Nitrative Stress and Auditory Dysfunction
Open accessAbstract
Nitrative stress is increasingly recognized as a critical mediator of apoptotic cell death in many pathological conditions. The accumulation of nitric oxide along with superoxide radicals leads to the generation of peroxynitrite that can eventually result in the nitration of susceptible proteins. Nitrotyrosine is widely used as a biomarker of nitrative stress and indicates oxidative damage to proteins. Ototoxic insults, such as exposure to noise and ototoxic drugs, enhance the generation of 3-nitrotyrosine in different cell types in the cochlea. Nitrated proteins can disrupt critical signaling pathways and eventually lead to apoptosis and loss of sensory receptor cells in the cochlea. Accumulating evidence shows that selective targeting of nitrative stress attenuates cellular damage. Anti-nitrative compounds, such as peroxynitrite decomposition catalysts and inducible nitric oxide synthase inhibitors, prevent nitrative stress-mediated auditory damage. However, the role of nitrative stress in acquired hearing loss and its potential significance as a promising interventional target is yet to be fully characterized. This review provides an overview of nitrative stress mechanisms, the induction of nitrative stress in the auditory tissue after ototoxic insults, and the therapeutic value of targeting nitrative stress for mitigating auditory dysfunction.
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
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?
P38 is a major pathway influencing cell proliferation, cell cycle, and apoptosis, and is activated in response to environmental stresses including inflammatory cytokines, oxidative and nitrosative stress, and DNA damage.
“P38 is a major pathway influencing cell proliferation, cell cycle, and apoptosis, and is activated in response to various environmental stresses, involving inflammatory cytokines, oxidative and nitrosative stress, and DNA damage (Shahab and Jamesdaniel 2022; Zhang et al. 2016).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Shahab and Jamesdaniel 2022
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Cillà, S. D., Farruggio, S., Vujosevic, S., Raina, G., Filippini, D. A., Gatti, V., Clemente, N., Mary, D., Vezzola, D., Casini, G., et al. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479441 · Cited by 5,154 · see citing works
Nitric oxide synthases: structure, function and inhibition
ALDERTON, W. K., COOPER, C. E., & KNOWLES, R. G. (2001) · Biochemical Journal · doi:10.1042/bj3570593 · Cited by 4,110 · see citing works
Nitric oxide synthases: structure, function and inhibition
ALDERTON, W. K., Cooper, C. E., & Knowles, R. G. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3570593 · Cited by 4,106 · see citing works
Protein S-nitrosylation: Purview and parameters
Hess, D. T., Matsumoto, A., Kim, S.-O., Marshall, H. E., & Stamler, J. S. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1569 · Cited by 2,153 · see citing works
Nitric oxide, oxidants, and protein tyrosine nitration
Radí, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307446101 · Cited by 1,456 · see citing works
MacMillan-Crow, L.-A., Crow, J. P., Kerby, J. D., Beckman, J. S., & Thompson, J. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11853 · Cited by 768 · see citing works
S-nitrosylation in health and disease
Foster, M. W., McMahon, T., & Stamler, J. S. (2003) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(03)00028-5 · Cited by 552 · see citing works
Nitric Oxide as a Bioregulator of Apoptosis
Chung, H.-T., Pae, H., Choi, B.-M., Billiar, T. R., & Kim, Y.-M. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4670 · Cited by 533 · see citing works
Greenacre, S., & Ischiropoulos, H. (2001) · Free Radical Research · doi:10.1080/10715760100300471 · Cited by 500 · see citing works
Singel, D. J., & Stamler, J. S. (2005) · Annual Review of Physiology · doi:10.1146/annurev.physiol.67.060603.090918 · Cited by 481 · see citing works
Cytochrome c Nitration by Peroxynitrite
Cassina, A. M., Hodara, R., Souza, J. M., Thomson, L., Castro, L., Ischiropoulos, H., Freeman, B. A., & Radi, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909978199 · Cited by 354 · see citing works
