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Gene Review

42S  -  DNA segment, 42S

Mus musculus

 
 
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Disease relevance of 42S

 

High impact information on 42S

  • The resulting T-cell hybridomas responded strongly to both mouse MOG-35-55 (42S) and human MOG-35-55 peptide (42P), regardless of which peptide was used for initial immunization, and were DRB1*1501 restricted [5].

References

  1. Initiation sites for translation of sindbis virus 42S and 26S messenger RNAs. Cancedda, R., Villa-Komaroff, L., Lodish, H.F., Schlesinger, M. Cell (1975) [Pubmed]
  2. Synthesis in vitro of full length genomic RNA and assembly of the nucleocapsid of vesicular stomatitis virus in a coupled transcription-translation system. Ghosh, K., Ghosh, H.P. Nucleic Acids Res. (1982) [Pubmed]
  3. Infection of neuroblastoma cells by Semliki Forest virus. The interference of viral capsid protein with the binding of host messenger RNAs into initiation complexes is the cause of the shut-off of host protein synthesis. van Steeg, H., Kasperaitis, M., Voorma, H.O., Benne, R. Eur. J. Biochem. (1984) [Pubmed]
  4. Oligonucleotide fingerprint analysis on Japanese encephalitis virus strains after passage histories. Hori, H., Igarashi, A., Yoshida, I., Takagi, M. Acta Virol. (1986) [Pubmed]
  5. T-cell hybridoma specific for myelin oligodendrocyte glycoprotein-35-55 peptide produced from HLA-DRB1*1501-transgenic mice. Chou, Y.K., Culbertson, N., Rich, C., LaTocha, D., Buenafe, A.C., Huan, J., Link, J., Wands, J.M., Born, W.K., Offner, H., Bourdette, D.N., Burrows, G.G., Vandenbark, A.A. J. Neurosci. Res. (2004) [Pubmed]
 
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