Pure and Applied Chemistry

CrossRef Cited-by Linking

• Cesàro Attilio, Bellich Barbara, Borgogna Massimiliano: Biophysical functionality in polysaccharides: from Lego-blocks to nano-particles. Eur Biophys J Biophys 2012, 41, 379. <http://dx.doi.org/10.1007/s00249-011-0753-9>
• Remmele Richard L., Zhang-van Enk Jian, Phan Duke, Yu Lei: Stabilization by Urea during Thermal Unfolding-Mediated Aggregation of Recombinant Human Interleukin-1 Receptor (Type II): Does Solvation Entropy Play a Role?. J. Phys. Chem. B 2012, 116, 7240. <http://dx.doi.org/10.1021/jp300398b>
• Potekhin S. A.: The potential of scanning microcalorimetry for studying thermotropic conformational transitions in biomacromolecules1. Polym. Sci. Ser. C 2012, 54, 108. <http://dx.doi.org/10.1134/S1811238212070053>
• Sanchez-Ruiz Jose M.: Probing Free-Energy Surfaces with Differential Scanning Calorimetry. Ann Rev Phys Chem 2011, 62, 231. <http://dx.doi.org/10.1146/annurev-physchem-032210-103504>
• Liu Honglin, Yin Peidong, He Shengnan, Sun Zhihu, Tao Ye, Huang Yan, Zhuang Hao, Zhang Guobin, Wei Shiqiang: ATP-induced noncooperative thermal unfolding of hen lysozyme. BIOPHYS BIOCHEM RES COMMUN 2010, 397, 598. <http://dx.doi.org/10.1016/j.bbrc.2010.06.005>
• Sanchez-Ruiz Jose M.: Protein kinetic stability. biophys chem 2010, 148, 1. <http://dx.doi.org/10.1016/j.bpc.2010.02.004>
• Shang Yongbiao, Xiong Youling L.: Xanthan Enhances Water Binding and Gel Formation of Transglutaminase-Treated Porcine Myofibrillar Proteins. J Fd Sci 2010, 75, E178. <http://dx.doi.org/10.1111/j.1750-3841.2010.01547.x>
• Chin Koo B., Go Mi Y., Xiong Youling L.: Konjac flour improved textural and water retention properties of transglutaminase-mediated, heat-induced porcine myofibrillar protein gel: Effect of salt level and transglutaminase incubation. Meat Sci 2009, 81, 565. <http://dx.doi.org/10.1016/j.meatsci.2008.10.012>
• Garden J.-L., Guillou H., Lopeandia A.F., Richard J., Heron J.-S., Souche G.M., Ong F.R., Vianay B., Bourgeois O.: Thermodynamics of small systems by nanocalorimetry: From physical to biological nano-objects. Thermochimica 2009, 492, 16. <http://dx.doi.org/10.1016/j.tca.2009.02.012>
• Serdyuk I. N.: Physical methods and molecular biology. Biophysics 2009, 54, 238. <http://dx.doi.org/10.1134/S0006350909020201>
• Tanaka Akiyoshi, Sturtevant Julian M., Flanagan John: Thermal unfolding of staphylococcal nuclease and several mutant forms thereof studied by differential scanning calorimetry. Protein Sci 2008, 2, 567. <http://dx.doi.org/10.1002/pro.5560020408>
• Horvath L.A., Sturtevant J.M., Prestegard J.H.: Kinetics and thermodynamics of thermal denaturation in acyl carrier protein. Protein Sci 2008, 3, 103. <http://dx.doi.org/10.1002/pro.5560030113>
• Tjahjono Martin, Garland Marc: Deuterium isotope effect on molar heat capacities and apparent molar heat capacities in dilute aqueous solutions: A multi-channel heat-flow microcalorimeter study. K J CHEM THERMODYN 2008, 40, 1600. <http://dx.doi.org/10.1016/j.jct.2008.06.008>
• Barreiro-Rodríguez G., Yáñez-Limón J. M., Contreras-Servin C. A., Herrera-Gomez A.: Testing of a scanning adiabatic calorimeter with Joule effect heating of the sample. Rev Sci Instrum 2008, 79, 014902. <http://dx.doi.org/10.1063/1.2821239>
