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Linked References

1. A. M. Fendrick, A. S. Monto, B. Nightengale, and M. Sarnes, “The economic burden of non-influenza-related viral respiratory tract infection in the United States,” Archives of Internal Medicine, vol. 163, no. 4, pp. 487–494, 2003. View at Publisher · View at Google Scholar · View at Scopus
2. T. J. Tuthill, E. Groppelli, J. M. Hogle, and D. J. Rowlands, “Picornaviruses,” Current Topics in Microbiology and Immunology, vol. 343, pp. 43–89, 2010. View at Scopus
3. H. Harvala and P. Simmonds, “Human parechoviruses: biology, epidemiology and clinical significance,” Journal of Clinical Virology, vol. 45, no. 1, pp. 1–9, 2009. View at Publisher · View at Google Scholar · View at Scopus
4. National Institute of Allergy and Infectious Diseases, “The common cold,” 2011, http://www.niaid.nih.gov/topics/commonCold/Pages/default.aspx.
5. M. Chambon, C. Archimbaud, J. L. Bailly, et al., “Circulation of enteroviruses and persistence of meningitis cases in the winter of 1999-2000,” Journal of Medical Virology, vol. 65, no. 2, pp. 340–347, 2001. View at Publisher · View at Google Scholar · View at Scopus
6. N. R. Grist, E. J. Bell, and F. Assaad, “Enteroviruses in human disease,” Progress in Medical Virology, vol. 24, pp. 114–157, 1978. View at Scopus
7. B. E. Lee and H. D. Davies, “Aseptic meningitis,” Current Opinion in Infectious Diseases, vol. 20, no. 3, pp. 272–277, 2007. View at Publisher · View at Google Scholar · View at Scopus
8. T. Vuorinen, R. Vainionpää, and T. Hyypiä, “Five years' experience of reverse-transcriptase polymerase chain reaction in daily diagnosis of enterovirus and rhinovirus infections,” Clinical Infectious Diseases, vol. 37, no. 3, pp. 452–455, 2003. View at Publisher · View at Google Scholar · View at Scopus
9. M. S. Oberste and M. A. Pallansch, “Establishing evidence for enterovirus infection in chronic disease,” Annals of the New York Academy of Sciences, vol. 1005, pp. 23–31, 2003. View at Publisher · View at Google Scholar · View at Scopus
10. K. Salminen, K. Sadeharju, M. Lönnrot et al., “Enterovirus infections are associated with the induction of β-cell autoimmunity in a prospective birth cohort study,” Journal of Medical Virology, vol. 69, no. 1, pp. 91–98, 2003. View at Publisher · View at Google Scholar · View at Scopus
11. A. Kotaniemi-Syrjänen, R. Vainionpää, T. M. Reijonen, M. Waris, K. Korhonen, and M. Korppi, “Rhinovirus-induced wheezing in infancy—the first sign of childhood asthma?” Journal of Allergy and Clinical Immunology, vol. 111, no. 1, pp. 66–71, 2003. View at Publisher · View at Google Scholar · View at Scopus
12. R. F. Lemanske, D. J. Jackson, R. E. Gangnon et al., “Rhinovirus illnesses during infancy predict subsequent childhood wheezing,” Journal of Allergy and Clinical Immunology, vol. 116, no. 3, pp. 571–577, 2005. View at Publisher · View at Google Scholar · View at Scopus
13. A. M. Q. King, M. J. Adams, E. B. Carstens, and E. Lefkowitz, “Virus taxonomy: classification and nomenclature of viruses,” 9th Report of the International Committee on the Taxonomy of Viruses, Elsevier Academic Press, San Diego, Calif, USA, 2011.
