Membrane manipulations by the ESCRT machinery
Open accessAbstract
The endosomal sorting complexes required for transport (ESCRTs) collectively comprise a machinery that was first known for its function in the degradation of transmembrane proteins in the endocytic pathway of eukaryotic cells. Since their discovery, however, ESCRTs have been recognized as playing important roles at the plasma membrane, which appears to be the original site of function for the ESCRT machinery. This article reviews some of the major research findings that have shaped our current understanding of how the ESCRT machinery controls membrane dynamics and considers new roles for the ESCRT machinery that might be driven by these mechanisms.
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?
ESCRT-III is one of the four multiprotein complexes required for multivesicular body formation and is responsible for membrane deformation that enables autophagosome initiation and endolysosomal trafficking.
“ESCRT-III is one of the four multiprotein complexes required for multivesicular body formation, and is responsible for the membrane deformation that enables autophagosome initiation and endolysosomal trafficking [263].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [263]
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
Extracellular vesicles: Exosomes, microvesicles, and friends
Raposo, G., & Stoorvogel, W. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201211138 · Cited by 8,099 · see citing works
Ceramide Triggers Budding of Exosome Vesicles into Multivesicular Endosomes
Trajković, K., Hsu, C., Chiantia, S., Rajendran, L., Wenzel, D., Wieland, F., Schwille, P., Brügger, B., & Simons, M. (2008) · Science · doi:10.1126/science.1153124 · Cited by 3,639 · see citing works
Syndecan–syntenin–ALIX regulates the biogenesis of exosomes
Baietti, M. F., Zhang, Z., Mortier, E., Melchior, A., Degeest, G., Geeraerts, A., Ivarsson, Y., Depoortere, F., Coomans, C., Vermeiren, E., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2502 · Cited by 1,899 · see citing works
Ectosomes and exosomes: shedding the confusion between extracellular vesicles
Cocucci, E., & Meldolesi, J. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.01.004 · Cited by 1,435 · see citing works
Katzmann, D. J., Babst, M., & Emr, S. D. (2001) · Cell · doi:10.1016/s0092-8674(01)00434-2 · Cited by 1,430 · see citing works
Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding
Garrus, J. E., von Schwedler, U. K., Pornillos, O. W., Morham, S. G., Zavitz, K. H., Wang, H. E., Wettstein, D. A., Stray, K. M., Côté, M., Rich, R. L., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00506-2 · Cited by 1,369 · see citing works
Babst, M., Katzmann, D. J., Estepa, E. J., Meerloo, T., & Emr, S. D. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00220-4 · Cited by 875 · see citing works
Raymond, C. K., Howald-Stevenson, I., Vater, C. A., & Stevens, T. H. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.12.1389 · Cited by 840 · see citing works
AIP1/ALIX Is a Binding Partner for HIV-1 p6 and EIAV p9 Functioning in Virus Budding
Strack, B., Calistri, A., Craig, S., Popova, E., & Göttlinger, H. G. (2003) · Cell · doi:10.1016/s0092-8674(03)00653-6 · Cited by 825 · see citing works
The Protein Network of HIV Budding
von Schwedler, U. K., Stuchell‐Brereton, M. D., Müller, B., Ward, D. M., Chung, H.-Y., Morita, E., Wang, H. E., Davis, T., He, G.-P., Cimbora, D. M., et al. (2003) · Cell · doi:10.1016/s0092-8674(03)00714-1 · Cited by 815 · see citing works
Molecular mechanism of multivesicular body biogenesis by ESCRT complexes
Wollert, T., & Hurley, J. H. (2010) · Nature · doi:10.1038/nature08849 · Cited by 804 · see citing works
Parallels Between Cytokinesis and Retroviral Budding: A Role for the ESCRT Machinery
