Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 157

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Emerging picture of host chaperone and cyclophilin roles in RNA virus replication

Nagy, P.D., Wang, R.Y., Pogany, J., Hafren, A., Makinen, K.·2011·Virology

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.virol.2010.12.061

Cites

2 of 2 references verified0 citation errors · 0 not checkable

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.

A few free checks a day · papers already verified open instantly · results are public

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 2 references

Research works printed but not linked: 110

  1. Ahsen, 1997, Molecular chaperones: towards a characterization of the heat-shock protein 70 family, Trends Cell Biol., 7, 129, 10.1016/S0962-8924(96)10056-8 · DOI
  2. Alzhanova, 2001, Cell-to-cell movement and assembly of a plant closterovirus: roles for the capsid proteins and Hsp70 homolog, EMBO J., 20, 6997, 10.1093/emboj/20.24.6997 · DOI
  3. Aparicio, 2005, Virus induction of heat shock protein 70 reflects a general response to protein accumulation in the plant cytosol, Plant Physiol., 138, 529, 10.1104/pp.104.058958 · DOI
  4. Aranda, 1996, Induction of HSP70 and polyubiquitin expression associated with plant virus replication, Proc. Natl. Acad. Sci. U. S. A., 93, 15289, 10.1073/pnas.93.26.15289 · DOI
  5. Arevalo-Rodriguez, 2004, Prolyl isomerases in yeast, Front. Biosci., 9, 2420, 10.2741/1405 · DOI
  6. Arndt, 2007, To be, or not to be—molecular chaperones in protein degradation, Cell. Mol. Life Sci., 64, 2525, 10.1007/s00018-007-7188-6 · DOI
  7. Babu, 2008, Altered gene expression changes in Arabidopsis leaf tissues and protoplasts in response to Plum pox virus infection, BMC Genomics, 9, 325, 10.1186/1471-2164-9-325 · DOI
  8. Berthoux, 2005, Cyclophilin A is required for TRIM5{alpha}-mediated resistance to HIV-1 in Old World monkey cells, Proc. Natl. Acad. Sci. U. S. A., 102, 14849, 10.1073/pnas.0505659102 · DOI
  9. Blatch, 1999, The tetratricopeptide repeat: a structural motif mediating protein-protein interactions, Bioessays, 21, 932, 10.1002/(SICI)1521-1878(199911)21:11<932::AID-BIES5>3.0.CO;2-N · DOI
  10. Brennan, 2008, TRIMCyp expression in Old World primates Macaca nemestrina and Macaca fascicularis, Proc. Natl. Acad. Sci. U. S. A., 105, 3569, 10.1073/pnas.0709511105 · DOI
  11. Brown, 2005, Evidence for an association between heat shock protein 70 and the respiratory syncytial virus polymerase complex within lipid-raft membranes during virus infection, Virology, 338, 69, 10.1016/j.virol.2005.05.004 · DOI
  12. Cajo, 2006, The role of the DIF motif of the DnaJ (Hsp40) co-chaperone in the regulation of the DnaK (Hsp70) chaperone cycle, J. Biol. Chem., 281, 12436, 10.1074/jbc.M511192200 · DOI
  13. Bukau, 1998, The Hsp70 and Hsp60 chaperone machines, Cell, 92, 351, 10.1016/S0092-8674(00)80928-9 · DOI
  14. Castorena, 2007, A functional heat shock protein 90 chaperone is essential for efficient flock house virus RNA polymerase synthesis in Drosophila cells, J. Virol., 81, 8412, 10.1128/JVI.00189-07 · DOI
  15. Chatterji, 2009, The isomerase active site of cyclophilin A is critical for hepatitis C virus replication, J. Biol. Chem., 284, 16998, 10.1074/jbc.M109.007625 · DOI
  16. Chatterji, 2010, HCV resistance to cyclosporin A does not correlate with a resistance of the NS5A-cyclophilin A interaction to cyclophilin inhibitors, J. Hepatol., 53, 50, 10.1016/j.jhep.2010.01.041 · DOI