14. E. Ehrenfeld, E. Domingo, and R. P. Roos, The Picornaviruses, ASM Press, Washington, DC, USA, 2010.
15. M. S. Oberste, K. Maher, D. R. Kilpatrick, and M. A. Pallansch, “Molecular evolution of the human enteroviruses: correlation of serotype with VP1 sequence and application to picornavirus classification,” Journal of Virology, vol. 73, no. 3, pp. 1941–1948, 1999. View at Scopus
16. J. Mercer and A. Helenius, “Virus entry by macropinocytosis,” Nature Cell Biology, vol. 11, no. 5, pp. 510–520, 2009. View at Publisher · View at Google Scholar · View at Scopus
17. M. Marsh and A. Helenius, “Virus entry: open sesame,” Cell, vol. 124, no. 4, pp. 729–740, 2006. View at Publisher · View at Google Scholar · View at Scopus
18. E. M. Damm and L. Pelkmans, “Systems biology of virus entry in mammalian cells,” Cellular Microbiology, vol. 8, no. 8, pp. 1219–1227, 2006. View at Publisher · View at Google Scholar · View at Scopus
19. J. Gruenberg, “Viruses and endosome membrane dynamics,” Current Opinion in Cell Biology, vol. 21, no. 4, pp. 582–588, 2009. View at Publisher · View at Google Scholar · View at Scopus
20. J. Mercer, M. Schelhaas, and A. Helenius, “Virus entry by endocytosis,” Annual Review of Biochemistry, vol. 79, pp. 803–833, 2010. View at Publisher · View at Google Scholar · View at Scopus
21. K. Sandvig, M. L. Torgersen, H. A. Raa, and B. Van Deurs, “Clathrin-independent endocytosis: from nonexisting to an extreme degree of complexity,” Histochemistry and Cell Biology, vol. 129, no. 3, pp. 267–276, 2008. View at Publisher · View at Google Scholar · View at Scopus
22. E. Van Meel and J. Klumperman, “Imaging and imagination: understanding the endo-lysosomal system,” Histochemistry and Cell Biology, vol. 129, no. 3, pp. 253–266, 2008. View at Publisher · View at Google Scholar · View at Scopus
23. G. J. Doherty and H. T. McMahon, “Mechanisms of endocytosis,” Annual Review of Biochemistry, vol. 78, pp. 857–902, 2009. View at Publisher · View at Google Scholar · View at Scopus
24. S. Mayor and R. E. Pagano, “Pathways of clathrin-independent endocytosis,” Nature Reviews Molecular Cell Biology, vol. 8, no. 8, pp. 603–612, 2007. View at Publisher · View at Google Scholar · View at Scopus
25. J. S. Bonifacino and R. Rojas, “Retrograde transport from endosomes to the trans-Golgi network,” Nature Reviews Molecular Cell Biology, vol. 7, no. 8, pp. 568–579, 2006. View at Publisher · View at Google Scholar · View at Scopus
26. J. A. Swanson, “Shaping cups into phagosomes and macropinosomes,” Nature Reviews Molecular Cell Biology, vol. 9, no. 8, pp. 639–649, 2008. View at Publisher · View at Google Scholar · View at Scopus
27. M. C. Kerr and R. D. Teasdale, “Defining macropinocytosis,” Traffic, vol. 10, no. 4, pp. 364–371, 2009. View at Publisher · View at Google Scholar · View at Scopus
28. A. T. Jones, “Macropinocytosis: searching for an endocytic identity and role in the uptake of cell penetrating peptides,” Journal of Cellular and Molecular Medicine, vol. 11, no. 4, pp. 670–684, 2007. View at Publisher · View at Google Scholar · View at Scopus
29. J. G. Donaldson, N. Porat-Shliom, and L. A. Cohen, “Clathrin-independent endocytosis: a unique platform for cell signaling and PM remodeling,” Cellular Signalling, vol. 21, no. 1, pp. 1–6, 2009. View at Publisher · View at Google Scholar · View at Scopus
