Myobolites: muscle-derived metabolites with paracrine and systemic effects
Open accessAbstract
Intracellular metabolism in skeletal muscle has been studied for more than a century and is the stuff of textbooks. In contrast, the extracellular secretion of metabolites by muscle cells, and their effects on non-muscle cells near or far, has been investigated much less extensively. Here, we describe a number of cases in which striated muscle secretes a metabolite that elicits complex responses in other cells or tissues, with involvements in normal physiology as well as obesity, type II diabetes, and cardiac remodeling. We focus on two recently identified secreted catabolic products of branched chain amino acid breakdown, β-aminoisobutyric acid and 3-hydroxyisobutyrate, and discuss common themes of inter-cellular signaling pathways driven by secreted metabolites.
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?
Skeletal muscle acts as a secretory organ in regulating energy homeostasis and obesity progression in other tissues.
“Emerging evidence has identified skeletal muscle as a secretory organ in regulating energy homeostasis and obesity progression in other tissues (Rai & Demontis, 2016; Ibrahim et al, 2017).”
From Exercise‐induced α‐ketoglutaric acid stimulates muscle hypertrophy and fat loss through OXGR1‐dependent adrenal activation (2020) · cites this paper as Ibrahim et al, 2017
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
Metabolite profiles and the risk of developing diabetes
Wang, T. J., Larson, M. G., Vasan, R. S., Cheng, S., Rhee, E. P., McCabe, E., Lewis, G. D., Fox, C. S., Jacques, P. F., Fernandez, C., et al. (2011) · Nature Medicine · doi:10.1038/nm.2307 · Cited by 3,143 · see citing works
PGC-1 coactivators: inducible regulators of energy metabolism in health and disease
Finck, B. N. (2006) · Journal of Clinical Investigation · doi:10.1172/jci27794 · Cited by 1,427 · see citing works
Hypothalamic mTOR Signaling Regulates Food Intake
Cota, D., Proulx, K., Smith, K. A. B., Kozma, S. C., Thomas, G., Woods, S. C., & Seeley, R. J. (2006) · Science · doi:10.1126/science.1124147 · Cited by 1,278 · see citing works
Krssak, M., Falk Petersen, K., Dresner, A., DiPietro, L., Vogel, S. M., Rothman, D. L., Shulman, G. I., & Roden, M. (1999) · Diabetologia · doi:10.1007/s001250051123 · Cited by 1,264 · see citing works
Goodpaster, B. H. (2001) · Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.86.12.5755 · Cited by 1,194 · see citing works
Adipose tissue browning and metabolic health
Bartelt, A., & Heeren, J. (2014) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2013.204 · Cited by 1,177 · see citing works
Ectopic Fat in Insulin Resistance, Dyslipidemia, and Cardiometabolic Disease
Shulman, G. I. (2014) · New England Journal of Medicine · doi:10.1056/nejmra1011035 · Cited by 1,126 · see citing works
Interplay between lipids and branched-chain amino acids in development of insulin resistance
Newgard, C. B. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.01.024 · Cited by 1,080 · see citing works
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 · see citing works
Self-citationAdaptations 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 · see citing works
Cardiac nucleotides in hypoxia: possible role in regulation of coronary blood flow
Berne, R. M. (1963) · American Journal of Physiology-Legacy Content · doi:10.1152/ajplegacy.1963.204.2.317 · Cited by 1,014 · see citing works
Joyner, M. J., & Casey, D. P. (2015) · Physiological Reviews · doi:10.1152/physrev.00035.2013 · Cited by 833 · see citing works
Plasma Amino Acid Levels and Insulin Secretion in Obesity
Felig, P., Marliss, E., & Cahill, G. F. (1969) · New England Journal of Medicine · doi:10.1056/nejm196910092811503 · Cited by 812 · see citing works
