| Year |
Citation |
Score |
| 2000 |
Tcherkasskaya O, Ptitsyn OB, Knutson JR. Nanosecond dynamics of tryptophans in different conformational states of apomyoglobin proteins. Biochemistry. 39: 1879-89. PMID 10677239 |
0.361 |
|
| 1999 |
Ptitsyn OB, Ting KL. Non-functional conserved residues in globins and their possible role as a folding nucleus. Journal of Molecular Biology. 291: 671-82. PMID 10448045 DOI: 10.1006/Jmbi.1999.2920 |
0.401 |
|
| 1999 |
Tcherkasskaya O, Ptitsyn OB. Molten globule versus variety of intermediates: influence of anions on pH-denatured apomyoglobin. Febs Letters. 455: 325-31. PMID 10437798 DOI: 10.1016/S0014-5793(99)00792-9 |
0.48 |
|
| 1999 |
Tcherkasskaya O, Ptitsyn OB. Direct energy transfer to study the 3D structure of non-native proteins: AGH complex in molten globule state of apomyoglobin. Protein Engineering. 12: 485-90. PMID 10388845 DOI: 10.1093/Protein/12.6.485 |
0.453 |
|
| 1999 |
Ptitsyn OB. Protein evolution and protein folding: non-functional conserved residues and their probable role. Pacific Symposium On Biocomputing. Pacific Symposium On Biocomputing. 494-504. PMID 10380222 DOI: 10.1142/9789814447300_0049 |
0.383 |
|
| 1998 |
Bychkova VE, Dujsekina AE, Fantuzzi A, Ptitsyn OB, Rossi GL. Release of retinol and denaturation of its plasma carrier, retinol-binding protein. Folding & Design. 3: 285-91. PMID 9710574 DOI: 10.1016/S1359-0278(98)00039-X |
0.405 |
|
| 1998 |
Afasizheva IIu, Dolgikh DA, Abdullaev ZKh, Latypov RF, Tiktopulo EI, Uverskiĭ VN, Ptitsyn OB, Kirpichnikov MP. [Effect of a biologically active interferon fragment on the structure of the synthetic protein carrier]. Biofizika. 43: 384-91. PMID 9702328 |
0.303 |
|
| 1998 |
Ptitsyn OB. Protein folding and protein evolution: common folding nucleus in different subfamilies of c-type cytochromes? Journal of Molecular Biology. 278: 655-66. PMID 9600846 DOI: 10.1006/Jmbi.1997.1620 |
0.325 |
|
| 1998 |
Ptitsyn OB. Protein folding: nucleation and compact intermediates. Biochemistry. Biokhimiia. 63: 367-73. PMID 9556519 |
0.43 |
|
| 1998 |
Aphasizheva IY, Dolgikh DA, Abdullaev ZK, Uversky VN, Kirpichnikov MP, Ptitsyn OB. Can grafting of an octapeptide improve the structure of a de novo protein? Febs Letters. 425: 101-4. PMID 9541015 DOI: 10.1016/S0014-5793(98)00201-4 |
0.558 |
|
| 1997 |
Uversky VN, Ptitsyn OB. All-or-none solvent-induced transitions between native, molten globule and unfolded states in globular proteins. Folding & Design. 1: 117-22. PMID 9079371 DOI: 10.1016/S1359-0278(96)00020-X |
0.588 |
|
| 1996 |
Bychkova VE, Dujsekina AE, Klenin SI, Tiktopulo EI, Uversky VN, Ptitsyn OB. Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface. Biochemistry. 35: 6058-63. PMID 8634247 DOI: 10.1021/Bi9522460 |
0.543 |
|
| 1996 |
Uversky VN, Ptitsyn OB. Further evidence on the equilibrium "pre-molten globule state": four-state guanidinium chloride-induced unfolding of carbonic anhydrase B at low temperature. Journal of Molecular Biology. 255: 215-28. PMID 8568868 DOI: 10.1006/Jmbi.1996.0018 |
0.603 |
|
| 1996 |
