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Targeting Aldehyde Dehydrogenase 2: New Therapeutic Opportunities
Open accessAbstract
A family of detoxifying enzymes called aldehyde dehydrogenases (ALDHs) has been a subject of recent interest, as its role in detoxifying aldehydes that accumulate through metabolism and to which we are exposed from the environment has been elucidated. Although the human genome has 19 ALDH genes, one ALDH emerges as a particularly important enzyme in a variety of human pathologies. This ALDH, ALDH2, is located in the mitochondrial matrix with much known about its role in ethanol metabolism. Less known is a new body of research to be discussed in this review, suggesting that ALDH2 dysfunction may contribute to a variety of human diseases including cardiovascular diseases, diabetes, neurodegenerative diseases, stroke, and cancer. Recent studies suggest that ALDH2 dysfunction is also associated with Fanconi anemia, pain, osteoporosis, and the process of aging. Furthermore, an ALDH2 inactivating mutation (termed ALDH2*2) is the most common single point mutation in humans, and epidemiological studies suggest a correlation between this inactivating mutation and increased propensity for common human pathologies. These data together with studies in animal models and the use of new pharmacological tools that activate ALDH2 depict a new picture related to ALDH2 as a critical health-promoting enzyme.
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Items 201–327 of 327
Wang, B., Wang, J., Zhou, S., Tan, S., He, X., Yang, Z., Xie, Y., Li, S., Zheng, C., & Ma, X. (2008) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2007.12.006 · Cited by 88
Churchill, E. N., Ferreira, J. C. B., Brum, P. C., Szweda, L. I., & Mochly‐Rosen, D. (2009) · Cardiovascular Research · doi:10.1093/cvr/cvp334 · Cited by 87
Self-citationFetal Alcohol Exposure: Consequences, Diagnosis, and Treatment
Pruett, D., Waterman, E. H., & Caughey, A. B. (2013) · Obstetrical & Gynecological Survey · doi:10.1097/ogx.0b013e31827f238f · Cited by 87
Discovery of a Novel Class of Covalent Inhibitor for Aldehyde Dehydrogenases
Khanna, M., Chen, C.-H., Kimble-Hill, A. C., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.293597 · Cited by 87
Self-citationChen, Y.-C., Peng, G.-S., Tsao, T., Wang, M.-F., Lu, R., & Yin, S. (2009) · Pharmacogenetics and Genomics · doi:10.1097/fpc.0b013e32832ecf2e · Cited by 86
Matsuda, T., Terashima, I., Matsumoto, Y., Yabushita, H., Matsui, S., & Shibutani, S. (1998) · Biochemistry · doi:10.1021/bi982134j · Cited by 83
MacArthur, A. C., McBride, M. L., Spinelli, J. J., Tamaro, S., Gallagher, R. P., & Theriault, G. P. (2008) · Cancer Causes & Control · doi:10.1007/s10552-007-9091-8 · Cited by 83
Nitroglycerin Use in Myocardial Infarction Patients - Risks and Benefits -
Ferreira, J. C. B., & Mochly‐Rosen, D. (2011) · Circulation Journal · doi:10.1253/circj.cj-11-1133 · Cited by 81
Self-citationMa, H., Yu, L., Byra, E. A., Hu, N., Kitagawa, K., Nakayama, K. I., Kawamoto, T., & Ren, J. T. (2010) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2010.03.017 · Cited by 81
Wenzel, P., Müller, J., Zurmeyer, S., Schuhmacher, S., Schulz, E., Oelze, M. W., Pautz, A., Kawamoto, T., Wojnowski, L., Kleinert, H., et al. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.12.089 · Cited by 80
The role of acetaldehyde in upper digestive tract cancer in alcoholics
