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Peer Reviewed Papers, Books, Chapters

Year Title Citation Authors
1. 2011 Regions of intrinsic disorder help identify a novel nuclear localization signal in Toxoplasma gondii histone acetyltransferase TgGCN5-B. Molecular and Biochemical Parasitology. 175 (2) 192-195 PMID: 21055425
2. 2011 Effects of HMGN variants on the cellular transcription profile. Nucleic Acid Research. In press
3. 2011 Toxic assemblies of alpha-synuclein in Parkinson's disease and other synucleinopathies. An Overview of Structure and Function of Oligomeric and Fibrillar Protein Assemblies Involved in Degenerative Diseases (Farid Rahimi and Gal Bitan, Editors), Springer, New York, USA. In press.
4. 2011 Modulating alpha-sinuclein misfolding and fibrillation in vitro by agrochemicals. Research and Reports in Biology. In press.
5. 2011 Flexible nets of malleable guardians: Intrinsically disordered chaperones in neurodegenerative diseases. Chemical Reviews. In press
6. 2011 Multitude of binding modes attainable by intrinsically disordered proteins: A portrait gallery of disorder-based complexes. Chemical Society Reviews. DOI: 10.1039/C0CS00057D In press
7. 2011 Systematic analysis of tropomodulin/tropomyosin interactions uncovers fine-tuned binding spe-cificity of intrinsically disordered proteins. Journal of Molecular Recognition. In press
8. 2011 Characterization of the non-fibrillar alpha-synuclein oligomers. Protein and Peptide Letters. In press
9. 2010 PONDR-FIT: A meta-predictor of intrinsically disordered amino acids. Biochim. Biophys. Acta - Proteins and Proteomics. 1804 (4) 996-1010
10. 2010 Seven lessons from one IDP structural analysis. Structure. 18 (9) 1069-1071. DOI: 10.1016/j.str.2010.08.003. PMID: 20826332
11. 2010 Retro-MoRFs: Identifying protein binding sites by normal and reverse alignment and intrinsic disorder prediction. International Journal of Molecular Sciences. 11 (10), 3725-3747. doi:10.3390/ijms11103725
12. 2010 A bimodal distribution of two distinct categories of intrinsically-disordered structures with separate functions in FG nucleoporins. Molecular and Cellular Proteomics. 9 (10) 2205-2224. PMID: 20214631
13. 2010 Drugs for 'protein clouds': Targeting intrinsically disordered transcription factors. Current Opinion in Pharmacology. 10 (6) 782-788. PMID: 20889377
14. 2010 Viral disorder or disordered viruses: Do viral proteins possess unique features? Protein and Peptide Letters Protein and Peptide Letters. 17 (8) 932-951. PMID: 20100603
15. 2010 Mysterious oligomerization of the amyloidogenic proteins FEBS Journal. 277 (14) 2940-2953. PMID: 20546306
16. 2010 Ca2+/Mg2+ selectivity of solitary helix-loop-helix Ca2+-binding motif: alpha-lactalbumin and Ca2+-binding lysozyme cases Proteins: Structure, Function, and Bioinformatics. 78 (12) 2609-2624. PMID: 20602456
17. 2010 Proteomic identification of Hsc70 as a mediator of RGS9-2 degradation by the in vivo interactome analysis. Molecular and Cellular Proteomics. 9(3), 1510-1521
18. 2010 The N-terminal domain of DELLA proteins belongs to the class of intrinsically unstructured proteins. J. Biol. Chem. 285 (15) 11557-11571
19. 2010 Intrinsically disordered chaperones and neurodegeneration. Protein Chaperones and Protection from Neurodegeneration (Witt S.N., Ed.) In The Wiley Series in Protein and Peptide Science (Uversky V.N. series Ed.), John Wiley & Sons, Inc, Hoboken, New Jersey, USA
20. 2010 Structural disorder and influenza virus virulence Flexible Viruses: Structural Disorder in Viral Proteins (Uversky V.N., Longhi S., Eds.) In The Wiley Series in Protein and Peptide Science (Uversky V.N. series Ed.), John Wiley & Sons, Inc, Hoboken, New Jersey, USA
21. 2010 Structural disorder in neuraminidase and hemagglutinin proteins from influenza A virus Flexible Viruses: Structural Disorder in Viral Proteins (Uversky V.N., Longhi S., Eds.) In The Wiley Series in Protein and Peptide Science (Uversky V.N. series Ed.), John Wiley & Sons, Inc, Hoboken, New Jersey, USA
22. 2010 Structural disorder in matrix proteins from HIV-related viruses. Flexible Viruses: Structural Disorder in Viral Proteins (Uversky V.N., Longhi S., Eds.) In The Wiley Series in Protein and Peptide Science (Uversky V.N. series Ed.), John Wiley & Sons, Inc, Hoboken, New Jersey, USA.
