezza, C. (2018) · Cell Death & Disease · doi:10.1038/s41419-018-0912-3 · Cited by 40
Formation of protein cross-links by singlet oxygen-mediated disulfide oxidation
Jiang, S., Carroll, L., Mariotti, M., Hägglund, P., & Davies, M. J. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101874 · Cited by 40
Pattern-Recognition Receptors and Immunometabolic Reprogramming: What We Know and What to Explore
Kumar, V., & Stewart, J. H. (2024) · Journal of Innate Immunity · doi:10.1159/000539278 · Cited by 39
Ooi, A., & Furge, K. A. (2012) · 癌症:英文版 · doi:10.5732/cjc.012.10102 · Cited by 38
Nalbantoğlu, S., & Karadağ, A. (2021) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2021.114031 · Cited by 34
Niehaus, T. D., & Hillmann, K. B. (2020) · FEBS Journal · doi:10.1111/febs.15284 · Cited by 34
New insights into Gasdermin D pore formation
Kappelhoff, S., Margheritis, E. G., & Cosentino, K. (2024) · Biochemical Society Transactions · doi:10.1042/bst20230549 · Cited by 31
Signals from the Circle: Tricarboxylic Acid Cycle Intermediates as Myometabokines
Maurer, J., Hoene, M., & Weigert, C. (2021) · Metabolites · doi:10.3390/metabo11080474 · Cited by 27
Dynamic regulators of ferroptosis: Post-translational modifications in ferroptotic cell death
Yan, Y.-X., Zhou, H., Shang, X.-G., Xu, P., Tang, X., Zheng, X., Yu, L., Li, C.-T., Xie, T., & Lou, J.-S. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2025.107815 · Cited by 24
Fumarate integrates metabolism and immunity in diseases
Cheng, J., Xiao, Y., & Jiang, P. (2025) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2025.03.008 · Cited by 25
Niehaus, T. D., Folz, J. S., McCarty, D. R., Cooper, A. J. L., Amador, D. M., Fiehn, O., & Hanson, A. D. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002925 · Cited by 24
Giallongo, S., Costa, F., Longhitano, L., Giallongo, C., Ferrigno, J., Tropea, E., Vicario, N., Volti, G. L., Parenti, R., Barbagallo, I. A., et al. (2023) · Metabolites · doi:10.3390/metabo13070880 · Cited by 22
Alur, V. C., Raju, V., Vastrad, B. M., Vastrad, C. M., Kavatagimath, S., & Kotrashetti, S. (2023) · Clinical Medicine Insights Endocrinology and Diabetes · doi:10.1177/11795514231155635 · Cited by 21
Succination of Protein Thiols in Human Brain Aging
Jové, M., Pradas, I., Mota‐Martorell, N., Cabré, R., Ayala, V., Ferrer, I., & Pamplona, R. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00052 · Cited by 22
Regulation of airway fumarate by host and pathogen promotes Staphylococcus aureus pneumonia
Chen, Y.-T., Liu, Z., Fucich, D., Giulieri, S. G., Liu, Z., Wadhwa, R., Rios-Delgado, G., Henschel, H., Tyagi, N., Olivier, F. A. B., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-62453-y · Cited by 18
Discovery of post-translational modifications in immunometabolism by chemical proteomics
Zhang, Y., Qin, W., & Wang, C. (2020) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2020.09.013 · Cited by 19
Unconventional metabolites in chromatin regulation
Gapa, L., Alfardus, H., & Fischle, W. (2022) · Bioscience Reports · doi:10.1042/bsr20211558 · Cited by 21
Ferroptosis in liver cancer: a key role of post-translational modifications
Xu, Y. C., Xing, Z., Suliman, R. A. I., Liu, Z., & Tang, F. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1375589 · Cited by 22
Matthews, A., Schönfelder, J., Lagies, S., Schleicher, E., Kammerer, B., Ellis, H. R., Stull, F. W., & Teufel, R. (2021) · FEBS Journal · doi:10.1111/febs.16193 · Cited by 18
A computational analysis of S-(2-succino)cysteine sites in proteins
Miglio, G., Sabatino, A., Veglia, E., Giraudo, M. T., Beccuti, M., & Cordero, F. (2015) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2015.11.003 · Cited by 16
Genie in a bottle: controlled release helps tame natural polypharmacology?