  17. Chen, 1998, Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery, J. Biol. Chem., 273, 35194, 10.1074/jbc.273.52.35194 · DOI
  18. Chen, 2010, Heat shock protein 72 is associated with the hepatitis C virus replicase complex and enhances viral RNA replication, J. Biol. Chem., 285, 28183, 10.1074/jbc.M110.118323 · DOI
  19. Chen, 2008, Influence of cytoplasmic heat shock protein 70 on viral infection of Nicotiana benthamiana, Mol. Plant Pathol., 9, 809, 10.1111/j.1364-3703.2008.00505.x · DOI
  20. Cimarelli, 1999, Translation elongation factor 1-alpha interacts specifically with the human immunodeficiency virus type 1 Gag polyprotein, J. Virol., 73, 5388, 10.1128/JVI.73.7.5388-5401.1999 · DOI
  21. Coelmont, 2010, DEB025 (Alisporivir) inhibits hepatitis C virus replication by preventing a cyclophilin A induced cis–trans isomerisation in domain II of NS5A, PLoS ONE, 5, e13687, 10.1371/journal.pone.0013687 · DOI
  22. Connor, 2007, Antiviral activity and RNA polymerase degradation following Hsp90 inhibition in a range of negative strand viruses, Virology, 362, 109, 10.1016/j.virol.2006.12.026 · DOI
  23. De Nova-Ocampo, 2002, Translation elongation factor-1alpha, La, and PTB interact with the 3′ untranslated region of dengue 4 virus RNA, Virology, 295, 337, 10.1006/viro.2002.1407 · DOI
  24. den Boon, 2010, Organelle-like membrane compartmentalization of positive-strand RNA virus replication factories, Annu. Rev. Microbiol., 64, 241, 10.1146/annurev.micro.112408.134012 · DOI
  25. Dreher, 1999, Functions of the 3′-untranslated regions of positive strand RNA viral genomes, Annu. Rev. Phytopathol., 37, 151, 10.1146/annurev.phyto.37.1.151 · DOI
  26. Dufresne, 2008, Heat shock 70 protein interaction with Turnip mosaic virus RNA-dependent RNA polymerase within virus-induced membrane vesicles, Virology, 374, 217, 10.1016/j.virol.2007.12.014 · DOI
  27. Frolova, 2006, Formation of nsP3-specific protein complexes during Sindbis virus replication, J. Virol., 80, 4122, 10.1128/JVI.80.8.4122-4134.2006 · DOI
  28. Gaither, 2010, Multiple cyclophilins involved in different cellular pathways mediate HCV replication, Virology, 397, 43, 10.1016/j.virol.2009.10.043 · DOI
  29. Galat, 2004, Function-dependent clustering of orthologues and paralogues of cyclophilins, Proteins, 56, 808, 10.1002/prot.20156 · DOI
  30. Galat, 2010, Molecular aspects of cyclophilins mediating therapeutic actions of their ligands, Cell. Mol. Life Sci., 67, 3467, 10.1007/s00018-010-0437-0 · DOI
  31. Geller, 2007, Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance, Genes Dev., 21, 195, 10.1101/gad.1505307 · DOI
  32. Gonzalez, 2009, The heat shock protein inhibitor Quercetin attenuates hepatitis C virus production, Hepatology, 50, 1756, 10.1002/hep.23232 · DOI
  33. Gursinsky, 2009, Replication of Tomato bushy stunt virus RNA in a plant in vitro system, Virology, 390, 250, 10.1016/j.virol.2009.05.009 · DOI
  34. Hafren, 2010, HSP70 and its cochaperone CPIP promote potyvirus infection in Nicotiana benthamiana by regulating viral coat protein functions, Plant Cell, 22, 523, 10.1105/tpc.109.072413 · DOI
  35. Hartl, 2002, Molecular chaperones in the cytosol: from nascent chain to folded protein, Science, 295, 1852, 10.1126/science.1068408 · DOI
