Область прикладного применения результатов научных исследований
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Избранные публикации
Kasyanenko N.A., Selman-Housein Sosa G., Uversky V.N., Frisman E.V. Study on the effect of Mn2+ and Mg2+ ions on DNA conformation. Mol. Biol (Moscow) (1987) 21, 140-146.
Rodionova N.A., Semisotnov G.V., Kutyshenko V.P., Uversky V.N., Bolotina I.A., Bychkova V.E., Ptitsyn O.B. Two-stage equilibrium unfolding of carbonic anhydrase B by strong denaturants. Mol. Biol (Moscow) (1989) 23, 683-692.
Semisotnov G.V., Uversky V.N., Sokolovski I.V., Gutin A.M., Razgulyaev O.I., Rodionova N.A. Two slow stages in refolding of bovine carbonic anhydrase B are due to proline isomerization. J. Mol. Biol. (1990) 213, 561-568.
Semisotnov G.V., Rodionova N.A., Razgulyaev O.I., Uversky V.N., Gripas’ A.F., Gilmanshin R.I. Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers (1991) 13, 119-128.
Uversky V.N., Leontiev V.V., Gudkov A.T. Triple point mutation Asp10-His, Asn101-Asp, Arg148-Ser in T4 phage lysozyme leads to the molten globule. Protein Engineering (1992) 5, 781-783.
Uversky V.N., Semisotnov G.V., Pain R.H., Ptitsyn O.B. “All-or-none” mechasnism of the molten globule unfolding. FEBS Letters (1992) 314, 89-92.
Uversky V.N., Semisotnov G.V., Ptitsyn O.B. Unfolding of the molten globule by strong denaturants follows the "all-or-none" principle. Biophysics (Moscow) (1993) 38, 31-39.
Uversky V.N., Leontiev V.V., Gudkov A.T. Effect of point amino acid replacements on the stability of phage T4 lysozyme. I. Asn101-Asp replacement. Biophysics (Moscow) (1993) 38, 619-622.
Leontiev V.V., Uversky V.N., Gryaznova O.I., Gudkov A.T. Effect of point amino acid replacements on the stability of phage T4 lysozyme. II. Transition of the protein molecule to the molten globule state for the replacements Asp10-His, Asn101-Asp and Arg148-Ser. Biophysics (Moscow) (1993) 38, 623-627.
Uversky V.N. Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule. Biochemistry (1993) 32, 13288-13298.
Leontiev V.V., Uversky V.N., Gudkov A.T. Comparative stability of dihydrofolate reductase mutants in vitro and in vivo. Protein Engineering (1993) 6, 81-84.
Leontiev V.V., Uversky V.N., Permyakov E.A., Murzin A.G. Introduction of Ca2+-binding amino-acid sequence into the T4 Lysozyme. Biochim. Biophys. Acta (1993) 1162, 84-88.
Medvedkin V.N., Permyakov E.A., Uversky V.N., Gripas A.F., Mitin Yu.V. A Quartz reaction-cuvette for fluorescent monitoring of the solid phase peptide synthesis. Bioorgan. Khimia (Moscow) (1994) 20, 635-644.
Uversky V.N. Gel-permeation chromatography as a unique instrument for quantitative and qualitative analysis of protein denaturation and unfolding. Int. J. Bio-Chromatography (1994) 1, 103-114.
Chemeris V.V., Dolgikh D.A., Fedorov A.N., Finkelstein A.V., Kirpichnikov M.P., Uversky V.N., Ptitsyn O.B. A new approach to artificial and modified proteins: theory-based design, synthesis in a cell-free system and fast testing of structural properties by radiolabeles. Protein Engineering (1994) 7, 1041-1052.
Protasova N.Yu., Kireeva M.L., Murzina N.V., Murzin A.G., Uversky V.N., Gryaznova O.I., Gudkov A.T. Circularly permuted dihydrofolate reductase of E.coli has functional activity and a destabilized tertiary structure. Protein Engineering (1994) 7, 1373-1377.
Ptitsyn O.B., Uversky V.N. The molten globule is a third thermodinamical state of protein molecules. FEBS Letters (1994) 341, 15-18.
Uversky V.N., Ptitsyn O.B. “Partly folded” state, a new equilibrium state of protein molecules: Four-state guanidinium chloride-induced unfolding of -lactamase at low temperature. Biochemistry (1994) 33, 2782-2791.
Vysotskaya V.S., Nassibulin U.F., Uverskii V.N., Vasilenko K.S., Narizhneva N.V., Garber M.B. (1995) Structural properties of ribosomal protein S8 from extreme thermophile Thermus thermophilus. Russian J. Bioorganic Chemistry 21, 423-428.
Ptitsyn O.B., Bychkova V.E., Uversky V.N. (1995) Kinetic and equilibrium folding intermediates. Phil. Trans. R. Soc. Lond. 348, 35-41.