Seitz, H. K., & Meier, P. (2007) · Translational research · doi:10.1016/j.trsl.2006.12.002 · Cited by 80
Bhatnagar, A. (1995) · Circulation Research · doi:10.1161/01.res.76.2.293 · Cited by 80
Diminished alcohol preference in transgenic mice lacking aldehyde dehydrogenase activity
Isse, T., Oyama, T., Kitagawa, K., Matsuno, K., Matsumoto, A., Yoshida, A., Nakayama, K., Nakayama, K., & Kawamoto, T. (2002) · Pharmacogenetics · doi:10.1097/00008571-200211000-00006 · Cited by 79
Yokoyama, A., & Omori, T. (2005) · Alcohol · doi:10.1016/j.alcohol.2005.04.003 · Cited by 78
Role of aldehyde dehydrogenase 2 Glu504lys polymorphism in acute coronary syndrome
Xu, F., Chen, Y. G., Li, X., Li, R. J., Zhang, H., Bian, Y., Zhang, C., Lv, R., Feng, J. B., & Zhang, Y. (2010) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2010.01181.x · Cited by 78
Wang, R., Nakajima, T., Kawamoto, T., & Honma, T. (2002) · Drug Metabolism and Disposition · doi:10.1124/dmd.30.1.69 · Cited by 78
Tsunehiro, O. (2005) · Frontiers in bioscience · doi:10.2741/1589 · Cited by 77
Unsaturated aldehydes including 4-OH-nonenal are elevated in patients with congestive heart failure
Mak, S. S., Lehotay, D. C., Yazdanpanah, M., Azevedo, E. R., Liu, P. P., & Newton, G. E. (2000) · Journal of Cardiac Failure · doi:10.1016/s1071-9164(00)90012-5 · Cited by 77
Ge, W., Guo, R., & Ren, J. T. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.08.002 · Cited by 76
Nakamura, K., KUSANO, K. F., Matsubara, H., Nakamura, Y., Miura, A., Nishii, N., Banba, K., Nagase, S., Miyaji, K., Morita, H., et al. (2005) · Journal of Cardiac Failure · doi:10.1016/j.cardfail.2004.05.005 · Cited by 75
Li, N., Zhou, J., Weiner, H., & Hurley, T. D. (1999) · Protein Science · doi:10.1110/ps.8.12.2784 · Cited by 75
Mitochondria Sentencing About Cellular Life and Death: A Matter of Oxidative Stress
Apostolova, N., Blas‐García, A., & Esplugues, J. V. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211798764924 · Cited by 75
Radovanović, S., Savic-Radojevic, A. R., Pljesa-Ercegovac, M. S., Djukic, T. I., Suvakov, S. R., Krotin, M., Šimić, D., Matic, M. G., Radojicic, Z. A., Pekmezovic, T. D., et al. (2012) · Journal of Cardiac Failure · doi:10.1016/j.cardfail.2012.04.003 · Cited by 73
Yokoyama, A., Omori, T., & Yokoyama, A. (2010) · The Keio Journal of Medicine · doi:10.2302/kjm.59.115 · Cited by 72
Specific Modulation of Na+Channels in Hippocampal Neurons by Protein Kinase Cϵ
Chen, Y., Cantrell, A. R., Messing, R. O., Scheuer, T., & Catterall, W. A. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.4089-04.2005 · Cited by 72
Systemic Oxidative Stress Associated with the Neurological Diseases of Aging
Serra, J. A., Domínguez, R. O., Marschoff, E. R., Guareschi, E. M., Famulari, A. L., & BOVERIS, A. (2009) · Neurochemical Research · doi:10.1007/s11064-009-9997-5 · Cited by 71
Lau, E. M. C., Chan, Y. H., Chan, M., Woo, J., Griffith, J. F., Chan, H. H. L., & Leung, P. C. (2000) · Calcified Tissue International · doi:10.1007/s002230050009 · Cited by 69
Cadoni, G., Boccia, S., Petrelli, L., Giannantonio, P. D., Arzani, D., Giorgio, A., Feo, E. D., Pandolfini, M., Gallì, P., Paludetti, G., et al. (2012) · Europe PMC (PubMed Central) · Cited by 68
Role of GABRA2 in Moderating Subjective Responses to Alcohol
Roh, S., Matsushita, S., Hara, S., Maesato, H., Matsui, T., Suzuki, G., Miyakawa, T., Ramchandani, V. A., Li, T., & Higuchi, S. (2010) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.2010.01357.x · Cited by 68
