Exosomes: Vehicles for the Transfer of Toxic Proteins Associated with Neurodegenerative Diseases?
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?
Under pathological conditions, exosomes increase propagation of neurotoxic proteins in neurodegenerative diseases and aggravate brain tumor metastasis and progression.
“Under pathological conditions, exosomes have been found to increase the propagation of neurotoxic proteins in neurodegenerative diseases51,52,53, and aggravate brain tumor metastasis and progression14.”
From Neurons secrete miR-132-containing exosomes to regulate brain vascular integrity (2017) · cites this paper as [53]
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
1 retracted
Tsigelny, I. F., Crews, L., Desplats, P., Shaked, G. M., Sharikov, Y., Mizuno, H., Spencer, B., Rockenstein, E., Trejo, M., Platoshyn, O., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003135 · Cited by 281 · see citing works
RetractedJohnstone, R. M., Adam, M., Hammond, J. R., Orr, L., & Turbide, C. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48095-7 · Cited by 2,931 · see citing works
Secretory Mechanisms and Intercellular Transfer of MicroRNAs in Living Cells
Kosaka, N., Iguchi, H., Yoshioka, Y., Takeshita, F., Matsuki, Y., & Ochiya, T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.107821 · Cited by 1,934 · see citing works
Li, J.-Y., Englund, E., Holton, J. L., Soulet, D., Hagell, P., Lees, A. J., Lashley, T., Quinn, N. P., Rehncrona, S., Björklund, A., et al. (2008) · Nature Medicine · doi:10.1038/nm1746 · Cited by 1,845 · see citing works
Transmission and spreading of tauopathy in transgenic mouse brain
Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803 · see citing works
Propagation of Tau Misfolding from the Outside to the Inside of a Cell
Frost, B., Jacks, R. L., & Diamond, M. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808759200 · Cited by 1,252 · see citing works
Emmanouilidou, E., Melachroinou, K., Roumeliotis, T., Garbis, S. D., Ntzouni, M., Margaritis, L. H., Stefanis, L., & Vekrellis, K. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5699-09.2010 · Cited by 1,115 · see citing works
Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives
Mattson, M. P. (1997) · Physiological Reviews · doi:10.1152/physrev.1997.77.4.1081 · Cited by 1,006 · cited 1× · see citing works
“…pathway of APP processing involves sequential cleavage by β- and γ-secretases. β-Secretase cleaves at the amino-terminus of Aβ (Seubert et al., 1993; Mattson, 1997) resulting in the release of secreted APP, and leaves intact Aβ as a membrane-associated, 99-amino-acid carboxy-terminal fragment…”
BackgroundSaman, S., Kim, W., Raya, M., Visnick, Y., Miro, S., Saman, S., Jackson, B., McKee, A. C., Alvarez, V. E., Lee, N. C. Y., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.277061 · Cited by 985 · see citing works
Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host
Meyer-Luehmann, M., Coomaraswamy, J., Bolmont, T., Kaeser, S., Schaefer, C., Kilger, E., Neuenschwander, A., Abramowski, D., Frey, P., Jaton, A. L., et al. (2006) · Science · doi:10.1126/science.1131864 · Cited by 971 · see citing works
Exosomes are released by cultured cortical neurones
Fauré, J., Lachenal, G., Court, M., Hirrlinger, J., Chatellard-Causse, C., Blot, B., Grange, J., Schoehn, G., Goldberg, Y., Boyer, V., et al. (2006) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2005.12.003 · Cited by 896 · see citing works
Hansen, C., Angot, E., Bergström, A.-L., Steiner, J. A., Pieri, L., Paul, G., Outeiro, T. F., Melki, R., Kallunki, P., Fog, K., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci43366 · Cited by 842 · see citing works
Yang, M., Chen, J., Su, F., Yu, B., Su, F., Lin, L., Liu, Y., Huang, J.-D., & Song, E. (2011) · Molecular Cancer · doi:10.1186/1476-4598-10-117 · Cited by 693 · see citing works
Alterations of the microRNA network cause neurodegenerative disease
Hébert, S. S., & De Strooper, B. (2009) · Trends in Neurosciences · doi:10.1016/j.tins.2008.12.003 · Cited by 452 · see citing works
MicroRNA regulation of Alzheimer's Amyloid precursor protein expression
Hébert, S. S., Horré, K., Nicolaï, L., Bergmans, B., Papadopoulou, A. S., Delacourte, A., & De Strooper, B. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.11.009 · Cited by 436 · see citing works
Potolicchio, I., Carven, G. J., Xu, X., Stipp, C., Riese, R. J., Stern, L. J., & Santambrogio, L. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.4.2237 · Cited by 365 · see citing works
Saba, R., Gushue, S., Huzarewich, R. L. C. H., Manguiat, K., Medina, S., Robertson, C., & Booth, S. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030832 · Cited by 151 · see citing works
Flagged first, then by citations
