The Inhibitory Effects of New Zealand Pine Bark (Enzogenol®) on α-Amylase, α-Glucosidase, and Dipeptidyl Peptidase-4 (DPP-4) Enzymes
Open accessAbstract
The New Zealand pine bark extract (Enzogenol®) has previously been shown to elicit acute hypoglycaemic effects in humans. The present study investigated the underlying mechanisms of Enzogenol® in reducing postprandial glucose in humans. The potential inhibitory action of Enzogenol® against digestive enzymes: α-amylase and α-glucosidase, and dipeptidyl peptidase-4 (DPP-4) enzyme was determined. Enzogenol® demonstrated the ability to inhibit all three enzymes: α-amylase enzyme activity (IC50 3.98 ± 0.11 mg/mL), α-glucosidase enzyme activity (IC50 13.02 ± 0.28 μg/mL), and DPP-4 enzyme activity (IC50 2.51 ± 0.04 mg/mL). The present findings indicate the potential for Enzogenol® to improve postprandial glycaemia by delaying carbohydrate digestion via the inhibition of digestive enzymes (α-amylase and α-glucosidase), and enhancing the incretin effect via inhibiting the dipeptidyl-peptidase-4 enzyme. The inhibitory actions of Enzogenol® on enzymes should therefore be further validated in humans for its potential use in type 2 diabetes mellitus prevention and management.
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?
Inhibiting α-amylase and α-glucosidase delays starch breakdown, glucose absorption, and reduces postprandial blood glucose spikes.
“A common antidiabetic strategy involves inhibiting α-amylase and α-glucosidase, enzymes that break down complex carbohydrates into glucose, thus delaying starch breakdown, glucose absorption and reducing postprandial blood glucose spikes [89].”
From Navigating the potential of algal peptides: health effects, market applications, and scientific challenges (2026) · cites this paper as [89]
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
Polyphenols: Food sources and bioavailability
Manach, C., Scalbert, A., Morand, C., Rémésy, C., & Jiménez, L. (2004) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/79.5.727 · Cited by 8,175 · cited 1× · see citing works
“The in vitro outcomes may also not translate into equivalent outcomes in humans, given the knowledge that plant polyphenols undergo extensive metabolism that may alter their enzymatic inhibitory effects [41,42].”
BackgroundGlobal aetiology and epidemiology of type 2 diabetes mellitus and its complications
Zheng, Y., Ley, S. H., & Hu, F. B. (2018) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2017.151 · Cited by 5,697 · cited 1× · see citing works
“Alongside genetics, environmental and socioeconomic factors, poor diet choices and sedentary lifestyle contributing to obesity play a major role in the development of type 2 diabetes mellitus (T2D), years before symptoms become visible [1,3,4].”
BackgroundDietary polyphenols and the prevention of diseases
Scalbert, A., Manach, C., Morand, C., Rémésy, C., & Jiménez, L. (2005) · Critical Reviews in Food Science and Nutrition · doi:10.1080/1040869059096 · Cited by 2,999 · cited 1× · see citing works
“The in vitro outcomes may also not translate into equivalent outcomes in humans, given the knowledge that plant polyphenols undergo extensive metabolism that may alter their enzymatic inhibitory effects [41,42].”
BackgroundPrediabetes: a high-risk state for diabetes development
Tabák, A. G., Herder, C., Rathmann, W., Brunner, E. J., & Kivimäki, M. (2012) · The Lancet · doi:10.1016/s0140-6736(12)60283-9 · Cited by 2,958 · cited 1× · see citing works
“Individuals with prediabetes are at high risk for developing diabetes [2].”
BackgroundBray, G. A., Kim, K. K., Wilding, J. P. H., & on behalf of the World Obesity Federation (2017) · Obesity Reviews · doi:10.1111/obr.12551 · Cited by 1,612 · see citing works
Impact of Dietary Polyphenols on Carbohydrate Metabolism
Hanhineva, K., Törrönen, R., Bondia‐Pons, I., Pekkinen, J., Kolehmainen, M., Mykkänen, H. M., & Poutanen, K. S. (2010) · International Journal of Molecular Sciences · doi:10.3390/ijms11041365 · Cited by 1,167 · see citing works
Inhibition of .ALPHA.-Glucosidase and .ALPHA.-Amylase by Flavonoids
Tadera, K., Minami, Y., TAKAMATSU, K., & MATSUOKA, T. (2006) · Journal of Nutritional Science and Vitaminology · doi:10.3177/jnsv.52.149 · Cited by 1,046 · cited 1× · see citing works
“Furthermore, many food/plant extracts have been tested for potential inhibitory action against α-glucosidase deriving from yeast, making this present study suitable to be compared between similar studies [39,40].”