30. T. J. Wickham, P. Mathias, D. A. Cheresh, and G. R. Nemerow, “Integrins α(v)β3 and α(v)β5 promote adenovirus internalization but not virus attachment,” Cell, vol. 73, no. 2, pp. 309–319, 1993. View at Publisher · View at Google Scholar · View at Scopus
31. M. Jin, J. Park, S. Lee et al., “Hantaan virus enters cells by clathrin-dependent receptor-mediated endocytosis,” Virology, vol. 294, no. 1, pp. 60–69, 2002. View at Publisher · View at Google Scholar · View at Scopus
32. V. O'Donnell, M. LaRocco, H. Duque, and B. Baxt, “Analysis of foot-and-mouth disease virus internalization events in cultured cells,” Journal of Virology, vol. 79, no. 13, pp. 8506–8518, 2005. View at Publisher · View at Google Scholar · View at Scopus
33. T. Hyypiä, C. Horsnell, M. Maaronen et al., “A distinct picornavirus group identified by sequence analysis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 89, no. 18, pp. 8847–8851, 1992. View at Scopus
34. G. Stanway, N. Kalkkinen, M. Roivainen et al., “Molecular and biological characteristics of echovirus 22, a representative of a new picornavirus group,” Journal of Virology, vol. 68, no. 12, pp. 8232–8238, 1994. View at Scopus
35. R. J. Colonno, J. H. Condra, S. Mizutani, P. L. Callahan, M. E. Davies, and M. A. Murcko, “Evidence for the direct involvement of the rhinovirus canyon in receptor binding,” Proceedings of the National Academy of Sciences of the United States of America, vol. 85, no. 15, pp. 5449–5453, 1988. View at Scopus
36. N. H. Olson, P. R. Kolatkar, M. A. Oliveira et al., “Structure of a human rhinovirus complexed with its receptor molecule,” Proceedings of the National Academy of Sciences of the United States of America, vol. 90, no. 2, pp. 507–511, 1993. View at Publisher · View at Google Scholar · View at Scopus
37. M. J. Otto, M. P. Fox, and M. J. Fancher, “In vitro activity of WIN 51711, a new broad-spectrum antipicornavirus drug,” Antimicrobial Agents and Chemotherapy, vol. 27, no. 6, pp. 883–886, 1985. View at Scopus
38. A. K. Patick, “Rhinovirus chemotherapy,” Antiviral Research, vol. 71, no. 2-3, pp. 391–396, 2006. View at Publisher · View at Google Scholar · View at Scopus
39. J. Seitsonen, P. Susi, O. Heikkilä et al., “Interaction of αVβ3 and αVβ6 integrins with human parechovirus 1,” Journal of Virology, vol. 84, no. 17, pp. 8509–8519, 2010. View at Publisher · View at Google Scholar · View at Scopus
40. J. M. Greve, G. Davis, A. M. Meyer et al., “The major human rhinovirus receptor is ICAM-1,” Cell, vol. 56, no. 5, pp. 839–847, 1989. View at Scopus
41. C. L. Mendelsohn, E. Wimmer, and V. R. Racaniello, “Cellular receptor for poliovirus: molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily,” Cell, vol. 56, no. 5, pp. 855–865, 1989. View at Scopus
42. R. O. Hynes, “Integrins: bidirectional, allosteric signaling machines,” Cell, vol. 110, no. 6, pp. 673–687, 2002. View at Publisher · View at Google Scholar · View at Scopus
43. T. Pellinen and J. Ivaska, “Integrin traffic,” Journal of Cell Science, vol. 119, no. 18, pp. 3723–3731, 2006. View at Publisher · View at Google Scholar · View at Scopus
44. M. R. Morgan, M. J. Humphries, and M. D. Bass, “Synergistic control of cell adhesion by integrins and syndecans,” Nature Reviews Molecular Cell Biology, vol. 8, no. 12, pp. 957–969, 2007. View at Publisher · View at Google Scholar · View at Scopus
