Cited by 674

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

The Pyruvate Dehydrogenase Complexes: Structure-based Function and Regulation

Patel, Mulchand S., Nemeria, Natalia S., Furey, William, Jordan, Frank·2014·Journal of Biological Chemistry

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1074/jbc.r114.563148

Cites

1 of 1 references verified0 citation errors · 0 not checkable

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.

A few free checks a day · papers already verified open instantly · results are public

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?

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

Flagged first, then by citations

Research works printed but not linked: 96

  1. Reed, 2001, A trial of research from lipoic acid to α-keto acid dehydrogenase complexes, J. Biol. Chem, 276, 38329, 10.1074/jbc.R100026200 · DOI
  2. Perham, 1991, Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: a paradigm in the design of a multifunctional protein, Biochemistry, 30, 8501, 10.1021/bi00099a001 · DOI
  3. Patel, 1990, Molecular biology and biochemistry of pyruvate dehydrogenase complexes, FASEB J, 4, 3224, 10.1096/fasebj.4.14.2227213 · DOI
  4. Patel, 2003, The biochemistry of the pyruvate dehydrogenase complex, Biochem. Mol. Biol. Educ, 31, 5, 10.1002/bmb.2003.494031010156 · DOI
  5. Korotchkina, 2006, Characterization of testis-specific isoenzyme of human pyruvate dehydrogenase, J. Biol. Chem, 281, 9688, 10.1074/jbc.M511481200 · DOI
  6. Harris, 2002, Regulation of the activity of the pyruvate dehydrogenase complex, Adv. Enzyme Regul, 42, 249, 10.1016/S0065-2571(01)00061-9 · DOI · Paper page
  7. Patel, 2006, Regulation of pyruvate dehydrogenase complex, Biochem. Soc. Trans, 34, 217, 10.1042/BST0340217 · DOI
  8. Patel, 1995, Mammalian α-keto acid dehydrogenase complexes: gene regulation and genetic defects, FASEB J, 9, 1164, 10.1096/fasebj.9.12.7672509 · DOI
  9. Imbard, 2011, Molecular characterization of 82 patients with pyruvate dehydrogenase complex deficiency. Structural implications of novel amino acid substitutions in E1 protein, Mol. Gen. Metab, 104, 507, 10.1016/j.ymgme.2011.08.008 · DOI
  10. Patel, 2012, The spectrum of pyruvate dehydrogenase complex deficiency: clinical, biochemical and genetic features in 371 patients, Mol. Genet. Metab, 106, 385, 10.1016/j.ymgme.2012.03.017 · DOI
  11. Jeoung, 2014, Regulation of pyruvate metabolism in metabolic-related diseases, Rev. Endocr. Metab. Disord, 15, 99, 10.1007/s11154-013-9284-2 · DOI
  12. Schulze, 2011, Flicking the Warburg switch-tyrosine phosphorylation of pyruvate dehydrogenase kinase regulates mitochondrial activity in cancer cells, Mol. Cell, 44, 846, 10.1016/j.molcel.2011.12.004 · DOI
  13. Kaplon, 2013, A key role for mitochondrial gatekeeper pyruvate dehydrogenase in oncogene-induced senescence, Nature, 498, 109, 10.1038/nature12154 · DOI · Paper page
  14. Sutendra, 2013, Pyruvate dehydrogenase kinase as a novel therapeutic target in oncology, Front. Oncol, 3, 38, 10.3389/fonc.2013.00038 · DOI
  15. Gudi, 1995, Diversity of the pyruvate dehydrogenase kinase gene family in humans, J. Biol. Chem, 270, 28989, 10.1074/jbc.270.48.28989 · DOI
  16. Roche, 2001, Distinct regulatory properties of pyruvate dehydrogenase kinase and phosphatase isoforms, Prog. Nucleic Acid Res. Mol. Biol, 70, 33, 10.1016/S0079-6603(01)70013-X · DOI
  17. Roche, 2003, Essential roles of lipoyl domains in the activated function and control of pyruvate dehydrogenase kinases and phosphatase isoform 1, Eur. J. Biochem, 270, 1050, 10.1046/j.1432-1033.2003.03468.x · DOI
  18. Huang, 1998, Isoenzymes of pyruvate dehydrogenase phosphatase: DNA-derived amino acid sequences, expression, and regulation, J. Biol. Chem, 273, 17680, 10.1074/jbc.273.28.17680 · DOI
  19. Brown, 1990, Pyruvate dehydrogenase E1α subunit genes in the mouse: mapping and comparison with human homologs, Somat. Cell. Mol. Genet, 16, 487, 10.1007/BF01233198 · DOI
