Methylglyoxal-derived stress: An emerging biological factor involved in the onset and progression of cancer
Abstract
Cancer is a disease characterised by uncontrolled growth and proliferation of cells. Tumours primarily show a higher rate of glucose uptake for lactate production even in the presence of functional mitochondria. An important metabolic consequence is intracellular formation of glucose-derived carbonyl reactive species such as methylglyoxal (MG). It has become clear that MG is the most potent glycation agent in our body, leading to alterations of proteins and DNA, and cellular dysfunction. In recent years, emerging evidence indicates that MG plays a role in the development of cancer. This review will examine studies regarding the effects of MG on cancer onset and progression and discuss their controversies. Finally, the utilisation of inhibitors and MG scavengers will be addressed in the context of MG-mediated stress blockade for cancer therapy.
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Methylglyoxal-mediated stress is involved in cancer progression and activates AKT signaling, suggesting that methylglyoxal scavengers may be more effective with AKT inhibitors in KRAS-mutant colorectal cancer cells.
“Methylglyoxal-mediated stress was shown to be involved in cancer progression41 and to be a potent activator of AKT signaling, suggesting that utilizing methylglyoxal scavengers in KRAS mutant colorectal cancer cells might be more effective when combined with AKT inhibitors40.”
From The metabolic landscape of RAS-driven cancers from biology to therapy (2021) · cites this paper as [41]
Cites
1 retracted
Antognelli, C., Palumbo, I., Aristei, C., & Talesa, V. N. (2014) · British Journal of Cancer · doi:10.1038/bjc.2014.280 · Cited by 57 · see citing works
RetractedBiochemistry and molecular cell biology of diabetic complications
Brownlee, M. (2001) · Nature · doi:10.1038/414813a · Cited by 9,107 · see citing works
The Warburg Effect: How Does it Benefit Cancer Cells?
Liberti, M. V., & Locasale, J. W. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.12.001 · Cited by 5,150 · see citing works
Otto Warburg's contributions to current concepts of cancer metabolism
Koppenol, W. H., Bounds, P. L., & Dang, C. V. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3038 · Cited by 3,427 · see citing works
Metabolic Reprogramming: A Cancer Hallmark Even Warburg Did Not Anticipate
Ward, P. S., & Thompson, C. B. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.02.014 · Cited by 3,233 · see citing works
Giovannucci, E., Harlan, D. M., Archer, M. C., Bergenstal, R. M., Gapstur, S. M., Habel, L. A., Pollak, M., Regensteiner, J. G., & Yee, D. (2010) · Diabetes Care · doi:10.2337/dc10-0666 · Cited by 2,366 · see citing works
The role of lipid peroxidation and antioxidants in oxidative modification of LDL
Esterbauer, H., Gebicki, J. M., Puhl, H., & Jürgens, G. (1992) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(92)90181-f · Cited by 2,307 · see citing works
Metformin—mode of action and clinical implications for diabetes and cancer
Pernicova, I., & Korbonits, M. (2014) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2013.256 · Cited by 1,345 · see citing works
Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose
Thornalley, P. J., LANGBORG, A., & Minhas, H. S. (1999) · Biochemical Journal · doi:10.1042/bj3440109 · Cited by 1,209 · see citing works
Hirsch, H. A., Iliopoulos, D., Tsichlis, P. N., & Struhl, K. (2009) · Cancer Research · doi:10.1158/0008-5472.can-09-2994 · Cited by 1,115 · see citing works
Effect of Collagen Turnover on the Accumulation of Advanced Glycation End Products
Verzijl, N., DeGroot, J., Thorpe, S. R., Bank, R. A., Shaw, J., Lyons, T. J., Bijlsma, J. W. J., Lafeber, F. P. J. G., Baynes, J., & TeKoppele, J. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006700200 · Cited by 964 · see citing works
Buzzai, M., Jones, R. G., Amaravadi, R. K., Lum, J. J., DeBerardinis, R. J., Zhao, F., Viollet, B., & Thompson, C. B. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-4447 · Cited by 923 · see citing works
Sahra, I. B., Laurent, K., Loubat, A., Giorgetti-Peraldi, S., Colosetti, P., Auberger, P., Tanti, J. F., Le Marchand-Brustel, Y., & Bost, F. (2008) · Oncogene · doi:10.1038/sj.onc.1211024 · Cited by 861 · see citing works
Curcumin Extract for Prevention of Type 2 Diabetes
Chuengsamarn, S., Rattanamongkolgul, S., Luechapudiporn, R., Phisalaphong, C., & Jirawatnotai, S. (2012) · Diabetes Care · doi:10.2337/dc12-0116 · Cited by 636 · see citing works
The Dual Roles of NRF2 in Cancer
Menegon, S., Columbano, A., & Giordano, S. (2016) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.05.002 · Cited by 633 · see citing works
Glyoxalase I – structure, function and a critical role in the enzymatic defence against glycation
Thornalley, P. J. (2003) · Biochemical Society Transactions · doi:10.1042/bst0311343 · Cited by 615 · see citing works
Ahmed, M. U., Frye, E. B., Degenhardt, T. P., Thorpe, S. R., & Baynes, J. (1997) · Biochemical Journal · doi:10.1042/bj3240565 · Cited by 605 · see citing works
Action des acides amines sur les sucres : formation des melanoidines par voie methodique
Maillard, L. (1912) · Medical Entomology and Zoology · Cited by 574 · see citing works
The formation of methylglyoxal from triose phosphates
Phillips, S. A., & Thornalley, P. J. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17638.x · Cited by 565 · see citing works
A census of amplified and overexpressed human cancer genes
Santarius, T., SHIPLEY, J. M., Brewer, D. S., Stratton, M. R., & Cooper, C. S. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2771 · Cited by 550 · see citing works
The glyoxalase system in health and disease
Thornalley, P. J. (1993) · Molecular Aspects of Medicine · doi:10.1016/0098-2997(93)90002-u · Cited by 535 · see citing works
Alimova, I. N., Liu, B., Fan, Z., Edgerton, S. M., Dillon, T., Lind, S. E., & Thor, A. D. (2009) · Cell Cycle · doi:10.4161/cc.8.6.7933 · Cited by 523 · see citing works
Glycoxidation and lipoxidation in atherogenesis
Baynes, J., & Thorpe, S. R. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00228-8 · Cited by 515 · see citing works
Shinohara, M., Thornalley, P. J., Giardino, I., Beisswenger, P. J., Thorpe, S. R., Onorato, J., & Brownlee, M. (1998) · Journal of Clinical Investigation · doi:10.1172/jci119885 · Cited by 513 · see citing works
The molecular basis for impaired hypoxia-induced VEGF expression in diabetic tissues
Thangarajah, H., Yao, D., Chang, E. I.-F., Shi, Y., Jazayeri, L., Vial, I. N., Galiano, R. D., Du, X.-L., Grogan, R. H., Galvez, M. G., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906670106 · Cited by 469 · see citing works
Metformin reduces systemic methylglyoxal levels in type 2 diabetes.
