The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage
Nishikawa, T., Edelstein, D., Du, X. L., Yamagishi, S.-I., Matsumura, T., Kaneda, Y., Yorek, M. A., Beebe, D., Oates, P. J., Hammes, H.-P., et al. (2000) · Nature · doi:10.1038/35008121 · Cited by 4,277
Mice lacking mitochondrial uncoupling protein are cold-sensitive but not obese
Enerbäck, S., Jacobsson, A., Simpson, E. M., Guerra, C., Yamashita, H., Harper, M.-E., & Kozak, L. P. (1997) · Nature · doi:10.1038/387090a0 · Cited by 1,379
Energy metabolism in uncoupling protein 3 gene knockout mice
Vidal-Puig, A. J., Grujic, D., Zhang, C.-Y., Hagen, T., Boss, O., Ido, Y., Szczepanik, A., Wade, J., Mootha, V., Cortright, R., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910179199 · Cited by 677
Diehl, A. M., & Hoek, J. B. (1999) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1005452624640 · Cited by 95
Cited by
ROS function in redox signaling and oxidative stress
Schieber, M., & Chandel, N. S. (2014) · Current Biology · doi:10.1016/j.cub.2014.03.034 · Cited by 6,931
Brown Adipose Tissue: Function and Physiological Significance
CANNON, B., & NEDERGAARD, J. (2004) · Physiological Reviews · doi:10.1152/physrev.00015.2003 · Cited by 6,433
Mittler, R. (2017) · Trends in Plant Science · doi:10.1016/j.tplants.2016.08.002 · Cited by 3,499
Physiological Roles of Mitochondrial Reactive Oxygen Species
Sena, L. A., & Chandel, N. S. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.09.025 · Cited by 2,632
Obesity and the regulation of energy balance
Spiegelman, B. M., & Flier, J. S. (2001) · Cell · doi:10.1016/s0092-8674(01)00240-9 · Cited by 2,398
St-Pierre, J., Drori, S., Uldry, M., Silvaggi, J. M., Rhee, J., Jäger, S., Handschin, C., Zheng, K., Lin, J., Yang, W., et al. (2006) · Cell · doi:10.1016/j.cell.2006.09.024 · Cited by 2,233
Puigserver, P., & Spiegelman, B. M. (2003) · Endocrine Reviews · doi:10.1210/er.2002-0012 · Cited by 2,076
Tlr signalling augments macrophage bactericidal activity through mitochondrial ros
West, A. P., Brodsky, I. E., Rahner, C., Woo, D. K., Erdjument-Bromage, H., Tempst, P., Walsh, M. C., Choi, Y., Shadel, G. S., & Ghosh, S. (2011) · Nature · doi:10.1038/nature09973 · Cited by 1,659
Superoxide activates mitochondrial uncoupling proteins
Echtay, K. S., Roussel, D., St-Pierre, J., Jekabsons, M. B., Cadenas, S., Stuart, J. A., Harper, J. A., Roebuck, S. J., Morrison, A., Pickering, S., et al. (2002) · Nature · doi:10.1038/415096a · Cited by 1,382
Mitochondria in innate immune responses
West, A. P., Shadel, G. S., & Ghosh, S. (2011) · Nature Reviews Immunology · doi:10.1038/nri2975 · Cited by 1,376
Mitochondrial ROS Signaling in Organismal Homeostasis
Shadel, G. S., & Horvath, T. L. (2015) · Cell · doi:10.1016/j.cell.2015.10.001 · Cited by 1,353
Role of Mitochondrial Dysfunction in Insulin Resistance
Kim, J.-A., Wei, Y., & Sowers, J. R. (2008) · Circulation Research · doi:10.1161/circresaha.107.165472 · Cited by 1,103
Mitochondrial superoxide: production, biological effects, and activation of uncoupling proteins
Brand, M. D., Affourtit, C., Esteves, T. C., Green, K., Lambert, A. J., Miwa, S., Pakay, J. L., & Parker, N. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.05.034 · Cited by 1,032
TNF and ROS crosstalk in inflammation
Blaser, H., Dostert, C., Mak, T. W., & Brenner, D. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.12.002 · Cited by 1,008
Zhang, C.-Y., Baffy, G., Perret, P., Krauss, S., Peroni, O., Grujic, D., Hagen, T., Vidal-Puig, A. J., Boss, O., Kim, Y.-B., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00378-6 · Cited by 917
Calorie restriction–the SIR2 connection