Shakhnovich E, Abkevich V, Ptitsyn O. Conserved residues and the mechanism of protein folding. Nature. 379: 96-8. PMID 8538750 DOI: 10.1038/379096A0 |
0.411 |
|
| 1995 |
Bychkova VE, Ptitsyn OB. [The functional state of denatured proteins: the principles of modelling and the first results]. Tsitologiia. 37: 1238-50. PMID 8714356 |
0.308 |
|
| 1995 |
Ptitsyn OB. Molten globule and protein folding. Advances in Protein Chemistry. 47: 83-229. PMID 8561052 DOI: 10.1016/s0065-3233(08)60546-x |
0.355 |
|
| 1995 |
Ptitsyn OB. Structures of folding intermediates. Current Opinion in Structural Biology. 5: 74-8. PMID 7773749 DOI: 10.1016/0959-440X(95)80011-O |
0.509 |
|
| 1995 |
Ptitsyn OB, Bychkova VE, Uversky VN. Kinetic and equilibrium folding intermediates. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 348: 35-41. PMID 7770484 DOI: 10.1098/Rstb.1995.0043 |
0.616 |
|
| 1995 |
Bychkova VE, Ptitsyn OB. Folding intermediates are involved in genetic diseases? Febs Letters. 359: 6-8. PMID 7531653 DOI: 10.1016/0014-5793(95)00004-S |
0.371 |
|
| 1995 |
Tiktopulo EI, Uversky VN, Lushchik VB, Klenin SI, Bychkova VE, Ptitsyn OB. "Domain" Coil-Globule Transition in Homopolymers Macromolecules. 28: 7519-7524. DOI: 10.1021/Ma00126A032 |
0.482 |
|
| 1994 |
Ptitsyn OB, Uversky VN. The molten globule is a third thermodynamical state of protein molecules. Febs Letters. 341: 15-8. PMID 8137915 DOI: 10.1016/0014-5793(94)80231-9 |
0.6 |
|
| 1994 |
Uversky VN, Ptitsyn OB. "Partly folded" state, a new equilibrium state of protein molecules: four-state guanidinium chloride-induced unfolding of beta-lactamase at low temperature. Biochemistry. 33: 2782-91. PMID 8130190 DOI: 10.1021/Bi00176A006 |
0.628 |
|
| 1994 |
Ptitsyn OB. Kinetic and equilibrium intermediates in protein folding. Protein Engineering. 7: 593-6. PMID 8073028 DOI: 10.1093/Protein/7.5.593 |
0.526 |
|
| 1994 |
Chemeris VV, Dolgikh DA, Fedorov AN, Finkelstein AV, Kirpichnikov MP, Uversky VN, Ptitsyn OB. A new approach to artificial and modified proteins: theory-based design, synthesis in a cell-free system and fast testing of structural properties by radiolabels. Protein Engineering. 7: 1041-52. PMID 7809031 DOI: 10.1093/Protein/7.8.1041 |
0.55 |
|
| 1994 |
Tiktopulo EI, Bychkova VE, Ricka J, Ptitsyn OB. Cooperativity of the Coil-Globule Transition in a Homopolymer: Microcalorimetric Study of Poly(N-isopropylacrylamide) Macromolecules. 27: 2879-2882. DOI: 10.1021/Ma00088A031 |
0.315 |
|
| 1993 |
Bychkova VE, Ptitsyn OB. [The state of unfolded globules of protein molecules is more quickly becoming a rule, rather than an exception]. Biofizika. 38: 58-66. PMID 8471645 |
0.432 |
|
| 1993 |
Uverskiĭ VN, Semisotnov GV, Ptitsyn OB. [Molten globule unfolding by strong denaturing agents occurs by the "all or nothing" principle]. Biofizika. 38: 37-46. PMID 8471644 |
0.414 |
|
| 1993 |
Ptitsyn OB, Zanotti G, Denesyuk AL, Bychkova VE. Mechanism of pH-induced release of retinol from retinol-binding protein. Febs Letters. 317: 181-4. PMID 8425602 DOI: 10.1016/0014-5793(93)81272-2 |
0.307 |
|
| 1993 |