ResultTundis, R., Loizzo, M. R., & Menichini, F. (2010) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/138955710791331007 · Cited by 851 · see citing works
Proanthocyanidins: A comprehensive review
Rauf, A., Imran, M., Abu‐Izneid, T., Ul‐Haq, I., Patel, S. V., Pan, X., Naz, S., Sanches-Silva, A. T., Saeed, F., & Suleria, H. A. R. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.108999 · Cited by 815 · see citing works
Polyphenols in foods are more complex than often thought
Cheynier, V. (2005) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/81.1.223s · Cited by 746 · cited 1× · see citing works
“The enzyme inhibitory efficacy of Enzogenol® may also be modified by several dietary factors such as the presence of macronutrients during a meal [43,44].”
BackgroundDietary factors affecting polyphenol bioavailability
Bohn, T. (2014) · Nutrition Reviews · doi:10.1111/nure.12114 · Cited by 577 · cited 1× · see citing works
“The enzyme inhibitory efficacy of Enzogenol® may also be modified by several dietary factors such as the presence of macronutrients during a meal [43,44].”
BackgroundInhibitory effect of pine extract on α-glucosidase activity and postprandial hyperglycemia
Kim, Y.-M., Jeong, Y.-K., Wang, M.-H., Lee, W.-Y., & Rhee, H.-I. (2005) · Nutrition · doi:10.1016/j.nut.2004.10.014 · Cited by 531 · cited 1× · see citing works
“69 μg/mL), although the exact phenolic composition contributing to its inhibitory action was not known [20].”
BackgroundDietary polyphenols modulate starch digestion and glycaemic level: a review
Sun, L., & Miao, M. (2019) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2018.1544883 · Cited by 435 · see citing works
Physiology and Pharmacology of DPP-4 in Glucose Homeostasis and the Treatment of Type 2 Diabetes
Deacon, C. F. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00080 · Cited by 429 · cited 1× · see citing works
“These mechanisms may have important clinical implications for individuals with impaired glycaemic control, by preventing or slowing carbohydrate digestion [13–15] and preserving biologically active incretins to stimulate glucose-dependent insulin secretion in the body thereby improving glycaemic control post-meal [17,…”
BackgroundEtxeberría, U., de la Garza, A. L., Campión, J., Martínez, J. A., & Milagro, F. I. (2012) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2012.664134 · Cited by 398 · cited 1× · see citing works
“Acarbose as an anti-diabetic drug is a strong amylase inhibitor known for causing gastrointestinal adverse effects due to the accumulation of undigested carbohydrates becoming readily available for bacterial fermentation [32,34].”
BackgroundPharmacology and therapeutic implications of current drugs for type 2 diabetes mellitus
Tahrani, A. A., Barnett, A. H., & Bailey, C. J. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.86 · Cited by 398 · see citing works
Possible effects of dietary polyphenols on sugar absorption and digestion
Williamson, G. (2012) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201200511 · Cited by 389 · see citing works
Dietary Polyphenols and Type 2 Diabetes: Current Insights and Future Perspectives
Xiao, J., & Högger, P. (2014) · Current Medicinal Chemistry · doi:10.2174/0929867321666140706130807 · Cited by 361 · cited 1× · see citing works
“, OH) and double bonds that determine its effective interaction with digestive enzymes, transmembrane glycoproteins such as DPP-4, apically located transporters and receptors involved in glucose metabolism during a meal [26].”
BackgroundA novel α-glucosidase inhibitor from pine bark
Kim, Y.-M., Wang, M., & Rhee, H.-I. (2004) · Carbohydrate Research · doi:10.1016/j.carres.2003.11.005 · Cited by 325 · see citing works
Akkarachiyasit, S., Charoenlertkul, P., Yibchok‐anun, S., & Adisakwattana, S. (2010) · International Journal of Molecular Sciences · doi:10.3390/ijms11093387 · Cited by 258 · see citing works
Acker, M. G., & Auld, D. S. (2014) · Perspectives in Science · doi:10.1016/j.pisc.2013.12.001 · Cited by 213 · cited 1× · see citing works
“likely contributed to the different IC50 values obtained [15,33].”
