The DOI matches its Crossref record; 64 of the 64 references it cites were found in a registry or an index.
Oxygen Consumption and Usage During Physical Exercise: The Balance Between Oxidative Stress and ROS-Dependent Adaptive Signaling
Open accessAbstract
The complexity of human DNA has been affected by aerobic metabolism, including endurance exercise and oxygen toxicity. Aerobic endurance exercise could play an important role in the evolution of Homo sapiens, and oxygen was not important just for survival, but it was crucial to redox-mediated adaptation. The metabolic challenge during physical exercise results in an elevated generation of reactive oxygen species (ROS) that are important modulators of muscle contraction, antioxidant protection, and oxidative damage repair, which at moderate levels generate physiological responses. Several factors of mitochondrial biogenesis, such as peroxisome proliferator-activated receptor-γ coactivator 1α (PGC-1α), mitogen-activated protein kinase, and SIRT1, are modulated by exercise-associated changes in the redox milieu. PGC-1α activation could result in decreased oxidative challenge, either by upregulation of antioxidant enzymes and/or by an increased number of mitochondria that allows lower levels of respiratory activity for the same degree of ATP generation. Endogenous thiol antioxidants glutathione and thioredoxin are modulated with high oxygen consumption and ROS generation during physical exercise, controlling cellular function through redox-sensitive signaling and protein–protein interactions. Endurance exercise-related angiogenesis, up to a significant degree, is regulated by ROS-mediated activation of hypoxia-inducible factor 1α. Moreover, the exercise-associated ROS production could be important to DNA methylation and post-translation modifications of histone residues, which create heritable adaptive conditions based on epigenetic features of chromosomes. Accumulating data indicate that exercise with moderate intensity has systemic and complex health-promoting effects, which undoubtedly involve regulation of redox homeostasis and signaling. Antioxid. Redox Signal. 18, 1208–1246. I. Introduction II. General Adaptations to Exercise III. Exercise, ROS, Antioxidant, and Housekeeping Systems A. ROS and antioxidants B. Thiols and redox signaling in exercise C. Oxidative damage and housekeeping IV. ROS, Metabolism, and Exercise A. Sirtuins as redox-sensitive energy sensors of exercise B. Redox signaling and biogenesis of mitochondria V. Exercise-Induced Inflammation and ROS VI. The Crucial Role of Redox Regulation on New Cell Formation in Skeletal Muscle and Brain VII. Exercise, ROS and Oxygen Sensing, HIF, and Vascular Endothelial Growth Factor A. Hypoxia in skeletal muscle B. HIF-1α-independent regulation of VEGF and angiogenesis C. p38γ MAPK/PGC-1α signaling regulation by physical exercise and its significance for mitochondrial biogenesis and angiogenesis in skeletal muscle D. Two-faced ROS in HIF activation E. Effect of exercise on HIF and VEGF signaling VIII. Exercise, ROS, and Epigenetics IX. Conclusion
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
Jaakkola, P., Mole, D. R., Tian, Y.-M., Wilson, M. I., Gielbert, J., Gaskell, S. J., Kriegsheim, A. V., Hebestreit, H. F., Mukherji, M., Schofield, C. J., et al. (2001) · Science · doi:10.1126/science.1059796 · Cited by 5,535
Exercise capacity and mortality among men referred for exercise testing
Myers, J., Prakash, M., Froelicher, V., Do, D., Partington, S., & Atwood, J. E. (2002) · New England Journal of Medicine · doi:10.1056/nejmoa011858 · Cited by 4,114
Running increases cell proliferation and neurogenesis in the adult mouse dentate gyrus
van Praag, H., Kempermann, G., & Gage, F. H. (1999) · Nature Neuroscience · doi:10.1038/6368 · Cited by 3,880
Neuronal replacement from endogenous precursors in the adult brain after stroke
Arvidsson, A., Collin, T., Kirik, D., Kokaia, Z., & Lindvall, O. (2002) · Nature Medicine · doi:10.1038/nm747 · Cited by 2,799
The nitrate-nitrite-nitric oxide pathway in physiology and therapeutics
Lundberg, J. O., Weitzberg, E., & Gladwin, M. T. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2466 · Cited by 2,739 · cited 1×
“However, alternative pathways can also be present to generate bioactive NO from nitrate and nitrite (10) and are involved in a wide range of processes, such as cellular signaling, regulation of blood flow, cellular metabolism, and hypoxic response (218).”