Guarente, L., & Picard, F. (2005) · Cell · doi:10.1016/j.cell.2005.01.029 · Cited by 793
Physiological functions of the mitochondrial uncoupling proteins UCP2 and UCP3
Brand, M. D., & Esteves, T. C. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.06.002 · Cited by 785
Kong, X., Wang, R., Xue, Y., Liu, X., Zhang, H., Chen, Y., Fang, F., & Chang, Y. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011707 · Cited by 718
Sirt1 Regulates Insulin Secretion by Repressing UCP2 in Pancreatic β Cells
Bordone, L., Motta, M. C., Picard, F., Robinson, A., Jhala, U. S., Apfeld, J., McDonagh, T., Lemieux, M., McBurney, M., Szilvasi, A., et al. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0040031 · Cited by 715
Thermogenic Mechanisms and Their Hormonal Regulation
Silva, J. E. (2006) · Physiological Reviews · doi:10.1152/physrev.00009.2005 · Cited by 687
Mitochondrial uncoupling, ROS generation and cardioprotection
Cadenas, S. (2018) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2018.05.019 · Cited by 591
Mattiasson, G., Shamloo, M., Gido, G., Mathi, K., Tomasevic, G., Yi, S., Warden, C. H., Castilho, R. F., Melcher, T., Gonzalez-Zulueta, M., et al. (2003) · Nature Medicine · doi:10.1038/nm903 · Cited by 515
Only UCP1 can mediate adaptive nonshivering thermogenesis in the cold
Golozoubova, V., Hohtola, E., Matthias, A., Jacobsson, A., Cannon, B., & Nedergaard, J. (2001) · The FASEB Journal · doi:10.1096/fj.00-0536fje · Cited by 503
UCP2 transports C4 metabolites out of mitochondria, regulating glucose and glutamine oxidation
Vozza, A., Parisi, G., De Leonardis, F., Lasorsa, F. M., Castegna, A., Amorese, D., Marmo, R., Calcagnile, V. M., Palmieri, L., Ricquier, D., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1317400111 · Cited by 407
Self-citationAbu-Elheiga, L., Oh, W., Kordari, P., & Wakil, S. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1733877100 · Cited by 389
Superoxide Activates Mitochondrial Uncoupling Protein 2 from the Matrix Side
Echtay, K. S., Murphy, M. P., Smith, R. A. J., Talbot, D. A., & Brand, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208262200 · Cited by 388
Mitochondria as a Cellular Hub in Infection and Inflammation
Andrieux, P., Chevillard, C., Cunha-Neto, E., & Nunes, J. P. S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111338 · Cited by 346
Uncoupling Protein-2 Overexpression Inhibits Mitochondrial Death Pathway in Cardiomyocytes
Teshima, Y., Akao, M., Jones, S. P., & Marbán, E. (2003) · Circulation Research · doi:10.1161/01.res.0000085581.60197.4d · Cited by 318
Superoxide-mediated activation of uncoupling protein 2 causes pancreatic β cell dysfunction
Krauss, S., Zhang, C.-Y., Scorrano, L., Dalgaard, L. T., St-Pierre, J., Grey, S. T., & Lowell, B. B. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200319774 · Cited by 401
Mitochondria, oxygen free radicals, and apoptosis
Raha, S., & Robinson, B. H. (2001) · American Journal of Medical Genetics · doi:10.1002/ajmg.1398 · Cited by 306
Mild mitochondrial uncoupling in mice affects energy metabolism, redox balance and longevity
Caldeira da Silva, C. C., Cerqueira, F. M., Barbosa, L. F., Medeiros, M. H. G., & Kowaltowski, A. J. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2008.00407.x · Cited by 306
Coppola, A., Liu, Z.-W., Andrews, Z. B., Paradis, E., Roy, M.-C., Friedman, J. M., Ricquier, D., Richard, D., Horvath, T. L., Gao, X.-B., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2006.12.002 · Cited by 295
Self-citationAMPK, Mitochondrial Function, and Cardiovascular Disease
Wu, S., & Zou, M.-H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21144987 · Cited by 286