23. 2010 Do viral proteins possess unique features? Flexible Viruses: Structural Disorder in Viral Proteins (Uversky V.N., Longhi S., Eds.) In The Wiley Series in Protein and Peptide Science (Uversky V.N. series Ed.), John Wiley & Sons, Inc, Hoboken, New Jersey, USA
24. 2010 Binding promiscuity of unfolded peptides Folding, Misfolding and Nonfolding of Peptides and Small Proteins (Schweitzer-Stenner R. Ed.) In The Wiley Series in Protein and Peptide Science (Uversky V.N. series Ed.), John Wiley & Sons, Inc, Hoboken, New Jersey, USA
25. 2010 Why are we interested in unfolded peptides and proteins? Folding, Misfolding and Nonfolding of Peptides and Small Proteins (Schweitzer-Stenner R. Ed.) In The Wiley Series in Protein and Peptide Science (Uversky V.N. series Ed.), John Wiley & Sons, Inc, Hoboken, New Jersey, USA
26. 2010 a-Synuclein and Metals Protein folding and metal ions – mechanisms, biology and disease (Gomes C.M., Wittung-Stafshede P., Eds.). Taylor & Francis Group, LLC, Boca Raton, FL, USA. ISBN: 978-1-4398-0964-8. pp
27. 2010 Large-scale identification of intrinsically disordered proteins. Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation (Uversky V.N., Longhi S., Eds.) In The Wiley Series in Protein and Peptide Science (Uversky V.N. series Ed.), John Wiley & Sons, Inc, Hoboken, New Jersey, USA. pp. 671-693
28. 2010 Conformational behavior of intrinsically disordered proteins: Effects of strong denaturants, temperature, pH, counter ions, and macromolecular crowding Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation (Uversky V.N., Longhi S., Eds.) In The Wiley Series in Protein and Peptide Science (Uversky V.N. series Ed.), John Wiley & Sons, Inc, Hoboken, New Jersey, USA. pp. 547-568
29. 2010 Analyzing intrinsically disordered proteins by size-exclusion chromatography Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation (Uversky V.N., Longhi S., Eds.) In The Wiley Series in Protein and Peptide Science (Uversky V.N. series Ed.), John Wiley & Sons, Inc, Hoboken, New Jersey, USA. pp. 525-544
30. 2010 Fluorescence spectroscopy of intrinsically disordered proteins Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation (Uversky V.N., Longhi S., Eds.) In The Wiley Series in Protein and Peptide Science (Uversky V.N. series Ed.), John Wiley & Sons, Inc, Hoboken, New Jersey, USA. pp. 323-344.