ALDH2 genetic polymorphism and the risk of type II diabetes mellitus in CAD patients
Xu, F., Chen, Y., Lv, R., Zhang, H., Tian, H., Bian, Y., Feng, J., Sun, Y., Li, R., Wang, R., et al. (2009) · Hypertension Research · doi:10.1038/hr.2009.178 · Cited by 68
Duan, J., McFadden, G., Borgerding, A. J., Norby, F. L., Ren, B. H., Ye, G., Epstein, P. N., & Ren, J. T. (2002) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00780.2001 · Cited by 68
Genetic Epidemiology of Ethanol Metabolic Enzymes: A Role for Selection
Goldman, D. A., & Enoch, M. (2015) · World review of nutrition and dietetics · doi:10.1159/000418505 · Cited by 68
Ge, W., & Ren, J. T. (2011) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2011.01347.x · Cited by 67
Preventive effects of Chlorella on cognitive decline in age-dependent dementia model mice
Nakashima, Y., Ohsawa, I., Konishi, F., Hasegawa, T., Kumamoto, S., Suzuki, Y., & Ohta, S. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.08.044 · Cited by 66
Brain atrophy and neuronal loss in alcoholism: a role for DNA damage?
Brooks, P. J. (2000) · Neurochemistry International · doi:10.1016/s0197-0186(00)00051-6 · Cited by 65
Okun, E., Arumugam, T. V., Tang, S., Gleichmann, M., Albeck, M., Sredni, B., & Mattson, M. P. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04615.x · Cited by 64
Yin, S., Liao, C., Lee, Y., Wu, C., & Jao, S. (1994) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.1994.tb00115.x · Cited by 63
Florang, V. R., Rees, J., Brogden, N. K., Anderson, D. G., Hurley, T. D., & Doorn, J. A. (2006) · NeuroToxicology · doi:10.1016/j.neuro.2006.07.018 · Cited by 63
Giuliani, N., Girasole, G., Vescovi, P., Passeri, G., & Pedrazzoni, M. (1999) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.1999.tb04126.x · Cited by 62
Russell, J. W., Karnes, J. L., & Dyck, P. J. B. (1996) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(95)00243-u · Cited by 62
Wang, H., Papoiu, A. D. P., Coghill, R. C., Patel, T. S., Wang, N., & Yosipovitch, G. (2009) · British Journal of Dermatology · doi:10.1111/j.1365-2133.2009.09628.x · Cited by 62
Vondriska, T. M., Klein, J. B., & Ping, P. (2001) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2001.280.4.h1434 · Cited by 62
Cho, Y.-J., Wang, H., Kozekov, I. D., Kurtz, A., Jacob, J., Voehler, M., Smith, J. A., Harris, T. M., Lloyd, R. S., Rizzo, C. J., et al. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050239z · Cited by 61
Ethnic differences in physical pain sensitivity: Role of acculturation
Chan, M. Y. P., Hamamura, T., & Janschewitz, K. (2012) · Pain · doi:10.1016/j.pain.2012.09.015 · Cited by 60
A Genome-Wide Association Study of Hypertension-Related Phenotypes in a Japanese Population
Hiura, Y., Tabara, Y., Kokubo, Y., Okamura, T., Miki, T., Tomoike, H., & Iwai, N. (2010) · Circulation Journal · doi:10.1253/circj.cj-10-0353 · Cited by 59
Solito, R., Corti, A., Chen, C., Mochly‐Rosen, D., Giachetti, A., Ziche, M., & Donnini, S. (2013) · Journal of Cell Science · doi:10.1242/jcs.117184 · Cited by 58
Self-citationDetermination of in vivo adducts of disulfiram with mitochondrial aldehyde dehydrogenase
Shen, M. L., Johnson, K. L., Mays, D. C., Lipsky, J. J., & Naylor, S. (2001) · Biochemical Pharmacology · doi:10.1016/s0006-2952(00)00586-4 · Cited by 57
Kinetic studies of Escherichia coli AlkB using a new fluorescence-based assay for DNA demethylation
