Pure and Applied Chemistry

CrossRef Cited-by Linking

• Bajaj Priyanka, Pande Abhay H.: Stabilization Studies on Bacterially Produced Human Paraoxonase 1 for Improving Its Shelf Life. Appl Biochem Biotechnol 2014, 172, 3798. <http://dx.doi.org/10.1007/s12010-014-0806-5>
• Ezhilarasi P.N., Indrani D., Jena B.S., Anandharamakrishnan C.: Freeze drying technique for microencapsulation of Garcinia fruit extract and its effect on bread quality. Journal of Food Engineering 2013, 117, 513. <http://dx.doi.org/10.1016/j.jfoodeng.2013.01.009>
• Hédoux Alain, Seo Jeong-Ah, Guinet Yannick, Paccou Laurent: Analysis of cold denaturation mechanism of β-lactoglobulin and comparison with thermal denaturation from Raman spectroscopy investigations. J Raman Spectry 2012, 43, 16. <http://dx.doi.org/10.1002/jrs.3009>
• Hédoux Alain, Guinet Yannick, Paccou Laurent: Analysis of the Mechanism of Lysozyme Pressure Denaturation from Raman Spectroscopy Investigations, and Comparison with Thermal Denaturation. J Phys Chem B 2011, 115, 6740. <http://dx.doi.org/10.1021/jp2014836>
• Meza B.E., Verdini R.A., Rubiolo A.C.: Effect of freezing on the viscoelastic behaviour of whey protein concentrate suspensions. Food Hydrocoll 2010, 24, 414. <http://dx.doi.org/10.1016/j.foodhyd.2009.11.008>
• Wang J., Zhu X.-P., Gao R., Lin C.-L., Li Y., Xu Q.-C., Piao C.-G., Li X.-D., Li H.-F., Tian G.-Z.: Genetic and serological analyses of elongation factor EF-Tu of paulownia witches’-broom phytoplasma (16SrI-D) : Genetic and serological analyses of PaWB EF-Tu. Plant Pathol 2010, 59, 972. <http://dx.doi.org/10.1111/j.1365-3059.2010.02316.x>
• Bhatnagar Bakul S., Bogner Robin H., Pikal Michael J.: Protein Stability During Freezing: Separation of Stresses and Mechanisms of Protein Stabilization. Pharm Dev Technol 2007, 12, 505. <http://dx.doi.org/10.1080/10837450701481157>
• Ashbaugh Henry S.: Colloquium: Scaled particle theory and the length scales of hydrophobicity. Rev Mod Phys 2006, 78, 159. <http://dx.doi.org/10.1103/RevModPhys.78.159>
• Bakk Audun: Is it always possible to distinguish two- and three-state systems by evaluating the van't Hoff enthalpy?. Phys Biol 2004, 1, 152. <http://dx.doi.org/10.1088/1478-3967/1/3/002>
• Debenedetti Pablo G: Supercooled and glassy water. J Phys Condens Matter 2003, 15, R1669. <http://dx.doi.org/10.1088/0953-8984/15/45/R01>
• Ashbaugh Henry S., Truskett Thomas M., Debenedetti Pablo G.: A simple molecular thermodynamic theory of hydrophobic hydration. J Chem Phys 2002, 116, 2907. <http://dx.doi.org/10.1063/1.1436479>
• Graziano Giuseppe: On the temperature-induced coil to globule transition of poly-N-isopropylacrylamide in dilute aqueous solutions. Intern J Biol Macromol 2000, 27, 89. <http://dx.doi.org/10.1016/S0141-8130(99)00122-1>
• Eftink Maurice R., Ramsay Glen D., Beavers Antonio: Studies of the unfolding of an unstable mutant of staphylococcal nuclease: Evidence for low temperature unfolding and compactness of the high temperature unfolded state. Proteins 1997, 28, 227. <http://dx.doi.org/10.1002/(SICI)1097-0134(199706)28:2<227::AID-PROT11>3.0.CO;2-K>
• Graziano G., Barone G., Catanzano F., Riccio A.: The extra-stability of thermophilic globular proteins: a thermodynamic approach. Thermochimica 1995, 269-270, 381. <http://dx.doi.org/10.1016/0040-6031(95)02563-4>
• Schiraldi Alberto, Pezzati Elisabetta: Thermodynamic approach to cold denaturation of proteins. Thermochimica 1992, 199, 105. <http://dx.doi.org/10.1016/0040-6031(92)80254-T>