Research works printed but not linked: 121
- Aguzzi A. Heikenwalder M. (2006). Pathogenesis of prion diseases: current status and future outlook. Nat. Rev. Microbiol. 4, 765– 775 10.1038/nrmicro1492 16980938 · DOI · Paper page
- Alais S. Simoes S. Baas D. Lehmann S. Raposo G. Darlix J. L. Leblanc P. (2008). Mouse neuroblastoma cells release prion infectivity associated with exosomal vesicles. Biol. Cell 100, 603– 615 10.1042/BC20080025 18422484 · DOI
- Alvarez-Erviti L. Seow Y. Schapira A. H. Gardiner C. Sargent I. L. Wood M. J. Cooper J. M. (2011a). Lysosomal dysfunction increases exosome-mediated alpha-synuclein release and transmission. Neurobiol. Dis. 42, 360– 367 10.1016/j.nbd.2011.01.029 21303699 PMC3107939 · DOI
- Alvarez-Erviti L. Seow Y. Q. Yin H. F. Betts C. Lakhal S. Wood M. J. A. (2011b). Delivery of siRNA to the mouse brain by systemic injection of targeted exosomes. Nat. Biotechnol. 29, 341– U179 10.1038/nbt.1807 21423189 · DOI · Paper page
- Arroyo J. D. Chevillet J. R. Kroh E. M. Ruf I. K. Pritchard C. C. Gibson D. F. Mitchell P. S. Bennett C. F. Pogosova-Agadjanyan E. L. Stirewalt D. L. Tait J. F. Tewari M. (2011). Argonaute2 complexes carry a population of circulating microRNAs independent of vesicles in human plasma. Proc. Natl. Acad. Sci. U.S.A. 108, 5003– 5008 10.1073/pnas.1019055108 21383194 PMC3064324 · DOI · Paper page
- Atarashi R. Moore R. A. Sim V. L. Hughson A. G. Dorward D. W. Onwubiko H. A. Priola S. A. Caughey B. (2007). Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein. Nat. Methods 4, 645– 650 10.1038/nmeth1066 17643109 · DOI
- Atarashi R. Sano K. Satoh K. Nishida N. (2011). Real-time quaking-induced conversion: a highly sensitive assay for prion detection. Prion 5, 150– 153 10.4161/pri.5.3.16893 21778820 PMC3226039 · DOI
- Atarashi R. Wilham J. M. Christensen L. Hughson A. G. Moore R. A. Johnson L. M. Onwubiko H. A. Priola S. A. Caughey B. (2008). Simplified ultrasensitive prion detection by recombinant PrP conversion with shaking. Nat. Methods 5, 211– 212 10.1038/nmeth0308-211 18309304 · DOI
- Baker H. F. Ridley R. M. Duchen L. W. Crow T. J. Bruton C. J. (1994). Induction of beta (A4)-amyloid in primates by injection of Alzheimer’s disease brain homogenate. Comparison with transmission of spongiform encephalopathy. Mol. Neurobiol. 8, 25– 39 10.1007/BF02778005 8086126 · DOI
- Balaj L. Lessard R. Dai L. Cho Y. J. Pomeroy S. L. Breakefield X. O. Skog J. (2011). Tumour microvesicles contain retrotransposon elements and amplified oncogene sequences. Nat. Commun. 2, 180 10.1038/ncomms1180 21285958 PMC3040683 · DOI
- Baron G. S. Magalhaes A. C. Prado M. A. Caughey B. (2006). Mouse-adapted scrapie infection of SN56 cells: greater efficiency with microsome-associated versus purified PrP-res. J. Virol. 80, 2106– 2117 10.1128/JVI.80.5.2106-2117.2006 16474119 PMC1395383 · DOI
- Baron G. S. Wehrly K. Dorward D. W. Chesebro B. Caughey B. (2002). Conversion of raft associated prion protein to the protease-resistant state requires insertion of PrP-res (PrP(Sc)) into contiguous membranes. EMBO J. 21, 1031– 1040 10.1093/emboj/21.8.1957 11867531 PMC125906 · DOI
- Bartel D. P. (2004). MicroRNAs: genomics, biogenesis, mechanism, and function. Cell 116, 281– 297 10.1016/S0092-8674(04)00045-5 14744438 · DOI
- Boissonneault V. Plante I. Rivest S. Provost P. (2009). MicroRNA-298 and microRNA-328 regulate expression of mouse beta-amyloid precursor protein-converting enzyme 1. J. Biol. Chem. 284, 1971– 1981 10.1074/jbc.M807530200 18986979 PMC2908704 · DOI
- Bruggink K. A. Kuiperij H. B. Ekholm-Pettersson F. Verbeek M. M. (2011). Detection of elevated levels of alpha-synuclein oligomers in CSF from patients with Parkinson disease. Neurology 77, 510– 511 10.1212/WNL.0b013e318219dd92 21810701 · DOI
- Cai X. Golde T. E. Younkin S. G. (1993). Release of excess amyloid b protein from a mutant amyloid b protein precursor. Science 259, 514– 516 10.1126/science.8424174 8424174 · DOI · Paper page
- Carrettiero D. C. Hernandez I. Neveu P. Papagiannakopoulos T. Kosik K. S. (2009). The cochaperone BAG2 sweeps paired helical filament- insoluble tau from the microtubule. J. Neurosci. 29, 2151– 2161 10.1523/JNEUROSCI.4660-08.2009 19228967 PMC2768429 · DOI
- Courageot M. P. Daude N. Nonno R. Paquet S. Di Bari M. A. Le Dur A. Chapuis J. Hill A. F. Agrimi U. Laude H. Vilette D. (2008). A cell line infectible by prion strains from different species. J. Gen. Virol. 89, 341– 347 10.1099/vir.0.83344-0 18089759 · DOI
- Croce C. M. Calin G. A. (2005). miRNAs, cancer, and stem cell division. Cell 122, 6– 7 10.1016/j.cell.2005.06.036 16009126 · DOI