Beisswenger, P. J., Howell, S. K., Touchette, A. D., Lal, S., & Szwergold, B. S. (1999) · Diabetes · doi:10.2337/diabetes.48.1.198 · Cited by 446 · see citing works
Methylglyoxal, glyoxalase 1 and the dicarbonyl proteome
Rabbani, N., & Thornalley, P. J. (2010) · Amino Acids · doi:10.1007/s00726-010-0783-0 · Cited by 431 · see citing works
An Oncogenomics-Based In Vivo RNAi Screen Identifies Tumor Suppressors in Liver Cancer
Zender, L., Xue, W., Zuber, J. A., Semighini, C. P., Krasnitz, A., Ma, B., Zender, P., Kubicka, S., Luk, J. M., Schirmacher, P., et al. (2008) · Cell · doi:10.1016/j.cell.2008.09.061 · Cited by 425 · see citing works
Altered metabolite levels in cancer: implications for tumour biology and cancer therapy
Sullivan, L. B., Gui, D. Y., & Heiden, M. G. V. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.85 · Cited by 406 · see citing works
Metformin induces unique biological and molecular responses in triple negative breast cancer cells
Liu, B., Fan, Z., Edgerton, S. M., Deng, X.-S., Alimova, I. N., Lind, S. E., & Thor, A. D. (2009) · Cell Cycle · doi:10.4161/cc.8.13.8814 · Cited by 392 · see citing works
Methylglyoxal Modification of Protein
Oya, T., Hattori, N., Mizuno, Y., Miyata, S., Maeda, S., Osawa, T., & Uchida, K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.26.18492 · Cited by 374 · see citing works
Ahmed, N., Argirov, O. K., Minhas, H. S., CORDEIRO, C. A., & Thornalley, P. J. (2002) · Biochemical Journal · doi:10.1042/bj3640001 · Cited by 336 · see citing works
André, F., Job, B., Dessen, P., Tordai, A., Michiels, S., Liedtke, C., Richon, C., Yan, K., Wang, B., Vassal, G., et al. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-1791 · Cited by 336 · see citing works
The role of methylglyoxal and the glyoxalase system in diabetes and other age-related diseases
Maessen, D. E., Stehouwer, C. D. A., & Schalkwijk, C. G. (2015) · Clinical Science · doi:10.1042/cs20140683 · Cited by 335 · see citing works
Self-citationHyperglycemia as a Risk Factor for Cancer Progression
Ryu, T. Y., Park, J., & Scherer, P. E. (2014) · Diabetes & Metabolism Journal · doi:10.4093/dmj.2014.38.5.330 · Cited by 331 · see citing works
Prevention of pancreatic cancer induction in hamsters by metformin
Schneider, M. B., Matsuzaki, H., Haorah, J., Ulrich, A. B., Standop, J., Ding, X., Adrian, T. E., & Pour, P. M. (2001) · Gastroenterology · doi:10.1053/gast.2001.23258 · Cited by 327 · see citing works
Kisfalvi, K., Eibl, G., Sinnett‐Smith, J. W., & Rozengurt, E. (2009) · Cancer Research · doi:10.1158/0008-5472.can-09-0418 · Cited by 315 · see citing works
Zhang, D.-H., Tai, L. K., Wong, L. L., Chiu, L.-L., Sethi, S. K., & Koay, E. S. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400221-mcp200 · Cited by 312 · see citing works
Xue, M., Rabbani, N., Momiji, H., Imbasi, P., Anwar, M. M., Kitteringham, N. R., Park, B. K., Souma, T., Moriguchi, T., Yamamoto, M. P., et al. (2011) · Biochemical Journal · doi:10.1042/bj20111648 · Cited by 302 · see citing works
Repositioning metformin for cancer prevention and treatment
Quinn, B. J., Kitagawa, H., Memmott, R. M., Gills, J. J., & Dennis, P. A. (2013) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2013.05.004 · Cited by 284 · see citing works
Jagt, D. L. V., Robinson, B., Taylor, K. K., & Hunsaker, L. A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42844-x · Cited by 280 · see citing works
Shipanova, I. N., Glomb, M. A., & Nagaraj, R. H. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0195 · Cited by 279 · see citing works
Mechanism for the formation of methylglyoxal from triosephosphates
Richard, J. P. (1993) · Biochemical Society Transactions · doi:10.1042/bst0210549 · Cited by 272 · see citing works
HSP27, 70 and 90, anti-apoptotic proteins, in clinical cancer therapy
Wang, X., Chen, M., Zhou, J., & Zhang, X. (2014) · International Journal of Oncology · doi:10.3892/ijo.2014.2399 · Cited by 272 · see citing works
Pompliano, D. L., Peyman, A., & Knowles, J. R. (1990) · Biochemistry · doi:10.1021/bi00465a005 · Cited by 272 · see citing works
In vitro metformin anti-neoplastic activity in epithelial ovarian cancer
Gotlieb, W. H., Saumet, J., Beauchamp, M.-C., Gu, J., Lau, S. K., Pollak, M., & Bruchim, I. (2008) · Gynecologic Oncology · doi:10.1016/j.ygyno.2008.04.008 · Cited by 267 · see citing works
Jagt, D. L. V., & Hunsaker, L. A. (2003) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00212-0 · Cited by 256 · see citing works
Zhuang, Y., & Miskimins, W. K. (2008) · Journal of Molecular Signaling · doi:10.1186/1750-2187-3-18 · Cited by 247 · see citing works
Ruggiero-Lopez, D., Lecomte, M., Moinet, G., Patereau, G., Lagarde, M., & Wiernsperger, N. F. (1999) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00263-4 · Cited by 238 · see citing works
Yao, D., Taguchi, T., Matsumura, T., Pestell, R. G., Edelstein, D., Giardino, I., Suske, G., Rabbani, N., Thornalley, P. J., Sarthy, V. P., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704703200 · Cited by 233 · see citing works
Increased Methylglyoxal and Oxidative Stress in Hypertensive Rat Vascular Smooth Muscle Cells
Wu, L., & Juurlink, B. H. J. (2002) · Hypertension · doi:10.1161/hy0302.105207 · Cited by 229 · see citing works
Westwood, M. E., & Thornalley, P. J. (1995) · Journal of Protein Chemistry · doi:10.1007/bf01886793 · Cited by 227 · see citing works
Role of aldo-keto reductase family 1 (AKR1) enzymes in human steroid metabolism
Rižner, T. L., & Penning, T. M. (2014) · Steroids · doi:10.1016/j.steroids.2013.10.012 · Cited by 217 · see citing works
Xue, J., Ray, R., Singer, D., Böhme, D., Burz, D. S., Rai, V., Hoffmann, R., & Shekhtman, A. (2014) · Biochemistry · doi:10.1021/bi500046t · Cited by 186 · see citing works
Kang, Y., Edwards, L. G., & Thornalley, P. J. (1996) · Leukemia Research · doi:10.1016/0145-2126(95)00162-x · Cited by 182 · see citing works
Acetone Metabolism in Humans During Diabetic Ketoacidosis
Reichard, G., Skutches, C. L., Hoeldtke, R. D., & Owen, O. E. (1986) · Diabetes · doi:10.2337/diab.35.6.668 · Cited by 177 · see citing works
Rabbani, N., Xue, M., & Thornalley, P. J. (2016) · Clinical Science · doi:10.1042/cs20160025 · Cited by 173 · see citing works
Curcumin Inhibits Glyoxalase 1—A Possible Link to Its Anti-Inflammatory and Anti-Tumor Activity
Santel, T., Pflug, G., Hemdan, N. Y. A., Schäfer, A., Hollenbach, M., Buchold, M., Hintersdorf, A., Lindner, I., Otto, A., Bigl, M., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003508 · Cited by 171 · see citing works
Methylglyoxal in food and living organisms
Nemet, I., Varga‐Defterdarovič, L., & Turk, Z. (2006) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200600065 · Cited by 170 · see citing works
Glyoxalase in tumourigenesis and multidrug resistance
Thornalley, P. J., & Rabbani, N. (2011) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2011.02.006 · Cited by 163 · see citing works
Glucose availability is a decisive factor for Nrf2-mediated gene expression
Heiß, E. H., Schachner, D., Zimmermann, K., & Dirsch, V. M. (2013) · Redox Biology · doi:10.1016/j.redox.2013.06.001 · Cited by 157 · see citing works
Ahmed, N., & Thornalley, P. J. (2002) · Biochemical Journal · doi:10.1042/bj3640015 · Cited by 154 · see citing works
Glyoxalase I is involved in resistance of human leukemia cells to antitumor agent-induced apoptosis
Sakamoto, H., Mashima, T., Kizaki, A., Dan, S., Hashimoto, Y., Naito, M., & Tsuruo, T. (2000) · Blood · doi:10.1182/blood.v95.10.3214 · Cited by 154 · see citing works
Metformin induces apoptosis of pancreatic cancer cells
Wang, L., Li, Z., Zou, D., Jin, Z., Gao, J., & Xu, G.-M. (2008) · World Journal of Gastroenterology · doi:10.3748/wjg.14.7192 · Cited by 153 · see citing works
Lederer, M. O., & Klaiber, R. (1999) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(99)00212-6 · Cited by 146 · see citing works
Methylglyoxal-induced nitric oxide and peroxynitrite production in vascular smooth muscle cells
Chang, T., Wang, R., & Wu, L. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.10.034 · Cited by 140 · see citing works
Modulation of Heat-shock Protein 27 (Hsp27) Anti-apoptotic Activity by Methylglyoxal Modification
Sakamoto, H., Mashima, T., Yamamoto, K., & Tsuruo, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207485200 · Cited by 139 · see citing works
Nokin, M., Durieux, F., Peixoto, P., Chiavarina, B., Peulen, O., Blomme, A., Turtoï, A., Costanza, B., Smargiasso, N., Baiwir, D., et al. (2016) · eLife · doi:10.7554/elife.19375 · Cited by 137 · see citing works
Self-citationDiabetes and cancer: Associations, mechanisms, and implications for medical practice
Xu, C. (2014) · World Journal of Diabetes · doi:10.4239/wjd.v5.i3.372 · Cited by 135 · see citing works
