| Year |
Citation |
Score |
| 2020 |
Privalov PL, Crane-Robinson C. Forces maintaining the DNA double helix. European Biophysics Journal : Ebj. PMID 32462263 DOI: 10.1007/S00249-020-01437-W |
0.388 |
|
| 2019 |
Dragan A, Privalov P, Crane-Robinson C. Thermodynamics of DNA: heat capacity changes on duplex unfolding. European Biophysics Journal : Ebj. 48: 773-779. PMID 31690971 DOI: 10.1007/S00249-019-01403-1 |
0.457 |
|
| 2018 |
Privalov PL, Crane-Robinson C. Forces maintaining the DNA double helix and its complexes with transcription factors. Progress in Biophysics and Molecular Biology. PMID 29378224 DOI: 10.1016/J.Pbiomolbio.2018.01.007 |
0.413 |
|
| 2018 |
Privalov PL, Crane-Robinson C. Translational Entropy and DNA Duplex Stability. Biophysical Journal. 114: 15-20. PMID 29320682 DOI: 10.1016/J.Bpj.2017.11.003 |
0.431 |
|
| 2016 |
Privalov PL, Crane-Robinson C. Role of water in the formation of macromolecular structures. European Biophysics Journal : Ebj. PMID 27457765 DOI: 10.1007/S00249-016-1161-Y |
0.391 |
|
| 2015 |
Vaitiekunas P, Crane-Robinson C, Privalov PL. The energetic basis of the DNA double helix: a combined microcalorimetric approach. Nucleic Acids Research. 43: 8577-89. PMID 26304541 DOI: 10.1093/Nar/Gkv812 |
0.455 |
|
| 2015 |
Tiktopulo EI, Privalov PL. Heat denaturation of ribonuclease. Biophysical Chemistry. 1: 349-57. PMID 23260423 DOI: 10.1016/0301-4622(74)85004-0 |
0.356 |
|
| 2012 |
Shukla H, Vaitiekunas P, Majumdar AK, Dragan AI, Dimitriadis EK, Kotova S, Crane-Robinson C, Privalov PL. The linker of the interferon response factor 3 transcription factor is not unfolded Biochemistry. 51: 6320-6327. PMID 22812703 DOI: 10.1021/Bi300260S |
0.33 |
|
| 2011 |
Privalov PL, Dragan AI, Crane-Robinson C. Interpreting protein/DNA interactions: Distinguishing specific from non-specific and electrostatic from non-electrostatic components Nucleic Acids Research. 39: 2483-2491. PMID 21071403 DOI: 10.1093/Nar/Gkq984 |
0.364 |
|
| 2010 |
Carrillo RJ, Privalov PL. Unfolding of bZIP dimers formed by the ATF-2 and c-Jun transcription factors is not a simple two-state transition. Biophysical Chemistry. 151: 149-54. PMID 20619956 DOI: 10.1016/J.Bpc.2010.06.004 |
0.383 |
|
| 2010 |
Carrillo RJ, Dragan AI, Privalov PL. Stability and DNA-binding ability of the bZIP dimers formed by the ATF-2 and c-Jun transcription factors Journal of Molecular Biology. 396: 431-440. PMID 19944700 DOI: 10.1016/J.Jmb.2009.11.050 |
0.342 |
|
| 2009 |
Privalov PL, Dragan AI, Crane-Robinson C. The cost of DNA bending Trends in Biochemical Sciences. 34: 464-470. PMID 19726198 DOI: 10.1016/J.Tibs.2009.05.005 |
0.41 |
|
| 2009 |
Privalov PL. Microcalorimetry of proteins and their complexes. Methods in Molecular Biology (Clifton, N.J.). 490: 1-39. PMID 19157077 DOI: 10.1007/978-1-59745-367-7_1 |
0.488 |
|
| 2009 |
Dragan AI, Russell DJ, Privalov PL. DNA hydration studied by pressure perturbation scanning microcalorimetry Biopolymers. 91: 95-101. PMID 18803275 DOI: 10.1002/Bip.21088 |
0.361 |
|
| 2008 |