Ptitsyn O.B., Uversky V.N. (1995) “Pre-molten globule” - a new equilibrium state of protein molecules. FASEB Journal 9, A1469.
Uversky V.N., Kirkitadze M.D., Narizhneva N.V., Potekhin S.A., Tomashevski A.Yu. (1995) Structural properties of -fetoprotein from human cord serum: the protein molecule at low pH possesses all the properties of the molten globule. FEBS Letters 364, 165-167.
Dolgikh D.A., Uversky V.N., Gabrielian A.E., Chemeris V.V., Fedorov A.N., Navolotskaya E.V., Zav'yalov V.P. & Kirpichnikov M.P. (1996). The de novo protein with grafted biological function: transferring of interferon blast-transformong activity to albebetin. Protein Engineering 9, 195-201.
Uversky V.N. & Ptitsyn O.B. (1996). Further evidence on the equilibrium “pre-molten globule state": Four-state GdmCl-induced unfolding of carbonic anhydrase B at low temperature. J. Mol. Biol. 255, 215-228.
Uversky V.N. & Ptitsyn O.B. (1996). All-or-none solvent-induced transitions between native, molten globule and unfolded states in globular proteins. Folding & Design, 1, 117-122.
Uversky V.N., Winter S. & Loeber G. (1996). Use of fluorescence decay times of 8-ANS-protein complexes to study the conformational transitions in proteins that unfold through the molten globule state. Biophys. Chem. 60, 79-88.
Bychkova V.E., Dujsekina A.E., Klenin S.I., Tiktopulo E.I., Uversky V.N. & Ptitsyn O.B. (1996). Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface. Biochemistry 35, 6058-6063.
Uversky V.N. & Ptitsyn O.B. (1996). Three-stage equilibrium unfolding of small globular proteins by strong denaturants: I. Carbonic anhydrase B. Mol. Biol. (Moscow) 30, 1124-1134.
Uversky V.N. & Ptitsyn O.B. (1996). Three-stage equilibrium unfolding of small globular proteins by strong denaturants: II. -Lactamase and general model. Mol. Biol. (Moscow) 30, 1135-1143.
Uversky V.N., Kutyshenko V.P., Protasova N.Yu., Rogov V.V., Vassilenko K.S. & Gudkov A.T. (1996). Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by the interaction with its ligands. Protein Science 5, 1844-1851.
Dolgikh D.A., Gabrielian A.E., Uversky V.N., Kirpichnikov M.P. (1996) Protein engineering of de nojo protein with predesigned structure ans activity. Applied Biochemistry and Biotechnology. Protein Engineering 61, 85-96.
Karnoup A.S., Uversky, V.N., Medvedkin V.N. (1996) Synthetic polyamino acids and polypeptides. Preparation by the N-carboxyanhydride method. Bioorgan. Khim. (Moscow) 22(8), 563-574.
Narizhneva N.V., Ivanova T.V., Tomashevski A.Yu., Uversky V.N. (1997) Comparison of structural properties of homologous proteins Human serum albumin and alpha-fetoprotein. Mol. Biol. (Moscow) 31, 1128-1133.
Uversky V.N., Narizhneva N.V., Kirschstein S.O., Löber G. (1997) Coformational transitions provoked by organic solvents in -lactoglobulin: Can a molten globule-like intermediate be induced by the decrease in dielectric constant? Folding & Design 2, 163-173.
Uversky V.N., Narizhneva N.V., Ivanova T.V., Kirkitadze M.D., Tomashevski A.Yu. (1997) Ligand-free form of human -fetoprotein: Evidence for the molten globule state. FEBS Letters 410, 280-284.
Ptitsyn O.B., Bychkova V.E., Dujsekina A.E., Rossi G.-L., Fantuzzi A., Uversky V.N., Tiktopulo E.I., Klenin S.I. (1997) Modelling of the molten globule state of protein near membranes. Protein Engineering 10, 32.
Narizhneva N.V., Uversky V.N. (1997) Human -fetoprotein is in the molten globule state under conditions modelling protein environment near the membrane surface. Protein and Peptide Letters 4, 243-249.
Uversky V.N., Narizhneva N.V., Ivanova T.V., Tomashevski A.Yu. (1997) Rigidity of human -fetoprotein structure is under the ligand control. Biochemistry 44, 13638-13645.
Karnoup A.S., Uversky V.N. (1997) Sequential compactization of random copolymer of hydrophilic and hydrophobic amino acid residues. Macromolecules 30, 7427-7434.
Abdullaev Z.K., Latypov R.F., Badretdinov A.Ya., Dolgikh D.A., Finkelstein A.V., Uversky V.N., Kirpichnikov M.P. (1997) S6 permutant shows that the unusual target topology does not responsible for the absence of rigid tertiary structure in the de novo protein albebetin. FEBS Letters 414, 243-246.