  36. Hayashi, 2009, Heat shock cognate protein 70 controls Borna disease virus replication via interaction with the viral non-structural protein X, Microbes Infect., 11, 394, 10.1016/j.micinf.2009.01.006 · DOI
  37. Heck, 2009, Cyclophilin B stimulates RNA synthesis by the HCV RNA dependent RNA polymerase, Biochem. Pharmacol., 77, 1173, 10.1016/j.bcp.2008.12.019 · DOI
  38. Hennessy, 2005, Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions, Protein Sci., 14, 1697, 10.1110/ps.051406805 · DOI
  39. Hu, 2004, Requirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function, J. Virol., 78, 13122, 10.1128/JVI.78.23.13122-13131.2004 · DOI
  40. James, 1997, Functional specificity among Hsp70 molecular chaperones, Science, 275, 387, 10.1126/science.275.5298.387 · DOI
  41. Johnson, 2001, The NS5A protein of bovine viral diarrhoea virus interacts with the alpha subunit of translation elongation factor-1, J. Gen. Virol., 82, 2935, 10.1099/0022-1317-82-12-2935 · DOI
  42. Jockusch, 2001, Mutants of tobacco mosaic virus with temperature-sensitive coat proteins induce heat shock response in tobacco leaves, Mol. Plant Microbe Interact, 14, 914, 10.1094/MPMI.2001.14.7.914 · DOI
  43. Jonczyk, 2007, Exploiting alternative subcellular location for replication: tombusvirus replication switches to the endoplasmic reticulum in the absence of peroxisomes, Virology, 362, 320, 10.1016/j.virol.2007.01.004 · DOI
  44. Kampinga, 2010, The HSP70 chaperone machinery: J proteins as drivers of functional specificity, Nat. Rev. Mol. Cell Biol., 11, 579, 10.1038/nrm2941 · DOI
  45. Kaul, 2009, Essential role of cyclophilin A for hepatitis C virus replication and virus production and possible link to polyprotein cleavage kinetics, PLoS Pathog., 5, e1000546, 10.1371/journal.ppat.1000546 · DOI
  46. Kou, 2006, Hepatitis C virus NS4A inhibits cap-dependent and the viral IRES-mediated translation through interacting with eukaryotic elongation factor 1A, J. Biomed. Sci., 13, 861, 10.1007/s11373-006-9104-8 · DOI
  47. Lee, 2010, Current implications of cyclophilins in human cancers, J. Exp. Clin. Cancer Res., 29, 97, 10.1186/1756-9966-29-97 · DOI
  48. Li, 2008, Cdc34p ubiquitin-conjugating enzyme is a component of the tombusvirus replicase complex and ubiquitinates p33 replication protein, J. Virol., 82, 6911, 10.1128/JVI.00702-08 · DOI · Paper page
  49. Li, 2009, Translation elongation factor 1A is a component of the tombusvirus replicase complex and affects the stability of the p33 replication co-factor, Virology, 385, 245, 10.1016/j.virol.2008.11.041 · DOI
  50. Li, 2010, Translation elongation factor 1A facilitates the assembly of the tombusvirus replicase and stimulates minus-strand synthesis, PLoS Pathog., 6, e1001175, 10.1371/journal.ppat.1001175 · DOI
  51. Liu, 1999, Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeats, J. Biol. Chem., 274, 34425, 10.1074/jbc.274.48.34425 · DOI
  52. Liu, 2009, Cyclophilin A interacts with influenza A virus M1 protein and impairs the early stage of the viral replication, Cell Microbiol., 10.1111/j.1462-5822.2009.01286.x · DOI
  53. Liu, 2009, Critical role of cyclophilin A and its prolyl–peptidyl isomerase activity in the structure and function of the hepatitis C virus replication complex, J. Virol., 83, 6554, 10.1128/JVI.02550-08 · DOI
  54. Luban, 1993, Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B, Cell, 73, 1067, 10.1016/0092-8674(93)90637-6 · DOI
  55. Maggioni, 2005, Synthesis and quality control of viral membrane proteins, Curr. Top. Microbiol. Immunol., 285, 175