Roy, T. W., & Bhagwat, A. S. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm1031 · Cited by 57
Alter, B. P., Joenje, H., Oostra, A. B., & Pals, G. (2005) · Archives of Otolaryngology - Head and Neck Surgery · doi:10.1001/archotol.131.7.635 · Cited by 56
Nagayoshi, H., Matsumoto, A., Nishi, R., Kawamoto, T., Ichiba, M., & Matsuda, T. (2008) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/j.mrgentox.2008.11.009 · Cited by 56
Burke, W. J. (2003) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1568007033482913 · Cited by 55
Ohsawa, I., Kamino, K., Nagasaka, K., Ando, F., Niino, N., Shimokata, H., & Ohta, S. (2003) · Journal of Human Genetics · doi:10.1007/s10038-003-0046-y · Cited by 55
Idiopathic neuropathy: new paradigms, new promise
Singer, M. A., Vernino, S. A., & Wolfe, G. I. (2012) · Journal of the Peripheral Nervous System · doi:10.1111/j.1529-8027.2012.00395.x · Cited by 54
Mechanism for Benomyl Action as a Mitochondrial Aldehyde Dehydrogenase Inhibitor in Mice
Staub, R. E., Quistad, G. B., & Casida, J. E. (1998) · Chemical Research in Toxicology · doi:10.1021/tx980002l · Cited by 53
Membrane alteration as a basis of aging and the protective effects of calorie restriction
Yu, B. P. (2005) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2005.03.020 · Cited by 51
Characterization of the East Asian Variant of Aldehyde Dehydrogenase-2
Beretta, M., Gorren, A. C. F., Wenzl, M. V., Weis, R., Russwurm, M., Koesling, D., Schmidt, K., & Mayer, B. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.014548 · Cited by 51
Nakamura, K., Miura, D., KUSANO, K. F., Fujimoto, Y., Yoshikawa, W. S., Fuke, S., Nishii, N., Nagase, S., Hata, Y., Morita, H., et al. (2009) · Journal of Cardiac Failure · doi:10.1016/j.cardfail.2009.04.008 · Cited by 51
Interrelationship between Alcohol, Smoking, Acetaldehyde and Cancer
Salaspuro, M. P. (2006) · Novartis Foundation symposium · doi:10.1002/9780470511848.ch6 · Cited by 50
Meta-Analysis of Aldehyde Dehydrogenase 2 Gene Polymorphism and Alzheimer's Disease in East Asians
Hao, P., Chen, Y., Wang, J., Wang, X. L., & Zhang, Y. (2011) · Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques · doi:10.1017/s0317167100011938 · Cited by 49
Ishikawa, H., Ishikawa, T., Yamamoto, H., Fukao, A., & Yokoyama, K. (2007) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2006.11.026 · Cited by 46
Marietta, C. A., Thompson, L. H., Lamerdin, J. E., & Brooks, P. J. (2009) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2009.03.011 · Cited by 46
Shimizu, Y., Sakai, A., Menuki, K., Mori, T., Isse, T., Oyama, T., Kawamoto, T., & Nakamura, T. (2011) · Bone · doi:10.1016/j.bone.2011.01.008 · Cited by 46
Ikehara, S., Iso, H., Yamagishi, K., Yamamoto, S., Inoue, M., Tsugane, S., & the JPHC Study Group (2009) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.2009.00923.x · Cited by 45
Singh, R., Sandhu, J. K., Kaur, B., Jurén, T., Steward, W. P., Segerbäck, D., & Farmer, P. B. (2009) · Chemical Research in Toxicology · doi:10.1021/tx900106y · Cited by 44
Inhibition of aldehyde detoxification in CNS mitochondria by fungicides
Leiphon, L. J., & Picklo, M. J. (2006) · NeuroToxicology · doi:10.1016/j.neuro.2006.08.008 · Cited by 44
Chang, Y., Chiu, Y., Lee, I., Ho, L.-T., Hung, Y., Hsiung, C. A., Quertermous, T., Donlon, T. A., Lee, W., Lee, P., et al. (2012) · BMC Cardiovascular Disorders · doi:10.1186/1471-2261-12-58 · Cited by 44