  20. Dahl, 1990, A testis-specific form of the human pyruvate dehydrogenase E1α subunit is coded by an intronless gene on chromosome 4, Genomics, 8, 225, 10.1016/0888-7543(90)90275-Y · DOI
  21. De Marcucci, 1985, Component X. An immunologically distinct polypeptide associated with mammalian pyruvate dehydrogenase multi-enzyme complex, Eur. J. Biochem, 149, 641, 10.1111/j.1432-1033.1985.tb08972.x · DOI
  22. Jilka, 1986, Properties of a newly characterized protein of the bovine kidney pyruvate dehydrogenase complex, J. Biol. Chem, 261, 1858, 10.1016/S0021-9258(17)36021-0 · DOI
  23. Harris, 1997, Dihydrolipoamide-binding protein of the human pyruvate dehydrogenase complex: DNA-derived amino acid sequence, expression, and reconstitution of the pyruvate dehydrogenase complex, J. Biol. Chem, 272, 19746, 10.1074/jbc.272.32.19746 · DOI
  24. Chen, 1996, Activation function of the pyruvate dehydrogenase phosphatase through Ca2+-facilitated binding to the inner lipoyl domain of the dihydrolipoyl acetyltransferase, J. Biol. Chem, 271, 28064, 10.1074/jbc.271.45.28064 · DOI
  25. Reed, 1990, Structure-function relationships in dihydrolipoamide acyltransferases, J. Biol. Chem, 265, 8971, 10.1016/S0021-9258(19)38795-2 · DOI
  26. Perham, 2000, Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions, Annu. Rev. Biochem, 69, 961, 10.1146/annurev.biochem.69.1.961 · DOI
  27. Sanderson, 1996, Stoichiometry, organization and catalytic function of protein X of the pyruvate dehydrogenase complex from bovine heart, Eur. J. Biochem, 236, 68, 10.1111/j.1432-1033.1996.00068.x · DOI
  28. Hiromasa, 2004, Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and their capacities to bind the E1 and E3 components, J. Biol. Chem, 279, 6921, 10.1074/jbc.M308172200 · DOI
  29. Brautigam, 2009, Subunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complex, J. Biol. Chem, 284, 13086, 10.1074/jbc.M806563200 · DOI · Paper page
  30. Vijayakrishnan, 2010, Solution structure and characterization of the human pyruvate dehydrogenase complex core assembly, J. Mol. Biol, 399, 71, 10.1016/j.jmb.2010.03.043 · DOI
  31. Ciszak, 2003, Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase, J. Biol. Chem, 278, 21240, 10.1074/jbc.M300339200 · DOI
  32. Brautigam, 2005, Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations, J. Mol. Biol, 350, 543, 10.1016/j.jmb.2005.05.014 · DOI
  33. Ciszak, 2006, How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex, J. Biol. Chem, 281, 648, 10.1074/jbc.M507850200 · DOI
  34. Brautigam, 2006, Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex, Structure, 14, 611, 10.1016/j.str.2006.01.001 · DOI
  35. Seifert, 2007, Phosphorylation of serine 264 impedes active site accessibility in the E1 component of the human pyruvate dehydrogenase multienzyme complex, Biochemistry, 46, 6277, 10.1021/bi700083z · DOI
  36. Arjunan, 2002, Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 Å resolution, Biochemistry, 41, 5213, 10.1021/bi0118557 · DOI
  37. Arjunan, 2004, Structural determinants of enzyme binding affinity: the E1 component of pyruvate dehydrogenase from Escherichia coli in complex with the inhibitor thiamin thiazolone diphosphate, Biochemistry, 43, 2405, 10.1021/bi030200y · DOI
  38. Arjunan, 2006, A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct, J. Biol. Chem, 281, 15296, 10.1074/jbc.M600656200 · DOI
  39. Chandrasekhar, 2013, Insight to the interaction of the dihydrolipoamide acetyltransferase (E2) core with the peripheral components in the Escherichia coli pyruvate dehydrogenase complex via multifaceted structural approaches, J. Biol. Chem, 288, 15402, 10.1074/jbc.M113.466789 · DOI
  40. Yu, 2008, Structures of the human pyruvate dehydrogenase complex cores: a highly conserved catalytic center with flexible N-terminal domains, Structure, 16, 104, 10.1016/j.str.2007.10.024 · DOI