Dragan AI, Privalov PL. Chapter 9 Use of Fluorescence Resonance Energy Transfer (FRET) in Studying Protein-induced DNA Bending Methods in Enzymology. 450: 185-199. PMID 19152861 DOI: 10.1016/S0076-6879(08)03409-5 |
0.358 |
|
| 2008 |
Dragan AI, Carrillo R, Gerasimova TI, Privalov PL. Assembling the Human IFN-β Enhanceosome in Solution Journal of Molecular Biology. DOI: 10.1016/J.Jmb.2008.09.015 |
0.323 |
|
| 2007 |
Dragan AI, Hargreaves VV, Makeyeva EN, Privalov PL. Mechanisms of activation of interferon regulator factor 3: the role of C-terminal domain phosphorylation in IRF-3 dimerization and DNA binding. Nucleic Acids Research. 35: 3525-34. PMID 17483521 DOI: 10.1093/Nar/Gkm142 |
0.321 |
|
| 2007 |
Privalov PL, Dragan AI, Crane-Robinson C, Breslauer KJ, Remeta DP, Minetti CA. What drives proteins into the major or minor grooves of DNA? Journal of Molecular Biology. 365: 1-9. PMID 17055530 DOI: 10.1016/J.Jmb.2006.09.059 |
0.419 |
|
| 2007 |
Privalov PL, Dragan AI. Microcalorimetry of biological macromolecules Biophysical Chemistry. 126: 16-24. PMID 16781052 DOI: 10.1016/J.Bpc.2006.05.004 |
0.368 |
|
| 2007 |
Privalov PL. Thermodynamic problems in structural molecular biology Pure and Applied Chemistry. 79: 1445-1462. DOI: 10.1351/Pac200779081445 |
0.356 |
|
| 2006 |
Crane-Robinson C, Dragan AI, Privalov PL. The extended arms of DNA-binding domains: a tale of tails Trends in Biochemical Sciences. 31: 547-552. PMID 16920361 DOI: 10.1016/J.Tibs.2006.08.006 |
0.334 |
|
| 2006 |
Dragan AI, Li Z, Makeyeva EN, Milgotina EI, Liu Y, Crane-Robinson C, Privalov PL. Forces driving the binding of homeodomains to DNA Biochemistry. 45: 141-151. PMID 16388589 DOI: 10.1021/Bi051705M |
0.572 |
|
| 2005 |
Hargreaves VV, Makeyeva EN, Dragan AI, Privalov PL. Stability and DNA binding ability of the DNA binding domains of interferon regulatory factors 1 and 3. Biochemistry. 44: 14202-9. PMID 16245936 DOI: 10.1021/Bi051115O |
0.357 |
|
| 2004 |
Dragan AI, Potekhin SA, Sivolob A, Lu M, Privalov PL. Kinetics and thermodynamics of the unfolding and refolding of the three-stranded α-helical coiled coil, Lpp-56 Biochemistry. 43: 14891-14900. PMID 15554696 DOI: 10.1021/Bi048365+ |
0.434 |
|
| 2004 |
Dragan AI, Frank L, Liu Y, Makeyeva EN, Crane-Robinson C, Privalov PL. Thermodynamic signature of GCN4-bZIP binding to DNA indicates the role of water in discriminating between the AP-1 and ATF/CREB sites Journal of Molecular Biology. 343: 865-878. PMID 15476806 DOI: 10.1016/J.Jmb.2004.08.101 |
0.361 |
|
| 2004 |
Dragan AI, Liu Y, Mekeyeva EN, Privalov PL. DNA-binding domain of GCN4 induces bending of both the ATF-CREB and AP-1 binding sites of DNA Nucleic Acids Research. 32: 5192-5197. PMID 15459288 DOI: 10.1093/Nar/Gkh854 |
0.319 |
|
| 2004 |
Dragan AI, Read CM, Makeyeva EN, Milgotina EI, Churchill MEA, Crane-Robinson C, Privalov PL. DNA binding and bending by HMG boxes: Energetic determinants of specificity Journal of Molecular Biology. 343: 371-393. PMID 15451667 DOI: 10.1016/J.Jmb.2004.08.035 |
0.391 |
|
| 2003 |