• Spinozzi Francesco, Ortore Maria Grazia, Sinibaldi Raffaele, Mariani Paolo, Esposito Alessandro, Cinelli Stefania, Onori Giuseppe: Microcalorimetric study of thermal unfolding of lysozyme in water/glycerol mixtures: An analysis by solvent exchange model. J Chem Phys 2008, 129, 035101. <http://dx.doi.org/10.1063/1.2945303>
• Krivanek Roland, Okoro Linus, Winter Roland: Effect of Cholesterol and Ergosterol on the Compressibility and Volume Fluctuations of Phospholipid-Sterol Bilayers in the Critical Point Region: A Molecular Acoustic and Calorimetric Study. Biophysical Journal 2008, 94, 3538. <http://dx.doi.org/10.1529/biophysj.107.122549>
• Bao Lide, Chatterjee Shivani, Lohmer Sabine, Schomburg Dietmar: An Irreversible and Kinetically Controlled Process: Thermal Induced Denaturation of L-2-Hydroxyisocaproate Dehydrogenase from Lactobacillus confusus . Protein J 2007, 26, 143. <http://dx.doi.org/10.1007/s10930-006-9055-y>
• Gicquaud Claude R., Heppell Benoit: Three steps in the thermal unfolding of F-actin: An experimental evidence. Biopolymers (Biospectroscopy) 2006, 83, 374. <http://dx.doi.org/10.1002/bip.20567>
• Pfeiffer H., Klose G., Heremans K., Glorieux C.: Thermotropic phase behaviour of the pseudobinary mixtures of DPPC/C12E5 and DMPC/C12E5 determined by differential scanning calorimetry and ultrasonic velocimetry. J Chem Phys Lipids 2006, 139, 54. <http://dx.doi.org/10.1016/j.chemphyslip.2005.10.001>
• Khatri L., Taylor K.M.G., Craig D.Q.M., Palin K.: High sensitivity differential scanning calorimetry investigation of the interaction between liposomes, lactate dehydrogenase and tyrosinase. Int J of Pharmaceutics 2006, 322, 113. <http://dx.doi.org/10.1016/j.ijpharm.2006.05.036>
• Ostojić S., Pavlović M., Živić M., Filipović Z., Gorjanović S., Hranisavljević S., Dojčinović M.: Processing of whey from dairy industry waste. Environ Chem Lett 2005, 3, 29. <http://dx.doi.org/10.1007/s10311-005-0108-9>
• Gicquaud C.R., Aubin P.H., Heppell B., St-Gelais F.: F-actin has a very high calorimetric unfolding enthalpy. BIOPHYS BIOCHEM RES COMMUN 2005, 334, 145. <http://dx.doi.org/10.1016/j.bbrc.2005.06.064>
• Krumova Sashka B., Todinova Svetla J., Busheva Mira C., Taneva Stefka G.: Kinetic nature of the thermal destabilization of LHCII macroaggregates. JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY 2005, 78, 165. <http://dx.doi.org/10.1016/j.jphotobiol.2004.11.005>
• Mihalyi Elemer: Review of some unusual effects of calcium binding to fibrinogen. biophys chem 2004, 112, 131. <http://dx.doi.org/10.1016/j.bpc.2004.07.012>
• Garden J.-L., Château E., Chaussy J.: Highly sensitive ac nanocalorimeter for microliter-scale liquids or biological samples. Appl Phys Lett 2004, 84, 3597. <http://dx.doi.org/10.1063/1.1737794>
• Yao Haruhiko, Ema Kenji, Fukada Harumi, Takahashi Katsutada, Hatta Ichiro: ac nanocalorimeter for measuring heat capacity of biological macromolecules in solution. Rev Sci Instrum 2003, 74, 4164. <http://dx.doi.org/10.1063/1.1602958>