Carlton, J. G., & Martin-Serrano, J. (2007) · Science · doi:10.1126/science.1143422 · Cited by 764 · see citing works
Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis
Morita, E., Sandrin, V., Chung, H., Morham, S. G., Gygi, S. P., Rodesch, C. K., & Sundquist, W. I. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601850 · Cited by 724 · see citing works
Nabhan, J. F., Hu, R., Oh, R. S., Cohen, S. N., & Lu, Q. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1200448109 · Cited by 722 · see citing works
ESCRT Machinery Is Required for Plasma Membrane Repair
Jiménez, A. J., Maiuri, P., Lafaurie-Janvore, J., Divoux, S., Piel, M., & Perez, F. (2014) · Science · doi:10.1126/science.1247136 · Cited by 670 · see citing works
Babst, M., Katzmann, D. J., Snyder, W. B., Wendland, B., & Emr, S. D. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00219-8 · Cited by 662 · see citing works
Fab1p PtdIns(3)P 5-Kinase Function Essential for Protein Sorting in the Multivesicular Body
Odorizzi, G., Babst, M., & Emr, S. D. (1998) · Cell · doi:10.1016/s0092-8674(00)81707-9 · Cited by 656 · see citing works
Self-citationMembrane scission by the ESCRT-III complex
Wollert, T., Wunder, C., Lippincott‐Schwartz, J., & Hurley, J. H. (2009) · Nature · doi:10.1038/nature07836 · Cited by 634 · see citing works
Multivesicular Body Morphogenesis
Hanson, P. I., & Cashikar, A. G. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154152 · Cited by 583 · see citing works
Cortical Constriction During Abscission Involves Helices of ESCRT-III–Dependent Filaments
Guizetti, J., Schermelleh, L., Mäntler, J., Maar, S., Poser, I., Leonhardt, H., Müller-Reichert, T., & Gerlich, D. (2011) · Science · doi:10.1126/science.1201847 · Cited by 496 · see citing works
Proteomics of extracellular vesicles: Exosomes and ectosomes
Choi, D., Kim, D., Kim, Y., & Gho, Y. S. (2014) · Mass Spectrometry Reviews · doi:10.1002/mas.21420 · Cited by 462 · see citing works
Plasma membrane deformation by circular arrays of ESCRT-III protein filaments
Hanson, P. I., Roth, R., Lin, Y., & Heuser, J. E. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200707031 · Cited by 427 · see citing works
Dysferlin Interacts with Annexins A1 and A2 and Mediates Sarcolemmal Wound-healing
Lennon, N. J., Kho, A. T., Bacskai, B. J., Perlmutter, S. L., Hyman, B. T., & Brown, R. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307247200 · Cited by 407 · see citing works
Polarized release of T-cell-receptor-enriched microvesicles at the immunological synapse
Choudhuri, K., Llodrá, J., Roth, E. W., Tsai, J., Gordo, S., Wucherpfennig, K. W., Kam, L. C., Stokes, D. L., & Dustin, M. L. (2014) · Nature · doi:10.1038/nature12951 · Cited by 397 · see citing works
Martin‐Serrano, J., Yaravoy, A., Pérez-Caballero, D., & Bieniasz, P. D. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2133846100 · Cited by 397 · see citing works
Elia, N., Sougrat, R., Spurlin, T. A., Hurley, J. H., & Lippincott‐Schwartz, J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102714108 · Cited by 389 · see citing works
A Role for the ESCRT System in Cell Division in Archaea
Samson, R. Y., Obita, T., Freund, S. M. V., Williams, R. L., & Bell, S. D. (2008) · Science · doi:10.1126/science.1165322 · Cited by 368 · see citing works
Helical Structures of ESCRT-III Are Disassembled by VPS4
Lata, S., Schoehn, G., Jain, A., Vieira-Pires, R. S., Piehler, J., Göttlinger, H. G., & Weissenhorn, W. (2008) · Science · doi:10.1126/science.1161070 · Cited by 352 · see citing works
The Vps27p–Hse1p complex binds ubiquitin and mediates endosomal protein sorting
Bilodeau, P. S., Urbanowski, J. L., Winistorfer, S. C., & Piper, R. C. (2002) · Nature Cell Biology · doi:10.1038/ncb815 · Cited by 346 · see citing works
A unique cell division machinery in the Archaea