BackgroundInhibitory Effect of α-Glucosidase Inhibitors Varies According to Its Origin
Oki, T., Matsui, T., & Osajima, Y. (1999) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf980788t · Cited by 209 · see citing works
Zhang, B., Li, X., Sun, W., Xing, Y., Xiu, Z., Zhuang, C., & Dong, Y. (2017) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.7b02531 · Cited by 206 · see citing works
Zhao, C., Yang, C., Wai, S. T. C., Zhang, Y., P. Portillo, M., Paoli, P., Wu, Y., San Cheang, W., Liu, B., Carpéné, C., et al. (2019) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2018.1501658 · Cited by 199 · see citing works
Hogan, S. P., Zhang, L., Li, J., Sun, S., Canning, C., & Zhou, K. (2010) · Nutrition & Metabolism · doi:10.1186/1743-7075-7-71 · Cited by 183 · see citing works
Inhibition of human α-amylase by dietary polyphenols
Nyambe-Silavwe, H., Villa-Rodríguez, J. A., Ifie, I., Holmes, M. J., Aydın, E., Jensen, J. M., & Williamson, G. (2015) · Journal of Functional Foods · doi:10.1016/j.jff.2015.10.003 · Cited by 169 · see citing works
Almasri, I. M., Mohammad, M. K., & Taha, M. O. (2009) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756360802610761 · Cited by 160 · cited 1× · see citing works
“Alpha-amylase, α-glucosidase and DPP-4 enzyme inhibition assays were conducted on Enzogenol® based on previous studies but with some modifications [24,25].”
MethodZhang, L., Hogan, S. P., Li, J., Sun, S., Canning, C., Zheng, S. J., & Zhou, K. (2010) · Food Chemistry · doi:10.1016/j.foodchem.2010.11.016 · Cited by 137 · see citing works
Schäfer, A., & Högger, P. (2007) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2006.10.011 · Cited by 136 · see citing works
13C-breath tests: Current state of the art and future directions
Braden, B., Lembcke, B., Küker, W., & Caspary, W. F. (2007) · Digestive and Liver Disease · doi:10.1016/j.dld.2007.06.012 · Cited by 127 · see citing works
Tao, W., Zhang, Y., Shen, X., Cao, Y., Shi, J., Ye, X., & Chen, S. (2019) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12444 · Cited by 123 · see citing works
Satoh, T. K., Igarashi, M., Yamada, S., Takahashi, N., & Watanabe, K. (2014) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2014.12.009 · Cited by 122 · see citing works
Heacock, P. M., Hertzler, S. R., Williams, J. A. S., & Wolf, B. W. (2005) · Journal of the American Dietetic Association · doi:10.1016/j.jada.2004.11.001 · Cited by 106 · cited 1× · see citing works
“The inhibition of Enzogenol® on α-amylase and α-glucosidase could be verified in hydrogen tests [45] and 13C breath tests [46–48] in humans after a mixed meal to quantify degree of carbohydrate malabsorption.”
BackgroundThe α-Glucosidase and α-Amylase Enzyme Inhibitory of Hydroxytyrosol and Oleuropein
Hadrich, F., Bouallagui, Z., Han, J., Isoda, H., & Sayadi, S. (2015) · Journal of Oleo Science · doi:10.5650/jos.ess15026 · Cited by 81 · see citing works
Natural phenolic compounds potentiate hypoglycemia via inhibition of Dipeptidyl peptidase IV
Huang, P.-K., Lin, S., Chang, C., Tsai, M., Lee, D.-N., & Weng, C. (2019) · Scientific Reports · doi:10.1038/s41598-019-52088-7 · Cited by 76 · see citing works
Pine Bark Extracts: Nutraceutical, Pharmacological, and Toxicological Evaluation
Li, Y., Feng, J., Zhang, X.-L., & Cui, Y. (2015) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.114.220277 · Cited by 64 · cited 1× · see citing works
“Sample Preparation Enzogenol® was prepared using a water-based extraction from the New Zealand Pinus radiata trees [22,23].”
MethodThe Economics of Diabetes Prevention
Herman, W. H. (2011) · Medical Clinics of North America · doi:10.1016/j.mcna.2010.11.010 · Cited by 58 · cited 1× · see citing works
“Preventing or retarding the development of T2D by intervening early at the healthy or prediabetes stage may therefore help to delay or minimise the development of diabetic complications and potentially costly long-term drug therapy [5,6].”