Geng, J., Sun, X., Wang, P., Zhang, S., Wang, X., Wu, H., Hong, L., Xie, C., Li, X., Zhao, H., et al. (2015) · Nature Immunology · doi:10.1038/ni.3268 · Cited by 264
Microglial UCP2 mediates inflammation and obesity induced by high-fat feeding
Kim, J. D., Yoon, N. A., Jin, S., & Diano, S. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.08.010 · Cited by 240
UCP2-induced fatty acid synthase promotes NLRP3 inflammasome activation during sepsis
Moon, J.-S., Lee, S., Park, M.-A., Siempos, I. I., Haslip, M., Lee, P. J., Yun, M., Kim, C. K., Howrylak, J., Ryter, S. W., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci78253 · Cited by 238
RetractedUncoupling Protein 2 Knockout Mice Have Enhanced Insulin Secretory Capacity After a High-Fat Diet
Joseph, J. W., Koshkin, V., Zhang, C.-Y., Wang, J., Lowell, B. B., Chan, C. B., & Wheeler, M. B. (2002) · Diabetes · doi:10.2337/diabetes.51.11.3211 · Cited by 220
MacLellan, J. D., Gerrits, M. F., Gowing, A., Smith, P. J. S., Wheeler, M. B., & Harper, M.-E. (2005) · Diabetes · doi:10.2337/diabetes.54.8.2343 · Cited by 213
Pecqueur, C., Bui, T., Gelly, C., Hauchard, J., Barbot, C., Bouillaud, F., Ricquier, D., Miroux, B., & Thompson, C. B. (2008) · The FASEB Journal · doi:10.1096/fj.07-8945com · Cited by 209
Self-citationUCP1 deficiency increases susceptibility to diet‐induced obesity with age
Kontani, Y., Wang, Y., Kimura, K., Inokuma, K. ‐., Saito, M., Suzuki‐Miura, T., Wang, Z., Sato, Y., Mori, N., & Yamashita, H. (2005) · Aging Cell · doi:10.1111/j.1474-9726.2005.00157.x · Cited by 207
Free Fatty Acid-induced β-Cell Defects Are Dependent on Uncoupling Protein 2 Expression
Joseph, J. W., Koshkin, V., Saleh, M. C., Sivitz, W. I., Zhang, C.-Y., Lowell, B. B., Chan, C. B., & Wheeler, M. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409189200 · Cited by 206
Bordt, E. A., & Polster, B. M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.07.033 · Cited by 202
Andrews, Z. B., Horvath, B., Barnstable, C. J., Elseworth, J., Yang, L., Beal, M. F., Roth, R. H., Matthews, R. T., & Horvath, T. L. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4269-04.2005 · Cited by 199
BRAND, M. D., PAMPLONA, R., PORTERO-OTÍN, M., REQUENA, J. R., ROEBUCK, S. J., BUCKINGHAM, J. A., CLAPHAM, J. C., & CADENAS, S. (2002) · Biochemical Journal · doi:10.1042/bj20021077 · Cited by 184
The thermogenic effect of thyroid hormone and its clinical implications
Silva, J. E. (2003) · Annals of Internal Medicine · doi:10.7326/0003-4819-139-3-200308050-00010 · Cited by 173
Vitamin A and the regulation of fat reserves
Bonet, M. L., Ribot, J., Felipe, F., & Palou, A. (2003) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s00018-003-2290-x · Cited by 174
Mitochondrial uncoupling and lifespan
Mookerjee, S. A., Divakaruni, A. S., Jastroch, M., & Brand, M. D. (2010) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2010.03.010 · Cited by 169
Mitochondrial Proton Leak Plays a Critical Role in Pathogenesis of Cardiovascular Diseases
Cheng, J., Nanayakkara, G., Shao, Y., Cueto, R., Wang, L., Yang, W. Y., Tian, Y., Wang, H., & Yang, X. (2017) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-319-55330-6_20 · Cited by 168
Pi, J., Bai, Y., Daniel, K. W., Liu, D., Lyght, O., Edelstein, D., Brownlee, M., Corkey, B. E., & Collins, S. (2009) · Endocrinology · doi:10.1210/en.2008-1642 · Cited by 163
Self-citationCouplan, E., del Mar Gonzalez-Barroso, M., Alves-Guerra, M. C., Ricquier, D., Goubern, M., & Bouillaud, F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202535200 · Cited by 161
Self-citationCui, Y., Xu, X., Bi, H., Zhu, Q., Wu, J., Xia, X., Ren, Q., & Ho, P. C. P. (2006) · Experimental Eye Research · doi:10.1016/j.exer.2006.03.024 · Cited by 159