Bento, C. F., Fernandes, R., Ramalho, J. S., Marques, C., Shang, F., Taylor, A., & Pereira, P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015062 · Cited by 132 · see citing works
Thornalley, P. J., Waris, S., Fleming, T. H., Santarius, T., Larkin, S. J., Winklhofer‐Roob, B. M., Stratton, M. R., & Rabbani, N. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq306 · Cited by 125 · see citing works
Novel Biomarkers for Prostate Cancer Including Noncoding Transcripts
Romanuik, T. L., Ueda, T., Le, N., Haile, S., Yong, T. M. K., Thomson, T. A., Vessella, R. L., & Sadar, M. D. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.080868 · Cited by 125 · see citing works
Expression of glyoxalase I and II in normal and breast cancer tissues
Rulli, A., Carli, L., Romani, R., Baroni, T., Giovannini, E., Rosi, G., & Talesa, V. N. (2001) · Breast Cancer Research and Treatment · doi:10.1023/a:1010632919129 · Cited by 125 · see citing works
Sakamoto, H., Mashima, T., Sato, S., Hashimoto, Y., Yamori, T., & Tsuruo, T. (2001) · PubMed · Cited by 124 · see citing works
Sharaf, H., Matou‐Nasri, S., Wang, Q., Rabhan, Z., Al‐Eidi, H., Abdulrahman, A. A., & Ahmed, N. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.12.009 · Cited by 122 · see citing works
Ahmad, S., Moinuddin, Dixit, K., Shahab, U., Alam, K., & Ali, A. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.03.064 · Cited by 121 · see citing works
Identification of aldo-keto reductases as NRF2-target marker genes in human cells
Jung, K.-A., Choi, B.-H., Nam, C.-W., Song, M., Kim, S.-T., Lee, J. Y., & Kwak, M.-K. (2013) · Toxicology Letters · doi:10.1016/j.toxlet.2012.12.026 · Cited by 113 · see citing works
Kurys, G., Ambroziak, W., & Pietruszko, R. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83802-9 · Cited by 108 · see citing works
GLO1 —A novel amplified gene in human cancer
Santarius, T., Bignell, G. R., Greenman, C., Widaa, S., Chen, L., Mahoney, C., Butler, A. P., Edkins, S., Waris, S., Thornalley, P. J., et al. (2010) · Genes Chromosomes and Cancer · doi:10.1002/gcc.20784 · Cited by 107 · see citing works
Ashraf, J. M., Ahmad, S., Choi, I., Ahmad, N., Farhan, M., Tatyana, G., & Shahab, U. (2015) · IUBMB Life · doi:10.1002/iub.1450 · Cited by 106 · see citing works
Lin, J., Wu, C., Lu, C., Hsia, S., & Yen, G. (2016) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201500759 · Cited by 105 · see citing works
Methylglyoxal Can Modify GAPDH Activity and Structure
Lee, H. J., Howell, S. K., SANFORD, R. J., & Beisswenger, P. J. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1333.017 · Cited by 104 · see citing works
Alterations in renal mitochondrial respiration in response to the reactive oxoaldehyde methylglyoxal
Rosca, M. G., Monnier, V. M., Szweda, L. I., & Weiss, M. F. (2002) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00302.2001 · Cited by 103 · see citing works
Scavenging system efficiency is crucial for cell resistance to ROS-mediated methylglyoxal injury
Amicarelli, F., Colafarina, S., Cattani, F., Cimini, A., Ilio, C. D., Cerù, M. P., & Miranda, M. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00438-6 · Cited by 103 · see citing works
Cancerostatic Action of Methylglyoxal
Együud, L. G., & Szent‐Györgyi, A. (1968) · Science · doi:10.1126/science.160.3832.1140 · Cited by 102 · see citing works
Lou, H., Du, S., Ji, Q., & Stolz, A. (2006) · Molecular Pharmacology · doi:10.1124/mol.105.019794 · Cited by 100 · see citing works
The functional genomic studies of curcumin
Huminiecki, Ł., Horbańczuk, J. O., & Atanasov, A. G. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.04.002 · Cited by 96 · see citing works
Herreweghe, F. V., Mao, J., Chaplen, F. W. R., Grooten, J., Gevaert, K., Vandekerckhove, J. S., & Vancompernolle, K. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.012432399 · Cited by 96 · see citing works
Posttranslational Modification of Human Glyoxalase 1 Indicates Redox-Dependent Regulation
Birkenmeier, G., Stegemann, C., Hoffmann, R., Günther, R., Huse, K., & Birkemeyer, C. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010399 · Cited by 95 · see citing works
GLO1 overexpression in human malignant melanoma
Bair, W. B., Cabello, C. M., Uchida, K., Bause, A. S., & Wondrak, G. T. (2010) · Melanoma Research · doi:10.1097/cmr.0b013e3283364903 · Cited by 94 · see citing works
Periyasamy, P., Bidasee, K. R., Ayaki, M., Augusteyn, R. C., Chan, J. Y., & Shinohara, T. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.04.010 · Cited by 91 · see citing works
Shen, Y., Yang, J., Li, J., Shi, X., Ouyang, L., Tian, Y., & Lü, J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0104632 · Cited by 89 · see citing works
Plasma α-Oxoaldehyde Levels in Diabetic and Nondiabetic Chronic Kidney Disease Patients
Nakayama, K., Nakayama, M., Iwabuchi, M., Terawaki, H., Sato, T., Kohno, M., & Ito, S. (2008) · American Journal of Nephrology · doi:10.1159/000139653 · Cited by 87 · see citing works
Morgenstern, J., Fleming, T. H., Schumacher, D., Eckstein, V., Freichel, M., Herzig, S., & Nawroth, P. P. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.760132 · Cited by 82 · see citing works
Metformin sensitizes endometrial cancer cells to chemotherapy by repressing glyoxalase I expression
Dong, L., Zhou, Q., Zhang, Z., Zhu, Y., Duan, T., & Feng, Y. (2012) · Journal of obstetrics and gynaecology research · doi:10.1111/j.1447-0756.2011.01839.x · Cited by 77 · see citing works
Phalitakul, S., Okada, M., Hara, Y., & Yamawaki, H. (2013) · Acta Physiologica · doi:10.1111/apha.12139 · Cited by 77 · see citing works
Nishimoto, S., Koike, S., Inoue, N., Suzuki, T., & Ogasawara, Y. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.01.024 · Cited by 75 · see citing works
Murata‐Kamiya, N., Kamiya, H., Kaji, H., & Kasai, H. (2000) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/s1383-5718(00)00044-9 · Cited by 73 · see citing works
van Heijst, J. W. J., Niessen, H. W. M., Musters, R. J. P., van Hinsbergh, V. W. M., Hoekman, K., & Schalkwijk, C. G. (2005) · Cancer Letters · doi:10.1016/j.canlet.2005.10.042 · Cited by 72 · see citing works
Self-citationAnalysis of glyoxalase-I from normal and tumor tissue
Ranganathan, S., & Tew, K. D. (1993) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/0925-4439(93)90074-b · Cited by 71 · see citing works
Synold, T. W., Xi, B., Wuenschell, G. E., Tamae, D., Figarola, J. L., Rahbar, S., & Termini, J. S. (2008) · Chemical Research in Toxicology · doi:10.1021/tx800224y · Cited by 69 · see citing works
A novel mechanism of methylglyoxal cytotoxicity in prostate cancer cells
Antognelli, C., Mezzasoma, L., Fettucciari, K., & Talesa, V. N. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.01.003 · Cited by 69 · see citing works
Guo, Y., Zhang, Y., Yang, X., Lu, P., Yan, X., Xiao, F., Zhou, H., Wen, C., Shi, M., Lü, J., et al. (2015) · Cancer Biology & Therapy · doi:10.1080/15384047.2015.1121346 · Cited by 67 · see citing works
Genomic sequence of human glyoxalase-I: analysis of promoter activity and its regulation
Ranganathan, S., Ciaccio, P. J., Walsh, E. S., & Tew, K. D. (1999) · Gene · doi:10.1016/s0378-1119(99)00420-5 · Cited by 67 · see citing works
Heat-shock protein 27 (Hsp27) as a target of methylglyoxal in gastrointestinal cancer
Oya‐Ito, T., Naito, Y., Takagi, T., Handa, O., Matsui, H., Yamada, M., Shima, K., & Yoshikawa, T. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.03.017 · Cited by 66 · see citing works
Chiavarina, B., Nokin, M., Bellier, J., Durieux, F., Blétard, N., Sherer, F., Lovinfosse, P., Peulen, O., Verset, L., Dehon, R., et al. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18010213 · Cited by 66 · see citing works
Self-citationMacLeod, A. K., Acosta-Jimenez, L., Coates, P. J., McMahon, M. J., Carey, F. A., Honda, T., Henderson, C. J., & Wolf, C. R. (2016) · British Journal of Cancer · doi:10.1038/bjc.2016.363 · Cited by 65 · see citing works
Rapid Suppression of Mitochondrial Permeability Transition by Methylglyoxal
Speer, O., Morkūnaitė‐Haimi, Š., Liobikas, J., Franck, M. C. M., Hensbo, L., Linder, M. D., Kinnunen, P. K. J., Wallimann, T., & Eriksson, O. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301990200 · Cited by 64 · see citing works
Chan, W., & Wu, H. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21489 · Cited by 64 · see citing works
Wang, H., Meng, Q. H., Chang, T., & Wu, L. (2006) · Life Sciences · doi:10.1016/j.lfs.2006.08.009 · Cited by 64 · see citing works
Brinkmann, E., Wells‐Knecht, K. J., Thorpe, S. R., & Baynes, J. (1995) · Journal of the Chemical Society Perkin Transactions 1 · doi:10.1039/p19950002817 · Cited by 63 · see citing works
Aminoacetone oxidase from goat liver. Formation of methylglyoxal from aminoacetone.
