Pure and Applied Chemistry

CrossRef Cited-by Linking

• Yoshidome Takashi, Kinoshita Masahiro: Physical origin of hydrophobicity studied in terms of cold denaturation of proteins: comparison between water and simple fluids. Phys. Chem. Chem. Phys. 2012, 14, 14554. <http://dx.doi.org/10.1039/c2cp41738c>
• Shushanyan Mikhael, Khoshtariya Dimitri E., Tretyakova Tatyana, Makharadze Maya, van Eldik Rudi: Diverse role of conformational dynamics in carboxypeptidase A-driven peptide and ester hydrolyses: Disclosing the “Perfect Induced Fit” and “Protein Local Unfolding” pathways by altering protein stability. Biopol 2011, 95, 852. <http://dx.doi.org/10.1002/bip.21688>
• Riccio Angelo, Graziano Giuseppe: Cold unfolding of β-hairpins: A molecular-level rationalization. Proteins 2011, 79, 1739. <http://dx.doi.org/10.1002/prot.22997>
• Boryskina O. P., Tkachenko M. Yu., Shestopalova A. V.: Protein-DNA complexes: specificity and DNA readout mechanisms. Biopolym. Cell 2011, 27, 3. <http://dx.doi.org/10.7124/bc.00007C>
• Graziano Giuseppe: On the molecular origin of cold denaturation of globular proteins. Phys Chem Chem Phys 2010, 12, 14245. <http://dx.doi.org/10.1039/c0cp00945h>
• Amano Ken-ichi, Yoshidome Takashi, Harano Yuichi, Oda Koji, Kinoshita Masahiro: Theoretical analysis on thermal stability of a protein focused on the water entropy. chem phys letts 2009, 474, 190. <http://dx.doi.org/10.1016/j.cplett.2009.04.025>
• Wang Bao-Yu, Rieth Stephen, Badjić Jovica D: Tuning the Rate of Molecular Translocation. J Am Chem Soc 2009, 131, 7250. <http://dx.doi.org/10.1021/ja9023868>
• Oshima Hiraku, Yoshidome Takashi, Amano Ken-ichi, Kinoshita Masahiro: A theoretical analysis on characteristics of protein structures induced by cold denaturation. J Chem Phys 2009, 131, 205102. <http://dx.doi.org/10.1063/1.3265985>
• Yoshidome Takashi, Kinoshita Masahiro: Hydrophobicity at low temperatures and cold denaturation of a protein. Phys Rev E 2009, 79, 030905. <http://dx.doi.org/10.1103/PhysRevE.79.030905>