Lindås, A., Karlsson, E. A., Lindgren, M. T., Ettema, T. J. G., & Bernander, R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809467105 · Cited by 345 · see citing works
Damage control: cellular mechanisms of plasma membrane repair
Andrews, N. W., de Almeida, P. E., & Corrotte, M. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.07.008 · Cited by 340 · see citing works
Teis, D., Saksena, S., & Emr, S. D. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.08.013 · Cited by 338 · see citing works
ESCRT-III recognition by VPS4 ATPases
Stuchell‐Brereton, M. D., Skalicky, J. J., Kieffer, C., Karren, M. A., Ghaffarian, S., & Sundquist, W. I. (2007) · Nature · doi:10.1038/nature06172 · Cited by 329 · see citing works
ESCRT-III Governs the Aurora B–Mediated Abscission Checkpoint Through CHMP4C
Carlton, J. G., Caballe, A., Agromayor, M., Kloc, M., & Martin‐Serrano, J. (2012) · Science · doi:10.1126/science.1217180 · Cited by 326 · see citing works
Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4
Obita, T., Saksena, S., Ghazi-Tabatabai, S., Gill, D. J., Perišić, O., Emr, S. D., & Williams, R. L. (2007) · Nature · doi:10.1038/nature06171 · Cited by 311 · see citing works
Functional Reconstitution of ESCRT-III Assembly and Disassembly
Saksena, S., Wahlman, J., Teis, D., Johnson, A. E., & Emr, S. D. (2009) · Cell · doi:10.1016/j.cell.2008.11.013 · Cited by 296 · see citing works
Cytokinetic Abscission: Molecular Mechanisms and Temporal Control
Mierzwa, B. E., & Gerlich, D. W. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.11.006 · Cited by 289 · see citing works
Evolution of the Multivesicular Body ESCRT Machinery; Retention Across the Eukaryotic Lineage
Leung, K. F., Dacks, J. B., & Field, M. C. (2008) · Traffic · doi:10.1111/j.1600-0854.2008.00797.x · Cited by 282 · see citing works
Ubiquitin‐dependent internalization and down‐regulation of plasma membrane proteins
Hicke, L. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.14.9409540 · Cited by 271 · see citing works
Midbody Targeting of the ESCRT Machinery by a Noncanonical Coiled Coil in CEP55
Lee, H. H., Elia, N., Ghirlando, R., Lippincott‐Schwartz, J., & Hurley, J. H. (2008) · Science · doi:10.1126/science.1162042 · Cited by 260 · see citing works
Structural Basis for Budding by the ESCRT-III Factor CHMP3
Muzioł, T. M., Pineda‐Molina, E., Ravelli, R. B. G., Zamborlini, A., Usami, Y., Göttlinger, H. G., & Weissenhorn, W. (2006) · Developmental Cell · doi:10.1016/j.devcel.2006.03.013 · Cited by 250 · see citing works
Ubiquitin interactions of NZF zinc fingers
Alam, S. L., Sun, J., Payne, M., Welch, B. D., Blake, B. K., Davis, D. R., Meyer, H. H., Emr, S. D., & Sundquist, W. I. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600114 · Cited by 248 · see citing works
The Endosomal Sorting Complex ESCRT-II Mediates the Assembly and Architecture of ESCRT-III Helices
Henne, W. M., Buchkovich, N. J., Zhao, Y., & Emr, S. D. (2012) · Cell · doi:10.1016/j.cell.2012.08.039 · Cited by 243 · see citing works
Membrane Fission Reactions of the Mammalian ESCRT Pathway
McCullough, J., Colf, L. A., & Sundquist, W. I. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072909-101058 · Cited by 238 · see citing works
Dynamics of ESCRT protein recruitment during retroviral assembly
Jouvenet, N., Zhadina, M., Bieniasz, P. D., & Simon, S. M. (2011) · Nature Cell Biology · doi:10.1038/ncb2207 · Cited by 228 · see citing works
Structural basis for ESCRT-III protein autoinhibition
Bajorek, M., Schubert, H., McCullough, J., Langelier, C., Eckert, D. M., Stubblefield, W. B., Uter, N. T., Myszka, D. G., Hill, C. P., & Sundquist, W. I. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1621 · Cited by 224 · see citing works
Surveillance of Nuclear Pore Complex Assembly by ESCRT-III/Vps4