BackgroundRaimundo, A., Félix, F. I. B., Andrade, R., García‐Conesa, M., González‐Sarrías, A., Gilsa-Lopes, J., Ó, D. D., Raimundo, A., Ribeiro, R. T., Rodriguez‐Mateos, A., et al. (2020) · European Journal of Nutrition · doi:10.1007/s00394-020-02189-1 · Cited by 55 · cited 1× · see citing works
“A recent meta-analysis also demonstrated that using natural health products extracted from plants as an adjunct to anti-diabetic pharmacological therapies further improved measures of blood glucose, particularly in the T2D cohort [11].”
BackgroundVazquez-Flores, A. A., Martinez-Gonzalez, A. I., ́Álvarez-Parrilla, E., Díaz‐Sánchez, Á. G., la Rosa, L. A. D., González-Aguilar, G. A., & Aguilar, C. N. (2018) · Journal of Food Science · doi:10.1111/1750-3841.14386 · Cited by 51 · cited 1× · see citing works
“Small oligomers of proanthocyanidin may be responsible for the interaction with enzyme proteins in specific active binding cavities during digestion [27].”
BackgroundProduction, composition and toxicology studies of Enzogenol® Pinus radiata bark extract
Frevel, M. A. E., Pipingas, A., Grigsby, W. J., Frampton, C. M., & Gilchrist, N. L. (2012) · Food and Chemical Toxicology · doi:10.1016/j.fct.2012.08.051 · Cited by 36 · see citing works
Józefczuk, J., Malikowska, K., Glapa-Nowak, A., Stawińska-Witoszyńska, B., Nowak, J. K., Bajerska, J., Lisowska, A., & Walkowiak, J. (2017) · Advances in Medical Sciences · doi:10.1016/j.advms.2017.03.002 · Cited by 33 · see citing works
The use of stable isotopes in the study of human pathophysiology
Charidemou, E., Ashmore, T., & Griffin, J. L. (2017) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.07.012 · Cited by 32 · see citing works
Lin, S., Chang, C., Tsai, M., Cheng, H., Chen, J.-C., Leong, M. K., & Weng, C. (2019) · Therapeutic Advances in Chronic Disease · doi:10.1177/2040622319875305 · Cited by 29 · see citing works
Prevention of diabetes: a strategic approach for individual patients
Shin, J., Lee, J., Kim, H., Choi, Y., Cho, J., & Yoon, K. (2012) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.2357 · Cited by 22 · cited 1× · see citing works
“Preventing or retarding the development of T2D by intervening early at the healthy or prediabetes stage may therefore help to delay or minimise the development of diabetic complications and potentially costly long-term drug therapy [5,6].”
BackgroundSaburi, W., Rachi-Otsuka, H., Hondoh, H., Okuyama, M., Mori, H., & Kimura, A. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.02.023 · Cited by 19 · cited 1× · see citing works
“The present study utilised yeast αglucosidase that is not precisely biologically similar to mammalian α-glucosidase [13,37].”
MethodLim, W. X. J., Chepulis, L. M., von Hurst, P. R., Gammon, C. S., & Page, R. (2020) · Nutrients · doi:10.3390/nu12020497 · Cited by 9 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Nakashima, Y., Yamamoto, N., Tsukioka, R., Sugawa, H., Ohshima, R., Aoki, K., Hibi, T., Onuki, K., Fukuchi, Y., Yasuda, S., et al. (2022) · Food Bioscience · doi:10.1016/j.fbio.2022.102051 · Cited by 15 · see citing works
Madhavi, B. G. K., Wijethunga, A. M., Okagu, O. D., & Sun, X. (2024) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.4c06539 · Cited by 5 · see citing works
Khaliq, M., Noor, Z., Moazzam, M., Saeed, F., Tul-Zohra, K., Tariq, E., Muhammad Shahbaz, H., & Khaliq, K. (2026) · Annals of Medicine · doi:10.1080/07853890.2026.2637282 · Cited by 4 · see citing works
“A common antidiabetic strategy involves inhibiting α-amylase and α-glucosidase, enzymes that break down complex carbohydrates into glucose, thus delaying starch breakdown, glucose absorption and reducing postprandial blood glucose spikes [89].”
Shirkhan, F., Mirdamadi, S., Mirzaei, M., Akbari‐adergani, B., & Nasoohi, N. (2025) · Journal of Diabetes & Metabolic Disorders · doi:10.1007/s40200-025-01610-y · Cited by 3 · see citing works
“%) against different concentrations of prebiotics [28].”