- Danzer K. M. Krebs S. K. Wolff M. Birk G. Hengerer B. (2009). Seeding induced by alpha-synuclein oligomers provides evidence for spreading of alpha-synuclein pathology. J. Neurochem. 111, 192– 203 10.1111/j.1471-4159.2009.06324.x 19686384 · DOI
- de Gassart A. Geminard C. Fevrier B. Raposo G. Vidal M. (2003). Lipid raft-associated protein sorting in exosomes. Blood 102, 4336– 4344 10.1182/blood-2003-03-0871 12881314 · DOI
- Deleault N. R. Harris B. T. Rees J. R. Supattapone S. (2007). From the cover: formation of native prions from minimal components in vitro. Proc. Natl. Acad. Sci. U.S.A. 104, 9741– 9746 10.1073/pnas.0702662104 17535913 PMC1887554 · DOI
- Desplats P. Lee H. J. Bae E. J. Patrick C. Rockenstein E. Crews L. Spencer B. Masliah E. Lee S. J. (2009). Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein. Proc. Natl. Acad. Sci. U.S.A. 106, 13010– 13015 10.1073/pnas.0903691106 19651612 PMC2722313 · DOI · Paper page
- Doxakis E. (2010). Post-transcriptional regulation of alpha-synuclein expression by mir-7 and mir-153. J. Biol. Chem. 285, 12726– 12734 10.1074/jbc.M109.086827 20106983 PMC2857101 · DOI
- El-Agnaf O. M. Salem S. A. Paleologou K. E. Curran M. D. Gibson M. J. Court J. A. Schlossmacher M. G. Allsop D. (2006). Detection of oligomeric forms of alpha-synuclein protein in human plasma as a potential biomarker for Parkinson’s disease. FASEB J. 20, 419– 425 10.1096/fj.03-1449com 16507759 · DOI · Paper page
- Escrevente C. Keller S. Altevogt P. Costa J. (2011). Interaction and uptake of exosomes by ovarian cancer cells. BMC Cancer 11, 108 10.1186/1471-2407-11-108 21439085 PMC3072949 · DOI
- Esquela-Kerscher A. Slack F. J. (2006). Oncomirs – microRNAs with a role in cancer. Nat. Rev. Cancer 6, 259– 269 10.1038/nrc1840 16557279 · DOI
- Fang Y. Wu N. Gan X. Yan W. Morrell J. C. Gould S. J. (2007). Higher-order oligomerization targets plasma membrane proteins and HIV gag to exosomes. PLoS Biol. 5, e158 10.1371/journal.pbio.0050158 17550307 PMC1885833 · DOI
- Fevrier B. Vilette D. Archer F. Loew D. Faigle W. Vidal M. Laude H. Raposo G. (2004). Cells release prions in association with exosomes. Proc. Natl. Acad. Sci. U.S.A. 101, 9683– 9688 10.1073/pnas.0308413101 15210972 PMC470735 · DOI
- Findeis M. A. (2000). Approaches to discovery and characterization of inhibitors of amyloid b-peptide polymerization. Biochim. Biophys. Acta 1502, 76– 84 10899433
- Gabizon R. Mckinley M. P. Groth D. F. Kenaga L. Prusiner S. B. (1988). Properties of scrapie prion protein liposomes. J. Biol. Chem. 263, 4950– 4955 3350818
- Gehrke S. Imai Y. Sokol N. Lu B. (2010). Pathogenic LRRK2 negatively regulates microRNA-mediated translational repression. Nature 466, 637– 641 10.1038/nature09191 20671708 PMC3049892 · DOI
- Gibbings D. J. Ciaudo C. Erhardt M. Voinnet O. (2009). Multivesicular bodies associate with components of miRNA effector complexes and modulate miRNA activity. Nat. Cell Biol. 11, 1143– 1149 10.1038/ncb1929 19684575 · DOI
- Gomes C. Keller S. Altevogt P. Costa J. (2007). Evidence for secretion of Cu,Zn superoxide dismutase via exosomes from a cell model of amyotrophic lateral sclerosis. Neurosci. Lett. 428, 43– 46 10.1016/j.neulet.2007.09.024 17942226 · DOI
- Gousset K. Schiff E. Langevin C. Marijanovic Z. Caputo A. Browman D. T. Chenouard N. De Chaumont F. Martino A. Enninga J. Olivo-Marin J. C. Mannel D. Zurzolo C. (2009). Prions hijack tunnelling nanotubes for intercellular spread. Nat. Cell Biol. 11, 328– 336 10.1038/ncb1841 19198598 · DOI
- Guo J. L. Lee V. M. (2011). Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles. J. Biol. Chem. 286, 15317– 15331 10.1074/jbc.M110.190892 21372138 PMC3083182 · DOI
- Haussecker D. Huang Y. Lau A. Parameswaran P. Fire A. Z. Kay M. A. (2010). Human tRNA-derived small RNAs in the global regulation of RNA silencing. RNA 16, 673– 695 10.1261/rna.2000810 20181738 PMC2844617 · DOI
- Hebert S. S. De Strooper B. (2007). Molecular biology. miRNAs in neurodegeneration. Science 317, 1179– 1180 10.1126/science.1148530 17761871 · DOI
- Hebert S. S. Horre K. Nicolai L. Papadopoulou A. S. Mandemakers W. Silahtaroglu A. N. Kauppinen S. Delacourte A. De Strooper B. (2008). Loss of microRNA cluster miR-29a/b-1 in sporadic Alzheimer’s disease correlates with increased BACE1/beta-secretase expression. Proc. Natl. Acad. Sci. U.S.A. 105, 6415– 6420 10.1073/pnas.0710263105 18434550 PMC2359789 · DOI · Paper page
- Hebert S. S. Papadopoulou A. S. Smith P. Galas M. C. Planel E. Silahtaroglu A. N. Sergeant N. Buee L. De Strooper B. (2010). Genetic ablation of Dicer in adult forebrain neurons results in abnormal tau hyperphosphorylation and neurodegeneration. Hum. Mol. Genet. 19, 3959– 3969 10.1093/hmg/ddq311 20660113 · DOI
- Hicke L. (2001). Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell Biol. 2, 195– 201 10.1038/35056583 11265249 · DOI