Long, M. J. C., Liu, X., & Aye, Y. (2019) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.02.014 · Cited by 14
Saatchi, F., & Kirchmaier, A. L. (2019) · Genetics · doi:10.1534/genetics.119.302238 · Cited by 13
Cellular Exposure to Chloroacetanilide Herbicides Induces Distinct Protein Destabilization Profiles
Quanrud, G. M., Lyu, Z., Balamurugan, S. V., Canizal, C., Wu, H., & Genereux, J. C. (2023) · ACS Chemical Biology · doi:10.1021/acschembio.3c00338 · Cited by 14
Boyer, F., Diotel, N., Girard, D., Rondeau, P., Essop, M. F., & Bourdon, E. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.03.068 · Cited by 13
The role of immunomodulatory metabolites in shaping the inflammatory response of macrophages
Park, D., Lim, G., Yoon, S., Yi, H., & Choi, D. W. (2022) · BMB Reports · doi:10.5483/bmbrep.2022.55.11.128 · Cited by 12
TopPICR: A Companion R Package for Top-Down Proteomics Data Analysis
Martin, E. A., Fulcher, J. M., Zhou, M., Monroe, M. E., & Petyuk, V. (2023) · Journal of Proteome Research · doi:10.1021/acs.jproteome.2c00570 · Cited by 13
Identification of a S-(2-succino)cysteine breakdown pathway that uses a novel S-(2-succino) lyase
Hillmann, K. B., Goethel, M. E., Erickson, N. A., & Niehaus, T. D. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102639 · Cited by 12
The Molecular Role of HIF1α Is Elucidated in Chronic Myeloid Leukemia
Singh, V. K., Singh, R., Kushwaha, R., Verma, S. P., Tripathi, A. K., & Mahdi, A. A. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.912942 · Cited by 11
Nrf2 protein in melanoma progression, as a new means of treatment
Feng, Q., Xu, X., & Zhang, S. (2023) · Pigment Cell & Melanoma Research · doi:10.1111/pcmr.13137 · Cited by 12
Mishra, A., & Surolia, A. (2017) · IUBMB Life · doi:10.1002/iub.1683 · Cited by 11
Kassir, M. F., Lee, H. G., Oleinik, N. V., Wofford, W., Walton, C., Atilgan, F. C., Janneh, A. H., Chakraborty, P., Calisir, K., Percin, E., et al. (2025) · Cancer Research · doi:10.1158/0008-5472.can-24-4740 · Cited by 10
Bezafibrate Reduces Elevated Hepatic Fumarate in Insulin-Deficient Mice
Frankó, A., Irmler, M., Prehn, C. P., Heinzmann, S. S., Schmitt‐Kopplin, P., Adamski, J., Beckers, J., von Kleist-Retzow, J., Wiesner, R. J., Häring, H., et al. (2022) · Biomedicines · doi:10.3390/biomedicines10030616 · Cited by 10
Disrupting metabolism to treat autoimmunity
Matsushita, M., & Pearce, E. J. (2018) · Science · doi:10.1126/science.aat4984 · Cited by 10
Yip, J., Wang, S., Tan, J., Lim, T. K., Lin, Q., Zhang, Y., Karmon, O., Pines, O., & Lehming, N. (2021) · iScience · doi:10.1016/j.isci.2021.103354 · Cited by 10
Endo, S., Nishiyama, A., Suyama, M., Takemura, M., Soda, M., Chen, H., Tajima, K., El-Kabbani, O. A. L., Bunai, Y., Hara, A., et al. (2014) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2014.09.023 · Cited by 10
Kawaguchi, S., Sato, K., Izawa, J., Takayama, N., Hayakawa, H., Tominaga, K., Endo, H., Kouki, T., Ohno, N., & Kanda, Y. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-08040-x · Cited by 9
Investigating the Relationship between Diabetes and Alzheimer’s Disease:
Sahrawat, T. R., & Dwivedi, J. (2020) · Journal of Science and Sustainable Development · doi:10.4314/jssd.v7i1.1 · Cited by 6
Target for Diverse Chemical Modifications
Seidler, N. W. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-4716-6_6 · Cited by 5
Novel Insights into FH-associated Disease are KEAPing the Lid on Oncogenic HIF Signalling
Adam, J., Ratcliffe, P. J., & Pollard, P. J. (2011) · Oncotarget · doi:10.18632/oncotarget.348 · Cited by 5
Ferroptosis in cancer: integrating multi-omics, AI-driven biomarkers, and translational challenges
Taki, A. G., Shareef, A., Arora, V., Oweis, R. J., Jyothi, S. R., Singh, U., Sahoo, S., Chauhan, A. S., Alimova, F., Sameer, H. N., et al. (2026) · Clinica Chimica Acta · doi:10.1016/j.cca.2026.121131 · Cited by 5
Multilayer metabolomic integration reveals bioenergetic disruption in Long COVID
García‐Hidalgo, M. C., Mota‐Martorell, N., González, J., Benitez, I. D., Jové, M., Barbé, F., Amigó, N., Pamplona, R., de Gonzalo‐Calvo, D., & Torres, G. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-07684-3 · Cited by 4
Activated Thiol Sepharose‐based proteomic approach to quantify reversible protein oxidation
Xu, Y., Andrade, J., Ueberheide, B. M., & Neel, B. G. (2019) · The FASEB Journal · doi:10.1096/fj.201900693r · Cited by 4
Global chemical modifications comparison of human plasma proteome from two different age groups
