Judith H. Prieto, Ph.D.

Affiliations: 
2005 University of California, San Diego, La Jolla, CA 
Area:
Structure, function, dynamics and thermodynamics of protein-protein interactions: NMR, mass spectrometry and kinetics
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"Judith Prieto"
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Elizabeth A. Komives grad student 2005 UCSD
 (Correlations between dynamic motions and function in modular proteins.)
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Publications

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Prieto JH. (2017) The Binding of Methylene Blue to Plasmodium Falciparum Glutathione Reductase Biophysical Journal. 112: 351a
Prieto JH, Fischer E, Koncarevic S, et al. (2015) Large-scale differential proteome analysis in Plasmodium falciparum under drug treatment. Methods in Molecular Biology (Clifton, N.J.). 1201: 269-79
Wang L, Delahunty C, Prieto JH, et al. (2014) Protein S-nitrosylation in Plasmodium falciparum. Antioxidants & Redox Signaling. 20: 2923-35
Finneran P, Darinzo N, Prieto JH. (2014) Putative Programmed Cell Death Pathway of the Malaria Parasite and the Role of Cytochrome C Biophysical Journal. 106: 595a-596a
Röseler A, Prieto JH, Iozef R, et al. (2012) Insight into the selenoproteome of the malaria parasite Plasmodium falciparum. Antioxidants & Redox Signaling. 17: 534-43
Guttman M, Prieto JH, Handel TM, et al. (2010) Structure of the minimal interface between ApoE and LRP. Journal of Molecular Biology. 398: 306-19
Guttman M, Prieto JH, Croy JE, et al. (2010) Decoding of lipoprotein-receptor interactions: properties of ligand binding modules governing interactions with apolipoprotein E. Biochemistry. 49: 1207-16
Koncarevic S, Rohrbach P, Deponte M, et al. (2009) The malarial parasite Plasmodium falciparum imports the human protein peroxiredoxin 2 for peroxide detoxification. Proceedings of the National Academy of Sciences of the United States of America. 106: 13323-8
Prieto JH, Koncarevic S, Park SK, et al. (2008) Large-scale differential proteome analysis in Plasmodium falciparum under drug treatment. Plos One. 3: e4098
Prieto JH, Sampoli Benitez BA, Melacini G, et al. (2005) Dynamics of the fragment of thrombomodulin containing the fourth and fifth epidermal growth factor-like domains correlate with function. Biochemistry. 44: 1225-33
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