31. 2010 Analysis of metabolites in apical area of Allium cepa roots by high resolution NMR spectroscopy Protein and Peptide Letters. 17 (1) 86-91
32. 2010 SPA: Short peptide analyzer on intrinsic disorder status . Genes to Cells. 15 (6) 635-646. PMID: 20497238
33. 2010 Unique physical properties and interactions of the domains of methylated DNA binding protein 2. Biochemistry. 49 (20) 4395-4410. PMID: 20405910
34. 2010 Archaic chaos: Intrinsically disordered proteins in Archaea BMC Systems Biology. 4 (Suppl. 1) S1. doi:10.1186/1752-0509-4-S1-S1
35. 2010 Protein tandem repeats: The more perfect the less structured. FEBS Journal. 277 (12) 2673-2682. PMID: 20491906
36. 2010 Functional dissection of an intrinsically disordered protein: Understanding the roles of different domains of Knr4 protein in protein-protein interactions Protein Science. 19 (7) 1376-1385. PMID: 20506404
37. 2010 Fluorescence quantum yield of thioflavin T in rigid environment when ultrafast intramolecular twisting is restricted. PLoS One. 5 (10) e15385. doi:10.1371/journal.pone.0015385
38. 2010 Targeting intrinsically disordered proteins in neurodegenerative and protein misfoding diseases: Another illustration of the D2 concept Expert Review of Proteomics. 7 (4) 543-564. PMID: 20653509
39. 2010 CCR molecular pathways: Oncogenic partnerships: EWS-FLI1 protein interactions initiate key pathways of Ewing's sarcoma Clinical Cancer Research. 16 (16) 4077-4083. PMID: 20547696
40. 2010 Understanding protein non-folding Biochim. Biophys. Acta - Proteins and Proteomics. 1804 (6) 1231–1264
41. 2010 The mysterious unfoldome: Structureless, underappreciated, yet a vital part of any given proteome Journal of Biomedicine and Biotechnology. Vol. 2010, Article ID 568068, 14 pages. DOI:10.1155/2010/568068. PMID: 20011072
42. 2010 Metalloproteomics and metal toxicology of a-synuclein Metallomics. 2, 378–392. DOI: 10.1039/b926659c.
43. 2010 Protein kingdom extended: Ordered and intrinsically disordered proteins, their folding, non-folding, supramolecular complex formation and aggregation Progress in Biophysics & Molecular Biology. 102 (2-3) 73-84. PMID: 20097220
44. 2010 Characterization of intrinsically disordered proteins with electrospray ionization mass spectrometry: conformational heterogeneity of a-synuclein Proteins: Structure, Function, and Bioinformatics. 78 (3) 714-722.
45. 2010 3, 4-Dihydroxyphenylacetic acid (DOPAC) impairs interaction of a-synuclein’s with lipids The Open Proteomics Journal. 3, 1-7
46. 2010 Effects of various flavonoids on the fibrillation of a-synuclein. Parkinson’s Disease. Volume 2010, Article ID 650794, 16 pages DOI: 10.4061/2010/650794.
47. 2010 Methionine oxidation stabilizes non-toxic oligomers of a-synuclein through strengthening the auto-inhibitory intra-molecular long-range interactions. Biochim. Biophys. Acta – Molecular Basis of Diseases. 1802 (3) 322–330.
48. 2010 Calbindin-D28K acts as a calcium-dependent chaperone suppressing α-synuclein fibrillation in vitro Central European Journal of Biology. 15 (1) 11-20.
49. 2009 Exploring the molecular design of protein interaction sites with molecular dynamics simulations and free energy calculations Biochemistry. 48 (2), 399-414.
50. 2009 Smoking and Parkinson’s disease: Does nicotine affect a-synuclein fibrillation? Biochim. Biophys. Acta - Proteins and Proteomics. 1794 (2), 282–290.
51. 2009 Intrinsically disordered proteins and their binding functions. Computational Protein-Protein Interactions (Nussinov R. and Schreiber G., Editors). Taylor & Francis Group, LLC, Boca Raton, FL, USA. pp.223-252
52. 2009 Intrinsically disordered proteins and their environment: Effects of strong denaturants, temperature, ph, counter ions, membranes, binding partners, osmolytes, and macromolecular crowding The Protein Journal. 28 (7-8) 305-325
53. 2009 Biophysics of Parkinson’s disease: Structure and aggregation of a-synuclein Current Protein and Peptide Science. 10 (5) 483-499
54. 2009 Mechanisms and consequences of protein aggregation: The role of folding intermediates. Current Protein and Peptide Science. 10 (5) 456-463
55. 2009 Acid denaturation and anion-induced folding of globular proteins: Multitude of equilibium partially folded intermediates Current Protein and Peptide Science. 10 (5) 447-455.