• Milhaud J, Ponsinet V, Takashi M, Michels B: Interactions of the drug amphotericin B with phospholipid membranes containing or not ergosterol: new insight into the role of ergosterol. Biochim Biophys Acta Biomembr 2002, 1558, 95. <http://dx.doi.org/10.1016/S0005-2736(01)00416-3>
• Gupta Pankaj, Singh Samer, Tiwari Ashutosh, Bhat Rajiv, Bhatnagar Rakesh: Effect of pH on Stability of Anthrax Lethal Factor: Correlation between Denaturation and Activity. Biochemical and Biophysical Research Communications 2001, 284, 568. <http://dx.doi.org/10.1006/bbrc.2001.5018>
• Rosengarth Anja, Rösgen Jörg, Hinz Hans-Jürgen, Gerke Volker: Folding energetics of ligand binding proteins II. Cooperative binding of Ca2+ to annexin I. Journal of Molecular Biology 2001, 306, 825. <http://dx.doi.org/10.1006/jmbi.2000.4358>
• Guzmán-Casado Mercedes, Cardenete Antonio, Giménez-Gallego Guillermo, Parody-Morreale Antonio: Myo-inositol hexasulphate and low molecular weight heparin binding to human acidic fibroblast growth factor: a calorimetric and FTIR study. Intern J Biol Macromol 2001, 28, 305. <http://dx.doi.org/10.1016/S0141-8130(01)00131-3>
• Vernon Brent, Kim Sung Wan, Bae You Han: Thermoreversible copolymer gels for extracellular matrix4. J Biomed Mater Res 2000, 51, 69. <http://dx.doi.org/10.1002/(SICI)1097-4636(200007)51:1<69::AID-JBM10>3.0.CO;2-6>
• Cesàro Attilio, Fabri Deborah, Sussich Fabiana, Paradossi Gaio: Structural and thermodynamic features of the polyhydroxybutyrate physical gels. Macromol Symp 1999, 138, 165. <http://dx.doi.org/10.1002/masy.19991380121>
• Yongli Chen, Xiufang Zhang, Yandao Gong, Nanming Zhao, Tingying Zeng, Xinqi Song: Conformational Changes of Fibrinogen Adsorption onto Hydroxyapatite and Titanium Oxide Nanoparticles. Journal of Colloid and Interface Science 1999, 214, 38. <http://dx.doi.org/10.1006/jcis.1999.6159>
• Rosengarth Anja, Rösgen Jörg, Hinz Hans-Jürgen, Gerke Volker: A comparison of the energetics of annexin I and annexin V. Journal of Molecular Biology 1999, 288, 1013. <http://dx.doi.org/10.1006/jmbi.1999.2732>
• Häckel Marko, Hinz Hans-Jürgen, Hedwig Gavin R: A new set of peptide-based group heat capacities for use in protein stability calculations. Journal of Molecular Biology 1999, 291, 197. <http://dx.doi.org/10.1006/jmbi.1999.2952>
• Thoumine Olivier, Ott Albrecht, Cardoso Olivier, Meister Jean-Jacques, Messana Irene, Misiti Francesco, el-Sherbini Said, Giardina Bruno, Castagnola Massimo, Mudd Courtney: Microplates: a new tool for manipulation and mechanical perturbation of individual cells. Journal of Biochemical and Biophysical Methods 1999, 39, 47. <http://dx.doi.org/10.1016/S0165-022X(98)00045-1>
• Ivanov I.T: Investigation of surface and shape changes accompanying the membrane alteration responsible for the heat-induced lysis of human erythrocytes. Colloids Surface B 1999, 13, 311. <http://dx.doi.org/10.1016/S0927-7765(99)00045-4>
• Welsh Liam C, Symmons Martyn F, Sturtevant Julian M, Marvin Donald A, Perham Richard N: Structure of the capsid of pf3 filamentous phage determined from X-ray fibre diffraction data at 3.1 Å resolution. Journal of Molecular Biology 1998, 283, 155. <http://dx.doi.org/10.1006/jmbi.1998.2081>