- Hunter M. P. Ismail N. Zhang X. Aguda B. D. Lee E. J. Yu L. Xiao T. Schafer J. Lee M. L. Schmittgen T. D. Nana-Sinkam S. P. Jarjoura D. Marsh C. B. (2008). Detection of microRNA expression in human peripheral blood microvesicles. PLoS ONE 3, e3694 10.1371/journal.pone.0003694 19002258 PMC2577891 · DOI
- Junn E. Lee K. W. Jeong B. S. Chan T. W. Im J. Y. Mouradian M. M. (2009). Repression of alpha-synuclein expression and toxicity by microRNA-7. Proc. Natl. Acad. Sci. U.S.A. 106, 13052– 13057 10.1073/pnas.0906277106 19628698 PMC2722353 · DOI · Paper page
- Kane M. D. Lipinski W. J. Callahan M. J. Bian F. Durham R. A. Schwarz R. D. Roher A. E. Walker L. C. (2000). Evidence for seeding of beta-amyloid by intracerebral infusion of Alzheimer brain extracts in beta-amyloid precursor protein-transgenic mice. J. Neurosci. 20, 3606– 3611 10804202 PMC6772682
- Kanu N. Imokawa Y. Drechsel D. N. Williamson R. A. Birkett C. R. Bostock C. J. Brockes J. P. (2002). Transfer of scrapie prion infectivity by cell contact in culture. Curr. Biol. 12, 523– 530 10.1016/S0960-9822(02)00722-4 11937020 · DOI
- Kim J. Inoue K. Ishii J. Vanti W. B. Voronov S. V. Murchison E. Hannon G. Abeliovich A. (2007). A MicroRNA feedback circuit in midbrain dopamine neurons. Science 317, 1220– 1224 10.1126/science.1146805 17761882 PMC2782470 · DOI
- Kokubo H. Saido T. C. Iwata N. Helms J. B. Shinohara R. Yamaguchi H. (2005). Part of membrane-bound Abeta exists in rafts within senile plaques in Tg2576 mouse brain. Neurobiol. Aging 26, 409– 418 10.1016/j.neurobiolaging.2004.04.008 15653169 · DOI
- Kordower J. H. Chu Y. Hauser R. A. Freeman T. B. Olanow C. W. (2008). Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson’s disease. Nat. Med. 14, 504– 506 10.1038/nm1747 18391962 · DOI · Paper page
- Kosik K. S. (2006). The neuronal microRNA system. Nat. Rev. Neurosci. 7, 911– 920 10.1038/nrn2037 17115073 · DOI
- Kramer-Albers E. M. Bretz N. Tenzer S. Winterstein C. Mobius W. Berger H. Nave K. A. Schild H. Trotter J. (2007). Oligodendrocytes secrete exosomes containing major myelin and stress-protective proteins: trophic support for axons? Proteomics Clin. Appl. 1, 1446– 1461 10.1002/prca.200700522 21136642 · DOI
- Lachenal G. Pernet-Gallay K. Chivet M. Hemming F. J. Belly A. Bodon G. Blot B. Haase G. Goldberg Y. Sadoul R. (2011). Release of exosomes from differentiated neurons and its regulation by synaptic glutamatergic activity. Mol. Cell. Neurosci. 46, 409– 418 10.1016/j.mcn.2010.11.004 21111824 · DOI
- Lee Y. S. Shibata Y. Malhotra A. Dutta A. (2009). A novel class of small RNAs: tRNA-derived RNA fragments (tRFs). Genes Dev. 23, 2639– 2649 10.1101/gad.1858709 19933153 PMC2779758 · DOI
- Li Y. Y. Cui J. G. Hill J. M. Bhattacharjee S. Zhao Y. Lukiw W. J. (2011). Increased expression of miRNA-146a in Alzheimer’s disease transgenic mouse models. Neurosci. Lett. 487, 94– 98 10.1016/j.neulet.2010.09.079 20934487 PMC5382794 · DOI · Paper page
- Long J. M. Lahiri D. K. (2011). MicroRNA-101 downregulates Alzheimer’s amyloid-beta precursor protein levels in human cell cultures and is differentially expressed. Biochem. Biophys. Res. Commun. 404, 889– 895 10.1016/j.bbrc.2010.12.053 21172309 PMC3372402 · DOI
- Luk K. C. Song C. O’Brien P. Stieber A. Branch J. R. Brunden K. R. Trojanowski J. Q. Lee V. M. (2009). Exogenous alpha-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells. Proc. Natl. Acad. Sci. U.S.A. 106, 20051– 20056 19892735 PMC2785290
- Lukiw W. J. Alexandrov P. N. (2012). Regulation of complement factor H (CFH) by multiple miRNAs in Alzheimer’s disease (AD) brain. Mol. Neurobiol. 10.1007/s12035-012-8234-4 22302353 PMC3703615 · DOI
- Lukiw W. J. Dua P. Pogue A. I. Eicken C. Hill J. M. (2011). Upregulation of micro RNA-146a (miRNA-146a), a marker for inflammatory neurodegeneration, in sporadic Creutzfeldt-Jakob disease (sCJD) and Gerstmann-Straussler-Scheinker (GSS) syndrome. J. Toxicol. Environ. Health Part A 74, 1460– 1468 10.1080/15287394.2011.618973 22043907 PMC3719866 · DOI
- Lukiw W. J. Pogue A. I. (2007). Induction of specific micro RNA (miRNA) species by ROS-generating metal sulfates in primary human brain cells. J. Inorg. Biochem. 101, 1265– 1269 10.1016/j.jinorgbio.2007.06.004 17629564 PMC2080079 · DOI
- Magalhaes A. C. Baron G. S. Lee K. S. Steele-Mortimer O. Dorward D. Prado M. A. Caughey B. (2005). Uptake and neuritic transport of scrapie prion protein coincident with infection of neuronal cells. J. Neurosci. 25, 5207– 5216 10.1523/JNEUROSCI.0653-05.2005 15917460 PMC6724812 · DOI
- Michael A. Bajracharya S. D. Yuen P. S. Zhou H. Star R. A. Illei G. G. Alevizos I. (2010). Exosomes from human saliva as a source of microRNA biomarkers. Oral. Dis. 16, 34– 38 10.1111/j.1601-0825.2009.01604.x 19627513 PMC2844919 · DOI