Delayed production of free radicals following noise exposure
Yamashita, D., Jiang, H.-Y., Schacht, J., & Miller, J. M. (2004) · Brain Research · doi:10.1016/j.brainres.2004.05.104 · Cited by 352 · see citing works
Reactive Nitrogen Species: Molecular Mechanisms and Potential Significance in Health and Disease
Martínez, M. C., & Andriantsitohaina, R. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1993 · Cited by 329 · see citing works
Factors Determining the Selectivity of Protein Tyrosine Nitration
Souza, J. M., Daikhin, E., Yudkoff, M., Raman, C. S., & Ischiropoulos, H. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1480 · Cited by 315 · see citing works
Zou, M., Martin, C., & Ullrich, V. (1997) · Biological Chemistry · doi:10.1515/bchm.1997.378.7.707 · Cited by 289 · see citing works
Functional Consequences of α-Synuclein Tyrosine Nitration
Hodara, R., Norris, E. H., Giasson, B. I., Mishizen-Eberz, A. J., Lynch, D. R., Lee, V. M. ‐., & Ischiropoulos, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408906200 · Cited by 286 · see citing works
Kil, J., Lobariñas, E., Spankovich, C., Griffiths, S. K., Antonelli, P. J., Lynch, E. D., & Prell, C. G. L. (2017) · The Lancet · doi:10.1016/s0140-6736(17)31791-9 · Cited by 270 · see citing works
Nitric Oxide as a Pro-apoptotic as well as Anti-apoptotic Modulator
Choi, B.-M., Pae, H., Jang, S. I., Kim, Y., & Chung, H. (2002) · BMB Reports · doi:10.5483/bmbrep.2002.35.1.116 · Cited by 253 · see citing works
Vadseth, C., Souza, J. M., Thomson, L., Seagraves, A., Nagaswami, C., Scheiner, T., Torbet, J., Vilaire, G., BENNETT, J. S., Murciano, J.-C., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m306101200 · Cited by 228 · see citing works
Özdemir, Y., Bolay, H., Sarıbaş, O., & Dalkara, T. (2000) · Stroke · doi:10.1161/01.str.31.8.1974 · Cited by 197 · see citing works
Oxidative imbalance in the aging inner ear
Jiang, H., Talaska, A. E., Schacht, J., & Sha, S. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.06.025 · Cited by 195 · see citing works
Reaction of Peroxynitrite with Mn-Superoxide Dismutase
Quijano, C., Hernández-Saavedra, D., Castro, L., McCord, J. M., Freeman, B. Α., & Radí, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009429200 · Cited by 185 · see citing works
Modulation of apoptosis by nitric oxide: implications in myocardial ischemia and heart failure
Razavi, H. M., HAMILTON, J., & Feng, Q. (2005) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2004.11.006 · Cited by 181 · see citing works
Nitric oxide-based protein modification: formation and site-specificity of protein S-nitrosylation
Kovács, I., & Lindermayr, C. (2013) · Frontiers in Plant Science · doi:10.3389/fpls.2013.00137 · Cited by 175 · see citing works
Protection from noise-induced lipid peroxidation and hair cell loss in the cochlea
Ohinata, Y., Miller, J. M., & Schacht, J. (2003) · Brain Research · doi:10.1016/s0006-8993(02)04205-1 · Cited by 170 · see citing works
Autophagy Attenuates Noise-Induced Hearing Loss by Reducing Oxidative Stress
Hu, Y., Wang, X., Hill, K., Chen, J., Lemasters, J. J., Yang, S., & Sha, S. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6004 · Cited by 165 · see citing works
Wu, S., Wu, Y., Wu, T.-P., & Wei, Y. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.10.034 · Cited by 159 · see citing works
Plasma proteins modified by tyrosine nitration in acute respiratory distress syndrome
Gole, M., Souza, J. M., Choi, I. Y., Hertkorn, C., Malcolm, S., Foust, R., Finkel, B., Lanken, P. N., & Ischiropoulos, H. (2000) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2000.278.5.l961 · Cited by 152 · see citing works
Post-exposure treatment attenuates noise-induced hearing loss
Yamashita, D., Jiang, H., Prell, C. G. L., Schacht, J., & Miller, J. M. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2005.04.015 · Cited by 150 · see citing works
Role of mitochondrial dysfunction and mitochondrial DNA mutations in age-related hearing loss
Yamasoba, T., Someya, S., Yamada, C., Weindruch, R. H., Prolla, T. A., & Tanokura, M. (2006) · Hearing Research · doi:10.1016/j.heares.2006.06.004 · Cited by 143 · see citing works
