The DOI matches its Crossref record; 75 of the 75 references it cites were found in a registry or an index.
Oxidatively modified proteins in aging and disease1, 2 1Guest Editor: Earl Stadtman 2This article is part of a series of reviews on “Oxidatively Modified Proteins in Aging and Disease” The full list of papers may be found on the homepage of the journal
Abstract
There is a large body of evidence implicating oxidative damage in the pathogenesis of both normal aging and neurodegenerative diseases. Oxidative damage to proteins has been well established. Although there are a large number of potential oxidative modifications only a few have been systematically studied. The most frequently studied marker of oxidative damage to proteins is protein carbonyl groups. 3-Nitrotyrosine is thought to be a relatively specific marker of oxidative damage mediated by peroxynitrite. Increased concentrations of both protein carbonyls and 3-nitrotyrosine have been documented in both normal aging as well as in Alzheimer's disease (AD), Parkinson's disease (PD), and amyotrophic lateral sclerosis (ALS). These findings help to provide a rationale for trials of antioxidants in neurodegenerative diseases.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Much evidence suggests that oxidative damage to proteins is associated with aging and is linked to protein misfolding [216,217].”
From Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease (2022) · cites this paper as [216]
Citations
Cites
A Controlled Trial of Selegiline, Alpha-Tocopherol, or Both as Treatment for Alzheimer's Disease
Sano, M., Ernesto, C., Thomas, R. G., Klauber, M. R., Schafer, K., Grundman, M., Woodbury, P., Growdon, J., Cotman, C. W., Pfeiffer, E., et al. (1997) · New England Journal of Medicine · doi:10.1056/nejm199704243361704 · Cited by 2,380
Giasson, B. I., Duda, J. E., Murray, I. V. J., Chen, Q., Souza, J. M., Hurtig, H. I., Ischiropoulos, H., Trojanowski, J. Q., & Lee, V. M. ‐. (2000) · Science · doi:10.1126/science.290.5493.985 · Cited by 1,567
Age-related changes in oxidized proteins.
Oliver, C. N., Ahn, B. W., Moerman, E. J., Goldstein, S., & Stadtman, E. R. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45598-6 · Cited by 1,306
Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease.
Smith, C. D., Carney, J. M., Starke-Reed, P. E., Oliver, C. N., Stadtman, E. R., Floyd, R. A., & Markesbery, W. R. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.23.10540 · Cited by 1,296
Widespread Peroxynitrite-Mediated Damage in Alzheimer’s Disease
Smith, M. A., Richey Harris, P. L., Sayre, L. M., Beckman, J. S., & Perry, G. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-08-02653.1997 · Cited by 1,239
Liberatore, G. T., Jackson-Lewis, V., Vukosavic, S., Mandir, A. S., Vila, M., McAuliffe, W. G., Dawson, V. L., Dawson, T. M., & Przedborski, S. (1999) · Nature Medicine · doi:10.1038/70978 · Cited by 1,046
Oxidative damage in Alzheimer's
Smith, M. A., Perry, G. L., Richey, P. L., Sayrec, L. M., Anderson, V. E., Beal, M. F., & Kowall, N. W. (1996) · Nature · doi:10.1038/382120b0 · Cited by 897
Self-citationBrowne, S. E., Bowling, A. C., Macgarvey, U., Baik, M. J., Berger, S. C., Muquit, M. M. K., Bird, E. D., & Beal, M. F. (1997) · Annals of Neurology · doi:10.1002/ana.410410514 · Cited by 885
Self-citationEvidence of Increased Oxidative Damage in Both Sporadic and Familial Amyotrophic Lateral Sclerosis
Ferrante, R. J., Browne, S. E., Shinobu, L. A., Bowling, A. C., Baik, M. J., MacGarvey, U. M., Kowall, N. W., Brown, R. H., & Beal, M. F. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69052064.x · Cited by 808
Self-citationSohal, R. S., Ku, H.-H., Agarwal, S., Forster, M. J., & Lal, H. (1994) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(94)90104-x · Cited by 788
Hensley, K., Hall, N., Subramaniam, R., Cole, P., Harris, M., Aksenov, M., Aksenova, M., Gabbita, S. P., Wu, J. F., Carney, J. M., et al. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.65052146.x · Cited by 779
Oliver, C., Starke-Reed, P. E., Stadtman, E. R., Liu, G. J., Carney, J. M., & Floyd, R. A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.13.5144 · Cited by 771