Liu, Y., Pan, X., Zhao, M., & Gao, Y. (2020) · Scientific Reports · doi:10.1038/s41598-020-72196-z · Cited by 6
Mashima, K., Sato, K., Ikeda, T., Izawa, J., Takayama, N., Hayakawa, H., Kawaguchi, S., Nakano, H., Nagayama, T., Umino, K., et al. (2022) · British Journal of Haematology · doi:10.1111/bjh.18082 · Cited by 3
Analysis of key genes and pathways associated with the pathogenesis of Type 2 diabetes mellitusPreprint
Alur, V. C., Raju, V., Vastrad, B. M., Vastrad, C. M., & Kotrashetti, S. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.08.12.456106 · Cited by 3
Cysteine S -acetylation is a post-translational modification involved in metabolic regulationPreprint
Keenan, E. K., Bareja, A., Lam, Y., Grimsrud, P. A., & Hirschey, M. D. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.21.595030 · Cited by 3
Wang, R., & Yan, Z. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1671115 · Cited by 2
Protein succination as a potential surrogate biomarker of airway obstruction. The ilervas project
González, J., Gràcia‐Lavedan, E., Pamplona, R., Fernández, E., Lecube, A., de-Torres, J. P., Barbé, F., Torres, G., Benabdelhak, I., Bermúdez-López, M., et al. (2020) · Respiratory Medicine · doi:10.1016/j.rmed.2020.106124 · Cited by 2
A big picture of the mitochondria-mediated signals: From mitochondria to organism
Acar, N. V., & Özgül, R. K. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.08.032 · Cited by 2
Sharkus, R., Thakkar, R., Kolson, D. L., & Constantinescu, C. S. (2023) · Biomedicines · doi:10.3390/biomedicines11051387 · Cited by 3
Modification of Cysteine Residues in Protein by Endogenous Oxidants and Electrophiles
Frizzell, N., & Baynes, J. (2009) · Wiley eBooks · doi:10.1002/9783527628100.ch2 · Cited by 2
Self-citationPomar, C. A., Martín‐Chamorro, R. A., Zouhar, P., Castillo, P., Čajka, T., Kopecký, J., Palou, A., Palou, M., & Picó, C. (2026) · The FASEB Journal · doi:10.1096/fj.202501729rrr · Cited by 1
Selective Biocatalytic Michael Addition Reactions
Wohlgemuth, R. (2026) · ChemSusChem · doi:10.1002/cssc.202502620 · Cited by 1
Pulmonary Hypertension as a Metabolic Disease
Fessel, J. P., & Oldham, W. M. (2015) · Springer eBooks · doi:10.1007/978-3-319-23594-3_8 · Cited by 1
Epigenetic and Posttranslational Regulation of Ferroptosis
Zhang, Y., Xiong, J., & Wang, M. (2023) · Springer eBooks · doi:10.1007/978-3-031-39171-2_18 · Cited by 1
Stop the “Vicious Cycle” induced by Glycative Stress.
Yonei, Y., Yagi, M., & Takabe, W. (2020) · doi:10.24659/gsr.7.1_13 · Cited by 1
Alam, Q., Krishnamurthy, S., & Tomar, M. (2023) · Research Square · doi:10.21203/rs.3.rs-2594608/v1 · Cited by 1
Molecular Biology and Genetics
Klomp, J. A., Dykema, K. J., Teh, B. T., & Furge, K. (2013) · Springer eBooks · doi:10.1007/978-1-4614-7236-0_2
Caracterização de interações proteína-DNA em tripanossomas.
Pariona-Llanos, R. (2014) · doi:10.11606/t.42.2014.tde-22092014-184950
news & analysis | Bioanalysis young investigator
Vooght-Johnson, R. D., & Place, A. (2012)
Metadata
- Authors
- Blatnik, M., Thorpe, S. R., & Baynes, J. W.
- Affiliations
- University of South Carolina (US)
- Corresponding author
- Baynes, John W.
- ORCID
- Blatnik, Matthew
- Venue
- Annals of the New York Academy of Sciences
- Publisher
- Wiley
- Published
- 2008-04
- Volume
- 1126
- Issue
- 1
- Pages
- 272-275
- ISSN
- 0077-8923 (ISSN-L)
- 1749-6632
- PMC
- PMC2423376
- OpenAlex
- W1673039816
- Cited by
- 109
- References
- 10
- Citations by year
- 2026: 7 · 2025: 7 · 2024: 6 · 2023: 14 · 2022: 9 · 2021: 10 · 2020: 8 · 2019: 8 · 2018: 8 · 2017: 2 · 2016: 5 · 2015: 2 · 2014: 4 · 2013: 5 · 2012: 5
- FWCI
- 1.99
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Annals of the New York Academy of Sciences (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- U.S. Public Health Service
- National Institute of Diabetes and Digestive and Kidney Diseases (R37DK019971, DK-19971)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Keywords
- fumarate, Michael addition, glyceraldehyde-3-phosphate dehydrogenase, enzyme inactivation, diabetes mellitus, diabetic muscle, mitochondrial stress, oxidative stress, glucotoxicity, biomarkers, diabetes complications
- MeSH terms
- Diabetes Mellitus, Fumarates, Glucosephosphate Dehydrogenase, Humans, Kinetics, Peptide Fragments, Proteins, Reference Values, Succinates, Diabetes Complications
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