Honkura, Y., Matsuo, H., Murakami, S., Sakiyama, M., Mizutari, K., Shiotani, A., Yamamoto, M. P., Morita, I., Shinomiya, N., Kawase, T., et al. (2016) · Scientific Reports · doi:10.1038/srep19329 · Cited by 130 · see citing works
Crystal Structure of the Antioxidant Enzyme Glutathione Reductase Inactivated by Peroxynitrite
Savvides, S. N., Scheiwein, M., Böhme, C. C., Arteel, G. E., Karplus, P. A., Becker, K., & Schirmer, R. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108190200 · Cited by 127 · see citing works
Protein and lipid nitration: Role in redox signaling and injury
Rubbo, H., & Radí, R. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.03.007 · Cited by 126 · see citing works
Fukuyama, N., Takizawa, S., Ishida, H., Hoshiai, K., Shinohara, Y., & Nakazawa, H. K. (1998) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-199802000-00001 · Cited by 122 · see citing works
Ebselen attenuates cochlear damage caused by acoustic trauma
Pourbakht, A., & Yamasoba, T. (2003) · Hearing Research · doi:10.1016/s0378-5955(03)00178-3 · Cited by 113 · see citing works
A central role for S-nitrosylation in apoptosis
Benhar, M., & Stamler, J. S. (2005) · Nature Cell Biology · doi:10.1038/ncb0705-645 · Cited by 111 · see citing works
Emerging Roles of S -Nitrosylation in Protein Misfolding and Neurodegenerative Diseases
Nakamura, T., & Lipton, S. A. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1858 · Cited by 107 · see citing works
S-nitrosylation regulates mitochondrial quality control via activation of parkin
Ozawa, K., Komatsubara, A. T., Nishimura, Y., Sawada, T., Kawafune, H., Tsumoto, H., Tsuji, Y., Zhao, J., Kyotani, Y., Tanaka, T., et al. (2013) · Scientific Reports · doi:10.1038/srep02202 · Cited by 96 · see citing works
Nitrosative Stress in the ER: A New Role for S-Nitrosylation in Neurodegenerative Diseases
Forrester, M. T., Benhar, M., & Stamler, J. S. (2006) · ACS Chemical Biology · doi:10.1021/cb600244c · Cited by 90 · see citing works
Shi, X., Ren, T., & Nuttall, A. L. (2002) · Hearing Research · doi:10.1016/s0378-5955(01)00409-9 · Cited by 74 · see citing works
Lynch, E. D., Gu, R., Pierce, C., & Kil, J. (2005) · Anti-Cancer Drugs · doi:10.1097/00001813-200506000-00013 · Cited by 65 · see citing works
Regulation of Apoptosis by Nitrosative Stress
Kim, K.-M., Kim, P. K. M., Kwon, Y., Bai, S.-K., Nam, W. D., & Kim, Y. (2002) · BMB Reports · doi:10.5483/bmbrep.2002.35.1.127 · Cited by 63 · see citing works
Rathinam, R., Ghosh, S., Neumann, W., & Jamesdaniel, S. (2015) · Cell Death Discovery · doi:10.1038/cddiscovery.2015.52 · Cited by 63 · see citing works
Self-citationLanone, S., Manivet, P., Callebert, J., Launay, J., Payen, D. M., Aubier, M., Boczkowski, J., & Mebazaa, A. (2002) · Biochemical Journal · doi:10.1042/bj20020339 · Cited by 61 · see citing works
Peroxynitrite inactivates human‐tissue inhibitor of metalloproteinase‐4
Donnini, S., Monti, M., Roncone, R., Morbidelli, L., Rocchigiani, M., Oliviero, S., Casella, L., Giachetti, A., Schulz, R., & Ziche, M. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.02.080 · Cited by 60 · see citing works
Protein S-nitrosylation: Role for nitric oxide signaling in neuronal death
Shahani, N., & Sawa, A. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.07.010 · Cited by 57 · see citing works
Yakovlev, V. A., Bayden, A. S., Graves, P. R., Kellogg, G. E., & Mikkelsen, R. B. (2010) · Biochemistry · doi:10.1021/bi100564w · Cited by 56 · see citing works
Possible Roles of Nitric Oxide in the Physiology and Pathophysiology of the Mammalian Cochlea
Ruan, R. (2002) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2002.tb04073.x · Cited by 50 · see citing works
Jamesdaniel, S., Coling, D., Hinduja, S., Ding, D., Li, J., Cassidy, L., Seigel, G. M., Qu, J., & Salvi, R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.297960 · Cited by 49 · see citing works
Self-citationIshiyama, G. P., Wester, J. L., López, I. A., Beltrán‐Parrazal, L., & Ishiyama, A. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01068 · Cited by 41 · see citing works
Heinrich, U., Selivanova, O., Feltens, R., Brieger, J., & Mann, W. J. (2005) · Brain Research · doi:10.1016/j.brainres.2005.04.023 · Cited by 36 · see citing works
