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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

CRYBB2  -  crystallin, beta B2

Bos taurus

 
 
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High impact information on CRYBB2

  • Phosphorylation of beta-crystallin B2 (beta Bp) in the bovine lens [1].
  • The imparted mineral affinity as a result of BP conjugation, as assessed by hydroxyapatite (HA) binding in vitro, was lost upon cleavage of the disulfide-linked BP [2].
  • In conclusion, disulfide-linked BP conjugates were shown to be readily cleavable by the amino acid cysteine and this resulted in the loss of imparted mineral affinity of the proteins [2].

References

  1. Phosphorylation of beta-crystallin B2 (beta Bp) in the bovine lens. Kleiman, N.J., Chiesa, R., Kolks, M.A., Spector, A. J. Biol. Chem. (1988) [Pubmed]
  2. Imparting mineral affinity to proteins with thiol-labile disulfide linkages. Bansal, G., Wright, J.E., Zhang, S., Zernicke, R.F., Uludag, H. Journal of biomedical materials research. Part A. (2005) [Pubmed]
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