45. M. A. Arnaout, S. L. Goodman, and J. P. Xiong, “Structure and mechanics of integrin-based cell adhesion,” Current Opinion in Cell Biology, vol. 19, no. 5, pp. 495–507, 2007. View at Publisher · View at Google Scholar · View at Scopus
46. E. Ruoslahti, “RGD and other recognition sequences for integrins,” Annual Review of Cell and Developmental Biology, vol. 12, pp. 697–715, 1996. View at Publisher · View at Google Scholar · View at Scopus
47. O. Heikkilä, P. Susi, G. Stanway, and T. Hyypiä, “Integrin αVβ6 is a high-affinity receptor for coxsackievirus A9,” Journal of General Virology, vol. 90, no. 1, pp. 197–204, 2009. View at Publisher · View at Google Scholar · View at Scopus
48. B. Nelsen-Salz, H. J. Eggers, and H. Zimmermann, “Integrin α(v)β3 (vitronectin receptor) is a candidate receptor for the virulent echovirus 9 strain Barty,” Journal of General Virology, vol. 80, no. 9, pp. 2311–2313, 1999. View at Scopus
49. M. D. Pierschbacher and E. Ruoslahti, “Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion,” Journal of Biological Chemistry, vol. 262, no. 36, pp. 17294–17298, 1987. View at Scopus
50. J. D. Humphries, A. Byron, and M. J. Humphries, “Integrin ligands at a glance,” Journal of Cell Science, vol. 119, no. 19, pp. 3901–3903, 2006. View at Publisher · View at Google Scholar · View at Scopus
51. C. H. Williams, T. Kajander, T. Hyypiä, T. Jackson, D. Sheppard, and G. Stanway, “ntegrin alpha v beta 6 is an RGD-dependent receptor for coxsackievirus A9,” Journal of Virology, vol. 78, no. 13, pp. 6967–6973, 2004. View at Publisher · View at Google Scholar · View at Scopus
52. P. Ylipaasto, M. Eskelinen, K. Salmeda, T. Hovi, and M. Roivainen, “Vitronectin receptors, αv integrins, are recognized by several non-RGD-containing echoviruses in a continuous laboratory cell line and also in primary human Langerhans' islets and endothelial cells,” Journal of General Virology, vol. 91, part 1, pp. 155–165, 2010. View at Publisher · View at Google Scholar · View at Scopus
53. E. Hendry, H. Hatanaka, E. Fry et al., “The crystal structure of coxsackievirus A9: new insights into the uncoating mechanisms of enteroviruses,” Structure, vol. 7, no. 12, pp. 1527–1538, 1999. View at Publisher · View at Google Scholar · View at Scopus
54. L. Xing, M. Huhtala, V. Pietiäinen et al., “Structural and functional analysis of integrin α2i domain interaction with echovirus 1,” Journal of Biological Chemistry, vol. 279, no. 12, pp. 11632–11638, 2004. View at Publisher · View at Google Scholar · View at Scopus
55. M. M. Zutter and S. A. Santoro, “Widespread histologic distribution of the α2β1 integrin cell-surface collagen receptor,” American Journal of Pathology, vol. 137, no. 1, pp. 113–120, 1990. View at Scopus
56. J. M. Bergelson, M. P. Shepley, B. M. C. Chan, M. E. Hemler, and R. W. Finberg, “Identification of the integrin VLA-2 as a receptor for echovirus 1,” Science, vol. 255, no. 5052, pp. 1718–1720, 1992. View at Scopus
57. J. M. Bergelson, B. M. C. Chan, R. W. Finberg, and M. E. Hemler, “The integrin VLA-2 binds echovirus 1 and extracellular matrix ligands by different mechanisms,” Journal of Clinical Investigation, vol. 92, no. 1, pp. 232–239, 1993. View at Scopus
