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Gene Review

Prrc2a  -  proline-rich coiled-coil 2A

Mus musculus

Synonyms: 3110039B05Rik, Bat-2, Bat2, D17H6S51E, G2, ...
 
 
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Disease relevance of Bat2

 

High impact information on Bat2

  • The Schizosaccharomyces pombe cdc5 gene product is a cell cycle regulator that exerts its effects at the G2/M transition in fission yeast [5].
  • Thus, Db and/or H2-Bat2/Tnf interval genes may regulate the immunogenicity of H2-Dsp2+ BMC [6].
  • An H2b gene capable of inhibiting expression of the H2sp2 Ag (or contributing to class I motifs capable of inhibiting NK cell mediated lysis of H2sp2 BMC) maps in the Bat2/Tnfa gene segment, but requires homozygosity for this function and may require the H2-Db gene as well [7].
  • The G1/G2 protein of PVM is probably a haemagglutinin since a monoclonal antibody directed against it has a high haemagglutination inhibition titre [8].
  • Furthermore, the results indicate that the antigenic determinants with hemagglutination activity are mainly on the G2 protein, and that the domains related to neutralizing activity and to HI activity are separate [2].
 

Biological context of Bat2

  • Early passage D9 cells showed a G1 arrest following ionizing radiation, while late passage D9 cells arrested in G2 or mitosis [9].
  • A point mutation in C-terminal region of cdc2 kinase causes a G2-phase arrest in a mouse temperature-sensitive FM3A cell mutant [10].
 

Anatomical context of Bat2

  • Our results indicate that stem cell donors that express the same class I Ag, but differ at genes between Bat2 and Tnfa in the H2-S/D interval, can differ in immunogenicity of transplanted stem cells [7].
 

Associations of Bat2 with chemical compounds

  • The G2 mutation was found to constitute a C to T substitution, altering the residue 944 from serine into the more hydrophobic phenylalanine and resulting in secondary structure alterations [4].
 

Analytical, diagnostic and therapeutic context of Bat2

  • Tryptic peptide mapping showed that the two major glycosylated polypeptides G1 and G2 were different forms of the same protein [8].

References

  1. Antibody responses to Four Corners hantavirus infections in the deer mouse (Peromyscus maniculatus): identification of an immunodominant region of the viral nucleocapsid protein. Yamada, T., Hjelle, B., Lanzi, R., Morris, C., Anderson, B., Jenison, S. J. Virol. (1995) [Pubmed]
  2. Characterization of glycoproteins of viruses causing hemorrhagic fever with renal syndrome (HFRS) using monoclonal antibodies. Dantas, J.R., Okuno, Y., Asada, H., Tamura, M., Takahashi, M., Tanishita, O., Takahashi, Y., Kurata, T., Yamanishi, K. Virology (1986) [Pubmed]
  3. Characterization of neutralizing monoclonal antibody escape mutants of Hantaan virus 76118. Kikuchi, M., Yoshimatsu, K., Arikawa, J., Yoshida, R., Yoo, Y.C., Isegawa, Y., Yamanishi, K., Tono-oka, S., Azuma, I. Arch. Virol. (1998) [Pubmed]
  4. Single amino acid substitutions in Puumala virus envelope glycoproteins G1 and G2 eliminate important neutralization epitopes. Hörling, J., Lundkvist, A. Virus Res. (1997) [Pubmed]
  5. Pombe Cdc5-related protein. A putative human transcription factor implicated in mitogen-activated signaling. Bernstein, H.S., Coughlin, S.R. J. Biol. Chem. (1997) [Pubmed]
  6. Murine marrow coexpressing H2-Dsp2 and H2-Db on host natural killer cell rejection. Liu, J., Sentman, C.L., Kumar, V., Bennett, M. Transplantation (1997) [Pubmed]
  7. Bone marrow cell transplants involving donors and hosts with haplotypes derived from spretus mice. Bennett, M., D'Orazio, T., Kumar, V., Stenoien, D., Blömer, K.C., Lindahl, K.F. Transplantation (1995) [Pubmed]
  8. Polypeptides of pneumonia virus of mice. II. Characterization of the glycoproteins. Ling, R., Pringle, C.R. J. Gen. Virol. (1989) [Pubmed]
  9. Spontaneous p53 mutation in murine mesothelial cells: increased sensitivity to DNA damage induced by asbestos and ionizing radiation. Cistulli, C.A., Sorger, T., Marsella, J.M., Vaslet, C.A., Kane, A.B. Toxicol. Appl. Pharmacol. (1996) [Pubmed]
  10. A point mutation in C-terminal region of cdc2 kinase causes a G2-phase arrest in a mouse temperature-sensitive FM3A cell mutant. Yasuda, H., Kamijo, M., Honda, R., Nakamura, M., Hanaoka, F., Ohba, Y. Cell Struct. Funct. (1991) [Pubmed]
 
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