Ray, M., & Ray, S. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45524-x · Cited by 62 · see citing works
Mir, A. R., Uddin, M., Alam, K., & Ali, A. (2014) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2014.05.057 · Cited by 62 · see citing works
Vaca, C. E., Fang, J., Conradi, M., & Hou, S. (1994) · Carcinogenesis · doi:10.1093/carcin/15.9.1887 · Cited by 61 · see citing works
Fonseca-Sánchez, M. A., Cuevas, S. R., Mendoza‐Hernández, G., Bautista‐Piña, V., Aréchaga-Ocampo, E., Hidalgo‐Miranda, A., Quintanar‐Jurado, V., Marchat, L. A., Álvarez-Sánchez, M. E., Pérez‐Plasencia, C., et al. (2012) · International Journal of Oncology · doi:10.3892/ijo.2012.1478 · Cited by 60 · see citing works
Hu, T.-Y., Liu, C., Chyau, C.-C., & Hu, M. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf302188a · Cited by 59 · see citing works
GLYOXALASE I ACTIVITY IN HUMAN PROSTATE CANCER: A POTENTIAL MARKER AND IMPORTANCE IN CHEMOTHERAPY
Davidson, S. D., CHERRY, J. P., CHOUDHURY, M. S., Tazaki, H., Mallouh, C., & Konno, S. (1999) · The Journal of Urology · doi:10.1016/s0022-5347(01)61996-7 · Cited by 59 · see citing works
Hosoda, F., Arai, Y., Okada, N., Shimizu, H., Miyamoto, M., Kitagawa, N., Katai, H., Taniguchi, H., Yanagihara, K., Imoto, I., et al. (2014) · Oncogene · doi:10.1038/onc.2014.57 · Cited by 57 · see citing works
Chiavarina, B., Nokin, M., Durieux, F., Bianchi, E., Turtoï, A., Peulen, O., Peixoto, P., Irigaray, P., Uchida, K., Belpomme, D., et al. (2014) · Oncotarget · doi:10.18632/oncotarget.2121 · Cited by 56 · see citing works
Self-citationGlyoxalase-I Is a Novel Prognosis Factor Associated with Gastric Cancer Progression
Cheng, W., Tsai, M.-M., Tsai, C., Huang, Y., Chen, C., Chi, H., Tseng, Y., Chao, I.-W., Lin, W.-C., Wu, S.-M., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034352 · Cited by 54 · see citing works
Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases
Yoshida, A., Ikawa, M., Hsu, L., & Tani, K. (1985) · Alcohol · doi:10.1016/0741-8329(85)90024-2 · Cited by 52 · see citing works
Wang, Y., Kuramitsu, Y., Ueno, T., Suzuki, N., Yoshino, S., Iizuka, N., Akada, J. K., Kitagawa, T., Oka, M., & Nakamura, K. (2012) · PubMed · Cited by 51 · see citing works
Interaction of Methylglyoxal and Hydrogen Sulfide in Rat Vascular Smooth Muscle Cells
Chang, T., Untereiner, A. A., Liu, J., & Wu, L. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2918 · Cited by 50 · see citing works
Glyoxalase I in detoxification: studies using a glyoxalase I transfectant cell line
Ranganathan, S., Walsh, E. S., & Tew, K. D. (1995) · Biochemical Journal · doi:10.1042/bj3090127 · Cited by 48 · see citing works
Antognelli, C., Mezzasoma, L., Fettucciari, K., Mearini, E. E., & Talesa, V. N. (2012) · The Prostate · doi:10.1002/pros.22547 · Cited by 47 · see citing works
Chakrabarti, A., Talukdar, D., Pal, A., & Ray, M. (2013) · Cellular Immunology · doi:10.1016/j.cellimm.2013.11.006 · Cited by 46 · see citing works
Han, Y., Randell, E. W., Vasdev, S., Gill, V. D., Curran, M., Newhook, L. A., Grant, M., Hagerty, D., & Schneider, C. (2009) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2008.12.016 · Cited by 43 · see citing works
de Hemptinne, V., Rondas, D., Toepoel, M., & Vancompernolle, K. (2009) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-009-0031-7 · Cited by 41 · see citing works
Schneider, M. U., Thoss, G., Hübner-Parajsz, C., Kientsch-Engel, R., Stahl, P., & Pischetsrieder, M. (2004) · Chemical Research in Toxicology · doi:10.1021/tx049929d · Cited by 41 · see citing works
Baunacke, M., Horn, L., Trettner, S., Engel, K. M., Hemdan, N. Y. A., Wiechmann, V., Stolzenburg, J., Bigl, M., & Birkenmeier, G. (2013) · The Prostate · doi:10.1002/pros.22728 · Cited by 41 · see citing works
Glo1 genetic amplification as a potential therapeutic target in hepatocellular carcinoma.
Zhang, S., Liang, X., Zheng, X., Huang, H., Chen, X., Wu, K., Wang, B., & Ma, S. (2014) · PubMed Central · Cited by 41 · see citing works
Mearini, E. E., Romani, R., Mearini, L., Antognelli, C., Zucchi, A., Baroni, T., Porena, M., & Talesa, V. N. (2002) · European Journal of Cancer · doi:10.1016/s0959-8049(02)00236-8 · Cited by 39 · see citing works
Glyoxalase 1 is up-regulated in hepatocellular carcinoma and is essential for HCC cell proliferation
Hu, X., Yang, X., He, Q., Chen, Q., & Yu, L. (2013) · Biotechnology Letters · doi:10.1007/s10529-013-1372-6 · Cited by 38 · see citing works
Ahmad, M., Ahmad, S., & Moinuddin, M. (2011) · PubMed · Cited by 36 · see citing works
MacLeod, A. K., Acosta-Jimenez, L., Coates, P. J., McMahon, M. J., Carey, F. A., Honda, T., Hayes, J. D., Henderson, C. J., & Wolf, C. R. (2017) · British Journal of Cancer · doi:10.1038/bjc.2017.80 · Cited by 36 · see citing works
Taniguchi, H., Horinaka, M., Yoshida, T., Yano, K., Goda, A. E., Yasuda, S., Wakada, M., & Sakai, T. (2012) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-12-0031 · Cited by 35 · see citing works
Su, Y., Qadri, S. M., Wu, L., & Liu, L. (2013) · Cardiovascular Diabetology · doi:10.1186/1475-2840-12-134 · Cited by 33 · see citing works
Dicarbonyl Stress and Apoptosis of Vascular Cells: Prevention by αB‐Crystallin
Nagaraj, R. H., Oya‐Ito, T., Bhat, M. B., & Liu, B.-F. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1333.020 · Cited by 33 · see citing works
Lin, C.-C., Chan, C.-M., Huang, Y., Hsu, S.-H., Huang, C., & Tsai, S. (2016) · Life Sciences · doi:10.1016/j.lfs.2016.02.060 · Cited by 33 · see citing works
Milanesa, D. M., CHOUDHURY, M. S., Mallouh, C., Tazaki, H., & Konno, S. (2000) · European Urology · doi:10.1159/000020226 · Cited by 32 · see citing works
Modulation of GLO1 Expression Affects Malignant Properties of Cells
Hutschenreuther, A., Bigl, M., Hemdan, N. Y. A., Debebe, T., Gaunitz, F., & Birkenmeier, G. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17122133 · Cited by 31 · see citing works
Loarca, L., Sassi‐Gaha, S., & Artlett, C. M. (2013) · Digestive and Liver Disease · doi:10.1016/j.dld.2013.05.005 · Cited by 29 · see citing works
A possible regulatory role of glyoxalase I in cell viability of human prostate cancer
Davidson, S., Milanesa, D. M., Mallouh, C., CHOUDHURY, M. S., Tazaki, H., & Konno, S. (2002) · Urological Research · doi:10.1007/s00240-002-0244-7 · Cited by 29 · see citing works
Jyoti, J., Mir, A. R., Habib, S., Siddiqui, S. S., Ali, A., & Moinuddin, M. (2016) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2016.02.019 · Cited by 29 · see citing works
Troglitazone overcomes doxorubicin-resistance in resistant K562 leukemia cells
Davies, G. F., Roesler, W. J., Juurlink, B. H. J., & Harkness, T. A. A. (2005) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428190500102555 · Cited by 28 · see citing works
Methylglyoxal induces mitochondria-dependent apoptosis in sarcoma
Ghosh, A., Bera, S., Ray, S., Banerjee, T., & Ray, M. (2011) · Biochemistry (Moscow) · doi:10.1134/s0006297911100105 · Cited by 27 · see citing works
He, T., Zhou, H., Li, C., Chen, Y., Chen, X., Li, C., Mao, J., Lyu, J., & Meng, Q. H. (2016) · Cancer Biology & Therapy · doi:10.1080/15384047.2016.1210736 · Cited by 26 · see citing works
Potential of glycative stress targeting for cancer prevention
Piperi, C., Adamopoulos, C., & Papavassiliou, A. G. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.01.020 · Cited by 25 · see citing works
Lactate formation and glyoxalase activity in normal and leukemic human leukocytes in vitro.