Webster, B. M., Colombi, P., Jäger, J., & Lusk, C. P. (2014) · Cell · doi:10.1016/j.cell.2014.09.012 · Cited by 219 · see citing works
Bro1 is an endosome-associated protein that functions in the MVB pathway in Saccharomyces cerevisiae
Odorizzi, G., Katzmann, D. J., Babst, M., Audhya, A., & Emr, S. D. (2003) · Journal of Cell Science · doi:10.1242/jcs.00395 · Cited by 213 · see citing works
Self-citationShim, S., Kimpler, L. A., & Hanson, P. I. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00584.x · Cited by 204 · see citing works
Live-cell visualization of dynamics of HIV budding site interactions with an ESCRT component
Baumgärtel, V., Ivanchenko, S. V., Dupont, A., Sergeev, M., Wiseman, P. W., Kräusslich, H., Bräuchle, C., Müller, B., & Lamb, D. C. (2011) · Nature Cell Biology · doi:10.1038/ncb2215 · Cited by 200 · see citing works
Distribution of ESCRT Machinery at HIV Assembly Sites Reveals Virus Scaffolding of ESCRT Subunits
van Engelenburg, S. B., Shtengel, G. E., Sengupta, P., Waki, K., Jarník, M., Ablan, S. D., Freed, E. O., Hess, H. F., & Lippincott‐Schwartz, J. (2014) · Science · doi:10.1126/science.1247786 · Cited by 191 · see citing works
Lafaurie-Janvore, J., Maiuri, P., Wang, I., Pinot, M., Manneville, J., Betz, T., Balland, M., & Piel, M. (2013) · Science · doi:10.1126/science.1233866 · Cited by 189 · see citing works
The P4-ATPase TAT-5 Inhibits the Budding of Extracellular Vesicles in C. elegans Embryos
Wehman, A. M., Poggioli, C., Schweinsberg, P. J., Grant, B. D., & Nance, J. (2011) · Current Biology · doi:10.1016/j.cub.2011.10.040 · Cited by 185 · see citing works
Adell, M. A. Y., Vogel, G. F., Pakdel, M., Müller, M., Lindner, H. H., Hess, M. W., & Teis, D. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201310114 · Cited by 182 · see citing works
Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding
Zamborlini, A., Usami, Y., Radoshitzky, S. R., Popova, E. N., Palù, G., & Göttlinger, H. G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603788103 · Cited by 180 · see citing works
Kieffer, C., Skalicky, J. J., Morita, E., Domenico, I. D., Ward, D. M., Kaplan, J., & Sundquist, W. I. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.05.014 · Cited by 167 · see citing works
Lin, Y., Kimpler, L. A., Naismith, T. V., Lauer, J. M., & Hanson, P. I. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413968200 · Cited by 157 · see citing works
Computational Model of Membrane Fission Catalyzed by ESCRT-III
Fabrikant, G., Lata, S., Riches, J. D., Briggs, J. A. G., Weissenhorn, W., & Kozlov, M. M. (2009) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000575 · Cited by 151 · see citing works
Caveolae internalization repairs wounded cells and muscle fibers
Corrotte, M., de Almeida, P. E., Tam, C. C., Castro‐Gomes, T., Fernandes, M. C., Millis, B. A., Cortéz, M., Miller, H. E., Song, W., Maugel, T. K., et al. (2013) · eLife · doi:10.7554/elife.00926 · Cited by 151 · see citing works
Structure of cellular ESCRT-III spirals and their relationship to HIV budding
Cashikar, A. G., Shim, S., Roth, R., Maldazys, M. R., Heuser, J. E., & Hanson, P. I. (2014) · eLife · doi:10.7554/elife.02184 · Cited by 136 · see citing works
Structural analysis and modeling reveals new mechanisms governing ESCRT-III spiral filament assembly
Shen, Q.-T., Schuh, A. L., Zheng, Y., Quinney, K., Wang, L., Hanna, M., Mitchell, J. C., Otegui, M. S., Ahlquist, P., Cui, Q., et al. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201403108 · Cited by 129 · see citing works
Carlson, L. A., & Hurley, J. H. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1211759109 · Cited by 94 · see citing works
Bro1 binding to Snf7 regulates ESCRT-III membrane scission activity in yeast
Wemmer, M., Azmi, I. F., West, M., Davies, B. A., Katzmann, D. J., & Odorizzi, G. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201007018 · Cited by 82 · see citing works