α-Synuclein Promotes Mitochondrial Deficit and Oxidative Stress
Hsu, L. J., Sagara, Y., Arroyo, A., Rockenstein, E. M., Sisk, A., Mallory, M. E., Wong, J., Takenouchi, T., Hashimoto, M., & Masliah, E. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64553-1 · Cited by 737
Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals
Moskovitz, J., Barnoy, S., Williams, W. M., Requena, J. R., Berlett, B. S., & Stadtman, E. R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.231472998 · Cited by 685
Przedborski, S., Jackson-Lewis, V. R., Yokoyama, R., Shibata, T., Dawson, V. L., & Dawson, T. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.10.4565 · Cited by 624
Oxidative damage during aging targets mitochondrial aconitase
Yan, L., Levine, R. L., & Sohal, R. S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.21.11168 · Cited by 620
Evidence of neuronal oxidative damage in Alzheimer's disease.
Good, P. F., Werner, P., Hsu, A., Olanow, C. W., & Perl, D. P. (1996) · Europe PMC (PubMed Central) · Cited by 600
Increased 3‐nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis
Beal, M. F., Ferrante, R. J., Browne, S. E., Matthews, R. T., Kowall, N. W., & Brown, R. H. (1997) · Annals of Neurology · doi:10.1002/ana.410420416 · Cited by 599
Self-citationDityrosine Cross-linking Promotes Formation of Stable α-Synuclein Polymers
Souza, J. M., Giasson, B. I., Chen, Q., Lee, V. M. ‐., & Ischiropoulos, H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000206200 · Cited by 572
Alam, Z. I., Daniel, S. E., Lees, A. J., Marsden, D. C., Jenner, P. G., & Halliwell, B. B. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69031326.x · Cited by 547
Protein Nitration in Parkinsonʼs Disease
Good, P. F., Hsu, A., Werner, P., Perl, D. P., & Olanow, C. W. (1998) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199804000-00006 · Cited by 540
Hensley, K., Maidt, M. L., Yu, Z., Sang, H., Markesbery, W. R., & Floyd, R. A. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-20-08126.1998 · Cited by 508
Lauderback, C. M., Hackett, J. M., Huang, F. F., Keller, J. N., Szweda, L. I., Markesbery, W. R., & Butterfield, D. A. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00451.x · Cited by 464
Age-dependent increases in oxidative damage to DNA, lipids, and proteins in human skeletal muscle
Mecocci, P., Fanò, G., Fulle, S., MacGarvey, U. M., Shinobu, L. A., Polidori, M. C., Cherubini, A., Vecchiet, J., Senin, U., & Beal, M. F. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00208-1 · Cited by 464
Self-citationInduction of α-Synuclein Aggregation by Intracellular Nitrative Insult
Paxinou, E., Chen, Q., Weisse, M., Giasson, B. I., Norris, E. H., Rueter, S. M., Trojanowski, J. Q., Lee, V. M. ‐., & Ischiropoulos, H. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-20-08053.2001 · Cited by 440
Inhibition of neuronal nitric oxide synthase prevents MPTP–induced parkinsonism in baboons
Hantraye, P., Brouillet, E., Ferrante, R. J., Palfi, S., Dolan, R., Matthews, R. T., & Beal, M. F. (1996) · Nature Medicine · doi:10.1038/nm0996-1017 · Cited by 422
Self-citationSchulz, J. B., Matthews, R. T., Muqit, M. M. K., Browne, S. E., & Beal, M. F. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.64020936.x · Cited by 417
Self-citationMitochondrial adenine nucleotide translocase is modified oxidatively during aging
Yan, L.-J., & Sohal, R. S. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.22.12896 · Cited by 414
Calingasan, N. Y., Uchida, K., & Gibson, G. E. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0720751.x · Cited by 400
Protein oxidation and proteolysis during aging and oxidative stress
Starke-Reed, P. E., & Oliver, C. N. (1989) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(89)90402-5 · Cited by 398
Pedersen, W. A., Fu, W., Keller, J. N., Markesbery, W. R., Appel, S. H., Smith, R. G., Kasarskis, E. J., & Mattson, M. P. (1998) · Annals of Neurology · doi:10.1002/ana.410440518 · Cited by 391
Protein oxidative damage is associated with life expectancy of houseflies.
