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Richard L. Sabina

Department of Biochemistry

Medical College of Wisconsin

Milwaukee

WI 53226

USA

[email]@mcw.edu

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Affiliation

Department of Biochemistry, Medical College of Wisconsin, Milwaukee, WI 53226, USA. 2000 - 2009

References

Ca2+-CaM activation of AMP deaminase contributes to adenine nucleotide dysregulation and phosphatidylserine externalization in human sickle erythrocytes. Sabina, R.L., Wandersee, N.J., Hillery, C.A. Br. J. Haematol. (2009) [Pubmed]
Adenine nucleotide pool perturbation is a metabolic trigger for AMP deaminase inhibitor-based herbicide toxicity. Sabina, R.L., Paul, A.L., Ferl, R.J., Laber, B., Lindell, S.D. Plant Physiol. (2007) [Pubmed]
The contribution of Ca+ calmodulin activation of human erythrocyte AMP deaminase (isoform E) to the erythrocyte metabolic dysregulation of familial phosphofructokinase deficiency. Sabina, R.L., Waldenström, A., Ronquist, G. Haematologica (2006) [Pubmed]
Towards an understanding of the functional significance of N-terminal domain divergence in human AMP deaminase isoforms. Sabina, R.L., Mahnke-Zizelman, D.K. Pharmacol. Ther. (2000) [Pubmed]