Self-citationGuo, R., Zhong, L., & Ren, J. T. (2009) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2009.05152.x · Cited by 44
Dandré, F., CASSAIGNE, A., & Iron, A. (1995) · Molecular and Cellular Probes · doi:10.1006/mcpr.1995.0030 · Cited by 43
Acetaldehyde Metabolism In Vivo During Ethanol Oxidation
Eriksson, C. J. P. (1977) · Advances in experimental medicine and biology · doi:10.1007/978-1-4899-5181-6_21 · Cited by 43
Ma, R., Yu, J., Xu, D., Yang, L., Lin, X., Zhao, F., & Bai, F. (2011) · Journal of Hypertension · doi:10.1097/hjh.0b013e32834e1e2e · Cited by 42
A selective ALDH-2 inhibitor reduces anxiety in rats
Overstreet, D. H., Knapp, D. J., Breese, G. R., & Diamond, I. (2009) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2009.09.004 · Cited by 42
Canova, C., Richiardi, L., Merletti, F., Pentenero, M., Gervasio, C. F., Tanturri, G., Garzino‐Demo, P., Pecorari, G., Talamini, R., Barzan, L., et al. (2010) · Tumori Journal · doi:10.1177/030089161009600101 · Cited by 41
Autophagy in ALDH2-elicited cardioprotection against ischemic heart disease: Slayer or savior?
Zhang, Y., & Ren, J. (2010) · Autophagy · doi:10.4161/auto.6.8.13652 · Cited by 41
Jp, L. (1999) · PubMed · Cited by 41
What is in that Drink: The Biological Actions of Ethanol, Acetaldehyde, and Salsolinol
Deehan, G. A., Brodie, M. S., & Rodd, Z. A. (2011) · Current topics in behavioral neurosciences · doi:10.1007/7854_2011_198 · Cited by 40
Ren, J. T., Babcock, S. A., Li, Q., Huff, A. F., Li, S., & Doser, T. A. (2009) · Toxicology Letters · doi:10.1016/j.toxlet.2009.02.019 · Cited by 40
Detoxification of reactive aldehydes in mitochondria: Effects of age and dietary restriction
Chen, J. J., & Yu, B. (1996) · Aging Clinical and Experimental Research · doi:10.1007/bf03339590 · Cited by 40
Lee, C., Wu, D., Wu, I., Goan, Y., Lee, J., Chou, S., Chan, T., Huang, H., Hung, Y.-H., Huang, M., et al. (2009) · International Journal of Cancer · doi:10.1002/ijc.24357 · Cited by 39
Discovery of novel regulators of aldehyde dehydrogenase isoenzymes
Parajuli, B., Kimble-Hill, A. C., Khanna, M., Ivanova, Y., Meroueh, S. O., & Hurley, T. D. (2011) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2011.02.018 · Cited by 39
Acetaldehyde Adducts in Circulation
Niemelä, O. J. (2006) · Novartis Foundation symposium · doi:10.1002/9780470511848.ch13 · Cited by 38
Mukerjee, N., & Pietruszko, R. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90239-s · Cited by 37
Nagasawa, H., Wada, M., Arawaka, S., Kawanami, T., Kurita, K., Daimon, M., Adachi, M., Hosoya, T., Emi, M., Muramatsu, M., et al. (2007) · European Journal of Neurology · doi:10.1111/j.1468-1331.2007.01700.x · Cited by 37
Park, J. W., Ji, Y. I., Choi, Y.-H., Kang, M.-Y., Jung, E. H., Cho, H.-Y., Cho, H.-Y., Kang, B. K., Joung, Y. S., Kim, D.-H., et al. (2009) · Experimental & Molecular Medicine · doi:10.3858/emm.2009.41.11.083 · Cited by 37
Replication of N2-Ethyldeoxyguanosine DNA Adducts in the Human Embryonic Kidney Cell Line 293
Upton, D. C., Wang, X., Blans, P., Perrino, F. W., Fishbein, J. C., & Akman, S. A. (2006) · Chemical Research in Toxicology · doi:10.1021/tx060084a · Cited by 36
Human aldehyde dehydrogenase: Catalytic activity in oriental liver
Ferencz‐Biro, K., & Pietruszko, R. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(84)91072-6 · Cited by 36
Preliminary report on clinical trials of antabuse.