58. S. L. King, J. A. Cunningham, R. W. Finberg, and J. M. Bergelson, “Echovirus 1 interaction with the isolated VLA-2 I domain,” Journal of Virology, vol. 69, no. 5, pp. 3237–3239, 1995. View at Scopus
59. S. L. King, T. Kamata, J. A. Cunningham et al., “Echovirus 1 interaction with the human very late antigen-2 (integrin α2β1) I domain: identification of two independent virus contact sites distinct from the metal ion-dependent adhesion site,” Journal of Biological Chemistry, vol. 272, no. 45, pp. 28518–28522, 1997. View at Publisher · View at Google Scholar · View at Scopus
60. P. Upla, V. Marjomäki, P. Kankaanpää et al., “Clustering induces a lateral redistribution of α2β1 integrin from membrane rafts to caveolae and subsequent protein kinase C-dependent internalization,” Molecular Biology of the Cell, vol. 15, no. 2, pp. 625–636, 2004. View at Publisher · View at Google Scholar · View at Scopus
61. J. Jokinen, D. J. White, M. Salmela et al., “Molecular mechanism of alpha2beta1 integrin interaction with human echovirus 1,” The EMBO Journal, vol. 29, no. 1, pp. 196–208, 2010. View at Scopus
62. L. Pelkmans, J. Kartenbeck, and A. Helenius, “Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER,” Nature Cell Biology, vol. 3, no. 5, pp. 473–483, 2001. View at Publisher · View at Google Scholar · View at Scopus
63. G. J. K. Praefcke and H. T. McMahon, “The dynamin superfamily: universal membrane tubulation and fission molecules?” Nature Reviews Molecular Cell Biology, vol. 5, no. 2, pp. 133–147, 2004. View at Publisher · View at Google Scholar · View at Scopus
64. M. Kirkham and R. G. Parton, “Clathrin-independent endocytosis: new insights into caveolae and non-caveolar lipid raft carriers,” Biochimica et Biophysica Acta, vol. 1746, no. 3, pp. 349–363, 2005. View at Scopus
65. A. Hayer, M. Stoeber, D. Ritz, S. Engel, H. H. Meyer, and A. Helenius, “Caveolin-1 is ubiquitinated and targeted to intralumenal vesicles in endolysosomes for degradation,” Journal of Cell Biology, vol. 191, no. 3, pp. 615–629, 2010. View at Publisher · View at Google Scholar · View at Scopus
66. V. Marjomäki, V. Pietiäinen, H. Matilainen et al., “Internalization of echovirus 1 in caveolae,” Journal of Virology, vol. 76, no. 4, pp. 1856–1865, 2002. View at Publisher · View at Google Scholar · View at Scopus
67. V. Pietiäinen, V. Marjomäki, P. Upla, L. Pelkmans, A. Helenius, and T. Hyypiä, “Echovirus 1 endocytosis into caveosomes requires lipid rafts, dynamin II, and signaling events,” Molecular Biology of the Cell, vol. 15, no. 11, pp. 4911–4925, 2004. View at Publisher · View at Google Scholar · View at Scopus
68. M. Karjalainen, E. Kakkonen, P. Upla et al., “A raft-derived, pak1-regulated entry participates in α2β1 integrin-dependent sorting to caveosomes,” Molecular Biology of the Cell, vol. 19, no. 7, pp. 2857–2869, 2008. View at Publisher · View at Google Scholar · View at Scopus
69. M. Karjalainen, N. Rintanen, M. Lehkonen, et al., “Echovirus 1 infection depends on biogenesis of novel multivesicular bodies,” Cellular Microbiology, vol. 13, no. 12, pp. 1975–1979, 2011.
70. N. Rintanen, M. Karjalainen, J. Alanko, et al., “Calpains promote alpha2beta1 integrin turnover in nonrecycling integrin pathway,” Molecular Biology of the Cell, vol. 23, no. 3, pp. 448–463, 2012.