  56. Mayer, 2005, Recruitment of Hsp70 chaperones: a crucial part of viral survival strategies, Rev. Physiol. Biochem. Pharmacol., 153, 1, 10.1007/s10254-004-0025-5 · DOI
  57. Mayer, 2010, Gymnastics of molecular chaperones, Mol. Cell, 39, 321, 10.1016/j.molcel.2010.07.012 · DOI
  58. Mayer, 2005, Hsp70 chaperones: cellular functions and molecular mechanism, Cell. Mol. Life Sci., 62, 670, 10.1007/s00018-004-4464-6 · DOI
  59. McCartney, 2005, Localization of the tomato bushy stunt virus replication protein p33 reveals a peroxisome-to-endoplasmic reticulum sorting pathway, Plant Cell, 17, 3513, 10.1105/tpc.105.036350 · DOI
  60. Mendu, 2010, Cpr1 cyclophilin and Ess1 parvulin prolyl isomerases interact with the tombusvirus replication protein and inhibit viral replication in yeast model host, Virology, 406, 342, 10.1016/j.virol.2010.07.022 · DOI · Paper page
  61. Miernyk, 2001, The J-domain proteins of Arabidopsis thaliana: an unexpectedly large and diverse family of chaperones, Cell Stress Chaperones, 6, 209, 10.1379/1466-1268(2001)006<0209:TJDPOA>2.0.CO;2 · DOI
  62. Miller, 2008, Modification of intracellular membrane structures for virus replication, Nat. Rev. Microbiol., 6, 363, 10.1038/nrmicro1890 · DOI
  63. Momose, 2002, Identification of Hsp90 as a stimulatory host factor involved in influenza virus RNA synthesis, J. Biol. Chem., 277, 45306, 10.1074/jbc.M206822200 · DOI
  64. Nagy, 2008, Yeast as a model host to explore plant virus–host interactions, Annu. Rev. Phytopathol., 46, 217, 10.1146/annurev.phyto.121407.093958 · DOI
  65. Nagy, 2010, Global genomics and proteomics approaches to identify host factors as targets to induce resistance against tomato bushy stunt virus, Adv. Virus Res., 76, 123, 10.1016/S0065-3527(10)76004-8 · DOI
  66. Naito, 2007, Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunits, J. Virol., 81, 1339, 10.1128/JVI.01917-06 · DOI
  67. Nakagawa, 2004, Specific inhibition of hepatitis C virus replication by cyclosporin A, Biochem. Biophys. Res. Commun., 313, 42, 10.1016/j.bbrc.2003.11.080 · DOI
  68. Nishikiori, 2006, Membrane-bound tomato mosaic virus replication proteins participate in RNA synthesis and are associated with host proteins in a pattern distinct from those that are not membrane bound, J. Virol., 80, 8459, 10.1128/JVI.00545-06 · DOI
  69. Novoa, 2005, Virus factories: associations of cell organelles for viral replication and morphogenesis, Biol. Cell, 97, 147, 10.1042/BC20040058 · DOI
  70. Okamoto, 2006, Hepatitis C virus RNA replication is regulated by FKBP8 and Hsp90, EMBO J., 25, 5015, 10.1038/sj.emboj.7601367 · DOI
  71. Panavas, 2005, The role of the p33:p33/p92 interaction domain in RNA replication and intracellular localization of p33 and p92 proteins of Cucumber necrosis tombusvirus, Virology, 338, 81, 10.1016/j.virol.2005.04.025 · DOI
  72. Parent, 2009, The heat shock cognate protein 70 is associated with hepatitis C virus particles and modulates virus infectivity, Hepatology, 49, 1798, 10.1002/hep.22852 · DOI
  73. Pastorino, 2009, Identification of cellular proteome modifications in response to West Nile virus infection, Mol. Cell. Proteomics, 8, 1623, 10.1074/mcp.M800565-MCP200 · DOI
  74. Pathak, 2008, The host Pex19p plays a role in peroxisomal localization of tombusvirus replication proteins, Virology, 379, 294, 10.1016/j.virol.2008.06.044 · DOI
