Global dynamics of proteins: bridging between structure and function
Open accessAbstract
Biomolecular systems possess unique, structure-encoded dynamic properties that underlie their biological functions. Recent studies indicate that these dynamic properties are determined to a large extent by the topology of native contacts. In recent years, elastic network models used in conjunction with normal mode analyses have proven to be useful for elucidating the collective dynamics intrinsically accessible under native state conditions, including in particular the global modes of motions that are robustly defined by the overall architecture. With increasing availability of structural data for well-studied proteins in different forms (liganded, complexed, or free), there is increasing evidence in support of the correspondence between functional changes in structures observed in experiments and the global motions predicted by these coarse-grained analyses. These observed correlations suggest that computational methods may be advantageously employed for assessing functional changes in structure and allosteric mechanisms intrinsically favored by the native fold.
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?
The conformational changes of proteins elicited by ligand binding closely overlap with one or more of the soft modes accessible in the unbound form.
“Applying ENMs to several systems showed that the conformational changes of proteins elicited by ligand binding closely overlap with one or more of the soft modes accessible in the unbound form (Bahar et al., 2010; Tobi and Bahar, 2005)”
From Allostery in Its Many Disguises: From Theory to Applications (2019) · cites this paper as Bahar et al., 2010
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
CHARMM: The biomolecular simulation program
Brooks, B. R., Brooks, C. L., MacKerell, A. D., Nilsson, L., Petrella, R. J., Roux, B., Won, Y., Archontis, G., Bartels, C., Boresch, S., et al. (2009) · Journal of Computational Chemistry · doi:10.1002/jcc.21287 · Cited by 8,994 · see citing works
ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.
Monod, J., Wyman, J., & Changeux, J. (1965) · Journal of Molecular Biology · doi:10.1016/s0022-2836(65)80285-6 · Cited by 7,681 · see citing works
[26] Raster3D: Photorealistic molecular graphics
Merritt, E. A., & Bacon, D. (1997) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(97)77028-9 · Cited by 3,749 · see citing works
Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits *
Koshland, D. E., Némethy, G., & Filmer, D. (1966) · Biochemistry · doi:10.1021/bi00865a047 · Cited by 3,019 · see citing works
Dynamic personalities of proteins
Henzler-Wildman, K., & Kern, D. (2007) · Nature · doi:10.1038/nature06522 · Cited by 2,545 · see citing works
Coifman, R. R., Lafon, S., Lee, A. B., Maggioni, M., Nadler, B., Warner, F., & Zucker, S. W. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500334102 · Cited by 1,675 · see citing works
Anisotropy of Fluctuation Dynamics of Proteins with an Elastic Network Model
Atılgan, A. R., Durell, S. R., Jernigan, R. L., Demirel, M. C., Keskin, Ö., & Bahar, İ. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)76033-x · Cited by 1,638 · see citing works
Self-citationLarge Amplitude Elastic Motions in Proteins from a Single-Parameter, Atomic Analysis
Tirion, M. M. (1996) · Physical Review Letters · doi:10.1103/physrevlett.77.1905 · Cited by 1,617 · see citing works
Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential
Bahar, İ., Atılgan, A. R., & Erman, B. (1997) · Folding and Design · doi:10.1016/s1359-0278(97)00024-2 · Cited by 1,377 · see citing works
Self-citationProtein Dynamism and Evolvability
Tokuriki, N., & Tawfik, D. S. (2009) · Science · doi:10.1126/science.1169375 · Cited by 932 · see citing works
Conformational change of proteins arising from normal mode calculations
Tama, F., & Sanejouand, Y. (2001) · Protein Engineering Design and Selection · doi:10.1093/protein/14.1.1 · Cited by 895 · see citing works
Harmonic dynamics of proteins: normal modes and fluctuations in bovine pancreatic trypsin inhibitor.