71. J. L. Dunphy, R. Moravec, K. Ly, T. K. Lasell, P. Melancon, and J. E. Casanova, “The Arf6 GEF GEP100/BRAG2 regulates cell adhesion by controlling endocytosis of β1 integrins,” Current Biology, vol. 16, no. 3, pp. 315–320, 2006. View at Publisher · View at Google Scholar · View at Scopus
72. O. Heikkilä, P. Susi, T. Tevaluoto et al., “Internalization of coxsackievirus A9 is mediated by β2-microglobulin, dynamin, and Arf6 but not by caveolin-1 or clathrin,” Journal of Virology, vol. 84, no. 7, pp. 3666–3681, 2010. View at Publisher · View at Google Scholar · View at Scopus
73. A. Dalwai, S. Ahmad, A. Pacsa, and W. Al-Nakib, “Echovirus type 9 is an important cause of viral encephalitis among infants and young children in Kuwait,” Journal of Clinical Virology, vol. 44, no. 1, pp. 48–51, 2009. View at Publisher · View at Google Scholar · View at Scopus
74. N. Khetsuriani, A. Lamonte-Fowlkes, S. Oberst, and M. A. Pallansch, “Enterovirus surveillance—United States, 1970–2005,” Morbidity and Mortality Weekly Report, vol. 55, no. 8, pp. 1–20, 2006. View at Scopus
75. M. Eisenhut, B. Algawi, T. Wreghitt et al., “Fatal Coxsackie A9 virus infection during an outbreak in a neonatal unit,” Journal of Infection, vol. 40, no. 3, pp. 297–298, 2000. View at Publisher · View at Google Scholar · View at Scopus
76. A. Cui, D. Yu, Z. Zhu et al., “An outbreak of aseptic meningitis caused by coxsackievirus A9 in Gansu, the People's Republic of China,” Virology Journal, vol. 7, article no. 72, 2010. View at Publisher · View at Google Scholar · View at Scopus
77. P. Andersson, K. Edman, and A. M. Lindberg, “Molecular analysis of the echovirus 18 prototype: evidence of interserotypic recombination with echovirus 9,” Virus Research, vol. 85, no. 1, pp. 71–83, 2002. View at Publisher · View at Google Scholar · View at Scopus
78. M. Roivainen, T. Hyypiä, L. Piirainen, N. Kalkkinen, G. Stanway, and T. Hovi, “RGD-dependent entry of coxsackievirus A9 into host cells and its bypass after cleavage of VP1 protein by intestinal proteases,” Journal of Virology, vol. 65, no. 9, pp. 4735–4740, 1991. View at Scopus
79. M. Roivainen, L. Piirainen, T. Hovi et al., “Entry of coxsackievirus a9 into host cells specific interactions with α(v)β3 integrin, the vitronectin receptor,” Virology, vol. 203, no. 2, pp. 357–365, 1994. View at Publisher · View at Google Scholar · View at Scopus
80. J. Santti, H. Harvala, L. Kinnunen, and T. Hyypiä, “Molecular epidemiology and evolution of coxsackievirus A9,” Journal of General Virology, vol. 81, no. 5, pp. 1361–1372, 2000. View at Scopus
81. P. J. Hughes, C. Horsnell, T. Hyypiä, and G. Stanway, “The coxsackievirus A9 RGD motif is not essential for virus viability,” Journal of Virology, vol. 69, no. 12, pp. 8035–8040, 1995. View at Scopus
82. M. Roivainen, L. Piirainen, and T. Hovi, “Efficient RGD-independent entry process of coxsackievirus A9,” Archives of Virology, vol. 141, no. 10, pp. 1909–1919, 1996. View at Scopus
83. O. Heikkilä, E. Karelehto, P. Merilahti, et al., “HSPA5 protein (GRP78) and b2-microglobulin mediate internalization and entry of coxsackievirus A9 via a novel Arf6-dependent entry pathway in human epithelial colon adenocarcinoma cells,” In press.
