The DOI matches its Crossref record.
On the nature of allosteric transitions: A plausible model
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
Cited by
Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
Howitz, K. T., Bitterman, K. J., Cohen, H. Y., Lamming, D. W., Lavu, S., Wood, J. G., Zipkin, R. E., Chung, P., Kisielewski, A., Zhang, L.-L., et al. (2003) · Nature · doi:10.1038/nature01960 · Cited by 3,796
Selforganization of matter and the evolution of biological macromolecules
Eigen, M. (1971) · Die Naturwissenschaften · doi:10.1007/bf00623322 · Cited by 3,788
Intrinsically disordered protein
Dunker, A. K., Lawson, J. D., Brown, C. J., Williams, R. M., Romero, P., Oh, J. S., Oldfield, C. J., Campen, A. M., Ratliff, C. M., Hipps, K. W., et al. (2001) · Journal of Molecular Graphics and Modelling · doi:10.1016/s1093-3263(00)00138-8 · Cited by 2,272
Sensors and regulators of intracellular pH
Casey, J. R., Grinstein, S., & Orlowski, J. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2820 · Cited by 2,218
The role of dynamic conformational ensembles in biomolecular recognition
Boehr, D. D., Nussinov, R., & Wright, P. E. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.232 · Cited by 2,008
Stamler (2001) · doi:10.1016/s0092-8674(01)00495-0 · Cited by 1,261
The ensemble nature of allostery
Motlagh, H. N., Wrabl, J. O., Li, J., & Hilser, V. J. (2014) · Nature · doi:10.1038/nature13001 · Cited by 1,247
Cassidy-Stone, A., Chipuk, J. E., Ingerman, E., Song, C., Yoo, C., Kuwana, T., Kurth, M. J., Shaw, J. T., Hinshaw, J. E., Green, D. R., et al. (2008) · Developmental Cell · doi:10.1016/j.devcel.2007.11.019 · Cited by 1,200
Inositol Trisphosphate Receptor Ca2+Release Channels
Foskett, J. K., White, C., Cheung, K.-H., & Mak, D.-O. D. (2007) · Physiological Reviews · doi:10.1152/physrev.00035.2006 · Cited by 1,188
Design principles of biochemical oscillators
Novák, B., & Tyson, J. J. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2530 · Cited by 1,137
Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions
Oldfield, C. J., & Dunker, A. K. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072711-164947 · Cited by 1,057
The Hill equation revisited: uses and misuses
Weiss, J. N. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.11.9285481 · Cited by 1,000
Structural Symmetry and Protein Function
Goodsell, D. S., & Olson, A. J. (2000) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.29.1.105 · Cited by 950
The logical analysis of continuous, non-linear biochemical control networks
Glass, L., & Kauffman, S. A. (1973) · Journal of Theoretical Biology · doi:10.1016/0022-5193(73)90208-7 · Cited by 940
Csermely, P., Palotai, R., & Nussinov, R. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.009 · Cited by 821
Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
Canagarajah, B. J., Khokhlatchev, A., Cobb, M. H., & Goldsmith, E. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80351-7 · Cited by 729
Acetylcholine Receptor: An Allosteric Protein
Changeux, J.-P., Devillers-Thiéry, A., & Chemouilli, P. (1984) · Science · doi:10.1126/science.6382611 · Cited by 623
Self-citationGlobal dynamics of proteins: bridging between structure and function
Bahar, I., Lezon, T. R., Yang, L.-W., & Eyal, E. (2010) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.093008.131258 · Cited by 610
Protein Allostery and Conformational Dynamics
Guo, J., & Zhou, H.-X. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00590 · Cited by 484
Allostery: Absence of a change in shape does not imply that allostery is not at play
Tsai, C.-J., del Sol, A., & Nussinov, R. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.02.034 · Cited by 453
Muscarinic acetylcholine receptors: novel opportunities for drug development
