Publications

Select Publications

Byrne, S.L., Steere, A.N., Chasteen, N.D., and Mason, A.B. (2010) Identification of a kinetically significant anion binding (KISAB) site in the N-lobe of human serum transferrin.  Biochemistry.  49, 4200-4207.

Steere, A.N., Roberts, S.E., Byrne, S.L., Chasteen, N.D., Bobst C.E., Kaltashov, I.A., Smith, V.C., MacGillivray, R.T.A.  (2010) Properties of a homogeneous C-lobe prepared by introduction of a TEV cleavage site between the lobes of human transferrin.  Pro. Expr. and Purif.  72, 32-41.

Byrne, S.L., Chasteen, N.D., Steere, A.N., and Mason, A.B. (2010) The unique kinetics of iron release from transferrin: The role of receptor, lobe-lobe interactions and salt at endosomal pH.  J. Mol. Biol, 396, 130-140.

Mason, A.B., Byrne, S.L., Everse, S.J., Roberts, S.E., Chasteen, N.D., Smith, V.C., MacGillivray, R.T.A., Kandemir, B., and Bou-Abdallah, F. (2009) A loop in the N-lobe of human serum transferrin is critical for binding to the transferrin receptor as revealed by mutagenesis, isothermal titration calorimetry, and epitope mapping.  J. Mol. Recog. 22, 521-529.

Byrne, S. L., and Mason, A. B. (2009) Human serum transferrin: A tale of two lobes.  Urea gel and steady-state fluorescence analysis of recombinant transferrins as a function of pH, time and the sTFR, J. Biol. Inorg. Chem. 14, 771-781.

Mason, A. B., Halbrooks, P. J., James, N.G., Byrne, S. L., Grady, J. K., Chasteen, N. D., Bobst, C. E., Kaltashov, I. A., Smith, V. C., MacGillivray, R. T. A., and Everse, S. J. (2009) Structural and functional consequences of the substitution of glycine 65 with arginine in the N-lobe of human transferrin, Biochemistry 48, 1945-1953.

James, N. G., Byrne, S. L., Steere, A. N., Smith, V. C., MacGillivray, R. T. A., and Mason, A. B. (2009) Inequivalent contribution of the five tryptophan residues in the C-lobe of human serum transferrin to the fluorescence increase when iron is released, Biochemistry 48, 2858-2867.

James, N. G.^*, Byrne, S. L.^*, and Mason, A. B. (2008) Incorporation of 5-hydroxytryptophan into transferrin and its receptor allows assignment of the pH induced changes in intrinsic fluorescence when iron is released, Biochim. Biophys. Acta 1794, 532-540. (^*authors contributed equally to this work)

Mason, A. B., Judson, G. L., Bravo, M. C., Edelstein, A., Byrne, S. L., James, N. G., Roush, E. D., Fierke, C. A., Bobst, C. E., Kaltashov, I. A., and Daughtery, M. A. (2008) Evolution reversed: the ability to bind iron restored to the N-lobe of the murine inhibitor of carbonic anhydrase by strategic mutagenesis, Biochemistry 47, 9847-9855.

James, N. G., Berger, C. L., Byrne, S. L., Smith, V. C., MacGillivray, R. T., and Mason, A. B. (2007) Intrinsic Fluorescence Reports a Global Conformational Change in the N-Lobe of Human Serum Transferrin following Iron Release, Biochemistry 46, 10603-10611.

Byrne, S. L., Leverence, R., Klein, J. S., Giannetti, A. M., Smith, V. C., MacGillivray, R. T., Kaltashov, I. A., and Mason, A. B. (2006) Effect of glycosylation on the function of a soluble, recombinant form of the transferrin receptor, Biochemistry 45, 6663-6673.