Uversky V.N. (1997) Diversity of compact forms of denatured globular proteins (Mini Review). Protein and Peptide Letters 4, 355-367.
Uversky V.N., Fink A.L. (1998) Structural effect of association on protein molecules in partially folded intermediates. Biochemistry (Moscow) 63, 456-462.
Uversky V.N., Fink A.L. (1998) Structural properties of staphylococcal nuclease in oligomeric A-forms. Biochemistry (Moscow) 63, 463-469.
Uversky V. N. (1998) Equilibrium unfolding of partially folded staphylococcal nuclease A2- and A3-forms is accompanied by the formation of an intermediate state. Biochemistry (Moscow) 63, 420-433.
Narizhneva N.V., Uversky V.N. (1998) Decrease of dielectric constant transforms the protein molecule into the molten globule state. Biochemistry (Moscow) 63, 448-455.
Uversky V.N., Narizhneva N.V. (1998) Effect of natural ligands on structural properties and conformational stability of proteins (Review). Biochemistry (Moscow) 63, 420-433.
Uversky V. N. (1998) Diversity of denatured forms of globular proteins. I. Anion-induced folding of staphylococcal nuclease. Mol. Biol. (Moscow) 32, 482-487.
Uversky V. N. (1998) Diversity of denatured forms of globular proteins. II. Structural properties of A-forms. Mol. Biol. (Moscow) 32, 488-497.
Karnoup A.S., Uversky V.N. (1998) Pre-molten globule state in the random copolymer consisting of hydrophobic and hydrophilic amino acid residues. Mol. Biol. (Moscow) 32, 550-556.
Latypov R.F., Abdullaev Z.Kh., Badretdinov A.Ya., Bocharov E.V., Mel’nik T.N., Afasizheva I.Yu., Arsen’ev A.S., Dolgikh D.A., Uverskii V.N., Finkelstein A.V., Kirpichnikov M.P. Circular permutation of the Thermus thermophylus ribosomal protein S6 imparing to it the topology of the artificial protein albebetin. Mol. Biol. (Moscow) 32, 109-116.
Uversky V.N. (1998) How many molten globule states there exist? Biofizika (Moscow) 43, 416-421.
Aphasizheva I.Yu., Dolgikh D.A., Abdullaev Z.K., Uversky V.N., Kirpichnikov M.P., Ptitsyn O.B. (1998) Can grafting of an octapeptide improve the structure of a de novo protein? FEBS Letters 425, 101-104.
Uversky V.N., Karnoup A.S., Segel D., Seshadri S., Doniach S., Fink A.L. (1998) Anion-induced folding of Staphylococcal nuclease: Characterization of multiple partially folded intermediates. J. Mol. Biol. 278, 879-894.
Uversky V.N., Winter S., Löber G. (1998) Self-association of 8-anilino-1-naphthalene-sulfonate molecules: Spectroscopic characterization and aplication to the investigation of protein folding. Biochim. Biophys. Acta 1388, 133-142.
Tomashevski A.Yu., Narizhneva N.V., Melnik T.N., Uversky V.N. (1998) -Fetoprotein structure depends on the protein purification procedure: Further evidence on the structure forming role of the ligands. Prot. Pept. Lett. 5, 295-301.
Uversky V.N., Winter S., Galzitskaya O.V., Kittler L., Löber G. (1998) Hyperphospho-rylation induces structural modification of tau-protein. FEBS Lett. 439, 21-25.
Aphasizheva, I.Y., Dolgikh, D.A., Abdullaev, Z.K., Latypov, R.F., Tiktopulo, E.I., Uversky, V.N., Ptitsyn, O.B., Kirpichnikov, M.P. (1998) Influence of a biologically active interferon fragment on the carrier de novo protein structure. Biofizika 43 (3), 384-391.
Uversky V.N., Karnoup A.S., Khurana R., Segel D., Doniach S., Fink A.L. (1999) Association of partially-folded intermediates of Staphylococcal nuclease induces structure and stability. Protein Sci. 8, 161-173.
Uversky V.N. (1999) A multiparametric approach to studies of self-organization of globular proteins. Review. Biochemistry (Moscow). 64, 250-266.
Uversky V.N. (1999) Studies on ANS fluorescence: I. Effect of self-association on structural properties of the dye. Cytology (St. Petersburg). 41, 173-182.
Uversky V.N. (1999) Studies on ANS fluorescence: II. Application of the dye fluorescence decay to investigate the structural transformations in globular proteins. Cytology (St. Petersburg). 41, 183-189.
Turoverov K.K., Kuznetsova I.M., Khaitlina S.Yu, Uversky V.N. (1999) Unusual combination of the distorted structure and frozen internal mobility in inactivated actin. Prot. Pept. Let. 6, 73-78.