- Mineo M. Garfield S. H. Taverna S. Flugy A. De Leo G. Alessandro R. Kohn E. C. (2012). Exosomes released by K562 chronic myeloid leukemia cells promote angiogenesis in a src-dependent fashion. Angiogenesis 15, 33– 45 10.1007/s10456-011-9241-1 22203239 PMC3595015 · DOI
- Minones-Moyano E. Porta S. Escaramis G. Rabionet R. Iraola S. Kagerbauer B. Espinosa-Parrilla Y. Ferrer I. Estivill X. Marti E. (2011). MicroRNA profiling of Parkinson’s disease brains identifies early downregulation of miR-34b/c which modulate mitochondrial function. Hum. Mol. Genet. 20, 3067– 3078 10.1093/hmg/ddr210 21558425 · DOI
- Montag J. Hitt R. Opitz L. Schulz-Schaeffer W. J. Hunsmann G. Motzkus D. (2009). Upregulation of miRNA hsa-miR-342-3p in experimental and idiopathic prion disease. Mol. Neurodegener. 4, 36 10.1186/1750-1326-4-36 19712440 PMC2743691 · DOI
- Montecalvo A. Larregina A. T. Shufesky W. J. Beer Stolz D. Sullivan M. L. Karlsson J. M. Baty C. J. Gibson G. A. Erdos G. Wang Z. Milosevic J. Tkacheva O. A. Divito S. J. Jordan R. Lyons-Weiler J. Watkins S. C. Morelli A. E. (2012). Mechanism of transfer of functional microRNAs between mouse dendritic cells via exosomes. Blood 119, 756– 766 10.1182/blood-2011-02-338004 22031862 PMC3265200 · DOI · Paper page
- Morales R. Duran-Aniotz C. Castilla J. Estrada L. D. Soto C. (2011). De novo induction of amyloid-beta deposition in vivo. Mol. Psychiatry. 10.1038/mp.2011.120 21968933 · DOI
- Morelli A. E. Larregina A. T. Shufesky W. J. Sullivan M. L. Stolz D. B. Papworth G. D. Zahorchak A. F. Logar A. J. Wang Z. Watkins S. C. Falo L. D. Jr. Thomson A. W. (2004). Endocytosis, intracellular sorting, and processing of exosomes by dendritic cells. Blood 104, 3257– 3266 10.1182/blood-2004-03-0824 15284116 · DOI
- Munch C. O’Brien J. Bertolotti A. (2011). Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells. Proc. Natl. Acad. Sci. U.S.A. 108, 3548– 3553 10.1073/pnas.1017275108 21321227 PMC3048161 · DOI
- Murakami K. Irie K. Morimoto A. Ohigashi H. Shindo M. Nagao M. Shimizu T. Shirasawa T. (2002). Synthesis, aggregation, neurotoxicity, and secondary structure of various A beta 1-42 mutants of familial Alzheimer’s disease at positions 21-23. Biochem. Biophys. Res. Commun. 294, 5– 10 10.1016/S0006-291X(02)00430-8 12054732 · DOI
- Nelson P. T. Wang W. X. (2010). MiR-107 is reduced in Alzheimer’s disease brain neocortex: validation study. J. Alzheimers Dis. 21, 75– 79 20413881 PMC2910235
- Orru C. D. Hughson A. G. Race B. Raymond G. J. Caughey B. (2012). Time course of prion seeding activity in cerebrospinal fluid of scrapie-infected hamsters after intratongue and intracerebral inoculations. J. Clin. Microbiol. 50, 1464– 1466 10.1128/JCM.06099-11 22238438 PMC3318555 · DOI
- Patel N. Hoang D. Miller N. Ansaloni S. Huang Q. Rogers J. T. Lee J. C. Saunders A. J. (2008). MicroRNAs can regulate human APP levels. Mol Neurodegener 3, 10 10.1186/1750-1326-3-10 18684319 PMC2529281 · DOI
- Pegtel D. M. Cosmopoulos K. Thorley-Lawson D. A. Van Eijndhoven M. A. Hopmans E. S. Lindenberg J. L. De Gruijl T. D. Wurdinger T. Middeldorp J. M. (2010). Functional delivery of viral miRNAs via exosomes. Proc. Natl. Acad. Sci. U.S.A. 107, 6328– 6333 10.1073/pnas.0914843107 20304794 PMC2851954 · DOI
- Pigati L. Yaddanapudi S. C. Iyengar R. Kim D. J. Hearn S. A. Danforth D. Hastings M. L. Duelli D. M. (2010). Selective release of microRNA species from normal and malignant mammary epithelial cells. PLoS ONE 5, e13515 10.1371/journal.pone.0013515 20976003 PMC2958125 · DOI
- Prusiner S. B. (1982). Novel proteinaceous infectious particles cause scrapie. Science 216, 136– 144 10.1126/science.6801762 6801762 · DOI
- Rabinowits G. Gercel-Taylor C. Day J. M. Taylor D. D. Kloecker G. H. (2009). Exosomal microRNA: a diagnostic marker for lung cancer. Clin. Lung Cancer 10, 42– 46 10.3816/CLC.2009.n.006 19289371 · DOI
- Rajendran L. Honsho M. Zahn T. R. Keller P. Geiger K. D. Verkade P. Simons K. (2006). Alzheimer’s disease beta-amyloid peptides are released in association with exosomes. Proc. Natl. Acad. Sci. U.S.A. 103, 11172– 11177 10.1073/pnas.0603838103 16837572 PMC1544060 · DOI · Paper page
- Ratajczak J. Miekus K. Kucia M. Zhang J. Reca R. Dvorak P. Ratajczak M. Z. (2006). Embryonic stem cell-derived microvesicles reprogram hematopoietic progenitors: evidence for horizontal transfer of mRNA and protein delivery. Leukemia 20, 847– 856 10.1038/sj.leu.2404296 16453000 · DOI · Paper page
- Ren P. H. Lauckner J. E. Kachirskaia I. Heuser J. E. Melki R. Kopito R. R. (2009). Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat. Cell Biol. 11, 219– 225 10.1038/ncb1830 19151706 PMC2757079 · DOI