Gr, M., & Rw, R. (1956) · PubMed · Cited by 25 · see citing works
Rulli, A., Antognelli, C., Prezzi, E., Baldracchini, F., Piva, F., Giovannini, E., & Talesa, V. N. (2005) · Breast Cancer Research and Treatment · doi:10.1007/s10549-005-9078-7 · Cited by 24 · see citing works
Troglitazone selectively inhibits glyoxalase I gene expression
Wu, L., Eftekharpour, E., Davies, G. F., Roesler, W. J., & Juurlink, B. H. J. (2001) · Diabetologia · doi:10.1007/s001250100004 · Cited by 24 · see citing works
Tu, C.-Y., Chen, Y.-F., Lii, C., & Wang, T. (2013) · Toxicology in Vitro · doi:10.1016/j.tiv.2013.02.011 · Cited by 24 · see citing works
de Hemptinne, V., Rondas, D., Vandekerckhove, J. S., & Vancompernolle, K. (2007) · Biochemical Journal · doi:10.1042/bj20070379 · Cited by 23 · see citing works
Antognelli, C., Buono, C. D., Baldracchini, F., Talesa, V. N., Cottini, E., Brancadoro, C., Zucchi, A., & Mearini, E. E. (2007) · Cancer Biology & Therapy · doi:10.4161/cbt.6.12.4961 · Cited by 21 · see citing works
Characterization of the Deoxyguanosine–Lysine Cross-Link of Methylglyoxal
Petrova, K. V., Millsap, A. D., Stec, D. F., & Rizzo, C. J. (2014) · Chemical Research in Toxicology · doi:10.1021/tx500068v · Cited by 16 · see citing works
Helgager, J. J., Li, J., Lubensky, I. A., Lonser, R. R., & Zhuang, Z. (2010) · Journal of Oncology · doi:10.1155/2010/373491 · Cited by 7 · see citing works
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Schalkwijk, C., & Stehouwer, C. D. A. (2019) · Physiological Reviews · doi:10.1152/physrev.00001.2019 · Cited by 630 · see citing works
Self-citationThe metabolic landscape of RAS-driven cancers from biology to therapy
Mukhopadhyay, S., Vander Heiden, M. G., & McCormick, F. (2021) · Nature Cancer · doi:10.1038/s43018-021-00184-x · Cited by 315 · see citing works
Microbial carcinogenesis: Lactic acid bacteria in gastric cancer
Vinasco, K., Mitchell, H. M., Kaakoush, N. O., & Castaño‐Rodríguez, N. (2019) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2019.07.004 · Cited by 173 · see citing works
Methylglyoxal, a potent inducer of AGEs, connects between diabetes and cancer
Bellier, J., Nokin, M., Lardé, E., Karoyan, P., Peulen, O., Castronovo, V., & Bellahcène, A. (2019) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2019.01.002 · Cited by 143 · see citing works
Self-citationMa, D., Bian, H., Gu, M., Wang, L., Chen, X., & Peng, X. (2024) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2024.215677 · Cited by 124 · see citing works
The role of protein lactylation: A kaleidoscopic post-translational modification in cancer
Iozzo, M., Pardella, E., Giannoni, E., & Chiarugi, P. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.02.011 · Cited by 122 · see citing works
Benefits, deleterious effects and mitigation of methylglyoxal in foods: A critical review
Zheng, J., Guo, H., Ou, J., Liu, P., Huang, C., Wang, M., Simal‐Gándara, J., Battino, M. A., Jafari, S. M., Zou, L., et al. (2020) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2020.10.031 · Cited by 102 · see citing works
Methylglyoxal – An emerging biomarker for diabetes mellitus diagnosis and its detection methods
Ramachandra, B. L., Vedantham, S., Krishnan, U. M., & Rayappan, J. B. B. (2019) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2019.03.010 · Cited by 100 · see citing works
Metabolite Repair Enzymes Control Metabolic Damage in Glycolysis
Bommer, G. T., SCHAFTINGEN, E. V., & Veiga‐da‐Cunha, M. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.07.004 · Cited by 94 · see citing works
Vaping, Environmental Toxicants Exposure, and Lung Cancer Risk
Shehata, S. A., Toraih, E. A., Ismail, E. A., Hagras, A. M., Elmorsy, E. M., & Fawzy, M. S. (2023) · Cancers · doi:10.3390/cancers15184525 · Cited by 101 · see citing works
“Recently, emerging evidence indicated that MGO plays a role in cancer development and progression [109].”
BackgroundDicarbonyl Stress at the Crossroads of Healthy and Unhealthy Aging
Nigro, C., Leone, A., Fiory, F., Prevenzano, I., Nicolò, A., Mirra, P., Bèguinot, F., & Miele, C. (2019) · Cells · doi:10.3390/cells8070749 · Cited by 91 · see citing works
“MGO directly modifies mitochondrial membrane proteins and antioxidant enzymes [49], while Glo1 overexpression is able to decrease dicarbonyl glycation of mitochondrial proteins and ROS production.”
BackgroundNokin, M., Bellier, J., Durieux, F., Peulen, O., Rademaker, G., Gabriel, M., Monseur, C., Charloteaux, B., Verbeke, L. P. C., Laere, S. V., et al. (2019) · Breast Cancer Research · doi:10.1186/s13058-018-1095-7 · Cited by 89 · see citing works
“Several studies depicted GLO1 as an amplified and/or overexpressed oncogene associated with a poor prognosis in various types of malignant tumors, thus considering the inhibition of GLO1 activity as a potential anti-cancer therapy (for review [10]).”
Self-citationNokin, M., Durieux, F., Bellier, J., Peulen, O., Uchida, K., Spiegel, D. A., Cochrane, J. R., Hutton, C. A., Castronovo, V., & Bellahcène, A. (2017) · Scientific Reports · doi:10.1038/s41598-017-12119-7 · Cited by 88 · see citing works
Self-citationThe Glyoxalase System—New Insights into an Ancient Metabolism
Morgenstern, J., Campos, M., Nawroth, P. P., & Fleming, T. H. (2020) · Antioxidants · doi:10.3390/antiox9100939 · Cited by 73 · see citing works
“Therefore, it is no surprise that Glo1 is generally overexpressed in numerous cancers potentially as a part of a survival strategy [15].”
BackgroundReactive metabolite production is a targetable liability of glycolytic metabolism in lung cancer
Luengo, A., Abbott, K. L., Davidson, S. M., Hosios, A. M., Faubert, B., Chan, S. H., Freinkman, E., Zacharias, L. G., Mathews, T. P., Clish, C. B., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13419-4 · Cited by 73 · see citing works
Glyoxalases in Urological Malignancies
Antognelli, C., & Talesa, V. N. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020415 · Cited by 64 · see citing works
“The two enzymes have been historically described to work in tandem as part of a system where Glo1 catalyzes the isomerization of the hemithioacetal formed non-enzymatically by the reaction of MG with reduced glutathione (GSH) into S-D-lactoylglutathione, and Glo2 the hydrolysis of S-D-lactoylglutathione to D-lactate,…”
BackgroundInfluentialThe Dual-Role of Methylglyoxal in Tumor Progression – Novel Therapeutic Approaches
Leone, A., Nigro, C., Nicolò, A., Prevenzano, I., Formisano, P., Bèguinot, F., & Miele, C. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.645686 · Cited by 59 · see citing works
“Compared to glucose, the glucose-derived glycolysis intermediates, especially MGO, form much more glycated proteins in a more rapid way (4).”