Kuwajima K, Semisotnov GV, Finkelstein AV, Sugai S, Ptitsyn OB. Secondary structure of globular proteins at the early and the final stages in protein folding. Febs Letters. 334: 265-8. PMID 8243629 DOI: 10.1016/0014-5793(93)80691-M |
0.714 |
|
| 1993 |
Ptitsyn OB, Chemeris VV, Dolgikh DA, Fedorov AN, Finkelstein AV, Kirpichnikov MP. A New Approach to Artificial Proteins: Theory-Based Design. Synthesis in the Cell-Free System and Structural Probing at the Nanogram Level Protein Engineering Design & Selection. 6: 122-122. DOI: 10.1093/Protein/6.Supplement.122 |
0.319 |
|
| 1992 |
Fedorov AN, Dolgikh DA, Chemeris VV, Chernov BK, Finkelstein AV, Schulga AA, Alakhov YuB, Kirpichnikov MP, Ptitsyn OB. De novo design, synthesis and study of albebetin, a polypeptide with a predetermined three-dimensional structure. Probing the structure at the nanogram level. Journal of Molecular Biology. 225: 927-31. PMID 1613798 DOI: 10.1016/0022-2836(92)90092-X |
0.434 |
|
| 1992 |
Bychkova VE, Berni R, Rossi GL, Kutyshenko VP, Ptitsyn OB. Retinol-binding protein is in the molten globule state at low pH. Biochemistry. 31: 7566-71. PMID 1510943 DOI: 10.1021/Bi00148A018 |
0.417 |
|
| 1992 |
Dolgikh DA, Kirpichnikov MP, Ptitsyn OB, Fedorov AN, Finkel'shteĭn AV, Chemeris VV. [De novo proteins with a given spatial structure: new approaches to design and analysis]. Molekuliarnaia Biologiia. 26: 1242-50. PMID 1491670 |
0.366 |
|
| 1992 |
Uversky VN, Semisotnov GV, Pain RH, Ptitsyn OB. 'All-or-none' mechanism of the molten globule unfolding. Febs Letters. 314: 89-92. PMID 1451808 DOI: 10.1016/0014-5793(92)81468-2 |
0.71 |
|
| 1992 |
Ptitsyn OB. Secondary structure formation and stability: Current Opinion in Structural Biology 1992, 2:13–20 Current Opinion in Structural Biology. 2: 13-20. DOI: 10.1016/0959-440X(92)90170-C |
0.318 |
|
| 1991 |
Ptitsyn OB. How does protein synthesis give rise to the 3D-structure? Febs Letters. 285: 176-81. PMID 1855587 DOI: 10.1016/0014-5793(91)80799-9 |
0.383 |
|
| 1990 |
Ptitsyn OB, Pain RH, Semisotnov GV, Zerovnik E, Razgulyaev OI. Evidence for a molten globule state as a general intermediate in protein folding. Febs Letters. 262: 20-4. PMID 2318308 DOI: 10.1016/0014-5793(90)80143-7 |
0.714 |
|
| 1990 |
Goldberg ME, Semisotnov GV, Friguet B, Kuwajima K, Ptitsyn OB, Sugai S. An early immunoreactive folding intermediate of the tryptophan synthease beta 2 subunit is a 'molten globule'. Febs Letters. 263: 51-6. PMID 1691989 DOI: 10.1016/0014-5793(90)80703-L |
0.683 |
|
| 1988 |
Bychkova VE, Pain RH, Ptitsyn OB. The 'molten globule' state is involved in the translocation of proteins across membranes? Febs Letters. 238: 231-4. PMID 3049159 DOI: 10.1016/0014-5793(88)80485-X |
0.477 |
|
| 1987 |
Gilmanshin RI, Ptitsyn OB. An early intermediate of refolding alpha-lactalbumin forms within 20 ms. Febs Letters. 223: 327-9. PMID 3666154 DOI: 10.1016/0014-5793(87)80313-7 |
0.361 |
|
| 1987 |
Finkelstein AV, Ptitsyn OB. Why do globular proteins fit the limited set of folding patterns? Progress in Biophysics and Molecular Biology. 50: 171-90. PMID 3332386 DOI: 10.1016/0079-6107(87)90013-7 |
0.358 |
|
| 1987 |