  41. Kern, 1997, How thiamine diphosphate is activated in enzymes, Science, 275, 67, 10.1126/science.275.5296.67 · DOI
  42. Seifert, 2006, Direct kinetic evidence for half-of-the-sites reactivity in the E1 component of the human pyruvate dehydrogenase multienzyme complex through alternating sites cofactor activation, Biochemistry, 45, 12775, 10.1021/bi061582l · DOI
  43. Nemeria, 2010, Communication between thiamin cofactors in the Escherichia coli pyruvate dehydrogenase complex E1 component active centers: evidence for direct pathway between the 4′-aminopyrimidine N1′ atoms, J. Biol. Chem, 285, 11197, 10.1074/jbc.M109.069179 · DOI
  44. Schellenberger, 1998, Sixty years of thiamin diphosphate biochemistry, Biochim. Biophys. Acta, 1385, 177, 10.1016/S0167-4838(98)00067-3 · DOI
  45. Jordan, 1978, N1′-Methylthiaminium diiodide: model study on the effect of a coenzyme bound positive charge on reaction mechanisms requiring thiamin pyrophosphate, J. Am. Chem. Soc, 100, 2534, 10.1021/ja00476a043 · DOI
  46. Jordan, 2002, Spectroscopic evidence for participation of the 1′,4′-imino tautomeric diphosphate in catalysis by yeast pyruvate decarboxylase, Bioorg. Chem, 30, 188, 10.1006/bioo.2002.1249 · DOI
  47. Jordan, 1982, Role of the aminopyrimidine ring in thiamin-catalyzed reactions: II. Proton NMR evidence for high barriers to amino group rotation in 4-aminopyrimidines, including thiamin, at low pH in water, J. Org. Chem, 47, 2748, 10.1021/jo00135a012 · DOI
  48. Nemeria, 2007, Elucidation of the chemistry of enzyme-bound thiamin diphosphate prior to substrate binding: defining internal equilibria among tautomeric and ionization states, Biochemistry, 46, 10739, 10.1021/bi700838q · DOI
  49. Nemeria, 2007, The 1′,4′-iminopyrimidine tautomer of thiamin diphosphate is poised for catalysis in asymmetric active centers on enzymes, Proc. Natl. Acad. Sci. U.S.A, 104, 78, 10.1073/pnas.0609973104 · DOI
  50. Nemeria, 2009, Reaction mechanisms of thiamin diphosphate enzymes: defining states of ionization and tautomerization of the cofactor at individual steps, FEBS J, 276, 2432, 10.1111/j.1742-4658.2009.06964.x · DOI
  51. Jordan, 2003, Dual catalytic apparatus of the thiamin diphosphate coenzyme: acid-base via the 1′,4′-iminopyrimidine tautomer along with its electrophilic role, J. Am. Chem. Soc, 125, 12732, 10.1021/ja0346126 · DOI
  52. Nemeria, 2004, Tetrahedral intermediates in thiamin diphosphate-dependent decarboxylations exist as a 1′,4′-imino tautomeric form of the coenzyme, unlike the Michaelis complex or the free coenzyme, Biochemistry, 43, 6565, 10.1021/bi049549r · DOI
  53. Baykal, 2006, Electronic and nuclear magnetic resonance spectroscopic features of the 1′,4′-iminopyrimidine tautomeric form of thiamin diphosphate, a novel intermediate on enzymes requiring this coenzyme, Biochemistry, 45, 7522, 10.1021/bi060395k · DOI
  54. Tittmann, 2003, NMR analysis of covalent intermediates in thiamin diphosphate enzymes, Biochemistry, 42, 7885, 10.1021/bi034465o · DOI
  55. Balakrishnan, 2012, Determination of pre-steady-state rate constants on the Escherichia coli pyruvate dehydrogenase complex reveals that loop movement controls the rate-limiting step, J. Am. Chem. Soc, 134, 18644, 10.1021/ja3062375 · DOI
  56. Flournoy, 1986, Pyruvate dehydrogenase and 3-fluoropyruvate: chemical competence of 2-acetylthiamin pyrophosphate as an acetyl group donor to dihydrolipoamide, Biochemistry, 25, 6036, 10.1021/bi00368a030 · DOI
  57. Gruys, 1989, 2-Acetylthiamin pyrophosphate (acetyl-TPP) pH-rate for hydrolysis of acetyl-TPP and isolation of acetyl-TPP as a transient species in pyruvate dehydrogenase catalyzed reactions, Biochemistry, 28, 9071, 10.1021/bi00449a018 · DOI
  58. Patel, 2014, Identification of charge transfer transitions related to thiamin-bound intermediates on enzymes provides a plethora of a signatures useful in mechanistic studies, Biochemistry, 53, 2145, 10.1021/bi4015743 · DOI