Uversky V.N., Abdullaev Z. Kh., Latypov R.F., Bocharov E., Melnik T.N., Vassilenko K.S., Arseniev, A.S., Dolgikh D.A., Kirpichnikov M.P. (1999) Structure and stability of the recombinant protein can depend on the extra N-terminal methionine residue: S6 permutein from direct and fusion expression systems. Biochem Biophys. Acta. 1432, 324-332.
Uversky V.N., Fink A.L. (1999) Do protein molecules have a native-like topology in the pre-molten globule state? Biochemistry (Moscow). 64, 552-555.
Veprintsev D.B., Narayan M., Permyakov S.E., Uversky V.N., Brooks C.L., Cherskaya A.M., Permyakov E.A., Berliner L.J. (1999) Fine tuning the N-terminus of a calcium binding protein: -lactalbumin. Proteins. Structure Function and Genetics. 37, 65-72.
Kuznetsova I.M., Turoverov K.K., Uversky V.N. (1999) Inactivated actin, an aggregate composed of partially-folded monomers, has an overall native-like packing density. Pro. Pept. Lett. 6, 173-178.
Tomashevski A.Yu., Uversky V.N. (1999) A new scheme of the human -fetoprotein isolation. Russian J. Bioorganic Chemistry. 25, 412-417.
Tomashevski A.Yu., Melnik T.N., Narizhneva N.V., Shavlovsky M.M., Vasiliev V.B., Uversky V.N. (1999) The -fetoprotein molecule has one or two rigid domains depending on the protein purification procedure. Prot. Pept. Lett.. 6 (4), 237-244.
Uversky V.N., Galzitskaya O.V., Winter S., Löber G. (1999) Effect of hyperphosphorylation on structural properties of tau-protein. Cytology (St. Petersburg). 41, 540-549.
Uversky V.N., Talapatra A., Gillespie J.R., Fink A.L. (1999) Protein deposits as the molecular basis of amyloidosis. Part I. Systemic amyloidoses. Med. Sci. Monitor. 5 (5), 1001-1012.
Uversky V.N., Talapatra A., Gillespie J.R., Fink A.L. (1999) Protein deposits as the molecular basis of amyloidosis. II. Localized amyloidosis and neurodegenerative disordres. Med. Sci. Monitor. 5 (6), 1238-1254.
Segel D.J., Eliezer D., Uversky V.N., Fink A.L., Hodgson K.O., Doniach S. (1999) Transient dimer in the refolding kinetics of cytochrome c characterized by small angle X-ray scattering. Biochemistry. 38 (46), 15352-15359.
Kuznetsova I.M., Biktashev A.G, Khaitlina S.Yu, Vassilenko K.S. Turoverov K.K., Uversky V.N. (1999) Effect of self-association on structural organization of partially-folded proteins: Inactivated actin. Biophys. J. 77, 2788-2800.
Permyakov S.E., Senin I.I., Uversky V.N., Cherskaya A.M., Shulga-Morskoy S.V., Zinchenko D.V., Alekseev A.M., Zargarov A.A., Lipkin V.M., Philippov P.P., Permyakov E.A. (1999) Point amino acid substitutions in the Ca2+-binding sites of recoverin. I. The mechanism of successive filling of the Ca2+-binding sites. Bioorg. Khim. (Moscow). 25 (10), 742-746.
Uversky V.N., Permyakov S.E., Senin I.I., Cherskaya A.M., Shulga-Morskoy S.V., Zinchenko D.V., Alekseev A.M., Zargarov A.A., Lipkin V.M., Philippov P.P., Permyakov E.A. (2000) Point amino acid substitutions in the Ca2+-binding of recoverin: II. The unusual behavior of the protein upon the binding of calcium ions. Bioorg. Khim. (Moscow). 26 (3), 173-178.
Permyakov S.E., Uversky V.N., Cherskaya A.M., Shulga-Morskoy S.V., Zinchenko D.V., Alekseev A.M., Zernyi E.Y., Zargarov A.A., Senin I.I., Lipkin V.M., Philippov P.P., Permyakov E.A. (2000) Point amino acid substitutions in the Ca2+-binding sites of recoverin. III. A mutant with the fourth reconstructed Ca2+-binding site. Bioorg. Khim. (Moscow). 26 (4), 285-289.
Gillespie, J.R., Uversky V.N. (2000) Structure and Function of -Fetoprotein: A biophysical overview. Biochim. Biophys. Acta 1480 (1-2), 41-56.
Uversky V.N., Gillespie J.R., Fink A.L. (2000). Why are “natively unfolded” proteins unstructured under the physiological conditions? Proteins: Structure, Function and Genetics. 42 (3), 415-427.
Tcherkasskaya O., Bychkova V.E., Uversky V.N., Gronenborn A.M. (2000) Multi-state fluorescence in proteins with multiple tryptophan residues: Apomyoglobin natural variants and site directed mutants. J. Biol. Chem. 275 (46), 36285-36194.