• Collett L. A., Brown M. E.: Biochemical and Biological Applications of Thermal Analysis. Journal of Thermal Analysis and Calorimetry 1998, 51, 693. <http://dx.doi.org/10.1007/BF03340206>
• Häckel Marko, Hinz Hans-Jürgen, Hedwig Gavin R.: Tripeptides in aqueous solution: Model compounds for the evaluation of the partial molar heat capacities of amino acid side-chains in proteins. Thermochimica 1998, 308, 23. <http://dx.doi.org/10.1016/S0040-6031(97)00326-2>
• Hedwig Gavin R., Hin Hans-Jürgen, Häckel Marko: The partial molar heat capacity and volume of the peptide backbone group of proteins in aqueous solution. biophys chem 1998, 73, 163. <http://dx.doi.org/10.1016/S0301-4622(98)00160-4>
• Vermeer Arnoldus W.P., Bremer Maria G.E.G., Norde Willem: Structural changes of IgG induced by heat treatment and by adsorption onto a hydrophobic Teflon surface studied by circular dichroism spectroscopy. General Subjects 1998, 1425, 1. <http://dx.doi.org/10.1016/S0304-4165(98)00048-8>
• Küpcü Seta, Lohnert Karl, Mader Christoph, Sleytr Uwe B.: Microcalorimetric study on the phase behaviour of Slayer coated liposomes. Molec Memb Biol 1998, 15, 69. <http://dx.doi.org/10.3109/09687689809027520>
• Kai T, Uchiyama S, Yoshida T, Kobayashi Y, Kajiyama K, Tomiyama T: NMR observation of two states of triple helix in the thermal transition of (Pro-Pro-Gly)10. chem phys letts 1997, 281, 86. <http://dx.doi.org/10.1016/S0009-2614(97)01211-6>
• Boutris C., Chatzi E.G., Kiparissides C.: Characterization of the LCST behaviour of aqueous poly(N-isopropylacrylamide) solutions by thermal and cloud point techniques. Poly 1997, 38, 2567. <http://dx.doi.org/10.1016/S0032-3861(97)01024-0>
• DeDecker Brian S., O'Brien Ronan, Fleming Patrick J., Geiger James H., Jackson Stephen P., Sigler Paul B.: The Crystal Structure of a Hyperthermophilic Archaeal TATA-box Binding Protein. Journal of Molecular Biology 1996, 264, 1072. <http://dx.doi.org/10.1006/jmbi.1996.0697>
• Milhaud J, Lancelin J.M, Michels B, Blume A: Association of polyene antibiotics with sterol-free lipid membranes: I. Hydrophobic binding of filipin to dimyristoylphosphatidylcholine bilayers. Biochim Biophys Acta Biomembr 1996, 1278, 223. <http://dx.doi.org/10.1016/0005-2736(95)00225-1>
• Todorova Roumiana T., Rogov Vladimir V., Vasilenko Kostia S., Permyakov Eugene A.: Study of tyrosine-containing mutants of ribosomal protein from Escherichia coli. biophys chem 1996, 62, 39. <http://dx.doi.org/10.1016/S0301-4622(96)02176-X>
• Relkin Perla, Mulvihill D. M.: Thermal unfolding of β‐lactoglobulin, α‐lactalbumin, and bovine serum albumin. A thermodynamic approach. Crit Rev Food Sci Technol 1996, 36, 565. <http://dx.doi.org/10.1080/10408399609527740>
• Lo Yu-Li, Rahman Yueh-Erh: Protein location in liposomes, a drug carrier: A prediction by differential scanning calorimetry. J Pharm Sci 1995, 84, 805. <http://dx.doi.org/10.1002/jps.2600840705>
• Kajiyama K., Tomiyama T., Uchiyama S., Kobayashi Y.: Phase transitions of sequenced polytripeptides observed by microcalorimetry. chem phys letts 1995, 247, 299. <http://dx.doi.org/10.1016/0009-2614(95)01211-5>