Dragan AI, Klass J, Read C, Churchill MEA, Crane-Robinson C, Privalov PL. DNA binding of a non-sequence-specific HMG-D protein is entropy driven with a substantial non-electrostatic contribution Journal of Molecular Biology. 331: 795-813. PMID 12909011 DOI: 10.1016/S0022-2836(03)00785-X |
0.43 |
|
| 2003 |
Dragan AI, Liggins JR, Crane-Robinson C, Privalov PL. The energetics of specific binding of AT-hooks from HMGA1 to target DNA. Journal of Molecular Biology. 327: 393-411. PMID 12628246 DOI: 10.1016/S0022-2836(03)00050-0 |
0.377 |
|
| 2002 |
Dragan AI, Privalov PL. Unfolding of a leucine zipper is not a simple two-state transition Journal of Molecular Biology. 321: 891-908. PMID 12206769 DOI: 10.1016/S0022-2836(02)00699-X |
0.501 |
|
| 2001 |
Yu YB, Privalov PL, Hodges RS. Contribution of translational and rotational motions to molecular association in aqueous solution Biophysical Journal. 81: 1632-1642. PMID 11509376 DOI: 10.1016/S0006-3495(01)75817-1 |
0.313 |
|
| 2000 |
Liggins JR, Privalov PL. Energetics of the specific binding interaction of the first three zinc fingers of the transcription factor TFIIIA with its cognate DNA sequence. Proteins. 50-62. PMID 11013400 DOI: 10.1002/1097-0134(2000)41:4+<50::Aid-Prot50>3.0.Co;2-H |
0.433 |
|
| 2000 |
Privalov GP, Privalov PL. Problems and prospects in microcalorimetry of biological macromolecules. Methods in Enzymology. 323: 31-62. PMID 10944746 DOI: 10.1016/S0076-6879(00)23360-0 |
0.387 |
|
| 2000 |
Hendrix T, Griko YV, Privalov PL. A calorimetric study of the influence of calcium on the stability of bovine alpha-lactalbumin. Biophysical Chemistry. 84: 27-34. PMID 10723542 DOI: 10.1016/S0301-4622(99)00140-4 |
0.408 |
|
| 2000 |
Jelesarov I, Crane-Robinson C, Privalov PL. The energetics of HMG box interactions with DNA: thermodynamic description of the target DNA duplexes. Journal of Molecular Biology. 294: 981-95. PMID 10588901 DOI: 10.1006/Jmbi.1999.3284 |
0.489 |
|
| 1999 |
Privalov PL, Jelesarov I, Read CM, Dragan AI, Crane-Robinson C. The energetics of HMG box interactions with DNA: Thermodynamics of the DNA binding of the HMG box from mouse Sox-5 Journal of Molecular Biology. 294: 997-1013. PMID 10588902 DOI: 10.1006/Jmbi.1999.3285 |
0.522 |
|
| 1999 |
Taylor JW, Greenfield NJ, Wu B, Privalov PL. A calorimetric study of the folding-unfolding of an alpha-helix with covalently closed N and C-terminal loops. Journal of Molecular Biology. 291: 965-76. PMID 10452900 DOI: 10.1006/Jmbi.1999.3025 |
0.462 |
|
| 1999 |
Yu YB, Lavigne P, Kay CM, Hodges RS, Privalov PL. Contribution of Translational and Rotational Entropy to the Unfolding of a Dimeric Coiled-Coil Journal of Physical Chemistry B. 103: 2270-2278. DOI: 10.1021/Jp983533R |
0.336 |
|
| 1998 |
Crane-Robinson C, Read CM, Cary PD, Driscoll PC, Dragan AI, Privalov PL. The energetics of HMG box interactions with DNA. Thermodynamic description of the box from mouse Sox-5 Journal of Molecular Biology. 281: 705-717. PMID 9710541 DOI: 10.1006/Jmbi.1998.1895 |
0.47 |
|
| 1997 |