Sohal, R. S., Agarwal, S., Dubey, A., & Orr, W. C. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.15.7255 · Cited by 354
Mitochondrial dysfunction and free radical damage in the Huntington R6/2 transgenic mouse
Tabrizi, S. J., Workman, J. M., Hart, P. E., Mangiarini, L., Mahal, A., Bates, G. P., Cooper, J. A. D., & Schapira, A. H. V. (2000) · Annals of Neurology · doi:10.1002/1531-8249(200001)47:1 · Cited by 353
Proteomic method identifies proteins nitrated in vivo during inflammatory challenge
Aulak, K. S., Miyagi, M., Yan, L., West, K. A., Massillon, D., Crabb, J. W., & Stuehr, D. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.221269198 · Cited by 350
Kong, S. K., Yim, M. B., Stadtman, E. R., & Chock, P. B. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.8.3377 · Cited by 337
Oxidative damage to protein in sporadic motor neuron disease spinal cord
Shaw, P. J., Ince, P. G., Falkous, G., & Mantle, D. (1995) · Annals of Neurology · doi:10.1002/ana.410380424 · Cited by 331
Glycoxidation and oxidative stress in Parkinson disease and diffuse Lewy body disease
Castellani, R. J., Smith, M. A., Richey, G. L., & Perry, G. L. (1996) · Brain Research · doi:10.1016/0006-8993(96)00729-9 · Cited by 315
Neural Heme Oxygenase-1 Expression in Idiopathic Parkinson's Disease
Schipper, H. M., Liberman, A., & Stopa, E. G. (1998) · Experimental Neurology · doi:10.1006/exnr.1997.6752 · Cited by 299
Neural roles for heme oxygenase: Contrasts to nitric oxide synthase
Barañano, D. E., & Snyder, S. H. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.191351298 · Cited by 293
Inducible nitric oxide synthase in tangle-bearing neurons of patients with Alzheimer's disease.
Yoram Vodovotz, B., Lucia, M. S., Flanders, K. C., Chesler, L., Xie, Q. W., Smith, T. W., Weidner, J. R., Mumford, R. A., Webber, R., Nathan, C., et al. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.184.4.1425 · Cited by 292
Acceleration of Peroxynitrite Oxidations by Carbon Dioxide
Uppu, R. M., Squadrito, G. L., & Pryor, W. A. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0131 · Cited by 278
Synphilin-1 is present in Lewy bodies in Parkinson's disease
Wakabayashi, K., Engelender, S., Yoshimoto, M., Tsuji, S., Ross, C. A., & Takahashi, H. (2000) · Annals of Neurology · doi:10.1002/1531-8249(200004)47:4 · Cited by 269
Abe, K., Pan, L.-H., Watanabe, M., Kato, T., & Itoyama, Y. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)12039-7 · Cited by 263
Increased oxidative damage to DNA in a transgenic mouse model of Huntington's disease
Bogdanov, M., Andreassen, O. A., Dedeoglu, A., Ferrante, R. J., & Beal, M. F. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00689.x · Cited by 248
Self-citationSmith, M. A., Rudnicka-Nawrot, M., Richey, P., Praprotnik, D., Mulvihill, P., Miller, C., Sayre, L., & Perry, G. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.64062660.x · Cited by 240
MacMillan-Crow, L. A., & Thompson, J. A. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1202 · Cited by 227
Smith, M. A., Sayre, L. M., Anderson, V. E., Harris, P. L. R., Beal, M. F., Kowall, N. W., & Perry, G. L. (1998) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215549804600605 · Cited by 222
Self-citationPansarasa, O., Bertorelli, L., Vecchiet, J., Felzani, G., & Marzatico, F. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00108-2 · Cited by 212
Stachowiak, O., Dolder, M., Wallimann, T., & Richter, C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.27.16694 · Cited by 189