• Battley Edwin H.: The advantages and disadvantages of direct and indirect calorimetry. Thermochimica 1995, 250, 337. <http://dx.doi.org/10.1016/0040-6031(94)01963-H>
• Fukada Harumi, Takahashi Katsutada, Sorai Michio, Kojima Masaki, Tanokura Masaru, Takashashi Kenji: Differential scanning calorimetric studies of the thermal unfolding of acid proteinase A from Aspergillus niger at various pHs. Thermochimica 1995, 267, 373. <http://dx.doi.org/10.1016/0040-6031(95)02494-8>
• Feng L., Andrade J. D.: Protein adsorption on low-temperature isotropic carbon: I. Protein conformational change probed by differential scanning calorimetry. J Biomed Mater Res 1994, 28, 735. <http://dx.doi.org/10.1002/jbm.820280611>
• Munson Mary, Regan Lynne, O'Brien Ronan, Sturtevant Julian M.: Redesigning the hydrophobic core of a four-helix-bundle protein. Protein Sci 1994, 3, 2015. <http://dx.doi.org/10.1002/pro.5560031114>
• Margomenou-Leonidopoulou G.: Thermotropic mesophases of ionic amphiphiles. J Thermal Anal 1994, 42, 1041. <http://dx.doi.org/10.1007/BF02547126>
• Uedaira Hatsuho, Kidokoro Shun-ichi, Ohgiya Satoru, Ishizaki Kozo, Shinriki Nariko: Thermal transition of plasmid pBR322 closed circular, open circular and linear DNAs. Thermochimica 1994, 232, 7. <http://dx.doi.org/10.1016/0040-6031(94)80040-5>
• Milardi Danilo, La Rosa Carmelo, Grasso Domenico: Differential scanning calorimetry of the irreversible denaturation of bovine superoxide dismutase. Thermochimica 1994, 246, 183. <http://dx.doi.org/10.1016/0040-6031(94)85104-2>
• Milardi Danilo, La Rosa Carmelo, Grasso Domenico: Extended theoretical analysis of irreversible protein thermal unfolding. biophys chem 1994, 52, 183. <http://dx.doi.org/10.1016/0301-4622(94)00033-G>
• Christensen Bjørn E., Knudsen Kenneth D., Smidsrød Olav, Kitamura Shinichi, Takeo Kenichi: Temperature-Induced conformational transition in xanthans with partially hydrolyzed side chains. Biopolymers (Biospectroscopy) 1993, 33, 151. <http://dx.doi.org/10.1002/bip.360330115>
• Bae Song-Ja, Sturtevant Julian M.: The effects of the p-nitrophenyl esters of the even-numbered fatty acids from caproic (C6) to stearic (C18) on the main phase transition of dimyristoylphosphatidylcholine. J Chem Phys Lipids 1993, 66, 47. <http://dx.doi.org/10.1016/0009-3084(93)90030-7>
• Shnyrov Valery L., Mateo Pedro L.: Thermal transitions in the purple membrane from Halobacterium halobium. FEBS Letters 1993, 324, 237. <http://dx.doi.org/10.1016/0014-5793(93)81400-T>
• Cesàro Attilio, Cumani Julo, Géciovà Renata, Michelazzo Federica: A calorimetric study of cooperative phase equilibria in microbial polysaccharides. Thermochimica 1993, 227, 167. <http://dx.doi.org/10.1016/0040-6031(93)80260-H>
• Schmitz H.-U., Hübner W.: A thermodynamic and spectroscopic study on the binding of berenil to poly d(AT) and to poly (dA) · poly (dT). biophys chem 1993, 48, 61. <http://dx.doi.org/10.1016/0301-4622(93)80042-H>
• Burjanadze Tengiz V., Bezhitadze Manama O.: Presence of a thermostable domain in the helical part of the type I collagen molecule and its role in the mechanism of triple helix folding. Biopolymers (Biospectroscopy) 1992, 32, 951. <http://dx.doi.org/10.1002/bip.360320806>