- Saba R. Goodman C. D. Huzarewich R. L. Robertson C. Booth S. A. (2008). A miRNA signature of prion induced neurodegeneration. PLoS ONE 3, e3652 10.1371/journal.pone.0003652 18987751 PMC2575400 · DOI · Paper page
- Schonrock N. Humphreys D. T. Preiss T. Gotz J. (2012). Target gene repression mediated by miRNAs miR-181c and miR-9 both of which are down-regulated by amyloid-beta. J. Mol. Neurosci. 46, 324– 335 10.1007/s12031-011-9587-2 21720722 · DOI
- Schonrock N. Ke Y. D. Humphreys D. Staufenbiel M. Ittner L. M. Preiss T. Gotz J. (2010). Neuronal microRNA deregulation in response to Alzheimer’s disease amyloid-beta. PLoS ONE 5, e11070 10.1371/journal.pone.0011070 20552018 PMC2884018 · DOI · Paper page
- Schorey J. S. Bhatnagar S. (2008). Exosome function: from tumor immunology to pathogen biology. Traffic 9, 871– 881 10.1111/j.1600-0854.2008.00734.x 18331451 PMC3636814 · DOI
- Selkoe D. J. (1996). Cell biology of the b-amyloid precursor protein and the genetics of Alzheimer’s disease. Cold Spring Harb. Symp. Quant. Biol. 61, 587– 596 10.1101/SQB.1996.061.01.059 9246485 · DOI
- Serpell L. C. Smith J. M. (2000). Direct visualisation of the b-sheet structure of synthetic Alzheimer’s amyloid. J. Mol. Biol. 299, 225– 231 10.1006/jmbi.2000.3650 10860734 · DOI
- Sethi P. Lukiw W. J. (2009). Micro-RNA abundance and stability in human brain: specific alterations in Alzheimer’s disease temporal lobe neocortex. Neurosci. Lett. 459, 100– 104 10.1016/j.neulet.2009.04.052 19406203 · DOI · Paper page
- Seubert P. Oltersdorf T. Lee M. G. Barbour R. Blomquist C. Davis D. L. Bryant K. Fritz L. C. Galasko D. Thal L. J. Lieberburg I. Schenk D. B. (1993). Secretion of b-amyloid precursor protein cleaved at the amino terminus of the b-amyloid peptide. Nature 361, 260– 263 10.1038/361260a0 7678698 · DOI
- Sharples R. A. Vella L. J. Nisbet R. M. Naylor R. Perez K. Barnham K. J. Masters C. L. Hill A. F. (2008). Inhibition of gamma-secretase causes increased secretion of amyloid precursor protein C-terminal fragments in association with exosomes. FASEB J. 22, 1469– 1478 10.1096/fj.07-9357com 18171695 · DOI
- Shioya M. Obayashi S. Tabunoki H. Arima K. Saito Y. Ishida T. Satoh J. (2010). Aberrant microRNA expression in the brains of neurodegenerative diseases: miR-29a decreased in Alzheimer disease brains targets neurone navigator 3. Neuropathol. Appl. Neurobiol. 36, 320– 330 10.1111/j.1365-2990.2010.01076.x 20202123 · DOI
- Simons M. Raposo G. (2009). Exosomes – vesicular carriers for intercellular communication. Curr. Opin. Cell Biol. 21, 575– 581 10.1016/j.ceb.2009.03.007 19442504 · DOI
- Skog J. Wurdinger T. Van Rijn S. Meijer D. H. Gainche L. Sena-Esteves M. Curry W. T. Jr. Carter B. S. Krichevsky A. M. Breakefield X. O. (2008). Glioblastoma microvesicles transport RNA and proteins that promote tumour growth and provide diagnostic biomarkers. Nat. Cell Biol. 10, 1470– 1476 10.1038/ncb1800 19011622 PMC3423894 · DOI · Paper page
- Smith P. Y. Delay C. Girard J. Papon M. A. Planel E. Sergeant N. Buee L. Hebert S. S. (2011). MicroRNA-132 loss is associated with tau exon 10 inclusion in progressive supranuclear palsy. Hum. Mol. Genet. 20, 4016– 4024 10.1093/hmg/ddr330 21807765 · DOI
- Sun D. M. Zhuang X. Y. Xiang X. Y. Liu Y. L. Zhang S. Y. Liu C. R. Barnes S. Grizzle W. Miller D. Zhang H. G. (2010). A novel nanoparticle drug delivery system: the anti-inflammatory activity of curcumin is enhanced when encapsulated in exosomes. Mol. Ther. 18, 1606– 1614 10.1038/mt.2010.105 20571541 PMC2956928 · DOI
- Taylor A. R. Robinson M. B. Gifondorwa D. J. Tytell M. Milligan C. E. (2007). Regulation of heat shock protein 70 release in astrocytes: role of signaling kinases. Dev. Neurobiol. 67, 1815– 1829 10.1002/dneu.20559 17701989 · DOI
- Taylor D. D. Gercel-Taylor C. (2008). MicroRNA signatures of tumor-derived exosomes as diagnostic biomarkers of ovarian cancer. Gynecol. Oncol. 110, 13– 21 10.1016/j.ygyno.2008.04.033 18589210 · DOI
- Taylor D. R. Hooper N. M. (2006). The prion protein and lipid rafts. Mol. Membr. Biol. 23, 89– 99 10.1080/09687860500449994 16611584 · DOI
- Thery C. Zitvogel L. Amigorena S. (2002). Exosomes: composition, biogenesis and function. Nat. Rev. Immunol. 2, 569– 579 12154376
- Tian T. Wang Y. Wang H. Zhu Z. Xiao Z. (2010). Visualizing of the cellular uptake and intracellular trafficking of exosomes by live-cell microscopy. J. Cell. Biochem. 111, 488– 496 10.1002/jcb.22709 20533300 · DOI
- Tokuda T. Qureshi M. M. Ardah M. T. Varghese S. Shehab S. A. Kasai T. Ishigami N. Tamaoka A. Nakagawa M. El-Agnaf O. M. (2010). Detection of elevated levels of alpha-synuclein oligomers in CSF from patients with Parkinson disease. Neurology 75, 1766– 1772 10.1212/WNL.0b013e3181fd613b 20962290 · DOI