Kruse, A. C., Kobilka, B. K., Gautam, D., Sexton, P. M., Christopoulos, A., & Wess, J. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4295 · Cited by 437
Hemoglobin S gelation and sickle cell disease
Eaton, W., & Hofrichter, J. (1987) · Blood · doi:10.1182/blood.v70.5.1245.1245 · Cited by 425
Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins
Hilser, V. J., & Thompson, E. B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700329104 · Cited by 406
A Unified View of “How Allostery Works”
Tsai, C.-J., & Nussinov, R. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003394 · Cited by 401
Rollema, H., Coe, J. W., Chambers, L. K., Hurst, R. S., Stahl, S. M., & Williams, K. E. (2007) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2007.05.003 · Cited by 400
Allostery in Its Many Disguises: From Theory to Applications
Wodak, S. J., Paci, E., Dokholyan, N. V., Berezovsky, I. N., Horovitz, A., Li, J., Hilser, V. J., Bahar, I., Karanicolas, J., Stock, G., et al. (2019) · Structure · doi:10.1016/j.str.2019.01.003 · Cited by 404
Self-citationLowry, O. H., Carter, J., Ward, J. B., & Glaser, L. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)34144-4 · Cited by 350
Nucleosome-mediated cooperativity between transcription factors
Mirny, L. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913805107 · Cited by 349
Gladwin, M. T., Raat, N. J. H., Shiva, S., Dezfulian, C., Hogg, N., Kim-Shapiro, D. B., & Patel, R. P. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00407.2006 · Cited by 329
Brain nicotinic receptors: structure and regulation, role in learning and reinforcement
Changeux, J.-P., Bertrand, D., Corringer, P.-J., Dehaene, S., Edelstein, S., Léna, C., Le Novère, N., Marubio, L., Picciotto, M., & Zoli, M. (1998) · Brain Research Reviews · doi:10.1016/s0165-0173(97)00040-4 · Cited by 322
Self-citationHemoglobin: Structure, Function and Allostery
Ahmed, M. H., Ghatge, M. S., & Safo, M. K. (2020) · Subcellular Biochemistry · doi:10.1007/978-3-030-41769-7_14 · Cited by 317
Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulation
Bahar, I., Chennubhotla, C., & Tobi, D. (2007) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.09.011 · Cited by 306
The functional nitrite reductase activity of the heme-globins
Gladwin, M. T., & Kim-Shapiro, D. B. (2008) · Blood · doi:10.1182/blood-2008-01-115261 · Cited by 293
Allostery: An Overview of Its History, Concepts, Methods, and Applications
Liu, J., & Nussinov, R. (2016) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1004966 · Cited by 281
Molecular Determinants of BK Channel Functional Diversity and Functioning
Latorre, R., Castillo, K., Carrasquel-Ursulaez, W., Sepulveda, R. V., Gonzalez-Nilo, F., Gonzalez, C., & Alvarez, O. (2017) · Physiological Reviews · doi:10.1152/physrev.00001.2016 · Cited by 271
On the role of organized multienzyme systems in cellular metabolism: a general synthesis
Welch, G. R. (1978) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(78)90019-6 · Cited by 260
MECHANISTIC ASPECTS OF ENZYMATIC CATALYSIS: Lessons from Comparison of RNA and Protein Enzymes
Narlikar, G. J., & Herschlag, D. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.19 · Cited by 262
Controlling Allosteric Networks in Proteins
Dokholyan, N. V. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00544 · Cited by 260
Treating sickle cell disease by targeting HbS polymerization
Eaton, W. A., & Bunn, H. F. (2017) · Blood · doi:10.1182/blood-2017-02-765891 · Cited by 255
Conformation, co-operativity and ligand binding in human hemoglobin
Cassoly, R., & Gibson, Q. H. (1975) · Journal of Molecular Biology · doi:10.1016/0022-2836(75)90382-4 · Cited by 259
Novel Allosteric Modulators of G Protein-coupled Receptors