  59. Jordan, 2005, Multiple modes of active center communication in thiamin diphosphate-dependent enzymes, Acc. Chem. Res, 38, 755, 10.1021/ar040244e · DOI
  60. Khailova, 1985, Half-of-the-site reactivity of the decarboxylating component of the pyruvate dehydrogenase complex from pigeon breast muscle with respect to 2-hydroxyethyl thiamin pyrophosphate, Biochem. Int, 11, 509
  61. Nemeria, 2005, Glutamate 636 of the Escherichia coli pyruvate dehydrogenase-E1 participates in active center communication and behaves as an engineered acetolactate synthase with unusual stereoselectivity, J. Biol. Chem, 280, 21473, 10.1074/jbc.M502691200 · DOI
  62. Frank, 2004, A molecular switch and proton wire synchronize the active sites in thiamin enzymes, Science, 306, 872, 10.1126/science.1101030 · DOI
  63. Jordan, 2004, How active sites communicate in thiamine enzymes, Science, 306, 818, 10.1126/science.1105457 · DOI
  64. Reed, 1985, Regulation of mammalian pyruvate α-keto acid dehydrogenase complexes by phosphorylation-dephosphorylation, Curr. Top. Cell Regul, 27, 41, 10.1016/B978-0-12-152827-0.50011-6 · DOI
  65. Korotchkina, 1995, Mutagenesis studies of the phosphorylation sites of recombinant human pyruvate dehydrogenase: site-specific regulation, J. Biol. Chem, 270, 14297, 10.1074/jbc.270.24.14297 · DOI
  66. Kolobova, 2001, Regulation of pyruvate dehydrogenase activity through phosphorylation at multiple sites, Biochem. J, 358, 69, 10.1042/bj3580069 · DOI
  67. Korotchkina, 2001, Probing the mechanism of inactivation of human pyruvate dehydrogenase by phosphorylation of three sites, J. Biol. Chem, 276, 5731, 10.1074/jbc.M007558200 · DOI
  68. Korotchkina, 2001, Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase, J. Biol. Chem, 276, 37223, 10.1074/jbc.M103069200 · DOI · Paper page
  69. Kato, 2008, Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops, Structure, 16, 1849, 10.1016/j.str.2008.10.010 · DOI
  70. Kale, 2007, A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 modulates substrate utilization and chemical communication with E2 component, J. Biol. Chem, 282, 28106, 10.1074/jbc.M704326200 · DOI
  71. Jordan, 2009, Multiple roles of mobile active center loops in the E1 component of the Escherichia coli pyruvate dehydrogenase complex: linkage of protein dynamics to catalysis, J. Mol. Catal. B Enzym, 61, 14, 10.1016/j.molcatb.2009.04.008 · DOI
  72. Kale, 2009, Conformational ensemble modulates cooperativity in the rate-determining catalytic step in the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex, J. Biol. Chem, 284, 33122, 10.1074/jbc.M109.065508 · DOI
  73. Wang, 2014, Structure and function of the catalytic domain of the dihydrolipoyl acetyltransferase component in Escherichia coli pyruvate dehydrogenase complex, J. Biol. Chem, 289, 15215, 10.1074/jbc.M113.544080 · DOI
  74. Frank, 2005, The molecular origins of specificity in the assembly of a multienzyme complex, Structure, 13, 1119, 10.1016/j.str.2005.04.021 · DOI
  75. Patel, 2009, Interaction of E1 and E3 components with the core proteins of the human pyruvate dehydrogenase complex, J. Mol. Catal. B Enzym, 61, 2, 10.1016/j.molcatb.2009.05.001 · DOI
  76. Park, 2004, Amino-terminal residues 1–45 of the Escherichia coli pyruvate dehydrogenase complex E1 subunit interact with the E2 subunit and are required for activity of the complex but not for reductive acetylation of the E2 subunit, Biochemistry, 43, 14037, 10.1021/bi049027b · DOI
  77. Song, 2010, Nuclear magnetic resonance evidence for the role of the flexible regions of the E1 component of the pyruvate dehydrogenase complex from Gram-negative bacteria, J. Biol. Chem, 285, 4680, 10.1074/jbc.M109.082842 · DOI
  78. Park, 2010, Characterization of interactions of dihydrolipoamide dehydrogenase with its binding protein in the human pyruvate dehydrogenase complex, Biochem. Biophys. Res. Commun, 395, 416, 10.1016/j.bbrc.2010.04.038 · DOI