56. 2009 Cryoenzymology: Enzyme action in slow motion Current Protein and Peptide Science. 10 (5) 408-415.
57. 2009 Anthony L. Fink (1943-2008): Scientist, Teacher and Artist Current Protein and Peptide Science. 10 (5) 395-396
58. 2009 Predicting intrinsic disorder in proteins: An overview. Cell Research. 19 (8), 929-949
59. 2009 Unfoldomics of human diseases: Linking protein intrinsic disorder with diseases Genomics. 10 (Suppl. 1), S7.
60. 2009 Intrinsic disorder in proteins associated with neurodegenerative diseases Frontiers in Bioscience. 14 (14), 5188-5238
61. 2009 Neuropathology and neurochemistry of Parkinson’s disease: The never-ending story or the story with no beginning? Minerva Psichiatrica. 50 (1), 1-26
62. 2009 Close encounters of the third kind: Disordered domains and the interactions of proteins. BioEssays. 31 (3), 328-335
63. 2009 Native globular and native partially or completely disordered proteins. Folding, supramolecular complex formation and aggregation Cytology (St. Petersburg). 51 (3), 190-203
64. 2009 Analysis of structured and intrinsically disordered regions of integral transmembrane proteins Molecular Biosystems. 5 (12) 1688
65. 2009 Unfoldomics of human genetic diseases: Illustrative examples of ordered and intrinsically disordered members of human diseasome Protein and Peptide Letters. 16 (12) 1533-1547
66. 2009 Solution structure and dynamics of the chimeric SH3 domains, SHH- and SHA-“Bergeracs”. Biochim. Biophys. Acta - Proteins and Proteomics. 1794, 1813-1822
67. 2009 Metal-controlled interdomain cooperativity in parvalbumins Cell Calcium. 46 (3), 163-175
68. 2009 Influence of sequence changes and environment on intrinsically disordered proteins PLoS Computational Biology. 5 (9), e1000497
69. 2009 Molecular mechanisms underlying the flavanoid-induced inhibition of a-synuclein fibrillation. Biochemistry. 48 (34), 8206-8224
70. 2009 Protein disorder in the human diseasome: Unfoldomics of human genetic diseases BMC Genomics. 10 (Suppl.1), S12
71. 2009 Order propensity of an intrinsically disordered protein, the cyclin-dependent-kinase inhibitor Sic1. Proteins: Structure, Function, and Bioinformatics. 76 (3), 731-746
72. 2009 Protein intrinsic disorder and influenza virulence: The 1918 H1N1 and H5N1 viruses Journal of Virology. 6, 69
73. 2009 Accelerated fibrillation of human a-synuclein induced by the combined action of macromolecular crowding and factors inducing partial folding Current Alzheimer Research. 6 (3) 252-260
74. 2009 CDF it all: Consensus prediction of intrinsically disordered proteins based on various cumulative distribution functions FEBS Letters. 583 (6) 1469-1474
75. 2009 At low concentrations, 3,4-Dihydroxyphenylacetic acid (DOPAC) binds non-covalently to a-synuclein and prevents its fibrillation . J. Mol. Biol. 388 (3) 597-610.
76. 2009 Intrinsic disorder in viral proteins genome-linked: Experimental and predictive analyses Virology Journal. 6, 23
77. 2009 The biophysical uniqueness of viral proteins Trends in Biochemical Sciences. 34(2), 53-59.