BackgroundInfluentialNanomaterial-Based Repurposing of Macrophage Metabolism and Its Applications
Meng, T., He, D., Han, Z., Shi, R., Wang, Y., Ren, B., Zhang, C., Mao, Z., Luo, G., & Deng, J. (2024) · Nano-Micro Letters · doi:10.1007/s40820-024-01455-9 · Cited by 63 · see citing works
“H 2 O 2 is the most stable and abundant endogenous ROS and acts as the precursor for producing other ROS at concentration ≥ 1 mΜ [89, 90], such as HClO [91].”
BackgroundLai, Y., Dang, Y., Li, F., Ding, C., Yu, H., Zhang, W., & Xu, Z. (2022) · Advanced Functional Materials · doi:10.1002/adfm.202200016 · Cited by 57 · see citing works
Tumor microbiome metabolism: A game changer in cancer development and therapy
Zhou, X., Kandalai, S., Hossain, F., & Zheng, Q. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.933407 · Cited by 51 · see citing works
Methylglyoxal Formation—Metabolic Routes and Consequences
Vašková, J., Sabolová, G., Pudelský, J., Palenčár, D., & Mičková, H. (2025) · Antioxidants · doi:10.3390/antiox14020212 · Cited by 54 · see citing works
Methylglyoxal interaction with superoxide dismutase 1
Polykretis, P., Luchinat, E., Boscaro, F., & Banci, L. (2020) · Redox Biology · doi:10.1016/j.redox.2019.101421 · Cited by 46 · see citing works
Methylglyoxal Scavengers Resensitize KRAS-Mutated Colorectal Tumors to Cetuximab
Bellier, J., Nokin, M.-J., Caprasse, M., Tiamiou, A., Blomme, A., Scheijen, J. L., Koopmansch, B., MacKay, G. M., Chiavarina, B., Costanza, B., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.01.012 · Cited by 38 · see citing works
“MGO levels in cancer cells result from the balance between MGO formation, mainly as a by-product of glycolysis, and its detoxification by the glyoxalase system (Bellahcène et al., 2018).”
BackgroundSelf-citationThe Human Glyoxalase Gene Family in Health and Disease
Farrera, D. O., & Galligan, J. J. (2022) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.2c00182 · Cited by 39 · see citing works
Jain, M., Muñoz‐Bodnar, A., & Gabriel, D. W. (2017) · Applied and Environmental Microbiology · doi:10.1128/aem.01670-17 · Cited by 38 · see citing works
“and detoxification via an upregulated glyoxalase system in tumor cell lines (24).”
BackgroundLi, H., Zheng, L., Chen, C., Liu, X., & Zhang, W. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01004 · Cited by 37 · see citing works
Lima, A. R., Pinto, J., Carvalho‐Maia, C., Jerónimo, C., Henrique, R., Bastos, M. D. L., Carvalho, M. C., & de Pinho, P. G. (2020) · Cancers · doi:10.3390/cancers12082017 · Cited by 34 · see citing works
“One well-established metabolic feature of cancer cells is increased aerobic glycolysis over oxidative respiration, which unavoidably leads to MG accumulation [19].”
Diet and Obesity-Induced Methylglyoxal Production and Links to Metabolic Disease
Hernandez-Castillo, C., & Shuck, S. C. (2021) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.1c00221 · Cited by 33 · see citing works
Ding, C., Wang, F., Dang, Y., Xu, Z., Li, L., Lai, Y., Yu, H., Luo, Y., Huang, R., Zhang, A., et al. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b03600 · Cited by 31 · see citing works
Beeraka, N. M., Bovilla, V. R., Doreswamy, S. H., Puttalingaiah, S., Srinivasan, A., & Madhunapantula, S. V. (2021) · Cancers · doi:10.3390/cancers13020281 · Cited by 28 · see citing works
“For example, tumor cells are characterized by a high glucose uptake to generate lactate in the mitochondria, where a glucose-derived carbonyl reactive species MGO (methyl glyoxal) is excessively generated [197].”
BackgroundThe “sweet” path to cancer: focus on cellular glucose metabolism
Iacobini, C., Vitale, M., Pugliese, G., & Menini, S. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1202093 · Cited by 24 · see citing works
The RAGE/multiligand axis: a new actor in tumor biology
Armando Rojas, R., Schneider, I., Lindner, C., González, I., & Morales, M. A. (2022) · Bioscience Reports · doi:10.1042/bsr20220395 · Cited by 23 · see citing works
Wang, J., Yang, X., Wang, Z., & Wang, J. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.857746 · Cited by 23 · see citing works
Härma, M., Adeshara, K. A., Istomin, N., Lehto, M. J., Blaut, M., Savolainen, M. J., Hörkkö, S., Groop, P., Koivukangas, V., & Hukkanen, J. (2020) · Surgery for Obesity and Related Diseases · doi:10.1016/j.soard.2020.10.021 · Cited by 22 · see citing works
Methylglyoxal: a novel upstream regulator of DNA methylation
Dube, G., Tiamiou, A., Bizet, M., Boumahd, Y., Gasmi, I., Crake, R., Bellier, J., Nokin, M., Calonne, E., Deplus, R., et al. (2023) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-023-02637-w · Cited by 21 · see citing works
“Another potentially important implication of linking MG stress and epigenetic deregulation concerns our understanding of the increased risk of cancer in diabetic patients [68].”
BackgroundSelf-citationSuh, E. H., Geraldes, C. F. G. C., Chirayil, S., Faubert, B., Ayala, R., DeBerardinis, R. J., & Sherry, A. D. (2021) · Cancer & Metabolism · doi:10.1186/s40170-021-00267-4 · Cited by 18 · see citing works
“Elevated glucose metabolism inevitably produces more MG as a byproduct [29, 30].”
BackgroundDang, Y., Lai, Y., Chen, F., Sun, Q., Ding, C., Zhang, W., & Xu, Z. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.1c04076 · Cited by 18 · see citing works
Sruthi, C. R., & Raghu, K. G. (2022) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30215 · Cited by 17 · see citing works
“It is also implicated as an emerging biological factor in cancer development and progression.(10) Pathophysiological complications implicated in MGO stress can be minimized by reducing the MGO accumulation by strategies like prevention or reduction of MGO formation, scavenging of MGO, or by using inducers for glyoxala…”
BackgroundLeveraging histone glycation for cancer diagnostics and therapeutics
Knörlein, A., Xiao, Y. F., & David, Y. (2023) · Trends in cancer · doi:10.1016/j.trecan.2023.01.005 · Cited by 17 · see citing works
Electrophilic Signaling: The Role of Reactive Carbonyl Compounds
Kosmachevskaya, O. V., Шумаев, К. Б., & Topunov, A. F. (2019) · Biochemistry (Moscow) · doi:10.1134/s0006297919140128 · Cited by 17 · see citing works
Targeting KRAS in NSCLC: Old Failures and New Options for “Non-G12c” Patients
Jacobs, F., Cani, M., Malapelle, U., Novello, S., Napoli, V. M., & Bironzo, P. (2021) · Cancers · doi:10.3390/cancers13246332 · Cited by 17 · see citing works
“Finally, changes in lipid metabolism through increased lipogenesis have also been reported [15,16].”