Arany, Z., He, H., Lin, J., Hoyer, K., Handschin, C., Toka, O., Ahmad, F., Matsui, T., Chin, S., Wu, P.-H., et al. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.03.002 · Cited by 694 · see citing works
Self-citationMichael, L. F., Wu, Z., Cheatham, R. B., Puigserver, P., Adelmant, G., Lehman, J. J., Kelly, D. P., & Spiegelman, B. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.061035098 · Cited by 663 · see citing works
Roberts, L. D., Boström, P., O’Sullivan, J. F., Schinzel, R. T., Lewis, G. D., Dejam, A., Lee, Y.-K., Palma, M. J., Calhoun, S., Georgiadi, A., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2013.12.003 · Cited by 643 · see citing works
A Ceramide-Centric View of Insulin Resistance
Chavez, J. A., & Summers, S. A. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.002 · Cited by 620 · see citing works
Liu, C., Wu, J., Zhu, J., Kuei, C., Yu, J., Shelton, J., Sutton, S. W., Li, X., Yun, S. J., Mirzadegan, T., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806409200 · Cited by 606 · see citing works
Activation of PPARγ Coactivator-1 Through Transcription Factor Docking
Puigserver, P., Adelmant, G., Wu, Z., Fan, M., Xu, J., O’Malley, B. W., & Spiegelman, B. M. (1999) · Science · doi:10.1126/science.286.5443.1368 · Cited by 596 · see citing works
Jang, C., Oh, S. F., Wada, S., Rowe, G. C., Liu, L., Chan, M. C., Rhee, J., Hoshino, A., Kim, B., Ibrahim, A., et al. (2016) · Nature Medicine · doi:10.1038/nm.4057 · Cited by 591 · see citing works
Self-citationLotta, L. A., Scott, R. A., Sharp, S. J., Burgess, S., Luan, J., Tillin, T., Schmidt, A. F., Imamura, F., Stewart, I. D., Perry, J. R. B., et al. (2016) · PLOS Medicine · doi:10.1371/journal.pmed.1002179 · Cited by 417 · see citing works
Role of diacylglycerol activation of PKCθ in lipid-induced muscle insulin resistance in humans
Szendroedi, J., Yoshimura, T., Phielix, E., Koliaki, C., Marcucci, M., Zhang, D., Jelenik, T., Müller, J., Herder, C., Nowotny, P., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1409229111 · Cited by 415 · see citing works
The Emerging Role of Branched-Chain Amino Acids in Insulin Resistance and Metabolism
Yoon, M.-S. (2016) · Nutrients · doi:10.3390/nu8070405 · Cited by 395 · see citing works
Cao, L., Choi, E., Liu, X., Martin, A. S., Wang, C., Xu, X., & During, M. J. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.06.020 · Cited by 380 · see citing works
She, P., Reid, T., Bronson, S. K., Vary, T. C., Hajnal, A. S., Lynch, C. J., & Hutson, S. M. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.08.003 · Cited by 360 · see citing works
Choi, C. S., Befroy, D. E., Codella, R., Kim, S., Reznick, R. M., Hwang, Y.-J., Liu, Z.-X., Lee, H.-Y., Distefano, A., Samuel, V. T., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810339105 · Cited by 279 · see citing works
Oxygen regulation of breathing through an olfactory receptor activated by lactate
Chang, A. J., Ortega, F. E., Riegler, J., Madison, D. V., & Krasnow, M. A. (2015) · Nature · doi:10.1038/nature15721 · Cited by 276 · see citing works
GLYCOGEN FORMATION IN THE LIVER FROM d- AND l-LACTIC ACID
Cori, C. F., & Cori, G. T. (1929) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83822-4 · Cited by 268 · see citing works
Adenosine Concentrations in the Interstitium of Resting and Contracting Human Skeletal Muscle
Hellsten, Y., MacLean, D. A., Rådegran, G., Saltin, B., & Bangsbo, J. (1998) · Circulation · doi:10.1161/01.cir.98.1.6 · Cited by 233 · see citing works
Plasma Amino Acid Levels and Insulin Secretion in Obesity
Felig, P. (1970) · Laboratory Medicine · doi:10.1093/labmed/1.9.39 · Cited by 213 · see citing works
Dobson, J. G., Rubio, R., & Berne, R. M. (1971) · Circulation Research · doi:10.1161/01.res.29.4.375 · Cited by 205 · see citing works
METABOLISM OF THYMINE (METHYL-C14 OR −2-C14) BY RAT LIVER IN VITRO
Fink, K., Cline, R. E., Henderson, R. B., & Fink, R. M. (1956) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65261-5 · Cited by 203 · see citing works