• Galisteo María L., Conejero-Lara Francisco, Núñez Josefa, Sánchez-Ruiz Jose M., Mateo Pedro L.: A calorimetric approach to the kinetics of the irreversible thermal denaturation of proteins. Thermochimica 1992, 199, 147. <http://dx.doi.org/10.1016/0040-6031(92)80258-X>
• CLADERA Josep, GALISTEO M. Luisa, SABES Manuel, MATEO Perdro L., PADROS Esteve: The role of retinal in the thermal stability of the purple membrane. Eur J Biochem 1992, 207, 581. <http://dx.doi.org/10.1111/j.1432-1033.1992.tb17084.x>
• Sturtevant Julian M., Holtzer Marilyn Emerson, Holtzer Alfred: A scanning calorimetric study of the thermally induced unfolding of various forms of tropomyosin. Biopolymers (Biospectroscopy) 1991, 31, 489. <http://dx.doi.org/10.1002/bip.360310504>
• Castronuovo Giuseppina: Proteins in aqueous solutions. calorimetric studies and thermodynamic characterization. Thermochimica 1991, 193, 363. <http://dx.doi.org/10.1016/0040-6031(91)80193-M>
• Uedaira H., Kidokoro S.: Characteristics of an adiabatic differential scanning microcalorimeter. Thermochimica 1991, 183, 323. <http://dx.doi.org/10.1016/0040-6031(91)80468-X>
• CONEJERO-LARA Francisco, SANCHEZ-RUIZ Jose M., MATEO Pedro L., BURGOS Francisco J., VENDRELL Josep, AVILES Francesc X.: Differential scanning calorimetric study of carboxypeptidase B, procarboxypeptidase B and its globular activation domain. Eur J Biochem 1991, 200, 663. <http://dx.doi.org/10.1111/j.1432-1033.1991.tb16230.x>
• Hajdu Joseph, Sturtevant Julian M.: Phospholipids showing complex bilayer phase transitions. II. Four sulfur-containing phosphatidylcholines. J Chem Phys Lipids 1990, 55, 323. <http://dx.doi.org/10.1016/0009-3084(90)90170-V>
• Vonderviszt Ferenc, Uedaira Hatsuho, Kidokoro Shun-Ichi, Namba Keiichi: Structural organization of flagellin. Journal of Molecular Biology 1990, 214, 97. <http://dx.doi.org/10.1016/0022-2836(90)90149-G>
• Uedaira H., Kidokoro S., Iwakura M., Honda S., Ohashi S.: Thermal transition of a mutated dihydrofolate reductase. Thermochimica 1990, 163, 123. <http://dx.doi.org/10.1016/0040-6031(90)80387-E>
• UEDAIRA HATSUHO, KIDOKORO SHUN-ICHI, IWAKURA MASAHIRO, HONDA SHINYA, OHASHI SHINICHI: Thermal Stability of Dihydrofolate Reductase and Its Fused Proteins with Oligopeptides. Ann N Y Acad Sci 1990, 613, 352. <http://dx.doi.org/10.1111/j.1749-6632.1990.tb18177.x>
• Privalov Peter L.: Cold Denaturation of Protein. Crit Rev Biochem Mol Biol 1990, 25, 281. <http://dx.doi.org/10.3109/10409239009090612>
• Cold Denaturation of Protein. Crit Rev Biochem Mol Biol 1990, 25, 281. <http://dx.doi.org/10.3109/10409239009090613>
• Robert Charles H., Colosimo Alfredo, Gill Stanley J.: Allosteric formulation of thermal transitions in macromolecules, including effects of ligand binding and oligomerization. Biopolymers (Biospectroscopy) 1989, 28, 1705. <http://dx.doi.org/10.1002/bip.360281006>
• Privalov P.L., Plotnikov V.V.: Three generations of scanning microcalorimeters for liquids. Thermochimica 1989, 139, 257. <http://dx.doi.org/10.1016/0040-6031(89)87027-3>
• Novokhatny V.V., Matsuka Yu.V., Kudinov S.A.: Analysis of ligand, binding to kringles 4 and 5 fragments from human plasminogen. Thromb Research 1989, 53, 243. <http://dx.doi.org/10.1016/0049-3848(89)90099-6>