Su, J. H., Deng, G., & Cotman, C. W. (1997) · Brain Research · doi:10.1016/s0006-8993(97)81703-9 · Cited by 175
Tohgi, H., Abe, T., Yamazaki, K., Murata, T., Ishizaki, E., & Isobe, C. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00406-1 · Cited by 173
Oxidative stress and aging in the Mongolian gerbil (Meriones unguiculatus)
Sohal, R. S., Agarwal, S., & Sohal, B. H. (1995) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(94)01578-a · Cited by 171
Abe, K., Pan, L.-H., Watanabe, M., Konno, H., Kato, T., & Itoyama, Y. (1997) · Neurological Research · doi:10.1080/01616412.1997.11740784 · Cited by 167
Chou, S. M., Wang, H. S., & Komai, K. (1996) · Journal of Chemical Neuroanatomy · doi:10.1016/0891-0618(96)00137-8 · Cited by 153
Histochemical detection of 4-hydroxynonenal protein in Alzheimer amyloid
Ando, Y., Brännström, T., Uchida, K., Nyhlin, N., Näsman, B., Suhr, O. B., Yamashita, T., Olsson, T., Salhy, M. E., Uchino, M., et al. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00042-2 · Cited by 152
Berlett, B. S., Levine, R. L., & Stadtman, E. R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.2784 · Cited by 151
Nitric Oxide Synthase in Reactive Astrocytes Adjacent to β-Amyloid Plaques
Wallace, M. N., Geddes, J. G., Farquhar, D. A., & Masson, M. R. (1997) · Experimental Neurology · doi:10.1006/exnr.1996.6373 · Cited by 145
Superoxide Dismutase Concentration and Activity in Familial Amyotrophic Lateral Sclerosis
Bowling, A. C., Barkowski, E. E., McKenna‐Yasek, D., Sapp, P. C., Horvitz, H. R., Beal, M. F., & Brown, R. H. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.64052366.x · Cited by 129
Self-citationLyras, L., Perry, R. H., Perry, E. K., Ince, P. G., Jenner, A. M., Jenner, P. G., & Halliwell, B. B. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.71010302.x · Cited by 121
Yan, L., & Sohal, R. S. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00423-8 · Cited by 115
Modification of hepatic proteins in rats exposed to high oxygen concentration
Starke-Reed, P. E., Oliver, C. N., & Stadtman, E. R. (1987) · The FASEB Journal · doi:10.1096/fasebj.1.1.2886388 · Cited by 109
Catania, M. V., Aronica, E., Yankaya, B., & Troost, D. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-11-j0002.2001 · Cited by 91
Lyras, L., Evans, P., Shaw, P. J., Ince, P. G., & Halliwell, B. B. (1996) · Free Radical Research · doi:10.3109/10715769609088038 · Cited by 76
Reduced creatine kinase activity in transgenic amyotrophic lateral sclerosis mice
Wendt, S., Dedeoglu, A., Speer, O., Wallimann, T., Beal, M. F., & Andreassen, O. A. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00784-0 · Cited by 65
Self-citationZou, M., Daiber, A., Peterson, J. A., Shoun, H., & Ullrich, V. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1699 · Cited by 60
Detection of Nitrosyl Complexes in Human Substantia Nigra, in Relation to Parkinson's Disease
Shergill, J. K., Cammack, R., Cooper, C. E., Cooper, J. A. D., Mann, V. M., & Schapira, A. H. V. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1656 · Cited by 59
Altered Glycosylation Pattern of Proteins in Alzheimer Disease
Guevara, J., Espinosa, B., Zenteno, E., Vázquez, L., Luna, J., Perry, G. L., & Mena, R. (1998) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199810000-00003 · Cited by 53
Dimethylargininase, a nitric oxide regulatory protein, in Alzheimer disease