Transcriptional co-activator PGC-1α drives the formation of slow-twitch muscle fibres
Lin, J., Wu, H., Tarr, P. T., Zhang, C.-Y., Wu, Z., Boss, O., Michael, L. F., Puigserver, P., Isotani, E., Olson, E. N., et al. (2002) · Nature · doi:10.1038/nature00904 · Cited by 2,546
Chandel, N. S., McClintock, D. S., Feliciano, C. E., Wood, T. M., Melendez, J. A., Rodriguez, A. M., & Schumacker, P. T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001914200 · Cited by 2,000
Regulation of Mammalian O 2 Homeostasis by Hypoxia-Inducible Factor 1
Semenza, G. L. (1999) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.15.1.551 · Cited by 1,914 · cited 3×
“The regulation of VEGF in response to hypoxia is thought to be mediated primarily through the well-known HIF factors (355).”
Williamson, D., Lund, P., & Krebs, H. (1967) · Biochemical Journal · doi:10.1042/bj1030514 · Cited by 1,871
Blair, S. N. (1996) · JAMA: The Journal of the American Medical Association · doi:10.1001/jama.1996.03540030039029 · Cited by 1,819
The ageing systemic milieu negatively regulates neurogenesis and cognitive function
Villeda, S. A., Luo, J., Mosher, K. I., Zou, B., Britschgi, M., Bieri, G., Stan, T. M., Fainberg, N., Ding, Z., Eggel, A., et al. (2011) · Nature · doi:10.1038/nature10357 · Cited by 1,763
Free radicals and tissue damage produced by exercise
Davies, K. J. A., Quintanilha, A. T., Brooks, G. A., & Packer, L. (1982) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(82)80124-1 · Cited by 1,739
Jones, D. P. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.1865 · Cited by 1,726
SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
Hirschey, M. D., Shimazu, T., Goetzman, E., Jing, E., Schwer, B., Lombard, D. B., Grueter, C. A., Harris, C., Biddinger, S., Ilkayeva, O. R., et al. (2010) · Nature · doi:10.1038/nature08778 · Cited by 1,687
Topology of superoxide production from different sites in the mitochondrial electron transport chain
St-Pierre, J., Buckingham, J. A., Roebuck, S. J., & Brand, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207217200 · Cited by 1,545
Gene expression profile of aging and its retardation by caloric restriction
Lee, C.-K., Klopp, R. G., Weindruch, R., & Prolla, T. A. (1999) · Science · doi:10.1126/science.285.5432.1390 · Cited by 1,473
Steenken, S., & Jovanovic, S. V. (1997) · Journal of the American Chemical Society · doi:10.1021/ja962255b · Cited by 1,450
Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase
Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., et al. (2011) · Science · doi:10.1126/science.1207861 · Cited by 1,429
Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation
Qiu, X., Brown, K., Hirschey, M. D., Verdin, E., & Chen, D. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.015 · Cited by 1,310
The sites and topology of mitochondrial superoxide production
Brand, M. D. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.01.003 · Cited by 1,217
Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation
Lombard, D. B., Alt, F. W., Cheng, H.-L., Bunkenborg, J., Streeper, R. S., Mostoslavsky, R., Kim, J., Yancopoulos, G., Valenzuela, D., Murphy, A., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01636-07 · Cited by 1,216
The role of exercise and PGC1α in inflammation and chronic disease
Handschin, C., & Spiegelman, B. M. (2008) · Nature · doi:10.1038/nature07206 · Cited by 1,083
HIF-independent regulation of VEGF and angiogenesis by the transcriptional coactivator PGC-1α
Arany, Z., Foo, S.-Y., Ma, Y., Ruas, J. L., Bommi-Reddy, A., Girnun, G., Cooper, M., Laznik, D., Chinsomboon, J., Rangwala, S. M., et al. (2008) · Nature · doi:10.1038/nature06613 · Cited by 1,054
SIRT1 Functionally Interacts with the Metabolic Regulator and Transcriptional Coactivator PGC-1α
Nemoto, S., Fergusson, M. M., & Finkel, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501485200 · Cited by 1,047
Complex iii releases superoxide to both sides of the inner mitochondrial membrane
Muller, F. L., Liu, Y., & Van Remmen, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407715200 · Cited by 1,036
Adaptations of skeletal muscle to exercise: rapid increase in the transcriptional coactivator PGC-1
Baar, K., Wende, A. R., Jones, T. E., Marison, M., Nolte, L. A., Chen, M., Kelly, D. P., & Holloszy, J. O. (2002) · The FASEB Journal · doi:10.1096/fj.02-0367com · Cited by 1,020
Acute Exercise Remodels Promoter Methylation in Human Skeletal Muscle
Barrès, R., Yan, J., Egan, B., Treebak, J. T., Rasmussen, M., Fritz, T., Caidahl, K., Krook, A., O'Gorman, D. J., & Zierath, J. R. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.01.001 · Cited by 965 · cited 3×
“Hypomethylation of DNA has been reported immediately after a single bout of exercise in the skeletal muscle samples of healthy subjects at the promoter regions of PGC-1a, pyruvate dehydrogenase kinase isoenzyme 4, and PPAR-d (23).”