Permyakov S.E., Cherskaya A.M., Senin I.I., Zargarov A.A., Shulga-Morskoy S.V., Alekseev A.M., Zinchenko D.V., Lipkin V.M., Philippov P.P., Uversky V.N., Permyakov E.A. (2000) Effects of mutations in the calcium-binding sites of recoverin on its metal-binding properties, structure and stability. Protein Engineering 13 (11), 101-108.
Kuznetsova I.M., Biktashev AG., Malova L.N., Bushmarina N.A., Uversky V.N. Turoverov K.K. (2000) Understanding the contribution of individual tryptophan residues to intrinsic lysozyme fluorescence. Prot. Pept. Lett. 7 (6), 411-420.
Nishimura C., Uversky V.N., Fink A.L. (2001) The effect of salts on the stability and folding of Staphylococcal nuclease. Biochemistry 40 (7) 2113-2128.
Uversky V.N., Li, J., Fink A.L. (2001) Evidence for a partially-folded intermediate in -synuclein fibrillation. J. Biol. Chem. 276 (14), 10737-10744.
Kosarikov D.N., Young P., Uversky V.N., Gerber N.C. (2001) Human soluble guanylate cyclase. Functional expression, purification and structural characterization. Arch. Biochem. Biophys. 388 (2), 185-197.
Nielsen L., Khurana R., Coats A., Vyas S., Frokjaer S., Brange J., Uversky V.N., Fink A.L. (2001) The effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism. Biochemistry 40 (20), 6036-6046.
Abramov V.M., Vasiliev A.M., Vasilenko R.N., Kulikova N.L., Kosarev I.V., Khlebnikov V.S., Ishchenko A.T., MacIntyre S., Khurana R., Gillespie J.R., Korpela T., Fink A.L., Uversky V.N. (2001) Structural and functional similarity between Yersinia pestis capsular protein Caf1 and human interleukin-1. Biochemistry 40 (20), 6076-6084.
Khurana R., Uversky V.N., Nielsen L., Fink A.L. (2001) Is Congo red an amyloid specific dye? J. Biol. Chem. 276 (25), 22715-22721.
Tcherkasskaya O., Uversky V.N. (2001) Denatured collapsed states in protein folding: Example of apomyoglobin. Proteins: Structure Function and Genetics. 44, 244-254.
Uversky V.N., Li, J., Fink A.L. (2001) Pesticides directly accelerate the rate of -synuclein fibril formation: A possible factor in Parkinson’s disease. FEBS Lett. 500 (3), 105-108.
Nielsen L., Frokjaer S., Brange J., Uversky V.N., Fink A.L. (2001) Probing the mechanism of insulin fibril formation with insulin mutants. Biochemistry 40 (28), 8397-8409.
Oberg K.A., Uversky V.N. (2001) Secondary structure of homologous proteins, -fetoprotein and serum albumin, from their circular dichroism and infrared spectra. Prot. Pept. Lett. 8 (4), 297-302.
Li J., Uversky V.N., Fink A.L. (2001) Effect of familial Parkinson’s disease point mutations A30P and A53T on the structural properties, aggregation and fibrillation of human alpha-synuclein. Biochemistry 40 (38), 11604-11613.
Bushmarina N.A., Kuznetsova I.M., Biktashev A.G., Turoverov K.K., Uversky V.N. (2001) Partially folded conformations in the unfolding pathway of bovine carbonic anhydrase B: A fluorescence study. ChemBioChem 2, 813-821.
Uversky V.N., Lee H.-J., Li J., Fink A.L., Lee S.-J. (2001) Stabilization of partially folded conformation during synuclein oligomerization in both purified and cytosolic preparations. J. Biol. Chem. 276 (47), 43495-43498.
Uversky V.N., Li J., Fink A.L. (2001) Metal-triggered structural transformations, aggregation and fibril formation of human -synuclein. A possible molecular link between Parkinson’s disease and heavy metal exposure. J. Biol. Chem. 276 (47), 44284-44296.
Uversky V.N., Li J., Fink A.L. (2001) Trimethylamin-N-oxide-induced folding ofalpha-synuclein. FEBS Lett. 509 (1), 31-35.
Permyakov S.E., Uversky V.N., Veprintsev D.B., Cherskaya A.M., Brooks C.L., Permyakov E.A., Berliner L.J. (2001) Mutating aspartate in the calcium-binding site of -lactalbumin: Effects on the protein stability and cation binding. Protein Engineering 14 (10) 785-789.
Kosarikov D.N., Lee J., Uversky V.N., Gerber N.C. (2001) Role of conformational changes in the activation and inhibition of human soluble guanylate cyclase. J. Inorg. Biochem. 87 (4), 267-276.
Uversky V.N. (2002) What does it mean to be natively unfolded? Review. Eur. J. Biochem. 269 (1), 2-12.