Tamura A, Privalov PL. The entropy cost of protein association. Journal of Molecular Biology. 273: 1048-60. PMID 9367790 DOI: 10.1006/Jmbi.1997.1368 |
0.353 |
|
| 1997 |
Wintrode PL, Privalov PL. Energetics of target peptide recognition by calmodulin: A calorimetric study Journal of Molecular Biology. 266: 1050-1062. PMID 9086281 DOI: 10.1006/Jmbi.1996.0785 |
0.413 |
|
| 1997 |
Carra JH, Privalov PL. Energetics of folding and DNA binding of the MAT alpha 2 homeodomain. Biochemistry. 36: 526-35. PMID 9012668 DOI: 10.1021/Bi962206B |
0.429 |
|
| 1997 |
Carra JH, Murphy EC, Privalov PL. Thermodynamic effects of mutations on the denaturation of T4 lysozyme. Biophysical Journal. 71: 1994-2001. PMID 8889173 DOI: 10.1016/S0006-3495(96)79397-9 |
0.406 |
|
| 1997 |
Makhatadze GI, Lopez MM, Privalov PL. Heat capacities of protein functional groups Biophysical Chemistry. 64: 93-101. DOI: 10.1016/S0301-4622(96)02234-X |
0.663 |
|
| 1997 |
Privalov PL. Thermodynamics of protein folding The Journal of Chemical Thermodynamics. 29: 447-474. DOI: 10.1006/Jcht.1996.0178 |
0.398 |
|
| 1996 |
Makhatadze GI, Privalov PL. On the entropy of protein folding Protein Science. 5: 507-510. PMID 8868487 DOI: 10.1002/Pro.5560050312 |
0.638 |
|
| 1996 |
Hendrix TM, Griko Y, Privalov P. Energetics of structural domains in alpha-lactalbumin. Protein Science : a Publication of the Protein Society. 5: 923-31. PMID 8732764 DOI: 10.1002/Pro.5560050514 |
0.31 |
|
| 1996 |
Yu Y, Monera OD, Hodges RS, Privalov PL. Investigation of electrostatic interactions in two-stranded coiled-coils through residue shuffling. Biophysical Chemistry. 59: 299-314. PMID 8672718 DOI: 10.1016/0301-4622(95)00131-X |
0.386 |
|
| 1996 |
Privalov PL. Intermediate states in protein folding. Journal of Molecular Biology. 258: 707-25. PMID 8637003 DOI: 10.1006/Jmbi.1996.0280 |
0.422 |
|
| 1996 |
Privalov G, Kavina V, Freire E, Privalov PL. Precise scanning calorimeter for studying thermal properties of biological macromolecules in dilute solution. Analytical Biochemistry. 232: 79-85. PMID 8600837 DOI: 10.1006/Abio.1995.9957 |
0.422 |
|
| 1996 |
Carra JH, Privalov PL. Thermodynamics of denaturation of staphylococcal nuclease mutants: an intermediate state in protein folding. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 10: 67-74. PMID 8566550 DOI: 10.1096/Fasebj.10.1.8566550 |
0.408 |
|
| 1995 |
Makhatadze GI, Privalov PL. Energetics of protein structure Advances in Protein Chemistry. 47: 307-425. PMID 8561051 DOI: 10.1016/S0065-3233(08)60548-3 |
0.649 |
|
| 1995 |
Wintrode PL, Griko YV, Privalov PL. Structural energetics of barstar studied by differential scanning microcalorimetry Protein Science. 4: 1528-1534. PMID 8520478 DOI: 10.1002/Pro.5560040810 |
0.528 |
|
| 1995 |
Carra JH, Privalov PL. Energetics of denaturation and m values of staphylococcal nuclease mutants. Biochemistry. 34: 2034-41. PMID 7849061 DOI: 10.1021/Bi00006A025 |
0.391 |
|
| 1995 |
Griko YV, Freire E, Privalov G, van Dael H, Privalov PL. The unfolding thermodynamics of c-type lysozymes: a calorimetric study of the heat denaturation of equine lysozyme. Journal of Molecular Biology. 252: 447-59. PMID 7563064 DOI: 10.1006/Jmbi.1995.0510 |