BackgroundXie, N., Zhang, R., Bi, Z., Ren, W., You, K., Hu, H., Xu, Y. X., & Yao, H. (2022) · Cellular Oncology · doi:10.1007/s13402-022-00756-8 · Cited by 16 · see citing works
Liu, J., Li, M., Dang, Y., Lou, H., Xu, Z., & Zhang, W. (2022) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2022.114068 · Cited by 15 · see citing works
Glycation Leads to Increased Invasion of Glioblastoma Cells
Schildhauer, P., Selke, P., Scheller, C., Strauß, C., Horstkorte, R., Leisz, S., & Scheer, M. (2023) · Cells · doi:10.3390/cells12091219 · Cited by 15 · see citing works
Cardio-oncology: Shared Genetic, Metabolic, and Pharmacologic Mechanism
Zhao, Y., Jia, H., Hua, X., An, T., & Song, J. (2023) · Current Cardiology Reports · doi:10.1007/s11886-023-01906-6 · Cited by 18 · see citing works
Armando Rojas, R., Schneider, I., Lindner, C., González, I., & Morales, M. A. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04630-x · Cited by 13 · see citing works
“Of note, the Warburg effect is known to enhance the formation of methylglyoxal (MG), a reactive dicarbonyl known as the major precursor of advanced glycation end-products (AGEs) [111, 112], thus leading to the AGEs accumulation and consequently the activation of the receptor of advanced glycation end-products (RAGE),…”
BackgroundSchildhauer, P., Selke, P., Staege, M. S., Harder, A., Scheller, C., Strauß, C., Horstkorte, R., Scheer, M., & Leisz, S. (2023) · Cells · doi:10.3390/cells12232758 · Cited by 13 · see citing works
Deng, X., Wu, Q., & Liu, Y. (2024) · Food Science & Nutrition · doi:10.1002/fsn3.4416 · Cited by 13 · see citing works
“Accumulation of MGO has been implicated in the development and progression of various diseases, including diabetic complications, obesity, atherosclerosis, degenerative neurological disorders, and cancers (Bellahcène et al., 2018 ; Chun et al., 2016 ).”
BackgroundGlycation Interferes with the Expression of Sialyltransferases in Meningiomas
Selke, P., Bork, K., Zhang, T., Wuhrer, M., Strauß, C., Horstkorte, R., & Scheer, M. (2021) · Cells · doi:10.3390/cells10123298 · Cited by 13 · see citing works
“Several other studies propose MGO as a tumor-promoting agent [31,32].”
BackgroundGenova, V. M., Fernandes, A. C. F., Hiramatsu, E. Y., de Queirós, L. D., Macedo, J. A., & Macêdo, G. A. (2021) · Food Biotechnology · doi:10.1080/08905436.2020.1869564 · Cited by 12 · see citing works
Ma, H., Ding, Z., Xie, Y., Li, L., Li, D., Lou, K., Wang, W., & Xu, H. (2022) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2022.115910 · Cited by 12 · see citing works
Xiao, H., Wu, G., Tan, S., Tan, X., & Yang, Q. (2024) · Chemistry - An Asian Journal · doi:10.1002/asia.202301036 · Cited by 11 · see citing works
Gull, S., Shabbir, C. A., Khan, Z., Bukhari, D. A., & Rehman, A. (2024) · Arabian Journal of Chemistry · doi:10.1016/j.arabjc.2024.106069 · Cited by 10 · see citing works
Fluorescent probes for sensing and visualizing methylglyoxal: progress, challenges, and perspectives
Wen, J., Qing-ya, Z., & Zhou, L. (2024) · RSC Advances · doi:10.1039/d4ra07512a · Cited by 10 · see citing works
Xu, M., Zuo, D., Wang, Q., Lv, L., Zhang, Y., Jiao, H., Zhang, X., Yang, Y., Song, G., & Cheng, H. (2023) · BMC Genomics · doi:10.1186/s12864-023-09524-w · Cited by 10 · see citing works
Glycation of benign meningioma cells leads to increased invasion
Selke, P., Rosenstock, P., Bork, K., Strauß, C., Horstkorte, R., & Scheer, M. (2021) · Biological Chemistry · doi:10.1515/hsz-2020-0376 · Cited by 10 · see citing works
Kong, D., Huang, Y., Song, B., Zhang, X., & Yuan, J. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.4c06973 · Cited by 9 · see citing works
Methylglyoxal mutagenizes single-stranded DNA via Rev1-associated slippage and mispairing
Vijayraghavan, S., Ruggiero, A., Becker, S., Mieczkowski, P. A., Hanna, G. S., Hamann, M. T., & Saini, N. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf705 · Cited by 9 · see citing works
“…such as Parkinson’s [ 7 ], diabetes [ 8 ], cardio-vascular diseases and renal diseases [ 9 , 10 ], aging [ 11 ], obesity [ 12 ], and cancers [ 13 , 14 ] In cells, the primary mode of MG detoxification is via the evolutionarily conserved glyoxalase Glo1, which converts MG to S…”
Corcoran, C. J., Cuthbert, B. J., Glanville, D. G., Terrado, M., Valverde-Mendez, D., Bratton, B. P., Schemenauer, D. E., Tokars, V. L., Martin, T. G., Rasmussen, L. W., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-61469-8 · Cited by 7 · see citing works
Romaldi, B., Scirè, A., Minnelli, C., Frontini, A., Casari, G., Cianfruglia, L., Mobbili, G., Lidia de, B. A. R. I., Antognelli, C., Pallardó, F. V., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252010888 · Cited by 7 · see citing works
“The glyoxalase system is an important glutathione (GSH)-dependent pathway whose major role in all living organisms is the detoxification of methylglyoxal (MGO), a by-product of cell metabolism, especially glycolysis [1].”
BackgroundAcid-promoted fluorescent probe for monitoring endogenous methylglyoxal in tumors and gastritis
Xu, W., Liu, S., Cao, W., & Xiong, H. (2023) · Sensors & Diagnostics · doi:10.1039/d3sd00228d · Cited by 6 · see citing works
Methylglyoxal disturbs DNA repair and glyoxalase I system in Saccharomyces cerevisiae
Pavin, S. S., Prestes, A. D. S., dos Santos, M. M., de Macedo, G. T., Ferreira, S. A., Claro, M. T., Corte, C. L. D., & Barbosa, N. V. (2020) · Toxicology Mechanisms and Methods · doi:10.1080/15376516.2020.1838019 · Cited by 6 · see citing works
Hirahara, I., Kusano, E., Jin, D., & Takai, S. (2019) · The Journal of Biochemistry · doi:10.1093/jb/mvz077 · Cited by 6 · see citing works
Vizuete, A. F. K., & Gonçalves, C. (2024) · Neurochemical Research · doi:10.1007/s11064-024-04142-8 · Cited by 5 · see citing works
Zhang, W., Liao, Y., Liu, C., Liu, L., & Zhou, X. (2023) · Disease Markers · doi:10.1155/2023/6729717 · Cited by 5 · see citing works
“Discussion To address uncontrolled tumor growth, metastasis [10, 11], and resistance to a variety of anticancer drugs, more effective tumor targets are needed in order to develop novel drugs In fil tr at io n sc or e”
BackgroundChou, C., Yang, P.-C., Tsai, P.-Y., Yang, H., Tsai, K., Chen, T., Liao, K., Chen, C.-Y., & Lee, J. (2021) · Life · doi:10.3390/life11121319 · Cited by 5 · see citing works
RAS: Circuitry and therapeutic targeting
Singh, G., Thakur, N., & Kumar, U. (2022) · Cellular Signalling · doi:10.1016/j.cellsig.2022.110505 · Cited by 5 · see citing works
Cheng, M., He, Z., Wang, G., Yu, Y., Song, R., Qin, Y., Wang, Z., Guo, D., & Chen, H. (2025) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.5c11739 · Cited by 4 · see citing works
Wong, M., Martínez, T., Hendricks, N., & Talbot, P. (2025) · Frontiers in Toxicology · doi:10.3389/ftox.2025.1624794 · Cited by 3 · see citing works
“Methylglyoxal, although less extensively studied in the context of respiratory toxicity, has been implicated in the pathogenesis of diabetes-related complications and various cancers (Matafome et al., 2013; Bellahcène et al., 2018; Bellier et al., 2019; Schalkwijk and Stehouwer, 2020).”
Effect of Different Glucose Levels and Glycation on Meningioma Cell Migration and Invasion
Selke, P., Strauß, C., Horstkorte, R., & Scheer, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251810075 · Cited by 3 · see citing works
Altamirano, A., Ruzic, M., Cryan, A. E., & Hogan, D. A. (2025) · Journal of Bacteriology · doi:10.1128/jb.00394-24 · Cited by 2 · see citing works
Watanabe, M., Toyomura, T., Ikegami, R., Suwaki, Y., Sada, M., Wake, H., Nishinaka, T., Hatipoğlu, Ö. F., Takahashi, H. K., Nishibori, M., et al. (2022) · Molecular Biology Reports · doi:10.1007/s11033-022-07929-6 · Cited by 2 · see citing works
Cheng, G., Reisinger, S. A., Shields, P. G., Hatsukami, D. K., Balbo, S., & Hecht, S. S. (2020) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2020.109140 · Cited by 2 · see citing works
Scheffer, D., Kulcsár, G., & Czömpöly, T. (2019) · Cancer Biotherapy and Radiopharmaceuticals · doi:10.1089/cbr.2018.2673 · Cited by 2 · see citing works
“33 MG may have oncogenic roles 31 ; however, there are emerging evidences that excess level of MG can inhibit various cancer cells.”