Achten, J., & Jeukendrup, A. E. (2004) · International Journal of Sports Medicine · doi:10.1055/s-2003-45231 · Cited by 138 · see citing works
The many roles of PGC-1α in muscle — recent developments
Chan, M. C., & Arany, Z. P. (2014) · Metabolism · doi:10.1016/j.metabol.2014.01.006 · Cited by 125 · see citing works
Self-citationLactate inhibition of lipolysis in exercising man
BOYD, A. E., Giamber, S. R., Mager, M., & Lebovitz, H. E. (1974) · Metabolism · doi:10.1016/0026-0495(74)90081-x · Cited by 124 · see citing works
Shi, C.-X., Zhao, M.-X., Shu, X.-D., Xiong, X.-Q., Wang, J.-J., Gao, X.-Y., Chen, Q., Li, Y.-H., Kang, Y.-M., & Zhu, G.-Q. (2016) · Scientific Reports · doi:10.1038/srep21924 · Cited by 108 · see citing works
Regulation of the skeletal muscle blood flow in humans
Mortensen, S. P., & Saltin, B. (2014) · Experimental Physiology · doi:10.1113/expphysiol.2014.081620 · Cited by 104 · see citing works
The Glucose–Lactic Acid Cycle and Gluconeogenesis
Cori, C. F. (1981) · Current topics in cellular regulation · doi:10.1016/b978-0-12-152818-8.50028-1 · Cited by 99 · see citing works
PGC-1α Improves Glucose Homeostasis in Skeletal Muscle in an Activity-Dependent Manner
Summermatter, S., Shui, G., Maag, D., Santos, G., Wenk, M. R., & Handschin, C. (2012) · Diabetes · doi:10.2337/db12-0291 · Cited by 96 · see citing works
The Muscle Metabolome Differs between Healthy and Frail Older Adults
Fazelzadeh, P., Hangelbroek, R., Tieland, M., de Groot, C. P. G. M., Verdijk, L. B., van Loon, L. J. C., Smilde, A. K., Alves, R. D. A. M., Vervoort, J. J. M., Müller, M. M., et al. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00840 · Cited by 94 · see citing works
Cardiac myocyte–secreted cAMP exerts paracrine action via adenosine receptor activation
Sassi, Y., Ahles, A., Truong, D. J., Baqi, Y., Lee, S.-Y., Husse, B., Hulot, J., Foinquinos, A., Thum, T., Müller, C. E., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci74349 · Cited by 86 · see citing works
The roles of adenosine and related substances in exercise hyperaemia
Marshall, J. M. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2007.136416 · Cited by 83 · see citing works
Cori, C. F., & Cori, G. T. (1946) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.15.070146.001205 · Cited by 76 · see citing works
Real-Time Noninvasive Imaging of Fatty Acid Uptake in Vivo
Henkin, A. H., Cohen, A. S., Goun, E. A., Park, H. M., Nikitin, G. F., Auzias, M. G., Kazantzis, M., Bertozzi, C. R., & Stahl, A. (2012) · ACS Chemical Biology · doi:10.1021/cb300194b · Cited by 69 · see citing works
Regulation of cAMP homeostasis by the efflux protein MRP4 in cardiac myocytes
Sassi, Y., Abi‐Gerges, A., Fauconnier, J., Mougenot, N., Reiken, S. R., Haghighi, K., Kranias, E. G., Marks, A. R., Lacampagne, A., Engelhardt, S. H., et al. (2011) · The FASEB Journal · doi:10.1096/fj.11-194027 · Cited by 68 · see citing works
Skeletal muscle expresses the extracellular cyclic AMP–adenosine pathway
Chiavegatti, T., Costa, V. L., Araújo, M. S., & Godinho, R. O. (2007) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707648 · Cited by 62 · see citing works
Godinho, R. O., & Costa‐Jr, V. L. (2003) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705130 · Cited by 42 · see citing works
Proteomic profiling of non-obese type 2 diabetic skeletal muscle
Ohlendieck, K. (2010) · International Journal of Molecular Medicine · doi:10.3892/ijmm_00000364 · Cited by 42 · see citing works
Ballard, H. J., Cotterrell, D., & Karim, F. (1987) · The Journal of Physiology · doi:10.1113/jphysiol.1987.sp016580 · Cited by 39 · see citing works
Mendelian Randomization and Type 2 Diabetes
Swerdlow, D. I. (2016) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-016-6638-5 · Cited by 27 · see citing works
Contribution of non‐endothelium‐dependent substances to exercise hyperaemia: are they O2 dependent?