Gentry, P. R., Sexton, P. M., & Christopoulos, A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.662759 · Cited by 199
Allostery without a conformational change? Revisiting the paradigm
Nussinov, R., & Tsai, C.-J. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2014.11.005 · Cited by 202
From the stochasticity of molecular processes to the variability of synaptic transmission
Ribrault, C., Sekimoto, K., & Triller, A. (2011) · Nature Reviews Neuroscience · doi:10.1038/nrn3025 · Cited by 198
Ligand binding to proteins: The binding landscape model
Miller, D. W., & Dill, K. A. (1997) · Protein Science · doi:10.1002/pro.5560061011 · Cited by 178
Blair, J. B., Cimbala, M. A., Foster, J. L., & Morgan, R. A. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33408-7 · Cited by 170
Dynamic protein–DNA recognition: beyond what can be seen
Fuxreiter, M., Simon, I., & Bondos, S. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.04.006 · Cited by 167
Protein fluctuations and the thermodynamic uncertainty principle
Cooper, A. (1984) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(84)90008-7 · Cited by 166
Saa, P. A., & Nielsen, L. K. (2017) · Biotechnology Advances · doi:10.1016/j.biotechadv.2017.09.005 · Cited by 166
An allosteric model of circadian KaiC phosphorylation
van Zon, J. S., Lubensky, D. K., Altena, P. R. H., & ten Wolde, P. R. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608665104 · Cited by 161
Baum, B., Muley, L., Smolinski, M., Heine, A., Hangauer, D., & Klebe, G. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.02.007 · Cited by 157
Exploring the role of receptor flexibility in structure-based drug discovery
Feixas, F., Lindert, S., Sinko, W., & McCammon, J. A. (2014) · Biophysical Chemistry · doi:10.1016/j.bpc.2013.10.007 · Cited by 156
A gating mechanism of pentameric ligand-gated ion channels
Calimet, N., Simoes, M., Changeux, J.-P., Karplus, M., Taly, A., & Cecchini, M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1313785110 · Cited by 150
Self-citationLipid agonism: The PIP2 paradigm of ligand-gated ion channels
Hansen, S. B. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2015.01.011 · Cited by 146
Allosteric mechanisms can be distinguished using structural mass spectrometry
Dyachenko, A., Gruber, R., Shimon, L., Horovitz, A., & Sharon, M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1302395110 · Cited by 144
Xiao, Y., Fan, H., Musachio, J. L., Wei, Z.-L., Chellappan, S. K., Kozikowski, A. P., & Kellar, K. J. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.027318 · Cited by 141
Describing sequence–ensemble relationships for intrinsically disordered proteins
Mao, A. H., Lyle, N., & Pappu, R. V. (2013) · Biochemical Journal · doi:10.1042/bj20121346 · Cited by 135
A kinetic mechanism for nicotinic acetylcholine receptors based on multiple allosteric transitions.
Edelstein, S. J., Schaad, O., Henry, E., Bertrand, D., & Changeux, J.-P. (1996) · Biological Cybernetics · doi:10.1007/s004220050302 · Cited by 134
Self-citationPharmacological and Physiological Characterization of Murine Homomeric β3 GABAA Receptors
Wooltorton, J. R. A., Moss, S. J., & Smart, T. G. (1997) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1997.tb01641.x · Cited by 129
An update on the physiological and therapeutic relevance of GPCR oligomers
Farran, B. (2017) · Pharmacological Research · doi:10.1016/j.phrs.2017.01.008 · Cited by 115
Chennubhotla, C., Yang, Z., & Bahar, I. (2008) · Molecular BioSystems · doi:10.1039/b717819k · Cited by 102
Mechanism of action of isocitrate lyase from Pseudomonas indigofera
McFadden, B. A., Williams, J. O., & Roche, T. E. (1971) · Biochemistry · doi:10.1021/bi00784a017 · Cited by 99
Escapement mechanisms and the conversion of disequilibria; the engines of creation