Semisotnov GV, Rodionova NA, Kutyshenko VP, Ebert B, Blanck J, Ptitsyn OB. Sequential mechanism of refolding of carbonic anhydrase B. Febs Letters. 224: 9-13. PMID 2824244 DOI: 10.1016/0014-5793(87)80412-X |
0.667 |
|
| 1987 |
Ptitsyn O. Protein folding: Hypotheses and experiments Journal of Protein Chemistry. 6. DOI: 10.1007/BF00248050 |
0.301 |
|
| 1986 |
Pfeil W, Bychkova VE, Ptitsyn OB. Physical nature of the phase transition in globular proteins. Calorimetric study of human alpha-lactalbumin. Febs Letters. 198: 287-91. PMID 3956736 DOI: 10.1016/0014-5793(86)80422-7 |
0.422 |
|
| 1986 |
Damaschun G, Gernat C, Damaschun H, Bychkova V, Ptitsyn O. Comparison of intramolecular packing of a protein in native and ‘molten globule’ states International Journal of Biological Macromolecules. 8: 226-230. DOI: 10.1016/0141-8130(86)90031-0 |
0.411 |
|
| 1985 |
Brazhnikov EV, Chirgadze YuN, Dolgikh DA, Ptitsyn OB. Noncooperative temperature melting of a globular protein without specific tertiary structure: acid form of bovine carbonic anhydrase B. Biopolymers. 24: 1899-907. PMID 3935185 DOI: 10.1002/Bip.360241005 |
0.423 |
|
| 1985 |
Ptitsyn OB, Finkelstein AV, Murzin AG. Structural model for interferons. Febs Letters. 186: 143-8. PMID 3924661 DOI: 10.1016/0014-5793(85)80697-9 |
0.373 |
|
| 1985 |
Dolgikh DA, Abaturov LV, Bolotina IA, Brazhnikov EV, Bychkova VE, Gilmanshin RI, Lebedev YuO, Semisotnov GV, Tiktopulo EI, Ptitsyn OB. Compact state of a protein molecule with pronounced small-scale mobility: bovine alpha-lactalbumin. European Biophysics Journal : Ebj. 13: 109-21. PMID 3843533 DOI: 10.1007/Bf00256531 |
0.702 |
|
| 1985 |
Ptitsyn OB. Physical principles of protein structure and protein folding Journal of Biosciences. 8: 1-13. DOI: 10.1007/BF02703962 |
0.352 |
|
| 1984 |
Ptitsyn OB. [Protein as an edited random copolymer]. Molekuliarnaia Biologiia. 18: 574-90. PMID 6472260 |
0.312 |
|
| 1984 |
Dolgikh DA, Kolomiets AP, Bolotina IA, Ptitsyn OB. 'Molten-globule' state accumulates in carbonic anhydrase folding. Febs Letters. 165: 88-92. PMID 6420185 DOI: 10.1016/0014-5793(84)80020-4 |
0.483 |
|
| 1983 |
Ptitsyn OB, Finkelstein AV. Theory of protein secondary structure and algorithm of its prediction. Biopolymers. 22: 15-25. PMID 6673754 DOI: 10.1002/Bip.360220105 |
0.361 |
|
| 1983 |
Ptitsyn OB, Dolgikh DA, Gil'manshin RI, Shakhnovich EI, Finkel'shteĭn AV. [Fluctuating state of the protein globule]. Molekuliarnaia Biologiia. 17: 569-76. PMID 6410182 |
0.449 |
|
| 1982 |
Gil'manshin RI, Dolgikh DA, Ptitsyn OB, Finkel'shteĭn AV, Shakhnovich EI. [Protein globule without the unique three-dimensional structure: experimental data for alpha-lactalbumins and general model]. Biofizika. 27: 1005-16. PMID 7159610 |
0.426 |
|
| 1981 |
Dolgikh DA, Gilmanshin RI, Brazhnikov EV, Bychkova VE, Semisotnov GV, Venyaminov SYu, Ptitsyn OB. Alpha-Lactalbumin: compact state with fluctuating tertiary structure? Febs Letters. 136: 311-5. PMID 7327267 DOI: 10.1016/0014-5793(81)80642-4 |
0.73 |
|
| 1981 |
Semisotnov GV, Zikherman KK, Kasatkin SB, Ptitsyn OB, Anufrieva EV. Polarized luminescence and mobility of tryptophan residues in polypeptide chains Biopolymers. 20: 2287-2309. DOI: 10.1002/BIP.1981.360201102 |