78. 2008 The unfoldomics decade: An update on intrinsically disordered proteins BMC Genomics. 9 (Suppl. 2), S1
79. 2008 Intrinsic disorder in signaling scaffold proteins: Getting more from less. Progress in Biophysics & Molecular Biology. 98 (1), 85-106
80. 2008 Fluorescent proteins as biomarkers and biosensors: Throwing color lights on molecular and cellular processes Current Protein and Peptide Science. 9 (4), 338-369
81. 2008 Amyloidogenesis of natively unfolded proteins Current Alzheimer Research. 5 (3), 260-287.
82. 2008 Signal transduction via unstructured protein conduits Nature Chemical Biology. 4 (4) 229-230
83. 2008 Intrinsically disordered proteins in human diseases: Introducing the D2 concept Ann. Rev. Biophys. Mol. Biol. 37: 215-246
84. 2008 Flexible nets: Disorder and induced fit in the associations of p53 and 14-3-3 with their partners BMC Genomics. 9 (Suppl. 1), S1.
85. 2008 Intrinsically disordered human C/EBP homologous protein regulates biological activity of colon cancer cells during calcium stress J. Mol. Biol. 380 (2) 313-326
86. 2008 Apo-parvalbumin as an intrinsically disordered protein POTEINS Structure, Function, and Bioinformatics. 72 (3) 822-836
87. 2008 Potato virus A genome-linked protein VPg is an intrinsically disordered molten globule-like protein with a hydrophobic core. Virology. 377 (2) 280-288
88. 2008 Hen egg white lysozyme fibrillation: A deep UV resonance Raman spectroscopic study. Journal of Biophotonics. 1 (3) 215-229
89. 2008 Protein intrinsic disorder toolbox for comparative analysis of viral proteins. BMC Genomics. 9 (Suppl. 2), S4.
90. 2008 Short Linear Motifs recognized by SH2, SH3 and S/T Kinase domains are conserved in disordered protein regions BMC Genomics. In press
91. 2008 The Saccharomyces cerevisiae Knr4p is an intrinsically disordered protein, whose N-terminal tail is essential in the absence of a functional Pkc1p-Slt2p pathway Yeeast. 25 (8) 563-676
92. 2008 The effect of membranes on the in vitro fibrillation of an amyloidogenic light chain variable domain SMA J. Mol. Biol. 381 (4), 989-999
93. 2008 Effect of methionine oxidation on structural properties, conformational stability and aggregation of immunoglobulin light chain LEN Biochemistry. 47 (33), 8665-8677.
94. 2008 Guiding protein aggregation with macromolecular crowding Biochemistry. 47 (34), 8993-9006
95. 2008 Phase diagram method for analysis of protein folding Protein Structures: Methods in Protein Structure Analysis (Uversky V.N., Permyakov E.A., Eds.) Nova Science Publishers, Inc., Hauppauge, NY, USA. Pp. 257-318.
96. 2008 Natively unfolded proteins Unfolded Proteins: From Denatured to Intrinsically Disordered. (Creamer T.P., Ed.) In series “Scientific Revolutions” (Uversky V.N. series Ed.). Nova Science Publishers, Inc., Hauppauge, NY, USA. Pp. 237-294
97. 2008 Intrinsic disorder in proteins associated with neurodegenerative diseases Protein Folding and Misfolding: Neurodegenerative Diseases (Ovádi J., Orosz F., Eds) Springer, New York, USA. pp. 21-75
98. 2008 Structural characteristics of the a-synuclein oligomers stabilized by the flavonoid baicalein. J. Mol. Biol. 383 (1), 214-223
99. 2008 Understanding the role of Arg96 in structure and stability of green fluorescent protein PROTEINS Structure, Function, and Bioinformatics. 73 (3), 539-551
100. 2008 TOP-IDP-Scale: A new amino acid scale measuring propensity for intrinsic disorder. Protein and Peptide Letters. 15 (9), 956-963
101. 2008 A comparative analysis of viral matrix proteins using disorder predictors Virology Journal. 5, 126
102. 2008 Concert action of metals and macromolecular crowding on the fibrillation of a-synuclein. Protein and Peptide Letters. 15 (10), 1079-1085
103. 2008 Thioflavin T as a molecular rotor. Fluorescent properties of thioflavin T in solvents with different viscosity J. Phys. Chem. B. 112 (49), 15893-15902
104. 2008 Malleable machines in transcription regulation: The mediator complex PLoS Comp. Biol. 4 (12), e1000243