Permyakov S.E., Oberg K.A., Cherskaya A.M., Shavlovsky M.M., Vasiliev V.B., Permyakov E.A., Uversky V.N. (2002) Human -fetoprotein as a Zn2+-binding protein. Tight cation binding is not accompanied by global changes in protein structure and stability. Biochim. Biophys. Acta. 1586 (1), 1-10.
Manning-Bog A.B., McCormack A.L., Li J., Uversky V.N., Fink A.L., Di Monte D.A. (2002) The herbicide paraquate causes upregulation and aggregation of alpha-synuclein in mice. J. Biol. Chem. 277 (3), 1641-1644.
Vassilenko K.S., Uversky V.N. (2002) Circular dichroism spectra of the molten globules. Biochim. Biophys. Acta. 1594 (1), 168-177.
Cohlberg J.A., Li J., Uversky V.N., Fink A.L. (2002) Heparin and other glycosoamino-glycans stimulate the formation of amyloid fibrils from alpha-synuclein in vitro. Biochemistry. 41 (5), 1502-1511.
Uversky V.N. (2002) Natively unfolded proteins: A point where biology waits for physics. Review. Protein Sci. 11 (4), 739-756.
Uversky V.N., Li J., Souillac P.O., Millett I.S., Doniach S., Jakes R., Goedert M., Fink A.L. (2002) Biophysical properties of the synucleins and their propensities to fibrillate: Inhibition of alpha-synuclein assembly by beta- and gamma-synucleins. J. Biol. Chem. 277 (14), 11970-11978.
Uversky V.N. (2002) Cracking the folding code: Why do some proteins adopt partially folded conformation, whereas other don’t? FEBS Lett. 514 (2-3) 181-183.
Uversky V.N., Fink A.L. (2002) The chicken-egg scenario of protein folding revisited. FEBS Lett. 515 (1-3) 79-83.
Uversky V.N., Cooper E.M, Bower, K.S., Li J., Fink A.L. (2002) Accelerated alpha-synuclein fibrillation in crowded milieu. FEBS Lett. 515 (1-3) 99-103.
Uversky V.N., Permyakov S.E., Zagranichny V.E., Rodionov I.L., Fink A.L., Cherskaya A.M., Wasserman L.A., Permyakov E.A. (2002) Effect of zinc and temperature on the conformation of the subunit of retinal phosphodiesterase: A natively unfolded protein. J. Proteome Res. 1 (2), 149-159.
Souillac P.O., Uversky V.N., Millett I.S., Khurana R. Doniach S., Fink A.L. (2002) Effect of association state and conformational stability on the kinetics of immunoglobulin light chain amyloid fibril formation at physiological pH. J. Biol. Chem. 277 (15) 12657-12665.
Souillac P.O., Uversky V.N., Millett I.S., Khurana R. Doniach S., Fink A.L. (2002) Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. Evidence for an off-pathway oligomer at acidic pH. J. Biol. Chem. 277 (15) 12666-12679.
Uversky V.N., Yamin, G., Souillac P., Goers J., Glaser C.B., Fink A.L. (2002) Methionine oxidation inhibits fibrillation of human alpha-synuclein in vitro. FEBS Lett. 517 (1-3), 239-244.
Uversky V.N., Fink A.L. (2002) Minireview. Amino acid sequence determinants of alpha-synuclein aggregation: Putting together pieces of the puzzle. FEBS Lett. 522 (1-3) 9-13.
Parkhomenko T.V., Klicenko O.A., Shavlovski M.M., Kuznetsova I.M., Uversky V.N., Turoverov K.K. (2002) Biophysical characterization of albumin preparations from blood serum of healthy donors and patients with renal diseases. I. Spectrofluorometric analysis. Med. Sci. Monitor. 8 (7) BR261-265.
Parkhomenko T.V., Klicenko O.A., Shavlovski M.M., Poletaev A.I., Kuznetsova I.M., Uversky V.N., Turoverov K.K. (2002) Biophysical characterization of albumin preparations from blood serum of healthy donors and patients with renal diseases. II. Evidence for the enhancement of the haptoglobin level at the pathological conditions. Med. Sci. Monitor. 8 (7) BR266-271.
Abramov V.M., Vasiliev A.M., Khlebnikov V.S., Vasilenko R.N., Kulikova N.L., Kosarev I.V., Ishchenko A.T., Gillespie J.R., Millett I.S., Fink A.L., Uversky V.N. (2002) Structural and functional properties of Yersinia pestis Caf1 capsular antigen and their possible role in fulminant development of primary pneumonic plague. J. Proteome Res. 1 (4) 307-315.
Denning, D.P., Uversky V.N., Patel, S.S., Fink A.L., Rexach, M. (2002) The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein. J. Biol. Chem. 277 (36) 33447-33455.