Rg, B., & Hw, S. (1949) · PubMed · Cited by 35
Lin, Y.-P., & Cheng, T. (2002) · Medical Hypotheses · doi:10.1016/s0306-9877(02)00253-0 · Cited by 34
Ning, S., Budas, G. R., Churchill, E. N., Chen, C., Knox, S. J., & Mochly‐Rosen, D. (2012) · Radiation Research · doi:10.1667/rr2861.1 · Cited by 34
Self-citationMurata, C., Suzuki, Y., Muramatsu, T., Taniyama, M., Atsumi, Y., Matsuoka, K., Watanabe, T., & Okazaki, I. (2000) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.2000.tb00003.x · Cited by 33
Characteristics of aldehyde dehydrogenase 2 (Aldh2) knockout mice
Yu, H.-S., Oyama, T., Isse, T., 北川恭子, Ogawa, M., Pham, T.-T.-P., & Kawamoto, T. (2009) · Toxicology Mechanisms and Methods · doi:10.3109/15376510903401708 · Cited by 32
Jung, J. G., Kim, J. S., & Oh, M. K. (2010) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.2010.01256.x · Cited by 31
Acetaldehyde and Alcoholic Cardiomyopathy: Lessons from the ADH and ALDH2 Transgenic Models
Ren, J. T. (2006) · Novartis Foundation symposium · doi:10.1002/9780470511848.ch5 · Cited by 31
E3 Ubiquitin Ligases in Protein Quality Control Mechanism
Chhangani, D., Joshi, A. P., & Mishra, A. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8273-x · Cited by 31
Lai, C., Chao, Y., Chen, Y., Liao, C., Chen, M., Liu, Y., & Yin, S. (2000) · Alcoholism Clinical and Experimental Research · doi:10.1097/00000374-200011000-00004 · Cited by 30
Gong, D., Zhang, Y., Zhang, H., Gu, H., Jiang, Q., & Hu, S. (2012) · Cardiovascular Toxicology · doi:10.1007/s12012-012-9179-6 · Cited by 29
ALDH2/ADH2 Polymorphism Associated with Vasculopathy and Neuropathy in Type 2 Diabetes
Suzuki, Y., Taniyama, M., Muramatsu, T., Higuchi, S., Ohta, S., Atsumi, Y., & Matsuoka, K. (2004) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.2004.tb03227.x · Cited by 29
Disulfiram neuropathy: Two cases of distal axonopathy
Filosto, M., Tentorio, M., Broglio, L., Buzio, S., Lazzarini, C., Pasolini, M. P., Cotelli, M. S., Scarpelli, M., Mancuso, M., Choub, A., et al. (2008) · Clinical Toxicology · doi:10.1080/15563650701636390 · Cited by 28
Bian, Y., Chen, Y., Xu, F., Li, X., Ji, W., & Zhang, Y. (2010) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.221.107 · Cited by 28
Association of aldehyde dehydrogenase-2 polymorphism with alcoholic polyneuropathy in humans
Masaki, T., Mochizuki, H., Matsushita, S., Yokoyama, A., Kamakura, K., & Higuchi, S. (2004) · Neuroscience Letters · doi:10.1016/j.neulet.2004.04.009 · Cited by 28
Nakagawa, T., Kajiwara, A., Saruwatari, J., Hamamoto, A., Kaku, W., Oniki, K., 修一, 三., Ogata, Y., & Nakagawa, K. (2012) · Pharmacogenetics and Genomics · doi:10.1097/fpc.0b013e32835b1707 · Cited by 28
Mays, D. C., Ortiz‐Bermúdez, P., Lam, J. P., Tong, I. H., Fauq, A. H., & Lipsky, J. J. (1998) · Biochemical Pharmacology · doi:10.1016/s0006-2952(97)00686-2 · Cited by 27
Effects of 5-week ethanol feeding on the liver of aldehyde dehydrogenase 2 knockout mice
Matsumoto, A., Kawamoto, T., 武藤, 文., Isse, T., Oyama, T., Kitagawa, K., Nakayama, K. I., & Ichiba, M. (2008) · Pharmacogenetics and Genomics · doi:10.1097/fpc.0b013e328307a0a9 · Cited by 26