• Ohms J., Ackermann T.: A thermodynamic study on rA7U7. biophys chem 1989, 34, 137. <http://dx.doi.org/10.1016/0301-4622(89)80051-1>
• Kidokoro Shun-Ichi, Uedaira Hatsuho, Wada Akiyoshi: Determination of thermodynamic functions from scanning calorimetry data. II. For the system that includes self-dissociation / association process. Biopolymers (Biospectroscopy) 1988, 27, 271. <http://dx.doi.org/10.1002/bip.360270208>
• Chaires Jonathan B., Sturtevant Julian M.: Thermodynamics of the B to Z transition in poly(dGdC). Biopolymers (Biospectroscopy) 1988, 27, 1375. <http://dx.doi.org/10.1002/bip.360270905>
• Cladera Josep, Galisteo Ma Luisa, Dun˜ach Mireia, Mateo Pedro L., Padrós Esteve: Thermal denaturation of deionized and native purple membranes. Biochim Biophys Acta Biomembr 1988, 943, 148. <http://dx.doi.org/10.1016/0005-2736(88)90546-9>
• Makhatadze G.I, Privalov P.L: Partial specific heat capacity of benzene and of toluene in aqueous solution determined calorimetrically for a broad temperature range. K J CHEM THERMODYN 1988, 20, 405. <http://dx.doi.org/10.1016/0021-9614(88)90177-2>
• Bendzko Peter I., Pfeil Wolfgang A., Privalov Peter L., Tiktopulo Elizaveta I.: Temperature-induced phase transitions in proteins and lipids. biophys chem 1988, 29, 301. <http://dx.doi.org/10.1016/0301-4622(88)85052-X>
• Hecht Michael H., Sturtevant Julian M., Sauer Robert T.: Stabilization of λ repressor against thermal denaturation by site-directed Gly→Ala changes in α-helix 3. Proteins 1986, 1, 43. <http://dx.doi.org/10.1002/prot.340010108>
• Medved' L.V., Litvinovich S.V., Privalov P.L.: Domain organization of the terminal parts in the fibrinogen molecule. FEBS Letters 1986, 202, 298. <http://dx.doi.org/10.1016/0014-5793(86)80705-0>
• Privalov P.L., Griko Yu.V., Venyaminov S.Yu., Kutyshenko V.P.: Cold denaturation of myoglobin. Journal of Molecular Biology 1986, 190, 487. <http://dx.doi.org/10.1016/0022-2836(86)90017-3>
• Loseva O.I., Tlschenko V.M., Olšovská Z., Franěk F., Zav'yalov V.P.: Correlation of the character of intramolecular melting with digestibility by pepsin in precipitating and non-precipitating pig anti-DNP antibodies. Molec Immunol 1986, 23, 743. <http://dx.doi.org/10.1016/0161-5890(86)90085-4>
• Wadsö Ingemar: Bio-calorimetry. Trends in Biotechnol 1986, 4, 45. <http://dx.doi.org/10.1016/0167-7799(86)90153-8>
• Brazhnikov E. V., Chirgadze Yu. N., Dolgikh D. A., Ptitsyn O. B.: Noncooperative temperature melting of a globular protein without specific tertiary structure: Acid form of bovine carbonic anhydrase B. Biopolymers (Biospectroscopy) 1985, 24, 1899. <http://dx.doi.org/10.1002/bip.360241005>
• Norton I. T., Lee-Tuffnell C. D., Ablett S., Bociek S. M.: A calorimetric, NMR and X-ray diffraction study of the melting behavior of tripalmitin and tristearin and their mixing behavior with triolein. J Am Oil Chem Soc 1985, 62, 1237. <http://dx.doi.org/10.1007/BF02541834>
• Tsalkova Tamara N., Privalov Peter L.: Thermodynamic study of domain organization in troponin C and calmodulin. Journal of Molecular Biology 1985, 181, 533. <http://dx.doi.org/10.1016/0022-2836(85)90425-5>