Marshall, J. M., & Ray, C. J. (2012) · The Journal of Physiology · doi:10.1113/jphysiol.2012.240721 · Cited by 18 · see citing works
Cori, C. F., & Cori, G. T. (1933) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.02.070133.001021 · Cited by 4 · see citing works
Flagged first, then by citations
2 of the 54 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
The molecular athlete: exercise physiology from mechanisms to medals
Furrer, R., Hawley, J. A., & Handschin, C. (2023) · Physiological Reviews · doi:10.1152/physrev.00017.2022 · Cited by 232 · see citing works
Yuan, Y., Xu, P., Jiang, Q., Cai, X., Wang, T., Peng, W., Sun, J., Zhu, C., Zhang, C., Yue, D., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019103304 · Cited by 92 · see citing works
“Emerging evidence has identified skeletal muscle as a secretory organ in regulating energy homeostasis and obesity progression in other tissues (Rai & Demontis, 2016; Ibrahim et al , 2017).”
Diabetes and its complications: molecular mechanisms, prevention and treatment
Zhao, L., Yuan, J., Yang, Q., Ma, J., Yang, F., Zou, Y., Liu, K., & Liu, F. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02401-w · Cited by 80 · see citing works
Do skeletal muscle-secreted factors influence the function of pancreatic β-cells?
Barlow, J. P., & Solomon, T. P. J. (2017) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00353.2017 · Cited by 66 · see citing works
circPTPN4 regulates myogenesis via the miR-499-3p/NAMPT axis
Cai, B., Ma, M., Zhou, Z., Kong, S., Zhang, J., Zhang, X., & Nie, Q. (2022) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-021-00664-1 · Cited by 47 · see citing works
Cornish, S. M., Bugera, E. M., Duhamel, T. A., Peeler, J. D., & Anderson, J. E. (2020) · European Journal of Applied Physiology · doi:10.1007/s00421-020-04337-1 · Cited by 43 · see citing works
Saoi, M., Percival, M. E., Nemr, C. R., Li, A., Gibala, M. J., & Britz‐McKibbin, P. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b00149 · Cited by 34 · see citing works
LncEDCH1 improves mitochondrial function to reduce muscle atrophy by interacting with SERCA2
Cai, B., Ma, M., Zhang, J., Wang, Z., Kong, S., Zhou, Z., Lian, L., Zhang, J., Li, J., Wang, Y., et al. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.12.004 · Cited by 29 · see citing works
Long noncoding RNA ZFP36L2-AS functions as a metabolic modulator to regulate muscle development
Cai, B., Ma, M., Zhang, J., Kong, S., Zhou, Z., Li, Z., Abdalla, B. A., Xu, H., Zhang, X., Lawal, R. A., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04772-2 · Cited by 27 · see citing works
Nomikos, T., Methenitis, S., & Panagiotakos, D. B. (2022) · Lipids in Health and Disease · doi:10.1186/s12944-022-01692-0 · Cited by 23 · see citing works
Lyon, E. S., Rivera, M. E., Johnson, M. A., Sunderland, K., & Vaughan, R. A. (2019) · Nutrition Research · doi:10.1016/j.nutres.2019.03.012 · Cited by 23 · see citing works
“Ferrocrinology”—Iron Is an Important Factor Involved in Gluco- and Lipocrinology
Szklarz, M., Gontarz-Nowak, K., Matuszewski, W., & Bandurska-Stankiewicz, E. M. (2022) · Nutrients · doi:10.3390/nu14214693 · Cited by 20 · see citing works
Merz, K. E., Tunduguru, R., Ahn, M., Salunkhe, V. A., Veluthakal, R., Hwang, J. H., Bhattacharya, S., McCown, E. M., Garcia, P. A., Zhou, C., et al. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.821849 · Cited by 20 · see citing works