Szymańska, K., Levi, J. E., Menezes, A. M. B., Wünsch‐Filho, V., Eluf‐Neto, J., Koifman, S., Matos, E., Daudt, A. W., Curado, M. P., Villar, S., et al. (2009) · Carcinogenesis · doi:10.1093/carcin/bgp212 · Cited by 26
FANCA and FANCG are the major Fanconi anemia genes in the Korean population
Park, J. K., Chung, N., Chae, H., et al. (2012) · Clinical Genetics · doi:10.1111/cge.12042 · Cited by 25
ALDH2/ADH2 Polymorphism Associated with Vasculopathy and Neuropathy in Type 2 Diabetes
Suzuki, Y., Taniyama, M., Muramatsu, T., Higuchi, S., Ohta, S., Atsumi, Y., & Matsuoka, K. (2004) · Alcoholism Clinical and Experimental Research · doi:10.1097/01.alc.0000133583.44581.99 · Cited by 25
Suzuki, Y., Muramatsu, T., Taniyama, M., Atsumi, Y., Suematsu, M., Kawaguchi, R., Higuchi, S., Asahina, T., Murata, C., Handa, M., et al. (1996) · Diabetes Care · doi:10.2337/diacare.19.12.1423 · Cited by 25
Mechanism of Inhibition of Rat Liver Class 2 ALDH by 4-Hydroxynonenal
Luckey, S. W., Tjalkens, R. B., & Petersen, D. R. (1999) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-4735-8_9 · Cited by 24
Tsou, P., Page, N. A., Lee, S. G., Fung, S. M., Keung, W. M., & Fung, H. L. (2011) · The AAPS Journal · doi:10.1208/s12248-011-9295-4 · Cited by 24
The prevalence of diabetic neuropathy according to ethnicity
Sosenko, J. M. (2009) · Current Diabetes Reports · doi:10.1007/s11892-009-0071-0 · Cited by 24
Sublethal Total Body Irradiation Leads to Early Cerebellar Damage and Oxidative Stress
Cui, L., Pierce, D. R., Light, K. E., Melchert, R. B., Fu, Q., Kumar, K. S., & Hauer‐Jensen, M. (2010) · Current Neurovascular Research · doi:10.2174/156720210791184880 · Cited by 23
Fernández, E., Koek, W., Ran, Q., Gerhardt, G. A., France, C. P., & Strong, R. (2006) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.2006.00200.x · Cited by 23
Inhibition of Cardiac Myocyte Contraction by 4-Hydroxy-Trans-2-Nonenal
Aberle, N. S., Picklo, M. J., Amarnath, V., & Ren, J. T. (2004) · Cardiovascular Toxicology · doi:10.1385/ct:4:1:21 · Cited by 23
Guo, R., Chen, X., Guo, X., Chen, L., Li, D., Peng, J., & Li, Y. (2008) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2008.05.049 · Cited by 22
Matsumoto, A., Ichiba, M., Horita, M., 山下, 善., Takahashi, T., Isse, T., Oyama, T., Kawamoto, T., & Tomokuni, K. (2007) · Alcohol · doi:10.1016/j.alcohol.2007.01.004 · Cited by 22
Luo, H., Israel, Y., Tu, G., Eriksson, C. J. P., & Zhang, Y. (2005) · Biochemical Genetics · doi:10.1007/s10528-005-5213-8 · Cited by 21
Weng, H., Weng, Z., Lu, Y., Nakayama, K., & Morimoto, K. (2010) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/j.mrgentox.2010.05.013 · Cited by 19
S-methyl N-butylthiocarbamate sulfoxide
Staub, R. E., Quistad, G. B., & Casida, J. E. (1999) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00239-7 · Cited by 18
Murata, C., Taniyama, M., Kuriyama, S., Muramatsu, T., Atsumi, Y., Matsuoka, K., & Suzuki, Y. (2004) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2003.11.022 · Cited by 18
Enomoto, N., Takada, A., & Date, T. (1991) · Gastroenterologia Japonica · doi:10.1007/bf02782812 · Cited by 16
Weinshenker, D. (2010) · Nature Medicine · doi:10.1038/nm0910-969 · Cited by 15
Aldehyde dehydrogenase and acetaldehyde metabolism.