Bouillaud, F. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.01.003 · Cited by 146
Self-citationThe regulation and turnover of mitochondrial uncoupling proteins
Azzu, V., Jastroch, M., Divakaruni, A. S., & Brand, M. D. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.02.035 · Cited by 146
Masuda, Y., Haramizu, S., Oki, K., Ohnuki, K., Watanabe, T., Yazawa, S., Kawada, T., Hashizume, S.-I., & Fushiki, T. (2003) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00828.2002 · Cited by 143
Robson-Doucette, C. A., Sultan, S., Allister, E. M., Wikstrom, J. D., Koshkin, V., Bhattacharjee, A., Prentice, K. J., Sereda, S. B., Shirihai, O. S., & Wheeler, M. B. (2011) · Diabetes · doi:10.2337/db11-0132 · Cited by 136
Talbot, D. A., Lambert, A. J., & Brand, M. D. (2004) · FEBS Letters · doi:10.1016/s0014-5793(03)01386-3 · Cited by 131
Harper, M.-E., Dent, R., Monemdjou, S., Bézaire, V., Van Wyck, L., Wells, G., Kavaslar, G. N., Gauthier, A., Tesson, F., & McPherson, R. (2002) · Diabetes · doi:10.2337/diabetes.51.8.2459 · Cited by 129
The efficiency of cellular energy transduction and its implications for obesity
Harper, M.-E., Green, K., & Brand, M. D. (2008) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.28.061807.155357 · Cited by 121
Timing of nutrient restriction and programming of fetal adipose tissue development
Symonds, M. E., Pearce, S., Bispham, J., Gardner, D. S., & Stephenson, T. (2004) · Proceedings of the Nutrition Society · doi:10.1079/pns2004366 · Cited by 121
The uncoupling protein 2 modulates the cytokine balance in innate immunity☆
ROUSSET, S., EMRE, Y., JOINLAMBERT, O., HURTAUD, C., RICQUIER, D., & CASSARDDOULCIER, A. (2006) · Cytokine · doi:10.1016/j.cyto.2006.07.012 · Cited by 114
Self-citationDe Bilbao, F., Arsenijevic, D., Vallet, P., Hjelle, O. P., Ottersen, O. P., Bouras, C., Raffin, Y., Abou, K., Langhans, W., Collins, S., et al. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02432.x · Cited by 108
“Consistent with the recent marked progress in this field, our data support the role of UCP2 in oxidative pathophys- iology (Arsenijevic et al. 2000; Blanc et al. 2003) and further contribute to the understanding of the physiological function of UCP2.”
BackgroundMethodResultInfluentialSelf-citationPhysiological Levels of Mammalian Uncoupling Protein 2 Do Not Uncouple Yeast Mitochondria
Stuart, J. A., Harper, J. A., Brindle, K. M., Jekabsons, M. B., & Brand, M. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011566200 · Cited by 99
Metformin induces oxidative stress in white adipocytes and raises uncoupling protein 2 levels
Anedda, A., Rial, E., & González-Barroso, M. M. (2008) · Journal of Endocrinology · doi:10.1677/joe-08-0278 · Cited by 98
Lee, C.-H., Kang, K., Mehl, I. R., Nofsinger, R., Alaynick, W. A., Chong, L.-W., Rosenfeld, J. M., & Evans, R. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510815103 · Cited by 98
Morris, G., Anderson, G., Berk, M., & Maes, M. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8477-8 · Cited by 96
Reactive oxygen species and uncoupling protein 2 in pancreatic β ‐cell function
Pi, J., & Collins, S. (2010) · Diabetes, Obesity and Metabolism · doi:10.1111/j.1463-1326.2010.01269.x · Cited by 91
Self-citationMitochondrial recoupling: a novel therapeutic strategy for cancer
Baffy, G., Derdak, Z., & Robson, S. C. (2011) · British Journal of Cancer · doi:10.1038/bjc.2011.245 · Cited by 88
“To complete the process, adenine nucleotide translocase (ANT) exchanges ADP for ATP across the mitochondrial inner membrane (Nicholls and Ferguson, 1992).”