0.354 |
|
| 1994 |
Griko YV, Privalov PL. Thermodynamic puzzle of apomyoglobin unfolding. Journal of Molecular Biology. 235: 1318-25. PMID 8308894 DOI: 10.1006/Jmbi.1994.1085 |
0.502 |
|
| 1994 |
Wintrode PL, Makhatadze GI, Privalov PL. Thermodynamics of ubiquitin unfolding Proteins: Structure, Function and Genetics. 18: 246-253. PMID 8202465 DOI: 10.1002/Prot.340180305 |
0.626 |
|
| 1994 |
Yu Y, Makhatadze GI, Pace CN, Privalov PL. Energetics of ribonuclease T1 structure Biochemistry. 33: 3312-3319. PMID 8136367 DOI: 10.1021/Bi00177A023 |
0.644 |
|
| 1994 |
Griko YV, Freire E, Privalov PL. Energetics of the alpha-lactalbumin states: a calorimetric and statistical thermodynamic study. Biochemistry. 33: 1889-99. PMID 8110793 DOI: 10.1021/Bi00173A036 |
0.482 |
|
| 1994 |
Carra JH, Anderson EA, Privalov PL. Three-state thermodynamic analysis of the denaturation of staphylococcal nuclease mutants. Biochemistry. 33: 10842-50. PMID 8075087 DOI: 10.1021/Bi00201A035 |
0.427 |
|
| 1994 |
Carra JH, Anderson EA, Privalov PL. Thermodynamics of staphylococcal nuclease denaturation. II. The A-state. Protein Science : a Publication of the Protein Society. 3: 952-9. PMID 8069224 DOI: 10.1002/Pro.5560030610 |
0.416 |
|
| 1994 |
Carra JH, Anderson EA, Privalov PL. Thermodynamics of staphylococcal nuclease denaturation. I. The acid-denatured state. Protein Science : a Publication of the Protein Society. 3: 944-51. PMID 8069223 DOI: 10.1002/Pro.5560030609 |
0.508 |
|
| 1994 |
Makhatadze GI, Clore GM, Gronenborn AM, Privalov PL. Thermodynamics of unfolding of the all β-sheet protein interleukin-1β Biochemistry. 33: 9327-9332. PMID 8049234 DOI: 10.1021/bi00197a037 |
0.581 |
|
| 1994 |
Makhatadze GI, Privalov PL. Energetics of interactions of aromatic hydrocarbons with water Biophysical Chemistry. 50: 285-291. PMID 8011949 DOI: 10.1016/0301-4622(93)E0096-N |
0.597 |
|
| 1994 |
Griko YV, Makhatadze GI, Privalov PL, Hartley RW. Thermodynamics of barnase unfolding Protein Science. 3: 669-676. PMID 8003984 DOI: 10.1002/Pro.5560030414 |
0.705 |
|
| 1994 |
Griko YV, Gittis A, Lattman EE, Privalov PL. Residual structure in a staphylococcal nuclease fragment. Is it a molten globule and is its unfolding a first-order phase transition? Journal of Molecular Biology. 243: 93-9. PMID 7932744 DOI: 10.1006/Jmbi.1994.1632 |
0.406 |
|
| 1994 |
Makhatadze GI, Privalov PL. Hydration effects in protein unfolding Biophysical Chemistry. 51: 291-309. PMID 7919040 DOI: 10.1016/0301-4622(94)00050-6 |
0.678 |
|
| 1993 |
Privalov PL, Makhatadze GI. Contribution of hydration to protein folding thermodynamics. II. The entropy and Gibbs energy of hydration Journal of Molecular Biology. 232: 660-679. PMID 8393941 DOI: 10.1006/Jmbi.1993.1417 |
0.659 |
|
| 1993 |
Makhatadze GI, Privalov PL. Contribution of hydration to protein folding thermodynamics. I. The enthalpy of hydration Journal of Molecular Biology. 232: 639-659. PMID 8393940 DOI: 10.1006/Jmbi.1993.1416 |
0.677 |