Branscomb, E., Biancalani, T., Goldenfeld, N., & Russell, M. (2017) · Physics Reports · doi:10.1016/j.physrep.2017.02.001 · Cited by 96
Multitarget drugs of plants origin acting on Alzheimer’s disease
Russo, P., Frustaci, A., Del Bufalo, A., Fini, M., & Cesario, A. (2013) · Current Medicinal Chemistry · doi:10.2174/0929867311320130008 · Cited by 88
Optimal design of feedback control by inhibition: Dynamic Considerations
Savageau, M. A. (1975) · Journal of Molecular Evolution · doi:10.1007/bf01741242 · Cited by 86
Steensgaard, D. B., Schluckebier, G., Strauss, H. M., Norrman, M., Thomsen, J. K., Friderichsen, A. V., Havelund, S., & Jonassen, I. (2013) · Biochemistry · doi:10.1021/bi3008609 · Cited by 86
Evaluation of Hill Slopes and Hill Coefficients when the Saturation Binding or Velocity is not Known
ENDRENYI, L., KWONG, F. H. F., & FAJSZI, C. (1975) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1975.tb03931.x · Cited by 85
Greives, N., & Zhou, H.-X. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1407545111 · Cited by 82
Multiplicity of Steady States in Glycolysis and Shift of Metabolic State in Cultured Mammalian Cells
Mulukutla, B. C., Yongky, A., Grimm, S., Daoutidis, P., & Hu, W.-S. (2015) · PLOS ONE · doi:10.1371/journal.pone.0121561 · Cited by 81
Transplanting a unique allosteric effect from crocodile into human haemoglobin
Komiyama, N. H., Miyazaki, G., Tame, J., & Nagai, K. (1995) · Nature · doi:10.1038/373244a0 · Cited by 81
A multi-step, dynamic allosteric model of testosterone's binding to sex hormone binding globulin
Zakharov, M. N., Bhasin, S., Travison, T. G., Xue, R., Ulloor, J., Vasan, R. S., Carter, E., Wu, F., & Jasuja, R. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2014.09.001 · Cited by 81
Two pathways mediate interdomain allosteric regulation in pin1
Guo, J., Pang, X., & Zhou, H.-X. (2015) · Structure · doi:10.1016/j.str.2014.11.009 · Cited by 78
Verkhivker, G. M., Agajanian, S., Hu, G., & Tao, P. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00136 · Cited by 76
Fuxe, K., Marcellino, D., Borroto-Escuela, D. O., Frankowska, M., Ferraro, L., Guidolin, D., Ciruela, F., & Agnati, L. F. (2010) · Journal of Receptors and Signal Transduction · doi:10.3109/10799893.2010.506191 · Cited by 74
Protein flexibility in drug discovery: from theory to computation.
Buonfiglio, R., Recanatini, M., & Masetti, M. (2015) · ChemMedChem · doi:10.1002/cmdc.201500086 · Cited by 73
Di Cera, E. (2020) · Biophysics Reviews · doi:10.1063/5.0020997 · Cited by 73
Eaton, W. A., Henry, E. R., & Hofrichter, J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.10.4472 · Cited by 72
How ATP Inhibits the Open KATP Channel
Craig, T. J., Ashcroft, F. M., & Proks, P. (2008) · The Journal of General Physiology · doi:10.1085/jgp.200709874 · Cited by 67
Henry, E. R., Cellmer, T., Dunkelberger, E. B., Metaferia, B., Hofrichter, J., Li, Q., Ostrowski, D., Ghirlando, R., Louis, J. M., Moutereau, S., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1922004117 · Cited by 65
Allostery: Allosteric Cancer Drivers and Innovative Allosteric Drugs
Nussinov, R., Zhang, M., Maloney, R., Liu, Y., Tsai, C.-J., & Jang, H. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167569 · Cited by 66
The allosteric communication pathways in KIX domain of CBP
Palazzesi, F., Barducci, A., Tollinger, M., & Parrinello, M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1313548110 · Cited by 62
Flechsig, H. (2017) · Biophysical Journal · doi:10.1016/j.bpj.2017.06.043 · Cited by 59
MHC class I limits hippocampal synapse density by inhibiting neuronal insulin receptor signaling
Dixon-Salazar, T. J., Fourgeaud, L., Tyler, C. M., Poole, J. R., Park, J. J., & Boulanger, L. M. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.4642-12.2014 · Cited by 51