84. M. Triantafilou, K. Triantafilou, K. M. Wilson, Y. Takada, N. Fernandez, and G. Stanway, “Involvement of beta2-microglobulin and integrin alphavbeta3 molecules in the coxsackievirus A9 infectious cycle,” The Journal of General Virology, vol. 80, part 10, pp. 2591–2600, 1999. View at Scopus
85. S. Shakeel, J. Seitsonen, P. Laurinmäki, et al., “Structural and functional analysis of coxsackievirus A9 receptor binding and uncoating,” In press.
86. K. Triantafilou, D. Fradelizi, K. Wilson, and M. Triantafilou, “GRP78, a coreceptor for coxsackievirus A9, interacts with major histocompatibility complex class I molecules which mediate virus internalization,” Journal of Virology, vol. 76, no. 2, pp. 633–643, 2002. View at Publisher · View at Google Scholar · View at Scopus
87. N. J. McLeish, C. H. Williams, D. Kaloudas, et al., “Symmetry-related clustering of positive charges is a common mechanism for heparan sulfate binding in enteroviruses,” Journal of Virology, vol. 86, no. 20, pp. 11163–11170, 2012.
88. W. Hecker, J. Meyer, R. Boeni, and K. Bienz, “Pinocytotic uptake and intralysosomal crystal formation of Coxsackievirus A9 in monkey kidney cells—an electron microscopic autoradiographic study,” Archiv für die Gesamte Virusforschung, vol. 46, no. 1-2, pp. 167–174, 1974. View at Publisher · View at Google Scholar · View at Scopus
89. K. Triantafilou and M. Triantafilou, “Lipid raft microdomains: key sites for coxsackievirus A9 infectious cycle,” Virology, vol. 317, no. 1, pp. 128–135, 2003. View at Publisher · View at Google Scholar · View at Scopus
90. A. D. Stuart, H. E. Eustace, T. A. McKee, and T. D. K. Brown, “A novel cell entry pathway for a DAF-using human enterovirus is dependent on lipid rafts,” Journal of Virology, vol. 76, no. 18, pp. 9307–9322, 2002. View at Publisher · View at Google Scholar · View at Scopus
91. E. Macia, M. Ehrlich, R. Massol, E. Boucrot, C. Brunner, and T. Kirchhausen, “Dynasore, a cell-permeable inhibitor of dynamin,” Developmental Cell, vol. 10, no. 6, pp. 839–850, 2006. View at Publisher · View at Google Scholar · View at Scopus
92. K. Nishi and K. Saigo, “Cellular internalization of green fluorescent protein fused with herpes simplex virus protein VP22 via a lipid raft-mediated endocytic pathway independent of caveolae and Rho family GTPases but dependent on dynamin and Arf6,” Journal of Biological Chemistry, vol. 282, no. 37, pp. 27503–27517, 2007. View at Publisher · View at Google Scholar · View at Scopus
93. N. Naslavsky, R. Weigert, and J. G. Donaldson, “Characterization of a nonclathrin endocytic pathway: membrane cargo and lipid requirements,” Molecular Biology of the Cell, vol. 15, no. 8, pp. 3542–3552, 2004. View at Publisher · View at Google Scholar · View at Scopus
94. T. Ward, R. M. Powell, P. A. Pipkin, D. J. Evans, P. D. Minor, and J. W. Almond, “Role for β2-microglobulin in echovirus infection of rhabdomyosarcoma cells,” Journal of Virology, vol. 72, no. 7, pp. 5360–5365, 1998. View at Scopus
95. N. Naslavsky, R. Weigert, and J. G. Donaldson, “Convergence of non-clathrin- and clathrin-derived endosomes involves Arf6 inactivation and changes in phosphoinositides,” Molecular Biology of the Cell, vol. 14, no. 2, pp. 417–431, 2003. View at Publisher · View at Google Scholar · View at Scopus