|
| 1993 |
Makhatadze GI, Kim KS, Woodward C, Privalov PL. Thermodynamics of BPTI folding Protein Science. 2: 2028-2036. PMID 7507751 DOI: 10.1002/Pro.5560021204 |
0.679 |
|
| 1993 |
Griko YV, Rogov VV, Privalov PL. Domains in lambda Cro repressor. A calorimetric study. Biochemistry. 31: 12701-5. PMID 1472508 DOI: 10.1021/Bi00165A022 |
0.362 |
|
| 1993 |
Makhatadze GI, Fernandez J, Freire E, Lilley TH, Privalov PL. Thermodynamics of aqueous guanidinium hydrochloride solutions in the temperature range from 283.15 to 313.15 K Journal of Chemical & Engineering Data. 38: 83-87. DOI: 10.1021/Je00009A020 |
0.611 |
|
| 1992 |
Freire E, Murphy KP, Sanchez-Ruiz JM, Galisteo ML, Privalov PL. The molecular basis of cooperativity in protein folding. Thermodynamic dissection of interdomain interactions in phosphoglycerate kinase Biochemistry. 31: 250-256. PMID 1731874 DOI: 10.1021/Bi00116A034 |
0.402 |
|
| 1992 |
Griko YV, Privalov PL. Calorimetric study of the heat and cold denaturation of beta-lactoglobulin. Biochemistry. 31: 8810-5. PMID 1390668 DOI: 10.1021/Bi00152A017 |
0.534 |
|
| 1992 |
Makhatadze GI, Privalov PL. Protein interactions with urea and guanidinium chloride. A calorimetric study Journal of Molecular Biology. 226: 491-505. PMID 1322462 DOI: 10.1016/0022-2836(92)90963-K |
0.664 |
|
| 1992 |
Privalov PL, Makhatadze GI. Contribution of hydration and non-covalent interactions to the heat capacity effect on protein unfolding Journal of Molecular Biology. 224: 715-723. PMID 1314903 DOI: 10.1016/0022-2836(92)90555-X |
0.701 |
|
| 1991 |
Gitelson GI, Griko Yu V, Kurochkin AV, Rogov VV, Kutyshenko VP, Kirpichnikov MP, Privalov PL. Two-stage thermal unfolding of [Cys55]-substituted Cro repressor of bacteriophage lambda. Febs Letters. 289: 201-4. PMID 1833238 DOI: 10.1016/0014-5793(91)81069-K |
0.356 |
|
| 1990 |
Makhatadze GI, Gill SJ, Privalov PL. Partial molar heat capacities of the side chains of some amino acid residues in aqueous solution. The influence of the neighboring charges. Biophysical Chemistry. 38: 33-7. PMID 17056435 DOI: 10.1016/0301-4622(90)80037-8 |
0.638 |
|
| 1990 |
Makhatadze GI, Privalov PL. Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: Hydration effect Journal of Molecular Biology. 213: 375-384. PMID 2342113 DOI: 10.1016/S0022-2836(05)80197-4 |
0.675 |
|
| 1990 |
Murphy KP, Privalov PL, Gill SJ. Common features of protein unfolding and dissolution of hydrophobic compounds. Science (New York, N.Y.). 247: 559-61. PMID 2300815 DOI: 10.1126/Science.2300815 |
0.472 |
|
| 1990 |
Privalov PL. Cold denaturation of proteins. Critical Reviews in Biochemistry and Molecular Biology. 25: 281-305. PMID 2225910 DOI: 10.3109/10409239009090612 |
0.393 |
|
| 1990 |
Privalov PL, Makhatadze GI. Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: Protein unfolding effects Journal of Molecular Biology. 213: 385-391. PMID 2160545 DOI: 10.1016/S0022-2836(05)80198-6 |
0.69 |
|
| 1990 |