105. 2008 Function and structure of inherently disordered proteins. Current Opinion in Structural Biology. 18 (6), 756-764
106. 2008 Malleable machines take shape in transcription regulation. Nature Chemical Biology. 4 (12) 728-737
107. 2008 Protein folding, misfolding and aggregation: Classical themes and novel approaches. Edited by Victor Muñoz. ChemBioChem. 9 (16), 2750-2751
108. 2008 a-Synuclein misfolding and neurodegenerative diseases Current Protein and Peptide Science. 9 (5), 507-540
109. 2008 Flexible nets: Disorder and induced fit in the associations of p53 and 14-3-3 with their partners BMC Genomics. 9 (S1): S1
110. 2008 Comparative analysis of pathogenic and non-pathogenic apicomplexans. Molecular Biosystems. 4 (3), 328 - 340
111. 2008 Dynamics of oligomer formation by denatured carbonic anhydrase II. Biochim. Biophys. Acta. 1784 (5), 834-842
112. 2008 Assessing conservation of disordered regions in proteins The Open Proteomics Journal. 1 (1), 46-53
113. 2008 Protein disorder is positively correlated with gene expression in E. coli. Journal of Proteome Research. 7 (6), 2234–2245.
114. 2008 Prevalence of intrinsic disorder in the intracellular region of human single-pass type I proteins: The case of the Notch ligand Delta-4. Journal of Proteome Research. 7 (6), 2496–2506
115. 2007 Nanoimaging, protein misfolding and conformational diseases Nanomedicine. 2 (5) 615-643
116. 2007 Neuropathology, biochemistry, and biophysics of a-synuclein aggregation Journal of Neurochemistry. 103 (1) 17-37
117. 2007 Intrinsic disorder and functional proteomics. Biophysical Journal. 92 (5) 1439-1456
118. 2007 a-Synuclein aggregation and Parkinson’s disease Protein Misfolding, Aggregation and Conformational Diseases. Vol. II: Molecular Mechanisms of Conformational Diseases (Uversky V.N., Fink A.L., Eds.) Kluwer Academic/Plenum Publishers, New York, USA. pp. 61-110
119. 2007 Understanding protein non-folding To fold or not to fold: Some current concepts of protein chemistry (Zbilut J., Scheibel T., Eds) Nova Science Publishers, Inc., Hauppauge, NY, USA. pp. 55-92
120. 2007 Multiparametric approach in analysis of protein structure and unfolding-refolding reaction. Protein Structures: Methods in Protein Structure Analysis (Uversky V.N., Permyakov E.A., Eds.) Nova Science Publishers, Inc., Hauppauge, NY, USA. pp. 3-52
121. 2007 Size exclusion chromatography in protein structure analysis Protein Structures: Methods in Protein Structure Analysis (Uversky V.N., Permyakov E.A., Eds.) Nova Science Publishers, Inc., Hauppauge, NY, USA. pp. 261-280
122. 2007 Intrinsically disordered proteins: An update. Proceedings of the IEEE 7th International Symposium on Bioinformatics and Bioengineering (Boston, October 14-17, 2008). (Yang, J.Y., Yang M.Q., Zhu M.M., Zhang Y., Arabnia H.R., Deng Y., Bourbakis N., Eds.). The Institute of Electrical and Electronic Engineers, Inc., Piscataway. NJ, Vol. 1, pp. 49-58
123. 2007 Expression and localization of RGS9-2/G 5/R7BP complex in vivo is set by dynamic control of its constitutive degradation by cellular cysteine proteases Journal of Neuroscience. 27 (51) 14117-14127
124. 2007 ThT as an instrument for testing and investigation of amyloid and amyloid-like fibrils Proceedings of the International Conference on Lasers, Applications, and Technologies 2007: Environmental Monitoring and Ecological Applications; Optical Sensors in Biological, Chemical, and Engineering Technologies; and Femtosecond Laser Pulse Filamentation (Minsk, Belarus, June 15, 2007), (Matvienko G., Ivanov A., Nikitin P., Voropay E., Khodasevich M., Panchenko V., Golubev V., Eds.), Proc. SPIE Int. Soc. Opt. Eng. 2007. 6733 (1): 67331R
125. 2007 Protein Misfolding, Aggregation and Conformational Diseases: II. Molecular Mechanisms of Conformational Diseases Springer, New York, USA. (2007). (ISBN-10: 0-387-36529-X; ISBN-13: 978-0-387-36529-9; e-ISBN-10: 0-387-36534-6; e-ISBN-13: 978-0-387-36534-3).