Self-citationCC2D1A Is a Regulator of ESCRT-III CHMP4B
Martinelli, N., Hartlieb, B., Usami, Y., Sabin, C., Dordor, A., Miguet, N., Avilov, S., Ribeiro, E. A., Göttlinger, H. G., & Weissenhorn, W. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.02.044 · Cited by 66 · see citing works
Membrane-Elasticity Model of Coatless Vesicle Budding Induced by ESCRT Complexes
Różycki, B., Bouřa, E., Hurley, J. H., & Hummer, G. (2012) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002736 · Cited by 38 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Reverse-topology membrane scission by the ESCRT proteins
Schöneberg, J., Lee, I., Iwasa, J., & Hurley, J. H. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.121 · Cited by 426 · see citing works
Autophagy and ALS: mechanistic insights and therapeutic implications
Chua, J. P., De Calbiac, H., Kabashi, E., & Barmada, S. J. (2022) · Autophagy · doi:10.1080/15548627.2021.1926656 · Cited by 189 · see citing works
Identification of protein markers for extracellular vesicle (EV) subsets in cow's milk
Benmoussa, A., Gotti, C., Bourassa, S., Gilbert, C., & Provost, P. (2018) · Journal of Proteomics · doi:10.1016/j.jprot.2018.08.010 · Cited by 69 · see citing works
Dynamic and elastic shape transitions in curved ESCRT-III filaments
Chiaruttini, N., & Roux, A. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.07.002 · Cited by 51 · see citing works
The role of CHMP2BIntron5 in autophagy and frontotemporal dementia
Krasniak, C. S., & Ahmad, S. T. (2016) · Brain Research · doi:10.1016/j.brainres.2016.02.051 · Cited by 46 · see citing works
A Consensus View of ESCRT-Mediated Human Immunodeficiency Virus Type 1 Abscission
Lippincott‐Schwartz, J., Freed, E. O., & van Engelenburg, S. B. (2017) · Annual Review of Virology · doi:10.1146/annurev-virology-101416-041840 · Cited by 40 · see citing works
Emerging biosensing platforms for quantitative detection of exosomes as diagnostic biomarkers
Tan, J., Wen, Y., & Li, M. (2021) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2021.214111 · Cited by 38 · see citing works
How HIV-1 Gag Manipulates Its Host Cell Proteins: A Focus on Interactors of the Nucleocapsid Domain
Klingler, J., Anton, H., Réal, É., Zeiger, M., Moog, C., Mély, Y., & Boutant, E. (2020) · Viruses · doi:10.3390/v12080888 · Cited by 34 · see citing works
Super‐resolved insights into human immunodeficiency virus biology
Hanne, J., Žíla, V., Heilemann, M., Müller, B., & Kräusslich, H. (2016) · FEBS Letters · doi:10.1002/1873-3468.12186 · Cited by 28 · see citing works
Xia, H., Shao, D., Liu, X., Wang, Q., Zhou, Y., & Chen, K. (2017) · Journal of Insect Science · doi:10.1093/jisesa/iex055 · Cited by 3 · see citing works
Regulation of intracellular traffic by TBK1 and its relevance to ALS
Villarroel‐Campos, D. (2020) · UCL Discovery (University College London)
- Authors
- Odorizzi, G.
- Affiliations
- University of Colorado Boulder (US)
- Corresponding author
- Odorizzi, Greg
- ORCID
- Odorizzi, Greg
- Venue
- F1000Research
- Publisher
- F1000 Research Ltd
- Published
- 2015-08-07
- Volume
- 4
- Issue
- F1000 Faculty Rev
- Pages
- 516
- ISSN
- 2046-1402 (ISSN-L)
- PMC
- PMC4544380
- OpenAlex
- W1612512763
- Cited by
- 11
- References
- 65
- Citations by year
- 2021: 2 · 2020: 2 · 2018: 1 · 2017: 3 · 2016: 3
- FWCI
- 0.23
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- F1000Research (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institute of General Medical Sciences (R01GM111335)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- ESCRT machinery, membrane dynamics, plasma membrane, endosomal sorting, membrane trafficking, protein degradation, endocytosis, membrane fission
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