  75. Peremyslov, 1999, HSP70 homolog functions in cell-to-cell movement of a plant virus, Proc. Natl. Acad. Sci. U. S. A., 96, 14771, 10.1073/pnas.96.26.14771 · DOI
  76. Pogany, 2008, In vitro assembly of the Tomato bushy stunt virus replicase requires the host Heat shock protein 70, Proc. Natl. Acad. Sci. U. S. A., 105, 19956, 10.1073/pnas.0810851105 · DOI
  77. Qanungo, 2004, Two RNA polymerase complexes from vesicular stomatitis virus-infected cells that carry out transcription and replication of genome RNA, Proc. Natl. Acad. Sci. U. S. A., 101, 5952, 10.1073/pnas.0401449101 · DOI
  78. Qing, 2009, Cyclosporine inhibits flavivirus replication through blocking the interaction between host cyclophilins and viral NS5 protein, Antimicrob. Agents Chemother., 53, 3226, 10.1128/AAC.00189-09 · DOI
  79. Qiu, 2006, The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones, Cell. Mol. Life Sci., 63, 2560, 10.1007/s00018-006-6192-6 · DOI
  80. Rajan, 2009, Arabidopsis thaliana J-class heat shock proteins: cellular stress sensors, Funct. Integr. Genomics, 9, 433, 10.1007/s10142-009-0132-0 · DOI
  81. Rudiger, 1997, Interaction of Hsp70 chaperones with substrates, Nat. Struct. Biol., 4, 342, 10.1038/nsb0597-342 · DOI
  82. Russell, 1999, DnaJ dramatically stimulates ATP hydrolysis by DnaK: insight into targeting of Hsp70 proteins to polypeptide substrates, Biochemistry, 38, 4165, 10.1021/bi9824036 · DOI
  83. Serva, 2006, Proteomics analysis of the tombusvirus replicase: Hsp70 molecular chaperone is associated with the replicase and enhances viral RNA replication, J. Virol., 80, 2162, 10.1128/JVI.80.5.2162-2169.2006 · DOI · Paper page
  84. Sokolskaja, 2006, Cyclophilin, TRIM5, and innate immunity to HIV-1, Curr. Opin. Microbiol., 9, 404, 10.1016/j.mib.2006.06.011 · DOI
  85. Stahl, 2007, Chaperone activation of the hepadnaviral reverse transcriptase for template RNA binding is established by the Hsp70 and stimulated by the Hsp90 system, Nucleic Acids Res., 35, 6124, 10.1093/nar/gkm628 · DOI
  86. Strebel, 2009, Human cellular restriction factors that target HIV-1 replication, BMC Med., 7, 48, 10.1186/1741-7015-7-48 · DOI
  87. Summers, 2009, Polypeptide transfer from Hsp40 to Hsp70 molecular chaperones, Trends Biochem. Sci., 34, 230, 10.1016/j.tibs.2008.12.009 · DOI
  88. Szabo, 1994, The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE, Proc. Natl. Acad. Sci. U.S.A., 91, 10345, 10.1073/pnas.91.22.10345 · DOI
  89. Taguwa, 2009, Cochaperone activity of human butyrate-induced transcript 1 facilitates hepatitis C virus replication through an Hsp90-dependent pathway, J. Virol., 83, 10427, 10.1128/JVI.01035-09 · DOI
  90. Takeshita, 2010, Assembly of Q{beta} viral RNA polymerase with host translational elongation factors EF-Tu and -Ts, Proc. Natl. Acad. Sci. U. S. A., 107, 15733, 10.1073/pnas.1006559107 · DOI
  91. Takeuchi, 2007, Vif counteracts a cyclophilin A-imposed inhibition of simian immunodeficiency viruses in human cells, J. Virol., 81, 8080, 10.1128/JVI.02727-06 · DOI
  92. Tavis, 1998, The duck hepatitis B virus polymerase is activated by its RNA packaging signal, epsilon, J. Virol., 72, 5789, 10.1128/JVI.72.7.5789-5796.1998 · DOI
  93. Thivierge, 2008, Eukaryotic elongation factor 1A interacts with Turnip mosaic virus RNA-dependent RNA polymerase and VPg-Pro in virus-induced vesicles, Virology, 377, 216, 10.1016/j.virol.2008.04.015 · DOI
  94. Tomita, 2003, Mutation of host DnaJ homolog inhibits brome mosaic virus negative-strand RNA synthesis, J. Virol., 77, 2990, 10.1128/JVI.77.5.2990-2997.2003 · DOI