ATP Interaction with the Open State of the KATP Channel
Enkvetchakul, D., Loussouarn, G., Makhina, E., & Nichols, C. G. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)76051-1 · Cited by 56
Rowell, P. P., & Duggan, D. S. (1998) · Neuropharmacology · doi:10.1016/s0028-3908(97)00193-7 · Cited by 52
Current Advances in Allosteric Modulation of Muscarinic Receptors
Jakubik, J., & El-Fakahany, E. E. (2020) · Biomolecules · doi:10.3390/biom10020325 · Cited by 48
Local and Global Ligand-Induced Changes in the Structure of the GABAAReceptor
Muroi, Y., Czajkowski, C., & Jackson, M. B. (2006) · Biochemistry · doi:10.1021/bi060222v · Cited by 46
Allosteric conformational ensembles have unlimited capacity for integrating information
Biddle, J. W., Martinez-Corral, R., Wong, F., & Gunawardena, J. (2021) · eLife · doi:10.7554/elife.65498 · Cited by 41
Accurate prediction of protein assembly structure by combining AlphaFold and symmetrical docking
Jeppesen, M., & André, I. (2023) · Nature Communications · doi:10.1038/s41467-023-43681-6 · Cited by 44
Physiology of the sweet taste.
Faurion, A. (1987) · Progress in Sensory Physiology · doi:10.1007/978-3-642-71060-5_3 · Cited by 37
Changeux, J.-P. (2006) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2006.1832 · Cited by 31
Self-citationNamanja, A. T., Wang, J., Buettner, R., Colson, L., & Chen, Y. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.01.003 · Cited by 31
Oxidation of hemoglobin and myoglobin by alkyl nitrites inhibition by oxygen.
Doyle, M. P., LePoire, D. M., & Pickering, R. A. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43286-3 · Cited by 29
Are there physicochemical differences between allosteric and competitive ligands?
Smith, R. D., Lu, J., & Carlson, H. A. (2017) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1005813 · Cited by 27
Emergences of supramolecular chemistry: from supramolecular chemistry to supramolecular science
Vicens, J., & Vicens, Q. (2011) · Journal of Inclusion Phenomena and Macrocyclic Chemistry · doi:10.1007/s10847-011-0001-z · Cited by 27
Can You Hear Me Now? Regulating Transcriptional Activators by Phosphorylation
Gardner, K. H., & Montminy, M. (2005) · Science's STKE · doi:10.1126/stke.3012005pe44 · Cited by 25
Heusser, S. A., Lycksell, M., Wang, X., McComas, S. E., Howard, R. J., & Lindahl, E. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1809650115 · Cited by 23
Guo, H.-B., Varaljay, V. A., Kedziora, G., Taylor, K., Farajollahi, S., Lombardo, N., Harper, E., Hung, C., Gross, M., Perminov, A., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-30310-x · Cited by 22
Connection between the Bacterial Chemotactic Network and Optimal Filtering
Nakamura, K., & Kobayashi, T. J. (2021) · Physical Review Letters · doi:10.1103/physrevlett.126.128102 · Cited by 19
The conformational landscape of fold-switcher KaiB is tuned to the circadian rhythm timescale
Wayment-Steele, H. K., Otten, R., Pitsawong, W., Ojoawo, A. M., Glaser, A., Calderone, L. A., & Kern, D. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2412293121 · Cited by 19
Flexible backbone assembly and refinement of symmetrical homomeric complexes
Roy Burman, S. S., Yovanno, R. A., & Gray, J. J. (2019) · Structure · doi:10.1016/j.str.2019.03.014 · Cited by 18
Metadata
- Authors
- Monod, J., Wyman, J., & Changeux, J.-P.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1965-05
- Volume
- 12
- Issue
- 1
- Pages
- 88-118
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W1998093640
- Cited by
- 8,825
- References
- 0
- FWCI
- 91.59
- Type
- journal article
- Language
- en
- Open access
- closed
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.