• Müller K., Lipka G., Lohner K., Laggner P.: The effect of the detergent cetyltrimethylammoniumchloride on the phase behaviour of dipalmitoylphosphatidylcholine. Thermochimica 1985, 94, 187. <http://dx.doi.org/10.1016/0040-6031(85)85259-X>
• Müller Karl: Structural Aspects of Bile Salt-Lecithin Mixed Micelles. Hepatol 1984, 4, 134S. <http://dx.doi.org/10.1002/hep.1840040823>
• Norton I.T., Goodall D.M., Frangou S.A., Morris E.R., Rees D.A.: Mechanism and dynamics of conformational ordering in xanthan polysaccharide. Journal of Molecular Biology 1984, 175, 371. <http://dx.doi.org/10.1016/0022-2836(84)90354-1>
• Novokhatny Valery V., Kudinov Stanislav A., Privalov Peter L.: Domains in human plasminogen. Journal of Molecular Biology 1984, 179, 215. <http://dx.doi.org/10.1016/0022-2836(84)90466-2>
• Couchman P. R., Gajnos G. E., Ryan C. L., Karasz F. E.: Heat capacity increments: Conformational transitions in polypeptides. Biopolymers (Biospectroscopy) 1983, 22, 2411. <http://dx.doi.org/10.1002/bip.360221108>
• Thurén Tom, Virtanen Jorma A., Vainio Petri, Kinnunen Paavo K.J.: Hydrolysis of 1-triacontanoyl-2-(pyren-1-yl)hexanoyl-sn-glycero-3-phosphocholine by human pancreatic phospholipase A2. J Chem Phys Lipids 1983, 33, 283. <http://dx.doi.org/10.1016/0009-3084(83)90079-8>
• Jeremic K., Karasz F.E.: Heat capacity changes at the helix-coil transition of polypeptides in mixed organic solvents. Euro Poly J 1983, 19, 1037. <http://dx.doi.org/10.1016/0014-3057(83)90069-1>
• Epand Richard M., Moscarello Mario A.: The effect of bovine myelin basic protein on the phase transition properties of sphingomyelin. Biochim Biophys Acta Biomembr 1982, 685, 230. <http://dx.doi.org/10.1016/0005-2736(82)90105-5>
• Epand R.M., Boni L.T., Hui S.W.: Interaction of glucagon with sphingomyelins. Biochim Biophys Acta Biomembr 1982, 692, 330. <http://dx.doi.org/10.1016/0005-2736(82)90381-9>
• Medved L.V., Privalov P.L., Ugarova T.P.: Isolation of thermostable structure from the fibrinogen D Fragment. FEBS Letters 1982, 146, 339. <http://dx.doi.org/10.1016/0014-5793(82)80948-4>
• Privalov P.L., Medved' L.V.: Domains in the fibrinogen molecule. Journal of Molecular Biology 1982, 159, 665. <http://dx.doi.org/10.1016/0022-2836(82)90107-3>
• Potekhin Serge A., Privalov Peter L.: Co-operative blocks in tropomyosin. Journal of Molecular Biology 1982, 159, 519. <http://dx.doi.org/10.1016/0022-2836(82)90299-6>
• TISCHENKO Vladimir M., ZAV'YALOV Vladimir P., MEDGYESI Gyorgy A., POTEKHIN Sergei A., PRIVALOV Peter L.: A Thermodynamic Study of Cooperative Structures in Rabbit Immunoglobulin G. Eur J Biochem 1982, 126, 517. <http://dx.doi.org/10.1111/j.1432-1033.1982.tb06811.x>
• Mateo Pedro L., Privalov Peter L.: Pepsinogen denaturation is not a two-state transition. FEBS Letters 1981, 123, 189. <http://dx.doi.org/10.1016/0014-5793(81)80284-0>
• Privalov Petkr L., Mateo Pedro L., Khechinashvili Nikolai N., Stepanov Valentin M., Revina Lyudmila P.: Comparative thermodynamic study of pepsinogen and pepsin structure. Journal of Molecular Biology 1981, 152, 445. <http://dx.doi.org/10.1016/0022-2836(81)90253-9>