Brooks, B., & Karplus, M. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.21.6571 · Cited by 832 · see citing works
Gaussian Dynamics of Folded Proteins
Haliloǧlu, T., Bahar, İ., & Erman, B. (1997) · Physical Review Letters · doi:10.1103/physrevlett.79.3090 · Cited by 761 · see citing works
Self-citationAllosteric Mechanisms of Signal Transduction
Changeux, J., & Edelstein, S. J. (2005) · Science · doi:10.1126/science.1108595 · Cited by 744 · see citing works
Coarse-grained normal mode analysis in structural biology
Bahar, İ., & Rader, A. J. (2005) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2005.08.007 · Cited by 732 · see citing works
Self-citationDynamics of a small globular protein in terms of low-frequency vibrational modes.
Gō, N., Noguti, T., & Nishikawa, T. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.12.3696 · Cited by 729 · see citing works
Protein normal-mode dynamics: Trypsin inhibitor, crambin, ribonuclease and lysozyme
Levitt, M., Sander, C., & Stern, P. (1985) · Journal of Molecular Biology · doi:10.1016/0022-2836(85)90230-x · Cited by 728 · see citing works
Suhre, K., & Sanejouand, Y. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh368 · Cited by 689 · see citing works
Statistical thermodynamics of random networks
Flory, P. J. (1976) · Proceedings of the Royal Society of London A Mathematical and Physical Sciences · doi:10.1098/rspa.1976.0146 · Cited by 645 · see citing works
Normal Mode Analysis of Biomolecular Structures: Functional Mechanisms of Membrane Proteins
Bahar, İ., Lezon, T. R., Bakan, A., & Shrivastava, I. H. (2009) · Chemical Reviews · doi:10.1021/cr900095e · Cited by 534 · see citing works
Self-citationSmock, R. G., & Gierasch, L. M. (2009) · Science · doi:10.1126/science.1169377 · Cited by 508 · see citing works
Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins
Miyashita, O., Onuchic, J. N., & Wolynes, P. G. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2135471100 · Cited by 505 · see citing works
Usefulness and Limitations of Normal Mode Analysis in Modeling Dynamics of Biomolecular Complexes
Ma, J. (2005) · Structure · doi:10.1016/j.str.2005.02.002 · Cited by 481 · see citing works
Bahar, İ., Atılgan, A. R., Demirel, M. C., & Erman, B. (1998) · Physical Review Letters · doi:10.1103/physrevlett.80.2733 · Cited by 442 · see citing works
Self-citationTobi, D., & Bahar, İ. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507603102 · Cited by 380 · see citing works
Self-citationMaragakis, P., & Karplus, M. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.07.031 · Cited by 336 · see citing works
Anisotropic network model: systematic evaluation and a new web interface
Eyal, E., Yang, L., & Bahar, İ. (2006) · Bioinformatics · doi:10.1093/bioinformatics/btl448 · Cited by 324 · see citing works
Self-citationLindahl, E. R., Azuara, C., Koehl, P., & Delarue, M. H. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl082 · Cited by 309 · see citing works
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 · see citing works
Self-citationConformational changes associated with protein–protein interactions
Goh, C.-S., Milburn, D., & Gerstein, M. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.01.005 · Cited by 294 · see citing works
Bakan, A., & Bahar, İ. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904214106 · Cited by 278 · see citing works
Self-citation(2005) · Chapman & Hall/CRC eBooks · doi:10.1201/9781420035070 · Cited by 266 · see citing works
SYMMETRY, FORM, AND SHAPE: Guiding Principles for Robustness in Macromolecular Machines
Tama, F., & Brooks, C. L. (2006) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.35.040405.102010 · Cited by 266 · see citing works
Zheng, W., Brooks, B. R., & Thirumalai, D. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510426103 · Cited by 261 · see citing works
Protein elastic network models and the ranges of cooperativity
Yang, L., Song, G., & Jernigan, R. L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902159106 · Cited by 260 · see citing works
Self-citationDynamics of Proteins in Crystals: Comparison of Experiment with Simple Models
Kundu, S., Melton, J. S., Sorensen, D. C., & Phillips, G. N. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)75203-x · Cited by 254 · see citing works