- Trajkovic K. Hsu C. Chiantia S. Rajendran L. Wenzel D. Wieland F. Schwille P. Brugger B. Simons M. (2008). Ceramide triggers budding of exosome vesicles into multivesicular endosomes. Science 319, 1244– 1247 10.1126/science.1153124 18309083 · DOI
- Turchinovich A. Weiz L. Langheinz A. Burwinkel B. (2011). Characterization of extracellular circulating microRNA. Nucleic Acids Res. 39, 7223– 7233 10.1093/nar/gkr254 21609964 PMC3167594 · DOI · Paper page
- Valadi H. Ekstrom K. Bossios A. Sjostrand M. Lee J. J. Lotvall J. O. (2007). Exosome-mediated transfer of mRNAs and microRNAs is a novel mechanism of genetic exchange between cells. Nat. Cell Biol. 9, 654– U672 10.1038/ncb1596 17486113 · DOI · Paper page
- van den Boorn J. G. Schlee M. Coch C. Hartmann G. (2011). SiRNA delivery with exosome nanoparticles. Nat. Biotechnol. 29, 325– 326 10.1038/nbt.1830 21478846 · DOI · Paper page
- van Dommelen S. M. Vader P. Lakhal S. Kooijmans S. A. Van Solinge W. W. Wood M. J. Schiffelers R. M. (2011). Microvesicles and exosomes: Opportunities for cell-derived membrane vesicles in drug delivery. J. Control Release. 10.1016/j.jconrel.2011.11.021 22138068 · DOI
- van Niel G. Porto-Carreiro I. Simoes S. Raposo G. (2006). Exosomes: a common pathway for a specialized function. J. Biochem. 140, 13– 21 10.1093/jb/mvj128 16877764 · DOI
- Vandermeeren M. Mercken M. Vanmechelen E. Six J. Van De Voorde A. Martin J. J. Cras P. (1993). Detection of tau proteins in normal and Alzheimer’s disease cerebrospinal fluid with a sensitive sandwich enzyme-linked immunosorbent assay. J. Neurochem. 61, 1828– 1834 10.1111/j.1471-4159.1993.tb09823.x 8228996 · DOI
- Vella L. J. Greenwood D. L. Cappai R. Scheerlinck J. P. Hill A. F. (2008). Enrichment of prion protein in exosomes derived from ovine cerebral spinal fluid. Vet. Immunol. Immunopathol. 124, 385– 393 10.1016/j.vetimm.2008.04.002 18501435 · DOI
- Vella L. J. Sharples R. A. Lawson V. A. Masters C. L. Cappai R. Hill A. F. (2007). Packaging of prions into exosomes is associated with a novel pathway of PrP processing. J. Pathol. 211, 582– 590 10.1002/path.2145 17334982 · DOI
- Vickers K. C. Palmisano B. T. Shoucri B. M. Shamburek R. D. Remaley A. T. (2011). MicroRNAs are transported in plasma and delivered to recipient cells by high-density lipoproteins. Nat. Cell Biol. 13, 423– 433 10.1038/ncb2210 21423178 PMC3074610 · DOI · Paper page
- Vidal M. Mangeat P. Hoekstra D. (1997). Aggregation reroutes molecules from a recycling to a vesicle-mediated secretion pathway during reticulocyte maturation. J. Cell. Sci. 110(Pt 16), 1867– 1877 9296387
- Vilardo E. Barbato C. Ciotti M. Cogoni C. Ruberti F. (2010). MicroRNA-101 regulates amyloid precursor protein expression in hippocampal neurons. J. Biol. Chem. 285, 18344– 18351 10.1074/jbc.M110.112664 20395292 PMC2881760 · DOI
- Vilette D. (2008). Cell models of prion infection. Vet. Res. 39, 10 10.1051/vetres:2007049 18073097 · DOI
- Volpicelli-Daley L. A. Luk K. C. Patel T. P. Tanik S. A. Riddle D. M. Stieber A. Meaney D. F. Trojanowski J. Q. Lee V. M. (2011). Exogenous alpha-synuclein fibrils induce Lewy body pathology leading to synaptic dysfunction and neuron death. Neuron 72, 57– 71 10.1016/j.neuron.2011.08.033 21982369 PMC3204802 · DOI · Paper page
- Waehler R. Russell S. J. Curiel D. T. (2007). Engineering targeted viral vectors for gene therapy. Nat. Rev. Genet. 8, 573– 587 10.1038/nrg2141 17607305 PMC7097627 · DOI
- Wanet A. Tacheny A. Arnould T. Renard P. (2012). miR-212/132 expression and functions: within and beyond the neuronal compartment. Nucleic Acids Res. 10.1093/nar/gks151 22362752 PMC3367188 · DOI
- Wang F. Wang X. Yuan C. G. Ma J. (2010). Generating a Prion with bacterially expressed recombinant prion protein. Science 327, 1132– 1135 10.1126/science.1184096 20110469 PMC2893558 · DOI
- Wang F. Yang F. Hu Y. Wang X. Wang X. Jin C. Ma J. (2007). Lipid interaction converts prion protein to a PrPSc-like proteinase K-resistant conformation under physiological conditions. Biochemistry 46, 7045– 7053 10.1021/bi061994u 17503780 · DOI · Paper page
- Wang W. X. Huang Q. Hu Y. Stromberg A. J. Nelson P. T. (2011). Patterns of microRNA expression in normal and early Alzheimer’s disease human temporal cortex: white matter versus gray matter. Acta Neuropathol. 121, 193– 205 10.1007/s00401-010-0756-0 20936480 PMC3073518 · DOI · Paper page
- Wang W. X. Rajeev B. W. Stromberg A. J. Ren N. Tang G. Huang Q. Rigoutsos I. Nelson P. T. (2008). The expression of microRNA miR-107 decreases early in Alzheimer’s disease and may accelerate disease progression through regulation of beta-site amyloid precursor protein-cleaving enzyme 1. J. Neurosci. 28, 1213– 1223 10.1523/JNEUROSCI.0750-08.2008 18234899 PMC2837363 · DOI