126. 2007 Intrinsic disorder in the Protein Data Bank. J. Biomol. Struct. Dyn. 24 (4) 303-428
127. 2007 Analysis of folded, partially folded and misfolded proteins with fluorescent dyes. Protein Structures: Methods in Protein Structure Analysis (Uversky V.N., Permyakov E.A., Eds.) Nova Science Publishers, Inc., Hauppauge, NY, USA. pp. 73-104
128. 2007 Prediction of intrinsic disorder and its use in functional proteomics. Methods in Molecular Biology: Gene Function Analysis (editor: Michael F. Ochs), Humana Press, Totowa, NJ, USA. pp. 69-92
129. 2007 Attachment of LcrV from Yersinia pestis at dual binding sites to human TLR-2 and hman IFN-receptor Journal of Proteome Research. 6 (6) 2222-2231
130. 2007 Characterization of molecular recognition features, MoRFs, and MoRF-binding proteins. Journal of Proteome Research. 6 (6) 2351-2366.
131. 2007 Composition Profiler: A tool for discovery and visualization of amino acid composition properties. BMC Bioinformatics. 8 211.
132. 2007 Mining α-helix-forming molecular recognition features α-MoRFs with cross species sequence alignments. Biochemistry. 46 (47) 13468-13477
133. 2007 A computational investigation of allostery in the catabolite activator protein resulted in a new mechanism for transcription activation J. Am. Chem. Soc. 129 (50) 15668-15676.
134. 2007 Intrinsic disorder in protein-protein interaction networks: Case studies of complexes involving p53 and 14-3-3. Proceedings of the 2007 International Conference on Bioinformatics and Computational Biology. (Arabnia H.R., Yang M.Q., Yang, J.Y., Eds.), WORLDCOMP’2007 (June 25-28, 2007, Las Vegas Nevada, USA), CSREA Press, USA, Vol.2, pp. 553-564
135. 2007 Recoverin as a redox-sensitive protein. Journal of Proteome Research. 6 (5) 1855-1863.
136. 2007 Multiple aromatic side chains within a highly disordered structure confer activity to the transcriptional activation domain of the EWS oncoprotein. Proc. Natl. Acad. Sci. USA. 104 (2) 479-484
137. 2007 DisProt: The Database of Disordered Proteins Nucleic Acid Research. 35 (Database issue) D786-D793.
138. 2007 g-Synuclein-gamma targeting peptide inhibitor which enhances sensitivity of breast cancer cells to anti-microtubule drugs Cancer Research. 67 (2) 626-633.