Signal Propagation in Proteins and Relation to Equilibrium Fluctuations
Chennubhotla, C., & Bahar, İ. (2007) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0030172 · Cited by 230 · see citing works
Self-citationDiscriminating between homodimeric and monomeric proteins in the crystalline state
Ponstingl, H., Henrick, K., & Thornton, J. M. (2000) · Proteins Structure Function and Bioinformatics · doi:10.1002/1097-0134(20001001)41:1 · Cited by 226 · see citing works
Dynamics of large proteins through hierarchical levels of coarse‐grained structures
Doruker, P., Jernigan, R. L., & Bahar, İ. (2001) · Journal of Computational Chemistry · doi:10.1002/jcc.1160 · Cited by 224 · see citing works
Self-citationHarmonicity in slow protein dynamics
Hinsen, K., Petrescu, A., Dellerue, S., et al. (2000) · Chemical Physics · doi:10.1016/s0301-0104(00)00222-6 · Cited by 220 · see citing works
A comparative study of motor-protein motions by using a simple elastic-network model
Zheng, W., & Doniach, S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2235686100 · Cited by 212 · see citing works
Collective Motions in HIV-1 Reverse Transcriptase: Examination of Flexibility and Enzyme Function
Bahar, İ., Erman, B., Jernigan, R. L., Atılgan, A. R., & Covell, D. G. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2371 · Cited by 201 · see citing works
Self-citationEnzyme flexibility and enzyme action
Koshland, D. E. (1959) · Journal of Cellular and Comparative Physiology · doi:10.1002/jcp.1030540420 · Cited by 199 · see citing works
Xu, C., Tobi, D., & Bahar, İ. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.08.027 · Cited by 198 · see citing works
Self-citationYang, L., Song, G., Carriquiry, A., et al. (2008) · Structure · doi:10.1016/j.str.2007.12.011 · Cited by 172 · see citing works
Self-citationBahar, İ., Wallqvist, A., Covell, D. G., & Jernigan, R. L. (1998) · Biochemistry · doi:10.1021/bi9720641 · Cited by 167 · see citing works
Self-citationAlexandrov, V., Lehnert, U., Echols, N., Milburn, D., Engelman, D., & Gerstein, M. (2005) · Protein Science · doi:10.1110/ps.04882105 · Cited by 153 · see citing works
Markov propagation of allosteric effects in biomolecular systems: application to GroEL–GroES
Chennubhotla, C., & Bahar, İ. (2006) · Molecular Systems Biology · doi:10.1038/msb4100075 · Cited by 151 · see citing works
Self-citationProtein conformational transitions explored by mixed elastic network models
Zheng, W., Brooks, B. R., & Hummer, G. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21465 · Cited by 143 · see citing works
Yang, L., Eyal, E., Bahar, İ., & Kitao, A. (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp023 · Cited by 135 · see citing works
Self-citationYang, Z., Májek, P., & Bahar, İ. (2009) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000360 · Cited by 134 · see citing works
Self-citationYang, L., Eyal, E., Chennubhotla, C., et al. (2007) · Structure · doi:10.1016/j.str.2007.04.014 · Cited by 133 · see citing works
Self-citationAn Analysis of Core Deformations in Protein Superfamilies
Leo‐Macías, A., López‐Romero, P., Lupyan, D., Zerbino, D. R., & Ortíz, Á. R. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.052449 · Cited by 118 · see citing works
Structural flexibility in proteins: impact of the crystal environment
Hinsen, K. (2007) · Bioinformatics · doi:10.1093/bioinformatics/btm625 · Cited by 115 · see citing works
Suhre, K., Navaza, J., & Sanejouand, Y. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s090744490602244x · Cited by 111 · see citing works
Diamond, R. (1990) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390002082 · Cited by 109 · see citing works
Protein Structural Variation in Computational Models and Crystallographic Data
Kondrashov, D. A., Wynsberghe, A. W. V., Bannen, R. M., Cui, Q., & Phillips, G. N. (2007) · Structure · doi:10.1016/j.str.2006.12.006 · Cited by 104 · see citing works
Mouawad, L., & Perahia, D. G. S. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0257 · Cited by 103 · see citing works
Optimization and Evaluation of a Coarse-Grained Model of Protein Motion Using X-Ray Crystal Data
Kondrashov, D. A., Cui, Q., & Phillips, G. N. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.085894 · Cited by 103 · see citing works
Refinement of protein dynamic structure: normal mode refinement.