Adenosine amine congener mitigates noise-induced cochlear injury
Vlajkovic, S. M., Lee, K., Wong, A. C. Y., Guo, C. X., Gupta, R., Housley, G. D., & Thorne, P. R. (2010) · Purinergic Signalling · doi:10.1007/s11302-010-9188-5 · Cited by 35 · see citing works
Jamesdaniel, S., Rathinam, R., & Neumann, W. L. (2016) · Redox Biology · doi:10.1016/j.redox.2016.10.016 · Cited by 34 · see citing works
Self-citation1-Nitrosomelatonin is a spontaneous NO-releasing compound
Blanchard-Fillion, B., Servy, C., & Ducrocq, C. (2001) · Free Radical Research · doi:10.1080/10715760100301351 · Cited by 33 · see citing works
Photoreceptor Mitochondrial Tyrosine Nitration in Experimental Uveitis
Wu, G., Lee, T. D., Moore, R. E., & Rao, N. A. (2005) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.04-1525 · Cited by 31 · see citing works
Tauroursodeoxycholic acid attenuates gentamicin-induced cochlear hair cell death in vitro
Jia, Z., He, Q., Shan, C., & Li, F. (2018) · Toxicology Letters · doi:10.1016/j.toxlet.2018.05.007 · Cited by 31 · see citing works
Alvarado, J. C., Fuentes‐Santamaría, V., Gabaldón-Ull, M. C., Jareño-Flores, T., Miller, J. M., & Juiz, J. M. (2016) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2016.00019 · Cited by 30 · see citing works
Nagashima, R., Yamaguchi, T., Tanaka, H., & Ogita, K. (2010) · Journal of Pharmacological Sciences · doi:10.1254/jphs.10113fp · Cited by 28 · see citing works
Protective effect of polyphenols on presbycusis via oxidative/nitrosative stress suppression in rats
Sánchez‐Rodríguez, C., Martín-Sanz, E., Cuadrado, E., Granizo, J. J., & Fernández, R. S. (2016) · Experimental Gerontology · doi:10.1016/j.exger.2016.07.005 · Cited by 26 · see citing works
Attenuation of noise-induced hearing loss using methylene blue
Park, J.-S., Jou, I., & Park, S. M. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.170 · Cited by 25 · see citing works
Liang, J. H., Li, Y. N., Qi, J., & Jia, X. X. (2009) · Journal of Endocrinological Investigation · doi:10.1007/bf03346572 · Cited by 23 · see citing works
Yang, D., Xie, J., Liu, K., Peng, Z., Guo, J., Yu, S., Wang, G., & Gong, S. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.09.036 · Cited by 23 · see citing works
Toumpas, C., Clark, J. E., Harris, A., Beswick, R., & Nourse, C. B. (2014) · Journal of Paediatrics and Child Health · doi:10.1111/jpc.12776 · Cited by 21 · see citing works
Rosati, R., Shahab, M., Neumann, W. L., & Jamesdaniel, S. (2019) · Experimental Cell Research · doi:10.1016/j.yexcr.2019.05.008 · Cited by 19 · see citing works
Self-citationAstragaloside IV attenuates impulse noise-induced trauma in guinea pig
Xiong, M., Lai, H., He, Q., & Wang, J. (2011) · Acta Oto-Laryngologica · doi:10.3109/00016489.2011.568524 · Cited by 18 · see citing works
Nitric oxide synthase inhibitor reduces noise-induced cochlear damage in guinea pigs
Diao, M., Gao, W., & Sun, J. (2007) · Acta Oto-Laryngologica · doi:10.1080/00016480701242436 · Cited by 18 · see citing works
Ciodaro, F., Freni, F., Alberti, G., Forelli, M., Gazia, F., Bruno, R., Scherdel, E. P., Galletti, B., & Galletti, F. (2020) · International Archives of Otorhinolaryngology · doi:10.1055/s-0039-1697988 · Cited by 18 · see citing works
Downstream Targets of Lmo4 Are Modulated by Cisplatin in the Inner Ear of Wistar Rats
Jamesdaniel, S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0115263 · Cited by 17 · see citing works
Self-citationUp-regulation of autophagy and apoptosis of cochlear hair cells in mouse models for deafness
Xu, F., Cheng, Y., & Yan, W. (2018) · Archives of Medical Science · doi:10.5114/aoms.2018.75348 · Cited by 15 · see citing works
Is S-nitrosylation of Cochlear Proteins a Critical Factor in Cisplatin-Induced Ototoxicity?
Jamesdaniel, S., Manohar, S., & Hinduja, S. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4656 · Cited by 14 · see citing works
Self-citationShahab, M., Rosati, R., Meyer, D. N., Shields, J. N., Crofts, E. J., Baker, T. R., & Jamesdaniel, S. (2020) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2020.115342 · Cited by 12 · see citing works
Self-citationNoise-induced nitrotyrosine increase and outer hair cell death in guinea pig cochlea.