Uversky V.N., Li J., Bower, K.S., Fink A.L. (2002) Synergistic effects of pesticides and metals on the fibrillation of -synuclein: Implications for Parkinson’s disease. NeuroToxicology. 23 (4-5) 527-536.
Li J., Uversky V.N., Fink A.L. (2002) Conformational behavior of human alpha-synuclein is modulated by familial Parkinson’s disease point mutations A30P and A53T. NeuroToxicology 23 (4-5) 553-567.
Uversky V.N., Nielsen Garriques L., Millett I.S., Frokjaer S., Brange J., Doniach S., Fink A.L. (2003) Prediction of the association state of insulin using spectral parameters. J. Pharm. Sci. 92 (4) 847-858.
Tcherkasskaya O., Davidson E., Uversky V.N. (2003) Biophysical constraints for protein structure predictions. J. Proteome Res. 2 (1) 37-42.
Permyakov S.E., Cherskaya A.M., Wasserman L.A., Khokhlova T.I., Senin I.I., Zargarov A.A., Zinchenko D.V., Zernii E.Yu., Lipkin V.M., Philippov P.P, Uversky V.N., Permyakov E.A. (2003) Recoverin is a zinc-binding protein. J. Proteome Res. 2 (1) 51-57.
Munishkina L.A., Phelan C., Uversky V.N., Fink A.L. (2003) Conformational behavior and aggregation of human alpha-synuclein in organic solvents. Modeling the effect of membranes. Biochemistry 42 (9) 2720-2730.
Denning, D.P., Patel, S.S., Uversky, V.N., Fink, A.L., Rexach, M. (2003) Disorder in the pore. The FG nucleoporins of S. cerevisiae constitute a family of natively unfolded proteins. Proc. Natl. Acad. Sci. U.S.A. 100 (5) 2450-2455.
Goers J., Uversky V.N., Fink A.L. (2003) Polycation-induced oligomerization and accelerated fibrillation of human alpha-synuclein in vitro. Protein Sci. 12 (4) 702-707.
Permyakov E.A., Permyakov S.E., Deikus G.Y., Morozova-Roche L.A., Grishchenko V.M., Kalinichenko L.P., and Uversky V.N. (2003) Ultraviolet illumination-induced reduction of -lactalbumin disulfide bridges. Proteins: Structure, Function and Genetics. 51 (4) 498-503.
Yamin, G., Uversky V.N., Fink A.L. (2003) Nitration inhibits fibrillation of human alpha-synuclein in vitro by formation of soluble oligomers. FEBS Lett. 542 (1-3) 147-152.
Kataeva I.A., Uversky V.N., Ljungdahl L.G. (2003) Contribution of calcium and domain interactions to the conformation and thermal stability of cellobiohydrolase CbhA, a subunit from Clostridium thermocellum cellulosome. Biochem. J. 372 (1) 151-161.
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Tcherkasskaya O., Uversky V.N. (2003) Polymeric aspects of protein folding. Prot. Pept. Lett. 10 (3) 239-245.
Verkhusha V.V., Kuznetsova I.M., Stepanenko O.V., Zaraisky A.G., Shavlovsky M.M., Turoverov K.K., Uversky V.N. (2003) High Stability of Discosoma DsRed as Compared to Aequorea EGFP. Biochemistry 42 (26) 7879-7884.
Souillac P.O., Uversky V.N., Fink A.L. (2003) Structural transformation of oligomeric intermediates in the fibrillation of the immunoglobulin light chain LEN. Biochemistry 42 (26) 8094-8104.
Goers J., Manning-Bog A.B., McCormack A.L., Millett I.S., Doniach S., Di Monte D.A., Uversky V.N., Fink A.L. (2003) Nuclear localization of alpha-synuclein and its interaction with histones. Biochemistry 42 (28) 8465-8471.
Yamin, G., Glaser C., Uversky V.N., Fink A.L. (2003) Certain metals trigger fibrillation of the methionine-oxidazed alpha-synuclein. J. Biol. Chem. 278 (30) 27630–27635.
Uversky V.N. (2003) A protein-chameleon: Conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegenerative disorders. J. Biomol. Struct. Dyn. 21 (2) 211-234.
Georlette D., Damien B., Blaise V., Depiereux E., Uversky V.N., Gerday C., Feller G. (2003) Structural and functional adaptation to extreme temperatures in psychrophilic, mesophilic and thermophilic DNA ligases. J. Biol. Chem. 278 (39) 37015-37023.
Ahmad A., Millett, I.S., Doniach S., Uversky V.N. and Fink A.L. (2003) Partially folded intermediates in insulin fibrillation. Biochemistry 42 (39) 11404-11416.
Uversky V.N. (2003) Protein folding revisited. A polypeptide chain at the folding – misfolding – non-folding crossroads: Which way to go? Cell. Mol. Life Sci. 60 (9) 1852-1871.