Elucidating the effect of levothyroxine and triiodothyronine on methylglyoxal derived stress
Khan, H., Habib, S., Siddiqui, S. A., Ahmad, R., Husain, A., & Moinuddin, M. (2024) · Endocrine · doi:10.1007/s12020-024-03972-4 · Cited by 1 · see citing works
“It also plays a role in the development of cancer [5, 6].”
Methylglyoxal: Hijack-to-survive paradigm of cancer progression
Patel, M. D., Rawal, S. K., & Mani, S. (2026) · Gene Reports · doi:10.1016/j.genrep.2026.102455 · Cited by 1 · see citing works
Peng, M., Deng, L., Guo, L., Shen, Z., Zhu, Y., Wang, J., Chen, Y., Gao, J., & Zhou, M. (2026) · Current Research in Food Science · doi:10.1016/j.crfs.2026.101417 · Cited by 1 · see citing works
“MGO-induced ROS accumulation, DNA damage, and mitochondrial dysfunction activate cell-death signaling pathways, amplify apoptotic responses, and ultimately result in apoptosis (Bellahc ` ene et al., 2018; Redza-Dutordoir and Averill-Bates, 2016).”
Glycation stress in glioma: a metabolic vulnerability and therapeutic target
Umdor, S. B., & Sen, E. (2026) · Pharmacological Reports · doi:10.1007/s43440-026-00904-z · Cited by 1 · see citing works
Methylglyoxal and Its Role in Obesity-Associated Heart Failure with Preserved Ejection Fraction
Alomar, F. A., Moore, C. J., Abohelaika, S., Al‐Muhanna, F., Alshabeed, M. A., Hamel, F. G., Desouza, C. V., & Bidasee, K. R. (2021) · Advances in biochemistry in health and disease · doi:10.1007/978-3-030-84763-0_19 · Cited by 1 · see citing works
Methylglyoxal induces nuclear accumulation of p53 and γH2AX in normal and cancer cellsPreprint
Veß, A., & Hollemann, T. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.19.998773 · Cited by 1 · see citing works
Advanced Glycation Endproducts (AGEs) in Food: Health Implications and Mitigation Strategies
Birch, C., & Bonwick, G. (2019) · Royal Society of Chemistry eBooks · doi:10.1039/9781788016438-00191
Ahmad, S., Shahab, U., & Moinuddin, M. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.03.002
Glyoxal‑induced disruption of tumor cell progression in breast cancer
Rong, P., Li, Y., Nianchun, G., Qi, L., & Li, X. (2023) · Molecular and Clinical Oncology · doi:10.3892/mco.2023.2622
“via glycolysis, but low doses of MGO promoted tumorigenesis even in the same tissue (33,35,36).”
BackgroundRomaldi, B., Scirè, A., Minnelli, C., Frontini, A., Casari, G., Cianfruglia, L., Mobbili, G., Lidia de, B. A. R. I., Antognelli, C., & Armeni, T. (2023) · doi:10.22541/au.169514466.62008339/v1
Besinlerdeki Gizli Düşman: Metilglioksal
Melisa, A. K. O. L., & Taşkıran, D. (2023) · İzmir Katip Çelebi Üniversitesi Sağlık Bilimleri Fakültesi Dergisi · doi:10.61399/ikcusbfd.1274527
Xu, M., Zuo, D., Wang, Q., Lv, L., Zhang, Y., Jiao, H., Zhang, X., Yang, Y., Song, G., & Cheng, H. (2023) · Figshare · doi:10.6084/m9.figshare.24012997
Xu, M., Zuo, D., Wang, Q., Lv, L., Zhang, Y., Jiao, H., Zhang, X., Yang, Y., Song, G., & Cheng, H. (2023) · Figshare · doi:10.6084/m9.figshare.24013000
Xu, M., Zuo, D., Wang, Q., Lv, L., Zhang, Y., Jiao, H., Zhang, X., Yang, Y., Song, G., & Cheng, H. (2023) · Figshare · doi:10.6084/m9.figshare.24013003
Xu, M., Zuo, D., Wang, Q., Lv, L., Zhang, Y., Jiao, H., Zhang, X., Yang, Y., Song, G., & Cheng, H. (2023) · Figshare · doi:10.6084/m9.figshare.24012991
Xu, M., Zuo, D., Wang, Q., Lv, L., Zhang, Y., Jiao, H., Zhang, X., Yang, Y., Song, G., & Cheng, H. (2023) · Figshare · doi:10.6084/m9.figshare.24013009
Xu, M., Zuo, D., Wang, Q., Lv, L., Zhang, Y., Jiao, H., Zhang, X., Yang, Y., Song, G., & Cheng, H. (2023) · Figshare · doi:10.6084/m9.figshare.24013006
Effect of Aloe Vera against Natural and Chemical Toxicities
Shirvanian, K., Naghizadeh, M., Vali, R., Farkhondeh, T., Pourbagher‐Shahri, A. M., Aschner, M., Ahmadian, M., & Samarghandian, S. (2024) · Current Nutrition & Food Science · doi:10.2174/0115734013307300240906055446
Ruzic, M., Hefferan, A. I. A., Conaway, A., & Hogan, D. A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.25.615034
PIK3CA regulates lactate transport through MCT1,MCT4 in diffuse large B-cell lymphomaPreprint
Zhao, Y., Li, J., Yu, J. B., Wang, X., Pang, X., Ma, M., Ma, Z., Zhang, W., & Cui, W. (2024) · Research Square · doi:10.21203/rs.3.rs-5317703/v1
Omondi, R. O., Barnes, E. M., Gurajala, K. C., Fisette, G., Chaudray, I. A., & Erber, L. N. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.5c06852
Xu, M., Zuo, D., Wang, Q., Lv, L., Zhang, Y., Jiao, H., Zhang, X., Yang, Y., Song, G., & Cheng, H. (2023) · Figshare · doi:10.6084/m9.figshare.24012976
Suh, E. H., Geraldes, C. F. G. C., Chirayil, S., Faubert, B., Ayala, R., DeBerardinis, R. J., & Sherry, A. D. (2021) · Figshare · doi:10.6084/m9.figshare.16944345
Xu, M., Zuo, D., Wang, Q., Lv, L., Zhang, Y., Jiao, H., Zhang, X., Yang, Y., Song, G., & Cheng, H. (2023) · Figshare · doi:10.6084/m9.figshare.24012988
Xu, M., Zuo, D., Wang, Q., Lv, L., Zhang, Y., Jiao, H., Zhang, X., Yang, Y., Song, G., & Cheng, H. (2023) · Figshare · doi:10.6084/m9.figshare.24012985
Xu, M., Zuo, D., Wang, Q., Lv, L., Zhang, Y., Jiao, H., Zhang, X., Yang, Y., Song, G., & Cheng, H. (2023) · Figshare · doi:10.6084/m9.figshare.24012982
- Authors
- Bellahcène, A., Nokin, M.-J., Castronovo, V., & Schalkwijk, C.
- Affiliations
- University of Liège (BE)
- Maastricht University (NL)
- Corresponding author
- Bellahcène, Akeila
- Venue
- Seminars in Cancer Biology
- Publisher
- Elsevier BV
- Published
- 2018-04
- Volume
- 49
- Pages
- 64-74
- ISSN
- 1044-579X (ISSN-L)
- OpenAlex
- W2622101156
- Cited by
- 98
- References
- 158
- Citations by year
- 2026: 7 · 2025: 8 · 2024: 13 · 2023: 18 · 2022: 13 · 2021: 12 · 2020: 9 · 2019: 14 · 2018: 2 · 2017: 2
- FWCI
- 0.96
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Seminars in Cancer Biology (publishedVersion)
- PubMed (publishedVersion)
- Research Publications (Maastricht University) (submittedVersion)
- ORBi (University of Liège) (submittedVersion)
- Funders
- University of Liège
- “Télévie-National Fund for Scientific Research”, Belgium
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Life Sciences › Agricultural and Biological Sciences › Food Science › Potato Plant Research
- Keywords
- methylglyoxal, carbonyl stress, cancer onset, tumor progression, glycation, glucose metabolism, lactic acid production, protein carbonylation, DNA damage, cancer therapy
- MeSH terms
- Animals, Antineoplastic Agents, Cell Transformation, Neoplastic, Glycolysis, Glycosylation, Humans, Lactoylglutathione Lyase, Pyruvaldehyde, Biomarkers, Tumor, Signal Transduction, Drug Resistance, Neoplasm, Gene Silencing
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