BackgroundInfluentialPotassium channel openers are uncoupling protonophores: implication in cardioprotection
Holmuhamedov, E. L., Jahangir, A., Oberlin, A., Komarov, A., Colombini, M., & Terzic, A. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.05.031 · Cited by 90
Brandalise, M., Maia, I. G., Borecký, J., Vercesi, A. E., & Arruda, P. (2003) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1024603530043 · Cited by 76
Uncoupling Proteins: Role in Insulin Resistance and Insulin Insufficiency
B.Chan, C., & Harper, M.-E. (2006) · Current Diabetes Reviews · doi:10.2174/157339906777950660 · Cited by 71
Tang, S.-E., Wu, C.-P., Wu, S.-Y., Peng, C.-K., Perng, W.-C., Kang, B.-H., Chu, S.-J., & Huang, K.-L. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.034 · Cited by 70
Mitochondrial ros potentiates indirect activation of the aim2 inflammasome
Crane, D. D., Bauler, T. J., Wehrly, T. D., & Bosio, C. M. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00438 · Cited by 63
Stable transfection of UCP1 confers resistance to hypoxia/reoxygenation in a heart-derived cell line
Bienengraeber, M. (2003) · Journal of Molecular and Cellular Cardiology · doi:10.1016/s0022-2828(03)00147-0 · Cited by 62
Respiratory uncoupling by UCP1 and UCP2 and superoxide generation in endothelial cell mitochondria
Fink, B. D., Reszka, K. J., Herlein, J. A., Mathahs, M. M., & Sivitz, W. I. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00332.2004 · Cited by 53
Mozo, J., Ferry, G., Studeny, A., Pecqueur, C., Rodriguez, M., Boutin, J. A., & Bouillaud, F. (2006) · Biochemical Journal · doi:10.1042/bj20050494 · Cited by 52
Self-citationYu, X., Wester-Rosenlöf, L., Gimsa, U., Holzhueter, S.-A., Marques, A., Jonas, L., Hagenow, K., Kunz, M., Nizze, H., Tiedge, M., et al. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp432 · Cited by 47
Plataki, M., Cho, S. J., Harris, R. M., Huang, H.-R., Yun, H. S., Schiffer, K. T., & Stout-Delgado, H. W. (2019) · Scientific Reports · doi:10.1038/s41598-018-37438-1 · Cited by 42
Xu, M.-J., Song, P., Shirwany, N., Liang, B., Xing, J., Viollet, B., Wang, X., Zhu, Y., & Zou, M.-H. (2011) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.111.227991 · Cited by 39
The emerging neuroprotective role of mitochondrial uncoupling protein-2 in traumatic brain injury
Normoyle, K. P., Kim, M., Farahvar, A., Llano, D., Jackson, K., & Wang, H. (2015) · Translational Neuroscience · doi:10.1515/tnsci-2015-0019 · Cited by 36
Orhan, N., Kucukali, C. I., Cakir, U., Seker, N., & Aydin, M. (2012) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2011.09.012 · Cited by 36
Uncoupling protein 2 in the glial response to stress: Implications for neuroprotection
Barnstable, C., & Hass, D. (2016) · Neural Regeneration Research · doi:10.4103/1673-5374.189159 · Cited by 33
Díaz-Maroto Cicuéndez, I., Fernández-Díaz, E., García-García, J., Jordán, J., Fernández-Cadenas, I., Montaner, J., Serrano-Heras, G., & Segura, T. (2017) · NeuroMolecular Medicine · doi:10.1007/s12017-017-8470-x · Cited by 12
Metadata
- Authors
- Arsenijevic, D., Onuma, H., Pecqueur, C., Raimbault, S., Manning, B. S., Miroux, B., Couplan, E., Alves-Guerra, M.-C., Goubern, M., Surwit, R., Bouillaud, F., Richard, D., Collins, S., & Ricquier, D.
- Venue
- Nature Genetics
- Published
- 2000-12
- Volume
- 26
- Issue
- 4
- Pages
- 435-439
- ISSN
- 1061-4036 (ISSN-L)
- 1546-1718
- OpenAlex
- W1594539479
- Cited by
- 1,079
- References
- 4
- FWCI
- 45.92
- Type
- journal article
- Language
- en
- Open access
- closed
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
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.