Kidera, A., & Gō, N. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.10.3718 · Cited by 102 · see citing works
Hinsen, K., Reuter, N., Navaza, J., et al. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.050716 · Cited by 91 · see citing works
Application of Elastic Network Models to Proteins in the Crystalline State
Riccardi, D., Cui, Q., & Phillips, G. N. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2008.10.010 · Cited by 79 · see citing works
Eyal, E., Chennubhotla, C., Yang, L., et al. (2007) · Bioinformatics · doi:10.1093/bioinformatics/btm186 · Cited by 79 · see citing works
Self-citationvGNM: A Better Model for Understanding the Dynamics of Proteins in Crystals
Song, G., & Jernigan, R. L. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.03.059 · Cited by 74 · see citing works
Haliloǧlu, T., Keskin, Ö., Ma, B., & Nussinov, R. (2005) · Biophysical Journal · doi:10.1529/biophysj.104.051342 · Cited by 70 · see citing works
Folding core predictions from network models of proteins
Rader, A. J., & Bahar, İ. (2003) · Polymer · doi:10.1016/j.polymer.2003.10.080 · Cited by 67 · see citing works
Self-citationYang, L., & Chng, C. (2008) · Bioinformatics and Biology Insights · doi:10.4137/bbi.s460 · Cited by 64 · see citing works
Self-citationKryshtafovych, A., Fidelis, K. A., & Moult, J. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21769 · Cited by 63 · see citing works
Qian, B., Ortíz, Á. R., & Baker, D. A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404703101 · Cited by 62 · see citing works
Poon, B. K., Chen, X., Lu, M., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701204104 · Cited by 58 · see citing works
Zheng, W. (2008) · Biophysical Journal · doi:10.1529/biophysj.107.125831 · Cited by 55 · see citing works
Xu, Y., Colletier, J., Jiang, H., et al. (2008) · Protein Science · doi:10.1110/ps.083453808 · Cited by 51 · see citing works
Focused Functional Dynamics of Supramolecules by Use of a Mixed-Resolution Elastic Network Model
Kürkçüoğlu, Ö., Turgut, O. T., Cansu, S., Jernigan, R. L., & Doruker, P. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2009.06.009 · Cited by 46 · see citing works
Fetler, L., Kantrowitz, E. R., & Vachette, P. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607641104 · Cited by 43 · see citing works
Hydrophobicity at the surface of proteins
Scarsi, M., Majeux, N., & Caflisch, A. (1999) · Proteins Structure Function and Bioinformatics · doi:10.1002/(sici)1097-0134(19991201)37:4 · Cited by 42 · see citing works
Comment on elastic network models and proteins
Thorpe, M. F. (2007) · Physical Biology · doi:10.1088/1478-3975/4/1/n01 · Cited by 40 · see citing works
Lu, M., & Ma, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806072105 · Cited by 39 · see citing works
Global Motions of the Nuclear Pore Complex: Insights from Elastic Network Models
Lezon, T. R., Šali, A., & Bahar, İ. (2009) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000496 · Cited by 33 · see citing works
Self-citationAn efficient conformational sampling method for homology modeling
Han, R.-S., Leo‐Macías, A., Zerbino, D. R., Bastolla, U., Contreras‐Moreira, B., & Ortíz, Á. R. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21672 · Cited by 26 · see citing works
Lezon, T. R., Shrivastava, I. H., Yang, Z., & Bahar, İ. (2009) · World Scientific lecture notes in complex systems · doi:10.1142/9789812838803_0007 · Cited by 19 · see citing works
Self-citationErman, B., Kloczkowski, A., & Mark, J. E. (1989) · Macromolecules · doi:10.1021/ma00193a071 · Cited by 17 · see citing works
