Mary Prorok
Affiliations: | 1990 | University of Notre Dame, Notre Dame, IN, United States |
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Publications
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Dai Q, Dong M, Liu Z, et al. (2011) Ca 2+-induced self-assembly in designed peptides with optimally spaced gamma-carboxyglutamic acid residues. Journal of Inorganic Biochemistry. 105: 52-7 |
Cnudde SE, Prorok M, Jia X, et al. (2011) The crystal structure of the calcium-bound con-G[Q6A] peptide reveals a novel metal-dependent helical trimer. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 16: 257-66 |
Cnudde SE, Prorok M, Castellino FJ, et al. (2010) Metal ion determinants of conantokin dimerization as revealed in the X-ray crystallographic structure of the Cd(2+)/Mg (2+)-con-T[K7gamma] complex. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 15: 667-75 |
Dai Q, Xiao C, Dong M, et al. (2009) Non-strict strand orientation of the Ca2+-induced dimerization of a conantokin peptide variant with sequence-shifted gamma-carboxyglutamate residues. Peptides. 30: 866-72 |
Xiao C, Huang Y, Dong M, et al. (2008) NR2B-selective conantokin peptide inhibitors of the NMDA receptor display enhanced antinociceptive properties compared to non-selective conantokins. Neuropeptides. 42: 601-9 |
Sheng Z, Prorok M, Brown BE, et al. (2008) N-methyl-D-aspartate receptor inhibition by an apolipoprotein E-derived peptide relies on low-density lipoprotein receptor-associated protein. Neuropharmacology. 55: 204-14 |
Cnudde SE, Prorok M, Dai Q, et al. (2007) The crystal structures of the calcium-bound con-G and con-T[K7gamma] dimeric peptides demonstrate a metal-dependent helix-forming motif. Journal of the American Chemical Society. 129: 1586-93 |
Dai Q, Prorok M, Castellino FJ. (2005) Role of the hexapeptide disulfide loop in the gamma-carboxyglutamic acid domain of protein C in Ca2+-mediated structural and functional properties. Biochemistry. 44: 12508-14 |
Yang R, Prorok M, Castellino FJ, et al. (2004) A trimeric HIV-1 fusion peptide construct which does not self-associate in aqueous solution and which has 15-fold higher membrane fusion rate. Journal of the American Chemical Society. 126: 14722-3 |
Yang J, Prorok M, Castellino FJ, et al. (2004) Oligomeric beta-structure of the membrane-bound HIV-1 fusion peptide formed from soluble monomers. Biophysical Journal. 87: 1951-63 |