Makhatadze GI, Medvedkin VN, Privalov PL. Partial molar volumes of polypeptides and their constituent groups in aqueous solution over a broad temperature range Biopolymers. 30: 1001-1010. PMID 2081262 DOI: 10.1002/Bip.360301102 |
0.632 |
|
| 1989 |
Griko YV, Venyaminov SY, Privalov PL. Heat and cold denaturation of phosphoglycerate kinase (interaction of domains) Febs Letters. 244: 276-278. PMID 2646151 DOI: 10.1016/0014-5793(89)80544-7 |
0.453 |
|
| 1989 |
Privalov PL, Tiktopulo EI, Venyaminov SY, Griko YV, Makhatadze GI, Khechinashvili NN. Heat capacity and conformation of proteins in the denatured state Journal of Molecular Biology. 205: 737-750. PMID 2538636 DOI: 10.1016/0022-2836(89)90318-5 |
0.711 |
|
| 1989 |
Privalov PL, Gill SJ. The hydrophobic effect: a reappraisal Pure and Applied Chemistry. 61: 1097-1104. DOI: 10.1351/Pac198961061097 |
0.339 |
|
| 1989 |
Makhatadze GI, Privalov PL. Heat capacity of alcohols in aqueous solutions in the temperature range from 5 to 125°C Journal of Solution Chemistry. 18: 927-936. DOI: 10.1007/BF00647893 |
0.627 |
|
| 1988 |
Bendzko PI, Pfeil WA, Privalov PL, Tiktopulo EI. Temperature-induced phase transitions in proteins and lipids. Volume and heat capacity effects. Biophysical Chemistry. 29: 301-7. PMID 3390527 DOI: 10.1016/0301-4622(88)85052-X |
0.486 |
|
| 1988 |
Griko YV, Privalov PL, Sturtevant JM, Venyaminov SYu. Cold denaturation of staphylococcal nuclease. Proceedings of the National Academy of Sciences of the United States of America. 85: 3343-7. PMID 3368446 DOI: 10.1073/pnas.85.10.3343 |
0.399 |
|
| 1988 |
Griko YV, Privalov PL, Venyaminov SY, Kutyshenko VP. Thermodynamic study of the apomyoglobin structure. Journal of Molecular Biology. 202: 127-38. PMID 3172208 DOI: 10.1016/0022-2836(88)90525-6 |
0.42 |
|
| 1988 |
Privalov PL, Gill SJ. Stability of protein structure and hydrophobic interaction. Advances in Protein Chemistry. 39: 191-234. PMID 3072868 DOI: 10.1016/S0065-3233(08)60377-0 |
0.517 |
|
| 1988 |
Makhatadze GI, Privalov PL. Partial specific heat capacity of benzene and of toluene in aqueous solution determined calorimetrically for a broad temperature range The Journal of Chemical Thermodynamics. 20: 405-412. DOI: 10.1016/0021-9614(88)90177-2 |
0.618 |
|
| 1987 |
Privalov PL, Kutyshenko VP. Cold denaturation of myoglobin. Journal of Molecular Biology. 190: 487-98. PMID 3783710 DOI: 10.1016/0022-2836(86)90017-3 |
0.54 |
|
| 1986 |
Privalov PL, Potekhin SA. Scanning microcalorimetry in studying temperature-induced changes in proteins. Methods in Enzymology. 131: 4-51. PMID 3773768 DOI: 10.1016/0076-6879(86)31033-4 |
0.405 |
|
| 1985 |
Tsalkova TN, Privalov PL. Thermodynamic study of domain organization in troponin C and calmodulin. Journal of Molecular Biology. 181: 533-44. PMID 3999139 DOI: 10.1016/0022-2836(85)90425-5 |
0.359 |
|
| 1983 |
Yutani K, Khechinashvili NN, Lapshina EA, Privalov PL, Sugino Y. Calorimetric study of tryptophan synthase alpha-subunit and two mutant proteins. International Journal of Peptide and Protein Research. 20: 331-6. PMID 6816746 DOI: 10.1111/J.1399-3011.1982.Tb00898.X |
0.469 |
|
| 1982 |
