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ACTG2  -  actin, gamma 2, smooth muscle, enteric

Gallus gallus

 
 
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High impact information on ACTG2

 

Associations of ACTG2 with chemical compounds

  • This difference correlates with the deletion in smooth muscle gamma-actin of one out of four NH2-terminal acidic residues typical of skeletal and smooth muscle alpha-actin isoforms, suggesting that this additional acidic residue in alpha-actins is involved in the weak binding of cations which is essential for polymerization [3].
 

Analytical, diagnostic and therapeutic context of ACTG2

References

  1. Molecular cloning and expression of the chicken smooth muscle gamma-actin mRNA. Kovacs, A.M., Zimmer, W.E. Cell Motil. Cytoskeleton (1993) [Pubmed]
  2. ADP-ribosylation of actins by arginine-specific ADP-ribosyltransferase purified from chicken heterophils. Terashima, M., Mishima, K., Yamada, K., Tsuchiya, M., Wakutani, T., Shimoyama, M. Eur. J. Biochem. (1992) [Pubmed]
  3. Biochemical and theoretical approach to localization of metal-ion-binding sites in the actin primary structure. Strzelecka-Goøaszewska, H., Boguta, G., Zmorzyński, S., Moraczewska, J. Eur. J. Biochem. (1989) [Pubmed]
 
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