  95. Ujino, 2009, Heat-shock protein 90 is essential for stabilization of the hepatitis C virus nonstructural protein NS3, J. Biol. Chem., 284, 6841, 10.1074/jbc.M806452200 · DOI
  96. Wang, 2004, Forced expression of heat-shock protein 70 increases the secretion of Hsp70 and provides protection against tumour growth, Br. J. Cancer, 90, 926, 10.1038/sj.bjc.6601583 · DOI
  97. Wang, 2005, The cyclophilins, Genome Biol., 6, 226, 10.1186/gb-2005-6-7-226 · DOI
  98. Wang, 2006, Hepatitis C virus non-structural protein NS5A interacts with FKBP38 and inhibits apoptosis in Huh7 hepatoma cells, FEBS Lett., 580, 4392, 10.1016/j.febslet.2006.07.002 · DOI
  99. Wang, 2009, A key role for heat shock protein 70 in the localization and insertion of tombusvirus replication proteins to intracellular membranes, J. Virol., 83, 3276, 10.1128/JVI.02313-08 · DOI
  100. Wang, 2009, A temperature sensitive mutant of heat shock protein 70 reveals an essential role during the early steps of tombusvirus replication, Virology, 394, 28, 10.1016/j.virol.2009.08.003 · DOI
  101. Watashi, 2003, Cyclosporin A suppresses replication of hepatitis C virus genome in cultured hepatocytes, Hepatology, 38, 1282, 10.1053/jhep.2003.50449 · DOI
  102. Watashi, 2005, Cyclophilin B is a functional regulator of hepatitis C virus RNA polymerase, Mol. Cell, 19, 111, 10.1016/j.molcel.2005.05.014 · DOI
  103. Weeks, 2008, The heat shock protein 70 cochaperone YDJ1 is required for efficient membrane-specific flock house virus RNA replication complex assembly and function in Saccharomyces cerevisiae, J. Virol., 82, 2004, 10.1128/JVI.02017-07 · DOI
  104. Weeks, 2010, A targeted analysis of cellular chaperones reveals contrasting roles for heat shock protein 70 in flock house virus RNA replication, J. Virol., 84, 330, 10.1128/JVI.01808-09 · DOI
  105. Whitham, 2003, Diverse RNA viruses elicit the expression of common sets of genes in susceptible Arabidopsis thaliana plants, Plant J., 33, 271, 10.1046/j.1365-313X.2003.01625.x · DOI
  106. Whitham, 2006, Global impact: elucidating plant responses to viral infection, Mol. Plant-Microbe Interact., 19, 1207, 10.1094/MPMI-19-1207 · DOI
  107. Yamaji, 2006, In vivo interaction between Tobacco mosaic virus RNA-dependent RNA polymerase and host translation elongation factor 1A, Virology, 347, 100, 10.1016/j.virol.2005.11.031 · DOI
  108. Yang, 2008, Cyclophilin A is an essential cofactor for hepatitis C virus infection and the principal mediator of cyclosporine resistance in vitro, J. Virol., 82, 5269, 10.1128/JVI.02614-07 · DOI
  109. Yang, 2010, A major determinant of cyclophilin dependence and cyclosporine susceptibility of hepatitis C virus identified by a genetic approach, PLoS Pathog., 6, 10.1371/journal.ppat.1001118 · DOI
  110. Zeenko, 2002, Eukaryotic elongation factor 1A interacts with the upstream pseudoknot domain in the 3′ untranslated region of tobacco mosaic virus RNA, J. Virol., 76, 5678, 10.1128/JVI.76.11.5678-5691.2002 · DOI

Cited by

Metadata

Authors
Nagy, P. D., Wang, R. Y., Pogany, J., Hafren, A., & Makinen, K.
Venue
Virology
Publisher
Elsevier BV
Published
2011-03
Volume
411
Issue
2
Pages
374-382
ISSN
0042-6822
Cited by
157
References
2
Language
en
Funders
  • National Science Foundation (IOB-0517218)
  • NIH-NIAID
  • Acagemy of Finland (206870)

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.