0.601 |
|
| 1980 |
Bolotina IA, Chekhov VO, Lugauskas VIu, Finkel'shteĭn AV, Ptitsyn OB. [Determination of the secondary structure of proteins from their circular dichroism spectra. I. Protein reference spectra for alpha-, beta- and irregular structures]. Molekuliarnaia Biologiia. 14: 891-902. PMID 7421809 |
0.334 |
|
| 1980 |
Ptitsyn OB, Finkelstein AV. Similarities of protein topologies: evolutionary divergence, functional convergence or principles of folding? Quarterly Reviews of Biophysics. 13: 339-86. PMID 7012894 DOI: 10.1017/S0033583500001724 |
0.367 |
|
| 1979 |
Ptitsyn OB, Finkelstein AV. Mechanism of protein folding International Journal of Quantum Chemistry. 16: 407-418. DOI: 10.1002/QUA.560160302 |
0.331 |
|
| 1978 |
Timchenko AA, Ptitsyn OB, Troitsky AV, Denesyuk AI. The structure of phage T4 lysozyme in solution noticeably differs from its crystalline struction. Febs Letters. 88: 109-13. PMID 639977 DOI: 10.1016/0014-5793(78)80619-X |
0.392 |
|
| 1978 |
Timchenko AA, Ptitsyn OB, Dolgikh DA, Fedorov BA. The structure of ribonuclease in solution does not differ from its crystalline structure. Febs Letters. 88: 105-8. PMID 639976 DOI: 10.1016/0014-5793(78)80618-8 |
0.306 |
|
| 1977 |
Finkelstein AV, Ptitsyn OB, Kozitsyn SA. Theory of protein molecule self-organization. II. A comparison of calculated thermodynamic parameters of local secondary structures with experiments. Biopolymers. 16: 497-524. PMID 843599 DOI: 10.1002/Bip.1977.360160303 |
0.427 |
|
| 1977 |
Finkelstein AV, Ptitsyn OB. Theory of protein molecule self-organization. I. Thermodynamic parameters of local secondary structures in the unfolded protein chain. Biopolymers. 16: 469-95. PMID 843598 DOI: 10.1002/Bip.1977.360160302 |
0.37 |
|
| 1976 |
Finkelstein AV, Ptitsyn OB. A theory of protein molecule self-organization. IV. Helical and irregular local structures of unfolded protein chains. Journal of Molecular Biology. 103: 15-24. PMID 957423 DOI: 10.1016/0022-2836(76)90049-8 |
0.43 |
|
| 1975 |
Finkelstein AV, Kozitsyn SA, Ptitsyn OB. Prediction of the three-dimensional structure for ribosomal protein L25. Febs Letters. 60: 137-40. PMID 1227950 DOI: 10.1016/0014-5793(75)80436-4 |
0.354 |
|
| 1974 |
Denesiuk AI, Ptitsyn OB, Finkel'shteĭn AV. [Letter: Helical structure of unfolded protein chains]. Biofizika. 19: 549-61. PMID 4424525 |
0.364 |
|
| 1973 |
Ptitsyn OB, Denesyuk AI, Finkelstein AV, Lim VI. Prediction of the secondary structure of the L7, L12 proteins of the E. coli ribosome. Febs Letters. 34: 55-7. PMID 4580998 DOI: 10.1016/0014-5793(73)80701-X |
0.315 |
|
| 1967 |
Anufrieva EV, Birshtein TM, Bolotina IA, Burshtein LL, Eskin VE, Frolov VI, Illarionova NG, Kalikhevich VI, Korotkina OZ, Mitin YV, Ptitsyn OB, Purkinas AV, Volchek BZ. The models of the denaturation of globular proteins. III. The intramolecularβ-structure coil transitions in poly-S-carbobenzoxymethyl-l-cysteine Journal of Polymer Science Part C: Polymer Symposia. 16: 3533-3545. DOI: 10.1002/POLC.5070160646 |
0.302 |
|
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