Smith, M. A., Vašák, M., Knipp, M., Castellani, R. J., & Perry, G. L. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00119-1 · Cited by 52
No Evidence for Increased Oxidative Damage to Lipids, Proteins, or DNA in Huntington's Disease
Alam, Z. I., Halliwell, B. B., & Jenner, P. G. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750840.x · Cited by 50
Anneser, J. M. H., Cookson, M., Ince, P. G., Shaw, P. J., & Borasio, G. D. (2001) · Experimental Neurology · doi:10.1006/exnr.2001.7756 · Cited by 47
Exploitation of the HIV‐1 coat glycoprotein, gp120, in neurodegenerative studies in vivo
Corasaniti, M. T., Maccarrone, M., Nisticò, R., Malorni, W., Rotiroti, D., & Bagetta, G. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00537.x · Cited by 39
Neuronal nitric oxide synthase immunoreactivity in the spinal cord in amyotrophic lateral sclerosis
Sasaki, S., Shibata, N., & Iwata, M. (2001) · Acta Neuropathologica · doi:10.1007/s004010000282 · Cited by 37
Aging effects of vitamin C on a human lens protein produced in vitro
Russell, P., Garland, D. L., Zigler, J. S., Meakin, S. O., Tsui, L., & Breitman, M. L. (1987) · The FASEB Journal · doi:10.1096/fasebj.1.1.3301496 · Cited by 29
Role for peroxisome proliferator-activated receptor-gamma in Alzheimer's disease.
van Geel (2001) · Open Repository and Bibliography (University of Luxembourg) · doi:10.1002/1531-8249(20010201)49:2 · Cited by 7
Waldvogel (1999) · doi:10.1002/1531-8249(199907)46:1
Cited by
Sorted by citations
The role of antioxidants in the chemistry of oxidative stress: A review
Pisoschi, A. M., & Pop, A. (2015) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2015.04.040 · Cited by 2,963
Protein carbonyl groups as biomarkers of oxidative stress
Dalle‐Donne, I., Rossi, R., Giustarini, D., Milzani, A., & Colombo, R. (2003) · Clinica Chimica Acta · doi:10.1016/s0009-8981(03)00003-2 · Cited by 2,352
Physiological Implications of Hydrogen Sulfide: A Whiff Exploration That Blossomed
Wang, R. (2012) · Physiological Reviews · doi:10.1152/physrev.00017.2011 · Cited by 1,962
Oxidative DNA damage and disease: induction, repair and significance
Evans, M. D., Dizdaroglu, M., & Cooke, M. S. (2004) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2003.11.001 · Cited by 1,372
Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease
Ngo, V., & Duennwald, M. L. (2022) · Antioxidants · doi:10.3390/antiox11122345 · Cited by 1,130
Metadata
- Authors
- Beal, M. F.
- Affiliations
- NewYork–Presbyterian Hospital (US)
- Corresponding author
- Beal, M.Flint
- ORCID
- Beal, M.Flint
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2002-05
- Volume
- 32
- Issue
- 9
- Pages
- 797-803
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W1522890520
- Cited by
- 763
- References
- 75
- Citations by year
- 2026: 3 · 2025: 10 · 2024: 17 · 2023: 15 · 2022: 18 · 2021: 29 · 2020: 24 · 2019: 28 · 2018: 25 · 2017: 23 · 2016: 28 · 2015: 23 · 2014: 43 · 2013: 44 · 2012: 45
- FWCI
- 2.51
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Keywords
- oxidized proteins, oxidative damage, aging, neurodegenerative diseases, protein carbonyls, nitrotyrosine, peroxynitrite, Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, antioxidants
- MeSH terms
- Aging, Humans, Nerve Tissue Proteins, Oxidation-Reduction, Reactive Oxygen Species, Oxidative Stress, Neurodegenerative Diseases, Peroxynitrous Acid
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