Fucile, M., Lupia, C., Armentano, M., Marrelli, M., Zicarelli, L., Toma, C.-C., Statti, G. A., & Conforti, F. (2025) · Plants · doi:10.3390/plants14060851 · Cited by 2 · see citing works
Punyauppa-path, S., Taesuk, N., Maneerat, S., Najomtien, P., Kiatprasert, P., Kanchanarach, W., Kanpipit, N., & Phupaboon, S. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27104256 · Cited by 1 · see citing works
“…a dose-dependent activity versus concentration graph, in which data points for both standards at five distinct concentrations were fitted into a non-linear sigmoid curve, reflecting the non-linear concentration dependence of enzyme-inhibitor interactions at both low and high concentrations [38].”
Kishan, H., Choudhary, M., Sharma, S., Bamrah, P. K., & Choudhary, N. (2023) · Current Enzyme Inhibition · doi:10.2174/1573408019666230912123312
Lungu, C., Mihai, C. T., Vochița, G., Gherghel, D., Mangalagiu, I. I., Gafton, M., Miron, S. D., Tincu, C.-E., Nahar, L., Sarker, S. D., et al. (2025) · Plants · doi:10.3390/plants14101459
“Ait. bark [29 Enzogenol ® produced from Pinus radiata D. Don bark [30], and Abigenol ® bark [29], En-zogenol ® produced from Pinus radiata D. Don bark [30], and Abigenol ® originating from Abies alba Mill. originating from Abies alba Mill. bark [31].”
Lim, W. X. J., Page, R., Gammon, C. S., & Moughan, P. J. (2025) · Nutrients · doi:10.3390/nu17142277
Self-citationAkın, N., Demir, S., Çadır, M., İlhan, İ. Ö., & Ogan, A. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.152354
QiuruTan, Yang, Z., Mo, Y., Zhang, T., Wang, J., Xia, L., Chen, L., Ma, Y., & Wang, W. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.149341
Tanyitiku, M. N., & Petcheu, I. C. N. (2026) · International Journal of Food Science · doi:10.1155/ijfo/5948823
Kiatprasert, P., Punyauppa-path, S., Taesuk, N., Maneerat, S., Kanchanarach, W., Najomtien, P., & Phupaboon, S. (2026) · Life · doi:10.3390/life16081385
Nature-Derived DPP-4 Inhibitors: A Promising Alternative for Management of Diabetes Mellitus
Chakraborty, R. (2026) · Revista Brasileira de Farmacognosia · doi:10.1007/s43450-026-00810-8
Aldayel, M. F., Aljarba, N. H., Al‐Otaibi, W. A., AlMotwaa, S. M., & Soliman, M. K. Y. (2026) · Nanotechnology Reviews · doi:10.1515/ntrev-2025-0394
- Authors
- Lim, W. X. J., Gammon, C. S., von Hurst, P., Chepulis, L., & Page, R. A.
- Affiliations
- Riddet Institute (NZ)
- Massey University (NZ)
- School of Sport, Exercise and Nutrition, Massey University, Auckland 0632, New Zealand
- University of Waikato (NZ)
- Corresponding author
- Page, Rachel A.
- Venue
- Nutrients
- Publisher
- MDPI AG
- Published
- 2022-04-12
- Volume
- 14
- Issue
- 8
- Pages
- 1596
- ISSN
- 2072-6643 (ISSN-L)
- PMC
- PMC9029645
- OpenAlex
- W4223986530
- Cited by
- 15
- References
- 46
- Citations by year
- 2026: 7 · 2025: 5 · 2024: 1 · 2023: 1 · 2022: 1
- FWCI
- 1.48
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Nutrients (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Massey Research Online (Massey University) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Callaghan Innovation
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Natural Antidiabetic Agents Studies
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes Treatment and Management
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bioactive natural compounds
- Keywords
- α-amylase inhibition, α-glucosidase inhibition, DPP-4 inhibition, postprandial glycaemia, hypoglycemic effect, incretin effect, carbohydrate digestion, type 2 diabetes, enzyme inhibition
- MeSH terms
- alpha-Amylases, alpha-Glucosidases, Diabetes Mellitus, Type 2, Flavonoids, Humans, New Zealand, Plant Extracts, Quercetin, Plant Bark, Pinus, Dipeptidyl-Peptidase IV Inhibitors, Glycoside Hydrolase Inhibitors
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