Han, W., Shi, X.-R., & Nuttall, A. L. (2013) · PubMed · Cited by 11 · see citing works
Lu, S., Fan, Z., Xu, W., Han, Y., Zhang, G., Liu, W., Bai, X., Wang, X., Xin, H., Li, J., et al. (2011) · Neurological Research · doi:10.1179/1743132810y.0000000027 · Cited by 8 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging
Jomova, K., Raptova, R., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03562-9 · Cited by 2,638 · see citing works
Pathophysiology of the Effects of Oxidative Stress on the Skeletal System
Shinohara, I., Morita, M., Chow, S. K., Murayama, M., Sususki, Y., Gao, Q., & Goodman, S. B. (2025) · Journal of Orthopaedic Research® · doi:10.1002/jor.26075 · Cited by 29 · see citing works
Targeting regulated cell death (RCD) with naturally derived sesquiterpene lactones in cancer therapy
Xu, C., Wen, S., Du, X., Zou, X., Leung, E. L., Zhou, G., Wu, Q., & Shen, B. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107553 · Cited by 17 · see citing works
Quantitative profiling of cochlear synaptosomal proteins in cisplatin-induced synaptic dysfunction
Shahab, M., Rosati, R., Stemmer, P. M., Dombkowski, A. A., & Jamesdaniel, S. (2024) · Hearing Research · doi:10.1016/j.heares.2024.109022 · Cited by 14 · see citing works
Self-citationThe Role of Pericytes in Inner Ear Disorders: A Comprehensive Review
Maniaci, A., Briglia, M., Allia, F., Montalbano, G., Romano, G. L., Zaoualí, M. A., Hmida, D., Gagliano, C., Malaguarnera, R., Lentini, M., et al. (2024) · Biology · doi:10.3390/biology13100802 · Cited by 7 · see citing works
PFAS exposure induces hearing loss by targeting cochlear hair cells and spiral ganglion neurons
Bhatia, P., Roth, K., Yang, Z., Petriello, M. C., & Jamesdaniel, S. (2026) · Scientific Reports · doi:10.1038/s41598-026-51693-7 · Cited by 3 · see citing works
Self-citationKlider, L. M., Marques, A. A. M., Moreno, K. G. T., da Silva, G. P., Mizuno, G. A., Farias, K. D. S., Monteiro, L. M., de Almeida, V. P., Monchak, I. T., Silva, D. B., et al. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2024.118629 · Cited by 3 · see citing works
Shahab, M., Rosati, R., Bhatia, P., Doyon‐Reale, N., & Jamesdaniel, S. (2025) · Toxicology Reports · doi:10.1016/j.toxrep.2025.101967 · Cited by 2 · see citing works
Self-citationHuber, H. F., Li, C., Xie, D., Gerow, K., Register, T. C., Shively, C. A., Cox, L. A., & Nathanielsz, P. W. (2024) · GeroScience · doi:10.1007/s11357-024-01080-9 · Cited by 2 · see citing works
Audiometry and biochemical analysis in patients with tinnitus — preliminary findings
Osiński, S., Osiński, M., Kupczyk, D., Skubisz, Z., & Augustyńska, B. (2023) · Medical Research Journal · doi:10.5603/mrj.a2023.0005
Otoprotective effect of MnTBAP in cisplatin-induced hearing loss
Mehmood, S., Bhatia, P., & Jamesdaniel, S. (2026) · PLoS ONE · doi:10.1371/journal.pone.0351911
Self-citation
- Authors
- Shahab, M., & Jamesdaniel, S.
- Affiliations
- Wayne State University (US)
- Corresponding author
- Jamesdaniel, Samson
- Venue
- Pharmaceuticals
- Publisher
- MDPI AG
- Published
- 2022-05-24
- Volume
- 15
- Issue
- 6
- Pages
- 649
- ISSN
- 1424-8247 (ISSN-L)
- PMC
- PMC9227425
- OpenAlex
- W4281480116
- Cited by
- 11
- References
- 72
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 5 · 2023: 2
- FWCI
- 0.45
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Pharmaceuticals (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- NIH/NIEHS (P30 ES020957, K01 ES028750)
- Topics
- Life Sciences › Neuroscience › Sensory Systems › Hearing, Cochlea, Tinnitus, Genetics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- nitrative stress, auditory dysfunction, nitrotyrosine, peroxynitrite, nitric oxide, superoxide, ototoxicity, noise-induced hearing loss, ototoxic drugs, apoptosis, inducible nitric oxide synthase inhibitors, acquired hearing loss
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