InfluentialTao, R., Coleman, M. C., Pennington, J. D., Ozden, O., Park, S.-H., Jiang, H., Kim, H.-S., Flynn, C. R., Hill, S., Hayes McDonald, W., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.12.013 · Cited by 899
Sirtuin 1 Modulates Cellular Responses to Hypoxia by Deacetylating Hypoxia-Inducible Factor 1α
Lim, J.-H., Lee, Y.-M., Chun, Y.-S., Chen, J., Kim, J.-E., & Park, J.-W. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.05.023 · Cited by 758
Thioredoxin and Related Molecules–From Biology to Health and Disease
Lillig, C. H., & Holmgren, A. (2007) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.9.25 · Cited by 724
Babior, B. M. (2004) · Current Opinion in Immunology · doi:10.1016/j.coi.2003.12.001 · Cited by 705
Cardiovascular risk factors emerge after artificial selection for low aerobic capacity.
Wisløff, U., Najjar, S. M., Ellingsen, Ø., Haram, P. M., Swoap, S., Al-Share, Q., Fernström, M., Rezaei, K., Lee, S. J., Koch, L. G., et al. (2005) · Science · doi:10.1126/science.1108177 · Cited by 657
Myoglobin O2 desaturation during exercise. Evidence of limited O2 transport.
Richardson, R. S., Noyszewski, E. A., Kendrick, K. F., Leigh, J. S., & Wagner, P. D. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118237 · Cited by 647
Neurogenesis and Exercise: Past and Future Directions
van Praag, H. (2008) · NeuroMolecular Medicine · doi:10.1007/s12017-008-8028-z · Cited by 645
Handschin, C., Chin, S., Li, P., Liu, F., Maratos-Flier, E., LeBrasseur, N. K., Yan, Z., & Spiegelman, B. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704817200 · Cited by 611
Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
Bota, D. A., & Davies, K. J. A. (2002) · Nature Cell Biology · doi:10.1038/ncb836 · Cited by 557
SIRT1 Is Essential for Normal Cognitive Function and Synaptic Plasticity
Michan, S., Li, Y., Chou, M. M.-H., Parrella, E., Ge, H., Long, J. M., Allard, J. S., Lewis, K., Miller, M., Xu, W., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.0027-10.2010 · Cited by 541
Exercise-induced mitochondrial biogenesis begins before the increase in muscle PGC-1α expression.