  79. Nakai, 2008, Structural basis for the specific interactions between the E2 and E3 components of the Thermus thermophilus 2-oxo acid dehydrogenase complexes, J. Biochem, 143, 747, 10.1093/jb/mvn033 · DOI
  80. Mande, 1996, Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase, Structure, 4, 277, 10.1016/S0969-2126(96)00032-9 · DOI
  81. Song, 2012, Interchain acetyl transfer in the E2 component of bacterial pyruvate dehydrogenase suggests a model with different roles for each chain in a trimer of the homooligomeric component, Biochemistry, 51, 2795, 10.1021/bi201614n · DOI
  82. Huang, 2002, Regulation of pyruvate dehydrogenase kinase expression by peroxisome proliferator-activated receptor-α ligands, glucocorticoids, and insulin, Diabetes, 51, 276, 10.2337/diabetes.51.2.276 · DOI
  83. Kwon, 2004, Protein kinase B-α inhibits human pyruvate dehydrogenase kinase-4 gene induction by dexamethasone through inactivation of FOXO transcription factors, Diabetes, 53, 899, 10.2337/diabetes.53.4.899 · DOI
  84. Reed, 1951, Crystalline α-lipoic acid: a catalytic agent associated with pyruvate dehydrogenase, Science, 114, 93, 10.1126/science.114.2952.93 · DOI
  85. Hitosugi, 2011, Tyrosine phosphorylation of mitochondrial pyruvate dehydrogenase kinase 1 is important for cancer metabolism, Mol. Cell, 44, 864, 10.1016/j.molcel.2011.10.015 · DOI
  86. Steussy, 2001, Structure of pyruvate dehydrogenase kinase: novel folding pattern for a serine protein kinase, J. Biol. Chem, 276, 37443, 10.1074/jbc.M104285200 · DOI
  87. Kato, 2005, Crystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complex, EMBO J, 24, 1763, 10.1038/sj.emboj.7600663 · DOI
  88. Tso, 2006, Structural determinants for cross-talk between pyruvate dehydrogenase kinase 3 and lipoyl domain 2 of the human pyruvate dehydrogenase complex, J. Biol. Chem, 281, 27197, 10.1074/jbc.M604339200 · DOI
  89. Devedjiev, 2007, Crystal structure of an asymmetric complex of pyruvate dehydrogenase kinase 3 with lipoyl domain 2 and its biological implications, J. Mol. Biol, 370, 407, 10.1016/j.jmb.2007.04.083 · DOI
  90. Kato, 2007, Distinct structural mechanisms for inhibition of pyruvate dehydrogenase kinase isoforms by AZD7545, dichloroacetate, and radicicol, Structure, 15, 992, 10.1016/j.str.2007.07.001 · DOI
  91. Green, 2008, Structural and functional insights into the molecular mechanisms responsible for the regulation of pyruvate dehydrogenase kinase 2, J. Biol. Chem, 283, 15789, 10.1074/jbc.M800311200 · DOI
  92. Wynn, 2008, Pyruvate dehydrogenase kinase-4 structures reveal a metastable open conformation fostering robust core-free basal activity, J. Biol. Chem, 283, 25305, 10.1074/jbc.M802249200 · DOI
  93. Turkan, 2002, Structural requirements within the lipoyl domain for the Ca2+-dependent binding and activation of pyruvate dehydrogenase phosphatase isoform 1 or its catalytic subunit, J. Biol. Chem, 277, 14976, 10.1074/jbc.M108434200 · DOI
  94. Karpova, 2003, Characterization of the isozymes of pyruvate dehydrogenase phosphatase: implications for the regulation of pyruvate dehydrogenase activity, Biochim. Biophys. Acta, 1652, 126, 10.1016/j.bbapap.2003.08.010 · DOI
  95. Turkan, 2004, Formation of a complex of the catalytic subunit of pyruvate dehydrogenase phosphatase isoform 1 (PDP1c) and the L2 domain forms a Ca2+ binding site and captures PDP1c as a monomer, Biochemistry, 43, 15073, 10.1021/bi048901y · DOI
  96. Vassylyev, 2007, Crystal structure of pyruvate dehydrogenase phosphatase 1 and its functional implications, J. Mol. Biol, 370, 417, 10.1016/j.jmb.2007.05.002 · DOI

Cited by

Sorted by citations

Metadata

Authors
Patel, M. S., Nemeria, N. S., Furey, W., & Jordan, F.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2014-06
Volume
289
Issue
24
Pages
16615-16623
ISSN
0021-9258
Cited by
674
References
1
Language
en
Funders
National Institutes of Health (DK 20478, GM050380, GM061791)

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