Skeletal muscle-derived exosomes prevent osteoporosis by promoting osteogenesis
Xing, Z., Guo, L., Li, S., Huang, W., Su, J., Chen, X., Li, Y., & Zhang, J. (2024) · Life Sciences · doi:10.1016/j.lfs.2024.123079 · Cited by 20 · see citing works
Muscle Injuries Induce a Prostacyclin‐PPARγ/PGC1a‐FAO Spike That Boosts Regeneration
Luo, L., Chua, B. Y.-J., Liu, T., Liang, K., Min‐Wen, J. C., Ma, W., Goh, J., Wang, Y., Su, J., Ho, Y. S., et al. (2023) · Advanced Science · doi:10.1002/advs.202301519 · Cited by 15 · see citing works
Wu, Y., Han, M., Wang, Y., Gao, Y., Cui, X., Xu, P., Ji, C., Zhong, T., You, L., & Zeng, Y. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00741 · Cited by 7 · see citing works
Li, T., Guo, T., Zhi, Z., Wang, P., Zhou, J., Zhang, H., Cui, M., Zhang, J., & Zhang, J. (2025) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5c10158 · Cited by 3 · see citing works
Niu, Y., He, L., An, Z., Yuan, M., Ji, H., Wang, W., Wei, C., Han, R., Tian, W., Tian, Y., et al. (2026) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-026-01421-y · Cited by 1 · see citing works
Editorial overview: Muscle and bone are highly effective communicators
Taylor, J. M. (2017) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2017.11.005 · Cited by 1 · see citing works
Additional file 1 of circPTPN4 regulates myogenesis via the miR-499-3p/NAMPT axis
Cai, B., Ma, M., Zhou, Z., Kong, S., Zhang, J., Zhang, X., & Nie, Q. (2022) · Figshare · doi:10.6084/m9.figshare.19166915
Zhang, T., Zhang, B., Wu, J., Li, S., Gong, Y., Fang, S., Feng, D., Huang, B., Lian, J., Xiang, W., et al. (2025) · JCSM Communications · doi:10.1002/rco2.99
Fuentes-Barría, H., Aguilera-Eguía, R. A., Alarcón-Rivera, M., Flores-Fernández, C., Angarita, L., Aristizábal-Hoyos, J. A., & Soto, O. P. L. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1849847
- Authors
- Ibrahim, A., Neinast, M., & Arany, Z. P.
- Affiliations
- University of Pennsylvania (US)
- Corresponding author
- Arany, Zoltan P
- Venue
- Current Opinion in Pharmacology
- Publisher
- Elsevier BV
- Published
- 2017-06
- Volume
- 34
- Pages
- 15-20
- ISSN
- 1471-4892 (ISSN-L)
- PMC
- PMC5651206
- OpenAlex
- W2606538849
- Cited by
- 22
- References
- 54
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 1 · 2023: 2 · 2022: 5 · 2021: 1 · 2020: 2 · 2019: 3 · 2017: 3
- FWCI
- 0.20
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Current Opinion in Pharmacology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Heart, Lung, and Blood Institute (R01HL094499)
- National Institute of General Medical Sciences (T32GM007229)
- National Institute of Diabetes and Digestive and Kidney Diseases (F31DK111091, R01DK107667)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Epidemiology › Adipokines, Inflammation, and Metabolic Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
- Keywords
- extracellular secretion, paracrine signaling, systemic effects, skeletal muscle metabolism, branched-chain amino acids, beta-aminoisobutyric acid, 3-hydroxyisobutyrate, obesity, type 2 diabetes, cardiac remodeling, intercellular communication
- MeSH terms
- Adenosine, Cyclic AMP, Aminoisobutyric Acids, Animals, Fatty Acids, Fibrosis, Cardiomegaly, Humans, Liver, Myocardium, Vasodilation, Adipocytes, Muscle, Skeletal
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