Wright, D. C., Han, D.-H., Garcia-Roves, P. M., Geiger, P. C., Jones, T. E., & Holloszy, J. O. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m606116200 · Cited by 488
Diet and exercise signals regulate SIRT3 and activate AMPK and PGC-1α in skeletal muscle
Palacios, O. M., Carmona, J. J., Michan, S., Chen, K. Y., Manabe, Y., III, J. L. W., Goodyear, L. J., & Tong, Q. (2009) · Aging · doi:10.18632/aging.100075 · Cited by 487
Exercise-induced oxidative stress in humans: cause and consequences
Powers, S. K., Nelson, W. B., & Hudson, M. B. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.12.009 · Cited by 441
Ryanodine receptor oxidation causes intracellular calcium leak and muscle weakness in aging
Andersson, D. C., Betzenhauser, M. J., Reiken, S., Meli, A. C., Umanskaya, A., Xie, W., Shiomi, T., Zalk, R., Lacampagne, A., & Marks, A. R. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.05.014 · Cited by 424
PGC-1α regulation by exercise training and its influences on muscle function and insulin sensitivity
Lira, V. A., Benton, C. R., Yan, Z., & Bonen, A. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00755.2009 · Cited by 412 · cited 3×
“None of the p38 MAPK isoforms was required for endurance exercise-induced IIb-to-IIa fiber-type transformation in these mice (213).”
Yang, S.-R., Wright, J., Bauter, M., Seweryniak, K., Kode, A., & Rahman, I. (2007) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00308.2006 · Cited by 391
Biological control through regulated transcriptional coactivators
Spiegelman, B. M., & Heinrich, R. (2004) · Cell · doi:10.1016/j.cell.2004.09.037 · Cited by 377
Gomez‐Pinilla, F., Zhuang, Y., Feng, J., Ying, Z., & Fan, G. (2011) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2010.07508.x · Cited by 367
PNPASE Regulates RNA Import into Mitochondria
Wang, G., Chen, H.-W., Oktay, Y., Zhang, J., Allen, E. L., Smith, G. M., Fan, K. C., Hong, J. S., French, S. W., McCaffery, J. M., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.035 · Cited by 366 · cited 1×
“Recent data have revealed that mammalian polynucleotide phosphorylase (PNPase) is localized in the mitochondrial intermembrane space to regulate the translocation of RNA into mitochondria (425).”
Timmons, J. A., Knudsen, S., Rankinen, T., Koch, L. G., Sarzynski, M., Jensen, T., Keller, P., Scheele, C., Vollaard, N. B. J., Nielsen, S., et al. (2010) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01295.2009 · Cited by 358
Mitochondria and cellular oxygen sensing in the HIF pathway
Taylor, C. T. (2008) · Biochemical Journal · doi:10.1042/bj20071249 · Cited by 298
Fischer, C. P., Hiscock, N. J., Penkowa, M., Basu, S., Vessby, B., Kallner, A., Sjöberg, L., & Pedersen, B. K. (2004) · The Journal of Physiology · doi:10.1113/jphysiol.2004.066779 · Cited by 293 · cited 1×
“The observation that Vitamin C and E administration decreases the exercise-induced generation of IL-6 suggests that ROS are stimulators of IL-6 production in skeletal muscle (94).”
Physiological activation of hypoxia inducible factor‐1 in human skeletal muscle
Ameln, H., Gustafsson, T., Sundberg, C. J., Okamoto, K., Jansson, E., Poellinger, L., & Makino, Y. (2005) · The FASEB Journal · doi:10.1096/fj.04-2304fje · Cited by 276
Muscle-derived interleukin-6: lipolytic, anti-inflammatory and immune regulatory effects
Pedersen, B. K., Steensberg, A., Keller, P., Keller, C., Fischer, C., Hiscock, N., van Hall, G., Plomgaard, P., & Febbraio, M. A. (2003) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-002-0981-z · Cited by 228
Tracing Oxygen's Imprint on Earth's Metabolic Evolution
Falkowski, P. G. (2006) · Science · doi:10.1126/science.1125937 · Cited by 175
Pogozelski, A. R., Geng, T., Li, P., Yin, X., Lira, V. A., Zhang, M., Chi, J.-T., & Yan, Z. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007934 · Cited by 164 · cited 2×
“Meanwhile, calcineurin (CnA) nuclear factor of activated T-cell (NFAT) regulatory axis controls fiber-type transformation in endurance exerciseinduced skeletal muscle adaptation (288).”