Weiner, H., & Wang, X. (1994) · PubMed · Cited by 14
Matsumoto, A., Kawamoto, T., Horita, M., et al. (2007) · Alcohol · doi:10.1016/j.alcohol.2007.08.002 · Cited by 12
Stressed Out: Endogenous Aldehydes Damage Hematopoietic Stem Cells
Parmar, K., & D’Andrea, A. D. (2012) · Cell stem cell · doi:10.1016/j.stem.2012.10.007 · Cited by 10
Drosophila lacking a homologue of mammalian ALDH2 have multiple fitness defects
Chakraborty, M., & Fry, J. D. (2011) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2011.01.031 · Cited by 7
Suzuki, Y., Kuriyama, S., Atsumi, Y., Murata, C., Matsuoka, K., Suzuki, Y., Taniyama, M., Muramatsu, T., Suzuki, Y., & Ohta, S. (2003) · Diabetes Research and Clinical Practice · doi:10.1016/s0168-8227(03)00020-2 · Cited by 5
Lessons From the Besotted Heart
Karliner, J. S. (2009) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2009.06.052 · Cited by 5
Sinclair, D. (2006) · Biochemical Genetics · doi:10.1007/s10528-006-9041-2 · Cited by 4
Cited by
Millwood, I. Y., Walters, R. G., Mei, X. W., Guo, Y., Yang, L., Bian, Z., Bennett, D. A., Chen, Y., Dong, C., Hu, R., et al. (2019) · The Lancet · doi:10.1016/s0140-6736(18)31772-0 · Cited by 514
Wang, S., Wang, L., Qin, X., Turdi, S., Sun, D., Culver, B., Reiter, R. J., Wang, X., Zhou, H., & Ren, J. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0171-5 · Cited by 135
Disulfiram Treatment Normalizes Body Weight in Obese Mice
Bernier, M., Mitchell, S. J., Wahl, D., Diaz, A., Singh, A., Seo, W., Wang, M., Ali, A., Kaiser, T., Price, N. L., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.04.019 · Cited by 85
Huang, P.-H., Hu, C.-C., Chien, C.-H., Chen, L.-W., Chien, R.-N., Lin, Y.-S., Chao, M., Lin, C.-L., & Yeh, C.-T. (2019) · Journal of Cancer · doi:10.7150/jca.33221 · Cited by 15
Ferreira, I., Machado de Oliveira, R., Carvalho, A. S., Teshima, A., Beck, H. C., Matthiesen, R., Costa-Silva, B., & Macedo, M. P. (2022) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00353 · Cited by 9
Metadata
- Authors
- Chen, C.-H., Ferreira, J. C. B., Gross, E. R., & Mochly-Rosen, D.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2014-01
- Volume
- 94
- Issue
- 1
- Pages
- 1-34
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2110549318
- Cited by
- 614
- References
- 327
- FWCI
- 5.64
- Type
- journal article
- Language
- en
- Open access
- green
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 ›
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
