References
- Beaty B. J., Rayms-Keller A., Borucki M. K., Blair C D. LaCrosse encephalitis virus and mosquitoes: a remarkable host-parasite relationship. ASM News 2000, In press
- Calisher C. H. Medically important arboviruses of the United States and Canada. Clinical Microbiology Reviews 1994; 7: 89–116
- Farr G. W., Scharl E. C., Schumacher R. J., Sondek S., Hor-Wich A. L. Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and normative forms. Cell 1997; 89: 927–937
- Frydman J., Nimmesgern E., Ohtsuka K., Hartl F. U. Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature 1994; 370: 111–117
- Gao Y., Thomas J. O., Chow R. L., Lee G. H., Cowan N. J. A cytoplasmic chaperonin that catalyzes beta-actin folding. Cell 1992; 69: 1043–1050
- Kashuba E., Pokrovskaja K., Klein G., Szekely L. Epstein-Barr virus-encoded nuclear protein EBNA-3 interacts with the epsilon-subunit of the T-complex protein 1 chaperonin complex. journal of Human Virology 1999; 2: 33–37
- Kozak M. Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell 1986; 44: 283–292
- Kubota H., Hynes G., Came A., Ashworth A., Willison K. Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin. Current Biology 1994; 4: 89–99
- Kubota H., Hynes G., Willison K. The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubu-nit machinery assisting in protein folding and assembly in the eukaryotic cytosol. European Journal of Biochemistry 1995; 230: 3–16
- Kubota H., Yokota S., Yanagi H., Yura T. Structures and co-regulated expression of the genes encoding mouse cytosolic chaperonin CCT subunits. European Journal of Biochemistry 1999; 262: 492–500
- Lewis V. A., Hynes G. M., Zheng D., Saibil H., Willison K. T-complex polypeptide-l is a subunit of a hetero-meric particle in the eukaryotic cytosol. Nature 1992; 358: 249–252
- Lin P., Sherman F. The unique hetero-oligomeric nature of the subunits in the catalytic cooperativity of the yeast Cct chaperonin complex. The National Academy of Sciences of the United States of America 1997; 94: 10780–10785
- Lingappa J. R., Martin R. L., Wong M. L., Ganem D., Welch W. J., Lingappa V. R. A eukaryotic cytosolic chaperonin is associated with a high molecular weight intermediate in the assembly of hepatitis B virus capsid, a multimeric particle. Journal of Cell Biology 1994; 125: 99–111
- Llorca O., McCormack E. A., Hynes G., Grantham J., Cordell J., Carrascosa J. L., Willison K. R., Fernandez J. J., Valpuesta J. M. Eukaryotic type II chaperonin CCT interacts with actin through specific subunits. Nature 1999; 402: 693–696
- Melki R., Vainberg I. E., Chow R. L., Cowan N. J. Chaperonin-mediated folding of vertebrate actin-related protein and gamma-rubulin. Journal of Cell Biology 1993; 122: 1301–1310
- Proudfoot N. J., Brownlee G. G. 3 Non-coding region sequences in eukaryotic messenger RNA. Nature 1976; 263: 211–214
- Sternlicht H., Farr G. W., Sternlicht M. L., Driscoll J. K., Willison K., Yaffe M. B. The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo. Proceedings of the National Academy of Sciences of the United States of America 1993; 90: 9422–9426
- Storey K. B., Storey J. M. Metabolic rate depression and biochemical adaptation in anaerobiosis, hibernation and estivation. Quarterly Review of Biology 1990; 65: 145–174
- Thulasiraman V., Yang C. F., Frydman J. In vivo newly translated polypeptides are sequestered in a protected folding environment. EMBO Journal 1999; 18: 85–95
- Vinh D. B., Drubin D. G. A yeast TCP-1-like protein is required for actin function in vivo. Proceedings of the National Academy of Sciences of the United States of America 1994; 91: 9116–9120
- Watts D. M., Thompson W. H., Yuill T. M., DeFoliart G. R., Hanson R. P. Overwintering of La Crosse virus in Aedes triseriatus. American Journal of Tropical Medicine and Hygiene 1974; 23: 694–700
- Yaffe M. B., Farr G. W., Miklos D., Horwich A. L., Stemlicht M. L., Stemlicht H. TCP1 complex is a molecular chaperone in tubulin biogenesis. Nature 1992; 358: 245–248