96. R. Weigert, A. C. Yeung, J. Li, and J. G. Donaldson, “Rab22a regulates the recycling of membrane proteins internalized independently of clathrin,” Molecular Biology of the Cell, vol. 15, no. 8, pp. 3758–3770, 2004. View at Publisher · View at Google Scholar · View at Scopus
97. A. Ehrnst and M. Eriksson, “Epidemiological features of type 22 echovirus infection,” Scandinavian Journal of Infectious Diseases, vol. 25, no. 3, pp. 275–281, 1993. View at Scopus
98. P. Joki-Korpela and T. Hyypiä, “Diagnosis and epidemiology of echovirus 22 infections,” Clinical Infectious Diseases, vol. 27, no. 1, pp. 129–136, 1998. View at Scopus
99. S. Tauriainen, M. Martiskainen, S. Oikarinen et al., “Human parechovirus 1 infections in young children—no association with type 1 diabetes,” Journal of Medical Virology, vol. 79, no. 4, pp. 457–462, 2007. View at Publisher · View at Google Scholar · View at Scopus
100. R. Wigand and A. B. Sabin, “Properties of ECHO types 22, 23 and 24 viruses,” Archiv für die Gesamte Virusforschung, vol. 11, no. 2, pp. 224–247, 1961. View at Publisher · View at Google Scholar · View at Scopus
101. M. Koskiniemi, R. Paetau, and K. Linnavuori, “Severe encephalitis associated with disseminated echovirus 22 infection,” Scandinavian Journal of Infectious Diseases, vol. 21, no. 4, pp. 463–466, 1989. View at Scopus
102. E. Ruoslahti and M. D. Pierschbacher, “New perspectives in cell adhesion: RGD and integrins,” Science, vol. 238, no. 4826, pp. 491–497, 1987. View at Scopus
103. T. Pulli, E. Koivunen, and T. Hyypiä, “Cell-surface interactions of echovirus 22,” Journal of Biological Chemistry, vol. 272, no. 34, pp. 21176–21180, 1997. View at Publisher · View at Google Scholar · View at Scopus
104. K. Triantafilou, M. Triantafilou, Y. Takada, and N. Fernandez, “Human parechovirus 1 utilizes integrins αvβ3 and αvβ1 as receptors,” Journal of Virology, vol. 74, no. 13, pp. 5856–5862, 2000. View at Publisher · View at Google Scholar · View at Scopus
105. P. Joki-Korpela, V. Marjomäki, C. Krogerus, J. Heino, and T. Hyypiä, “Entry of human parechovirus 1,” Journal of Virology, vol. 75, no. 4, pp. 1958–1967, 2001. View at Publisher · View at Google Scholar · View at Scopus
106. Y. Boonyakiat, P. J. Hughes, F. Ghazi, and G. Stanway, “Arginine-glycine-aspartic acid motif is critical for human parechovirus 1 entry,” Journal of Virology, vol. 75, no. 20, pp. 10000–10004, 2001. View at Publisher · View at Google Scholar · View at Scopus
107. D. K. Sharma, J. C. Brown, A. Choudhury et al., “Selective stimulation of caveolar endocytosis by glycosphingolipids and cholesterol,” Molecular Biology of the Cell, vol. 15, no. 7, pp. 3114–3122, 2004. View at Publisher · View at Google Scholar · View at Scopus
108. A. M. Powelka, J. Sun, J. Li et al., “Stimulation-dependent recycling of integrin β1 regulated by ARF6 and Rab11,” Traffic, vol. 5, no. 1, pp. 20–36, 2004. View at Publisher · View at Google Scholar · View at Scopus
109. B. Snijder, R. Sacher, P. Ramo, et al., “Single-cell analysis of population context advances RNAi screening at multiple levels,” Molecular Systems Biology, vol. 8, article no. 579, 2012. View at Publisher · View at Google Scholar
110. D. Cox, M. Brennan, and N. Moran, “Integrins as therapeutic targets: lessons and opportunities,” Nature Reviews Drug Discovery, vol. 9, no. 10, pp. 804–820, 2010. View at Publisher · View at Google Scholar · View at Scopus