Voropay E.S., Samtsov M.P., Kaplevsky K.N., Maskevich A.A., Stepuro V.I., Povarova O.I., Kuznetsova I.M., Tutoverov K.K., Fink A.L., Uversky V.N. (2003) Spectral properties of Thioflavine T and its complexes with amyloid fibrils. Journal of Applied Spectroscopy (Moscow) 70 (6) 765-773.
Voropay E.S., Samtsov M.P., Kaplevsky K.N., Maskevich A.A., Stepuro V.I., Povarova O.I., Kuznetsova I.M., Tutoverov K.K., Fink A.L., Uversky V.N. (2003) Spectral properties of Thioflavine T and its complexes with amyloid fibrils. Journal of Applied Spectroscopy. 70 (6) 868-874.
Permyakov S.E., Millett I.S., Doniach, S., Permyakov E.A., Uversky V.N. (2003) Natively unfolded C-terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin. Proteins Structure, Function and Genetics. 53 (4) 855-862.
Georlette D., Blaise V., Dohmen C., Bouillenne F., Damien B., Depiereux E., Gerday C., Uversky V.N., Feller G. (2003) Cofactor binding modulates the conformational stabilities and unfolding patterns of the thermophilic and mesophilic NAD+-dependent DNA ligases. J. Biol. Chem. 278 (50) 49945-49953.
Georlette D., Blaise V., Bouillenne F., Damien B., Thorbjarnardóttir S.H., Depiereux E., Gerday C., Uversky V.N., Feller G. (2004) Adenylation-dependent conformation and unfolding pathways of the NAD+-dependent DNA ligase from the hyperthermophile Thermus scotoductus. Biophys. J. 86(2) 1089-1104.
Munishkina L.A, Henriques J.J., Uversky V.N., Fink A.L. (2004) The role of protein-water interactions and electrostatics in alpha-synuclein fibril formation. Biochemistry. 43(11) 3289-3300.
Ahmad A., Millett, I.S., Doniach S., Uversky V.N. and Fink A.L. (2004) Stimulation of insulin fibrillation by urea-induced intermediates. J. Biol. Chem. 279(15) 14999-15013.
Hokenson M., Uversky V.N., Goers J., Yamin, G., Fink A.L. (2004) Rrole of individual methionines in the fibrillation of methionine-oxidized alpha-synuclein. Biochemistry. 43(15) 4621-4633.
Uversky V.N., Fink A.L. (2004) Conformational constraints for the amyloid fibrillation: The importance of being unfolded. Biochim. Biophys. Acta. 1698(2) 131-153.
Permyakov S.E., Pershikova I.V., Khokhlova T.I., Uversky V.N., Permyakov E.A. (2004) No need to be HAMLET or BAMLET to interact with histones. Binding of monomeric -lactalbumin to histones and basic poly-amino acids. Biochemistry. 43(19) 5575-5582.
Kuznetsova I.M., Turoverov K.K., Uversky V.N. (2004) The use of the phase diagram method to analyze the protein unfolding-refolding reactions: Fishing out the “invisible” intermediates. J. Proteome Res. 3(3), 485-494.
Munishkina L.A., Cooper E.M., Uversky V.N., Fink A.L. (2004) The effect of macromolecular crowding on protein aggregation and amyloid fibril formation. J. Mol. Recognit. 17 (5) 456-464.
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Uversky V.N. (2004) Neurotoxin-induced animal models of Parkinson’s disease: Understanding the role of rotenone, maneb and paraquate in neurodegeneration. Cell & Tissue Res. 318 (1) 225-241.
Stepanenko O.V., Verkhusha V.V., Kazakov V.I., Shavlovsky M.M., Kuznetsova I.M., Uversky V.N., Turoverov K.K. (2004) Understanding the effect of quaternary structure on conformational stability of fluorescent proteins: Comparative studies on EGFP, mRFP1, HcRed, “dimer2” and DsRed. Biochemistry. 43 (47) 14913-14923.
Li J., Zhu M., Rajamani S., Uversky V.N., Fink A.L. (2004) Rifampicin inhibits alpha-synuclein fibrillation and disaggregates fibrils. Chem. Biol. 11 (11) 1513-1521.
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Vartapetian A.B., Uversky V.N. (2003) Prothymosin alpha: A simple yet mysterious protein. In: Protein Structures: Kaleidoscope of Structural Properties and Functions. (Uversky V.N., Ed.) Research Signpost, Trivandrum, Kerala, India, pp. 223-238.
Kosarikov D.N., Lee J., Uversky V.N., Gerber N.C. (2003) Human soluble guanylate cyclase – Structure and function. In: Protein Structures: Kaleidoscope of Structural Properties and Functions. (Uversky V.N., Ed.) Research Signpost, Trivandrum, Kerala, India, pp. 299-324.
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