Tiktopulo EI, Privalov PL, Odintsova TI, Ermokhina TM, Krasheninnikov IA, Aviles FX, Cary PD, Crane-Robinson C. The central tryptic fragment of histones H1 and H5 is a fully compacted domain and is the only folded region in the polypeptide chain. A thermodynamic study. European Journal of Biochemistry / Febs. 122: 327-31. PMID 7060579 DOI: 10.1111/J.1432-1033.1982.Tb05884.X |
0.312 |
|
| 1982 |
Privalov PL. Stability of proteins. Proteins which do not present a single cooperative system. Advances in Protein Chemistry. 35: 1-104. DOI: 10.1016/S0065-3233(08)60468-4 |
0.464 |
|
| 1980 |
Tsalkova TN, Privalov PL. Stability of troponin C. Biochimica Et Biophysica Acta. 624: 196-204. PMID 7407232 DOI: 10.1016/0005-2795(80)90238-X |
0.311 |
|
| 1980 |
Privalov PL. Stability of proteins: small globular proteins. Advances in Protein Chemistry. 33: 167-241. PMID 44431 DOI: 10.1016/S0065-3233(08)60460-X |
0.436 |
|
| 1979 |
Filimonov VV, Privalov PL, Glangloff J, Dirheimer G. A calorimetric investigation of melting of tRNAAsp from brewer's yeast. Biochimica Et Biophysica Acta. 521: 209-16. PMID 363156 DOI: 10.1016/0005-2787(78)90263-0 |
0.364 |
|
| 1978 |
Filimonov VV, Pfeil W, Tsalkova TN, Privalov PL. Thermodynamic investigations of proteins. IV. Calcium binding protein parvalbumin. Biophysical Chemistry. 8: 117-22. PMID 27259 DOI: 10.1016/0301-4622(78)80003-9 |
0.439 |
|
| 1977 |
Zav'yalov VP, Troitsky GV, Khechinashvili NN, Privalov PL. Thermally induced conformational transitions of Bence-Jones protein IVA and its proteolytic fragments. Biochimica Et Biophysica Acta. 492: 102-11. PMID 861245 DOI: 10.1016/0005-2795(77)90218-5 |
0.335 |
|
| 1977 |
Filimonov VV, Privalov PL, Hinz HJ, von der Haar F, Cramer F. Calorimetric investigations on thermal stability of tRNAIle (yeast) and tRNASer (yeast). European Journal of Biochemistry. 70: 25-31. PMID 795649 DOI: 10.1111/J.1432-1033.1976.Tb10951.X |
0.432 |
|
| 1977 |
Hinz HJ, Filimonov VV, Privalov PL. Calorimetric studies on melting of tRNA Phe (yeast). European Journal of Biochemistry. 72: 79-86. PMID 319003 DOI: 10.1111/J.1432-1033.1977.Tb11226.X |
0.381 |
|
| 1976 |
Pfeil W, Privalov PL. Thermodynamic investigations of proteins. II. Calorimetric study of lysozyme denaturation by guanidine hydrochloride. Biophysical Chemistry. 4: 33-40. PMID 1247649 DOI: 10.1016/0301-4622(76)80004-X |
0.425 |
|
| 1975 |
Privalov P, Plotnikov V, Filimonov V. Precision scanning microcalorimeter for the study of liquids The Journal of Chemical Thermodynamics. 7: 41-47. DOI: 10.1016/0021-9614(75)90079-8 |
0.309 |
|
| 1974 |
Privalov PL, Tiktopulo EI, Khechinashvili NN. Calorimetric investigation of ribonuclease thermal denaturation. International Journal of Peptide and Protein Research. 5: 229-37. PMID 4796696 DOI: 10.1111/J.1399-3011.1973.Tb03457.X |
0.456 |
|
| 1974 |
Privalov PL, Khechinashvili NN. A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. Journal of Molecular Biology. 86: 665-84. PMID 4368360 DOI: 10.1016/0022-2836(74)90188-0 |
0.495 |
|
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