Hypoxia increases sirtuin 1 expression in a hypoxia-inducible factor-dependent manner
Chen, R., Dioum, E. M., Hogg, R. T., Gerard, R. D., & Garcia, J. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.175414 · Cited by 155
Koltai, E., Hart, N., Taylor, A. W., Goto, S., Ngo, J. K., Davies, K. J. A., & Radak, Z. (2012) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00337.2011 · Cited by 152
Collins, A., Hill, L. E., Chandramohan, Y., Whitcomb, D., Droste, S. K., & Reul, J. M. H. M. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004330 · Cited by 145 · cited 1×
“It has been reported that exercise results in phosphoacetylation of histone H3 and induction of c-Fos gene in dentate gyrus (71).”
Ghosh, S., Lertwattanarak, R., Lefort, N., Molina-Carrion, M., Joya-Galeana, J., Bowen, B. P., Garduno-Garcia, J. D. J., Abdul-Ghani, M., Richardson, A., DeFronzo, R. A., et al. (2011) · Diabetes · doi:10.2337/db11-0121 · Cited by 128
Ogura, M., Nakamura, Y., Tanaka, D., Zhuang, X., Fujita, Y., Obara, A., Hamasaki, A., Hosokawa, M., & Inagaki, N. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.01.081 · Cited by 121
Chen, Q., & Lesnefsky, E. J. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.10.043 · Cited by 119
Heme proteins mediate the conversion of nitrite to nitric oxide in the vascular wall
Alzawahra, W. F., Talukder, M. A. H., Liu, X., Samouilov, A., & Zweier, J. L. (2008) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00374.2008 · Cited by 111
Bori, Z., Zhao, Z., Koltai, E., Fatouros, I. G., Jamurtas, A. Z., Douroudos, I. I., Terzis, G., Chatzinikolaou, A., Sovatzidis, A., Draganidis, D., et al. (2012) · Experimental Gerontology · doi:10.1016/j.exger.2012.03.004 · Cited by 108
Self-citationPetersen, A. C., McKenna, M. J., Medved, I., Murphy, K. T., Brown, M. J., Della Gatta, P., & Cameron‐Smith, D. (2012) · Acta Physiologica · doi:10.1111/j.1748-1716.2011.02344.x · Cited by 99
Cobley, J. N., McGlory, C., Morton, J. P., & Close, G. L. (2011) · International Journal of Sport Nutrition and Exercise Metabolism · doi:10.1123/ijsnem.21.6.451 · Cited by 76
Superoxide dismutase 1 knockdown induces oxidative stress and DNA methylation loss in the prostate
Bhusari, S. S., Dobosy, J. R., Fu, V., Almassi, N., Oberley, T., & Jarrard, D. F. (2010) · Epigenetics · doi:10.4161/epi.5.5.11853 · Cited by 50
Cited by
Oxidative stress, aging, and diseases
Liguori, I., Russo, G., Curcio, F., Bulli, G., Aran, L., Della-Morte, D., Gargiulo, G., Testa, G., Cacciatore, F., Bonaduce, D., et al. (2018) · Clinical Interventions in Aging · doi:10.2147/cia.s158513 · Cited by 3,979
The role of mitochondria in aging
Bratic, A., & Larsson, N.-G. (2013) · Journal of Clinical Investigation · doi:10.1172/jci64125 · Cited by 1,087
Running-induced systemic cathepsin B secretion is associated with memory function
Moon, H. Y., Becke, A., Berron, D., Becker, B., Sah, N., Benoni, G., Janke, E., Lubejko, S. T., Greig, N. H., Mattison, J. A., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.025 · Cited by 628
PGC-1α Is a Master Regulator of Mitochondrial Lifecycle and ROS Stress Response
Abu Shelbayeh, O., Arroum, T., Morris, S., & Busch, K. B. (2023) · Antioxidants · doi:10.3390/antiox12051075 · Cited by 552
Ticinesi, A., Lauretani, F., Milani, C., Nouvenne, A., Tana, C., Del Rio, D., Maggio, M., Ventura, M., & Meschi, T. (2017) · Nutrients · doi:10.3390/nu9121303 · Cited by 401
Metadata
- Authors
- Radak, Z., Zhao, Z., Koltai, E., Ohno, H., & Atalay, M.
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2013-04
- Volume
- 18
- Issue
- 10
- Pages
- 1208-1246
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W2118574229
- Cited by
- 605
- References
- 64
- FWCI
- 27.44
- 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 ›
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.