- Wilham J. M. Orru C. D. Bessen R. A. Atarashi R. Sano K. Race B. Meade-White K. D. Taubner L. M. Timmes A. Caughey B. (2010). Rapid end-point quantitation of prion seeding activity with sensitivity comparable to bioassays. PLoS Pathog. 6, e1001217 10.1371/journal.ppat.1001217 21152012 PMC2996325 · DOI
- Wubbolts R. Leckie R. S. Veenhuizen P. T. Schwarzmann G. Mobius W. Hoernschemeyer J. Slot J. W. Geuze H. J. Stoorvogel W. (2003). Proteomic and biochemical analyses of human B cell-derived exosomes. Potential implications for their function and multivesicular body formation. J. Biol. Chem. 278, 10963– 10972 10.1074/jbc.M207550200 12519789 · DOI
- Yamazaki T. Koo E. H. Selkoe D. J. (1996). Trafficking of cell-surface amyloid b-protein precursor.2. Endocytosis, recycling, and lysosomal targeting detected by immunolocalization. J. Cell. Sci. 109, 999– 1008 8743947
Cited by
Sorted by citations
Wiklander, O. P. B., Nordin, J. Z., O'Loughlin, A., Gustafsson, Y., Corso, G., Mäger, I., Vader, P., Lee, Y., Sork, H., Seow, Y., et al. (2015) · Journal of Extracellular Vesicles · doi:10.3402/jev.v4.26316 · Cited by 1,730 · see citing works
Brites, D., & Fernandes, A. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00476 · Cited by 599 · see citing works
“Exosomes released by prion-infected neuronal cells showed increased let-7b, let-7i, miR-128a, miR-21, miR-222, miR-29b, miR-342-3p and miR-424 levels, together with reduced miR146a levels as compared to non-infected exosomes (Bellingham et al., 2012a).”
BackgroundAlzheimer’s disease pathology propagation by exosomes containing toxic amyloid-beta oligomers
Sardar Sinha, M., Ansell-Schultz, A., Civitelli, L., Hildesjö, C., Larsson, M., Lannfelt, L., Ingelsson, M., & Hallbeck, M. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1868-1 · Cited by 527 · see citing works
Dinkins, M. B., Dasgupta, S., Wang, G., Zhu, G., & Bieberich, E. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.02.012 · Cited by 494 · see citing works
Neurons secrete miR-132-containing exosomes to regulate brain vascular integrity
Xu, B., Zhang, Y., Du, X.-F., Li, J., Zi, H.-X., Bu, J.-W., Yan, Y., Han, H., & Du, J.-L. (2017) · Cell Research · doi:10.1038/cr.2017.62 · Cited by 354 · see citing works
Glioblastoma: exosome and microRNA as novel diagnosis biomarkers
Saadatpour, L., Fadaee, E., Fadaei, S., Nassiri Mansour, R., Mohammadi, M., Mousavi, S. M., Goodarzi, M., Verdi, J., & Mirzaei, H. (2016) · Cancer Gene Therapy · doi:10.1038/cgt.2016.48 · Cited by 244 · see citing works
Ngolab, J., Trinh, I., Rockenstein, E., Mante, M., Florio, J., Trejo, M., Masliah, D., Adame, A., Masliah, E., & Rissman, R. A. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0445-5 · Cited by 200 · see citing works
RetractedFluid Biomarkers for Synaptic Dysfunction and Loss
Camporesi, E., Nilsson, J., Brinkmalm, A., Becker, B., Ashton, N. J., Blennow, K., & Zetterberg, H. (2020) · Biomarker Insights · doi:10.1177/1177271920950319 · Cited by 165 · see citing works
Exosome-Based Delivery of miR-124 in a Huntington’s Disease Model
Lee, S.-T., Im, W., Ban, J.-J., Lee, M., Jung, K.-H., Lee, S. K., Chu, K., & Kim, M. (2017) · Journal of Movement Disorders · doi:10.14802/jmd.16054 · Cited by 164 · see citing works
Annunziata, I., Patterson, A., Helton, D., Hu, H., Moshiach, S., Gomero, E., Nixon, R., & d’Azzo, A. (2013) · Nature Communications · doi:10.1038/ncomms3734 · Cited by 146 · see citing works
Sullivan, R., Maresh, G., Zhang, X., Salomon, C., Hooper, J., Margolin, D., & Li, L. (2017) · Frontiers in Endocrinology · doi:10.3389/fendo.2017.00194 · Cited by 112 · see citing works
Jiang, S., Maphis, N. M., Binder, J., Chisholm, D., Weston, L., Duran, W., Peterson, C., Zimmerman, A., Mandell, M. A., Jett, S. D., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109720 · Cited by 92 · see citing works
Extracellular vesicles in renal tissue damage and regeneration
Bruno, S., Porta, S., & Bussolati, B. (2016) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2016.06.058 · Cited by 74 · see citing works
Analysis of extracellular vesicles as emerging theranostic nanoplatforms
Xing, Y., Cheng, Z., Wang, R., Lv, C., James, T. D., & Yu, F. (2020) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2020.213506 · Cited by 67 · see citing works
Myeloid extracellular vesicles: messengers from the demented brain
Nigro, A., Colombo, F., Casella, G., Finardi, A., Verderio, C., & Furlan, R. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00017 · Cited by 26 · see citing works
- Authors
- Bellingham, S. A., Guo, B. B., Coleman, B. M., & Hill, A. F.
- Venue
- Frontiers in Physiology
- Publisher
- Frontiers Media SA
- Published
- 2012
- Volume
- 3
- ISSN
- 1664-042X
- PMC
- PMC3342525
- Cited by
- 355
- References
- 17
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