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
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.
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?
PDH is a ubiquitously expressed enzyme complex that catalyzes the conversion of pyruvate to acetyl-CoA, acting as a central node that links lipid metabolism, glucose metabolism, and the tricarboxylic acid cycle.
“PDH is a ubiquitously expressed enzyme complex that catalyzes the conversion of pyruvate to acetyl-CoA,48,49 acting as a central node that links lipid metabolism, glucose metabolism, and the tricarboxylic acid cycle.”
From (Pro)renin Receptor Inhibition Reprograms Hepatic Lipid Metabolism and Protects Mice From Diet-Induced Obesity and Hepatosteatosis (2018) · cites this paper as [48]
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
Fan, J., Shan, C., Kang, H.-B., Elf, S., Xie, J., Tucker, M., Gu, T.-L., Aguiar, M., Lonning, S., Chen, H., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.026 · Cited by 305
Flagged first, then by citations
Research works printed but not linked: 96
- 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
- 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
- Patel, 1990, Molecular biology and biochemistry of pyruvate dehydrogenase complexes, FASEB J, 4, 3224, 10.1096/fasebj.4.14.2227213 · DOI
- Patel, 2003, The biochemistry of the pyruvate dehydrogenase complex, Biochem. Mol. Biol. Educ, 31, 5, 10.1002/bmb.2003.494031010156 · DOI
- Korotchkina, 2006, Characterization of testis-specific isoenzyme of human pyruvate dehydrogenase, J. Biol. Chem, 281, 9688, 10.1074/jbc.M511481200 · DOI
- 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
- Patel, 2006, Regulation of pyruvate dehydrogenase complex, Biochem. Soc. Trans, 34, 217, 10.1042/BST0340217 · DOI
- Patel, 1995, Mammalian α-keto acid dehydrogenase complexes: gene regulation and genetic defects, FASEB J, 9, 1164, 10.1096/fasebj.9.12.7672509 · DOI
- 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
- 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
- Jeoung, 2014, Regulation of pyruvate metabolism in metabolic-related diseases, Rev. Endocr. Metab. Disord, 15, 99, 10.1007/s11154-013-9284-2 · DOI
- 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
- Kaplon, 2013, A key role for mitochondrial gatekeeper pyruvate dehydrogenase in oncogene-induced senescence, Nature, 498, 109, 10.1038/nature12154 · DOI · Paper page
- Sutendra, 2013, Pyruvate dehydrogenase kinase as a novel therapeutic target in oncology, Front. Oncol, 3, 38, 10.3389/fonc.2013.00038 · DOI
- Gudi, 1995, Diversity of the pyruvate dehydrogenase kinase gene family in humans, J. Biol. Chem, 270, 28989, 10.1074/jbc.270.48.28989 · DOI
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Reed, 1990, Structure-function relationships in dihydrolipoamide acyltransferases, J. Biol. Chem, 265, 8971, 10.1016/S0021-9258(19)38795-2 · DOI
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Kern, 1997, How thiamine diphosphate is activated in enzymes, Science, 275, 67, 10.1126/science.275.5296.67 · DOI
- 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
- 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
- Schellenberger, 1998, Sixty years of thiamin diphosphate biochemistry, Biochim. Biophys. Acta, 1385, 177, 10.1016/S0167-4838(98)00067-3 · DOI
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Tittmann, 2003, NMR analysis of covalent intermediates in thiamin diphosphate enzymes, Biochemistry, 42, 7885, 10.1021/bi034465o · DOI
- 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
- 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
- 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
- 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
- Jordan, 2005, Multiple modes of active center communication in thiamin diphosphate-dependent enzymes, Acc. Chem. Res, 38, 755, 10.1021/ar040244e · DOI
- 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
- 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
- Frank, 2004, A molecular switch and proton wire synchronize the active sites in thiamin enzymes, Science, 306, 872, 10.1126/science.1101030 · DOI
- Jordan, 2004, How active sites communicate in thiamine enzymes, Science, 306, 818, 10.1126/science.1105457 · DOI
- 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
- 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
- Kolobova, 2001, Regulation of pyruvate dehydrogenase activity through phosphorylation at multiple sites, Biochem. J, 358, 69, 10.1042/bj3580069 · DOI
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Reed, 1951, Crystalline α-lipoic acid: a catalytic agent associated with pyruvate dehydrogenase, Science, 114, 93, 10.1126/science.114.2952.93 · DOI
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
Hughes, E. R., Winter, M. G., Duerkop, B. A., Spiga, L., Furtado de Carvalho, T., Zhu, W., Gillis, C. C., Büttner, L., Smoot, M. P., Behrendt, C. L., et al. (2017) · Cell Host & Microbe · doi:10.1016/j.chom.2017.01.005 · Cited by 353
Neufeld-Cohen, A., Robles, M. S., Aviram, R., Manella, G., Adamovich, Y., Ladeuix, B., Nir, D., Rousso-Noori, L., Kuperman, Y., Golik, M., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1519650113 · Cited by 262
Yucel, N., Wang, Y. X., Mai, T., Porpiglia, E., Lund, P. J., Markov, G., Garcia, B. A., Bendall, S. C., Angelo, M., & Blau, H. M. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.05.092 · Cited by 159
Glucocorticoid resistance as a major drive in sepsis pathology
Dendoncker, K., & Libert, C. (2017) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2017.04.002 · Cited by 85
Ren, L., Sun, Y., Lu, H., Ye, D., Han, L., Wang, N., Daugherty, A., Li, F., Wang, M., Su, F., et al. (2018) · Circulation Research · doi:10.1161/circresaha.117.312422 · Cited by 59
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
- Licence
- 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