Kidera, A., Inaka, K., Matsushima, M., et al. (1992) · Biopolymers · doi:10.1002/bip.360320404 · Cited by 13 · see citing works
Use of normal modes for structural modeling of proteins: the case study of rat heme oxygenase 1
Maréchal, J., & Perahia, D. G. S. (2008) · European Biophysics Journal · doi:10.1007/s00249-008-0279-y · Cited by 11 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
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 · see citing works
Self-citationDesigning allostery-inspired response in mechanical networks
Rocks, J. W., Pashine, N., Bischofberger, I., Goodrich, C. P., Liu, A. J., & Nagel, S. R. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1612139114 · Cited by 204 · see citing works
Mapping allosteric communications within individual proteins
Wang, J., Jain, A., McDonald, L. R., Gambogi, C., Lee, A. L., & Dokholyan, N. V. (2020) · Nature Communications · doi:10.1038/s41467-020-17618-2 · Cited by 201 · see citing works
Low-resolution structural modeling of protein interactome
Vakser, I. A. (2013) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2012.12.003 · Cited by 62 · see citing works
Flechsig, H. (2017) · Biophysical Journal · doi:10.1016/j.bpj.2017.06.043 · Cited by 59 · see citing works
The Statistical Trends of Protein Evolution: A Lesson from AlphaFold Database
Tang, Q.-Y., Ren, W., Wang, J., & Kaneko, K. (2022) · Molecular Biology and Evolution · doi:10.1093/molbev/msac197 · Cited by 31 · see citing works
Wen, B., Peng, J., Zuo, X., Gong, Q., & Zhang, Z. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.07.005 · Cited by 20 · see citing works
Song, J., Gao, F., Cui, R. Z., Shuang, F., Liang, W., Huang, X., & Zhuang, W. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp304714q · Cited by 10 · see citing works
Unifying Constraints Linking Protein Folding and Native Dynamics Decoded from AlphaFold
Zhang, Z., Ren, W., Xie, L., Zheng, Y., Guan, X., Wang, J., Li, W., & Tang, Q.-Y. (2026) · Physical Review Letters · doi:10.1103/7j2j-f8f7 · Cited by 5 · see citing works
Wang, B., Wang, C., Chen, J., Liu, D., Sun, C., Zhang, J., Zhang, K., & Li, H. (2026) · Nature Machine Intelligence · doi:10.1038/s42256-026-01198-9 · Cited by 5 · see citing works
- Authors
- Bahar, I., Lezon, T. R., Yang, L.-W., & Eyal, E.
- Affiliations
- Department of Computational Biology, School of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania 15213; email:
- University of Pittsburgh (US)
- Venue
- Annual Review of Biophysics
- Publisher
- Annual Reviews
- Published
- 2010-04
- Volume
- 39
- Issue
- 1
- Pages
- 23-42
- ISSN
- 1936-122X (ISSN-L)
- 1936-1238
- PMC
- PMC2938190
- OpenAlex
- W2142595184
- Cited by
- 610
- References
- 83
- Citations by year
- 2026: 32 · 2025: 30 · 2024: 17 · 2023: 28 · 2022: 28 · 2021: 38 · 2020: 41 · 2019: 30 · 2018: 36 · 2017: 49 · 2016: 45 · 2015: 52 · 2014: 46 · 2013: 43 · 2012: 43
- FWCI
- 3.87
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Annual Review of Biophysics (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM086238)
- U.S. National Library of Medicine (R01LM007994)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- protein dynamics, elastic network model, normal mode analysis, allosteric mechanism, structure-function relationship, ligand binding, protein complexes, coarse-grained models
- MeSH terms
- Models, Biological, Protein Conformation, Proteins, Structure-Activity Relationship, Protein Folding
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