139. 2006 Assessing protein disorder and induced folding POTEINS Structure, Function, and Bioinformatics. 62 (1) 24-45
140. 2006 Protein Misfolding, Aggregation and Conformational Diseases: I. Protein Aggregation and Conformational Disorders Springer, New York, USA. (2006). (ISBN-10: 0-387-25918-X; ISBN-13: 978-0387-25918-5)
141. 2006 Folding and misfolding of a-synuclein Molecular Mechanisms in Parkinson's Disease (Kahle P. and Haass C, Eds.). Landes Bioscience, Georgetown, USA. In press
142. 2006 New views of protein structure: Applications to the caseins. Protein structure and functionality. Macromolecules (Fishman, M., Qi, P.X., Eds.) American Chemical Society Publishers: Washington, DC. pp. 52-70
143. 2006 New views of protein structure: Implications for potential new protein structure-function relationships. Protein structure and functionality Macromolecules (Fishman M., Qi P.X., Eds.) American Chemical Society Publishers: Washington, DC. pp.1-18.
144. 2006 Structural and conformational prerequisites of amyloidogenesis. Protein Misfolding, Aggregation and Conformational Diseases. Vol. I: Protein Aggregation and Conformational Diseases (Uversky V.N., Fink A.L., Eds.) Kluwer Academic/Plenum Publishers, New York, USA, pp 1-20.
145. 2006 Nanotools for megaproblems: Probing protein misfolding diseases using nanomedicine modus operandi Journal of Proteome Research. 5 (10) 2505-2522
146. 2006 Nanoimaging applications for protein misfolding and related diseases Journal of Cellular Biochemistry. 99 (1) 52-70
147. 2006 Rational drug design via intrinsically disordered protein Trends in Biotechnology. 24 (10) 435-442
148. 2006 Functional anthology of intrinsic disorder. III. Ligands, postranslational modifications and diseases associated with intrinsically disordered proteins. Journal of Proteome Research. 6 (5) 1917-1932
149. 2006 Functional anthology of intrinsic disorder. II. Cellular components, domains, technical terms, developmental processes and coding sequence diversities correlated with long disordered regions. Journal of Proteome Research. 6 (5) 1899-1916.
150. 2006 Functional anthology of intrinsic disorder. I. Biological processes and functions of proteins with long disordered regions. Journal of Proteome Research. 6 (5) 1882-1898.
151. 2006 Spectral properties of thioflavin T in solvents with different dielectric properties and in a fibril-incorporated form J. Proteome Research. 6 (4) 1392-1401
152. 2006 The disordered amino-terminus of SIMPL interacts with members of the 70 kDa heat shock protein family. DNA and Cell Biology. 25 (12) 704-714
153. 2006 Lipid-binding activity of natively unfolded cytoplasmic domains of multichain immune recognition receptor signaling subunits. Biochemistry
154. 2006 Conformational properties of the SDS-bound state of a-synuclein probed by limited proteolysis: Unexpected rigidity of the acidic C-terminal tail. Biochemistry. 45 (38) 11523-11531
155. 2006 Analysis of molecular recognition features (MoRFs). J. Mol. Biol. 362 (5) 1043-1059
156. 2006 Abundance of intrinsic disorder in proteins associated with cardiovascular disease Biochemistry. 45(35) 10448-10460
157. 2006 Protein intrinsic disorder and human papillomaviruses: Increased amount of disorder in E6 and E7 oncoproteins from high risk HPVs Journal of Proteome Research. 5 (8) 1829-1842.
158. 2006 Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes PLoS Computational Biology. 2 (8) e100 (0001-0012)
159. 2006 Local flexibility in molecular function paradigm. Molecular and Cellular Proteomics. 5 (7) 1212-1223
160. 2006 Role of lysine versus arginine in enzyme cold-adaptation: Modifying lysine to homo-arginine stabilizes the cold-adapted a-amylase from Pseudoalteramonas haloplanktis. POTEINS Structure, Function, and Bioinformatics. 64 (2) 486-501
161. 2006 Intrinsic disorder in transcription factors. Biochemistry. 45 (22) 6773-6888
162. 2006 Functional profiling by alternative splicing and intrinsic protein disorder. Proc. Natl. Acad. Sci. USA. 103 (22) 8390-8395
163. 2006 Conservation of intrinsic disorder in protein domains and families: II. Functions of conserved disorder. Journal of Proteome Research. 5 (4) 888-898
164. 2006 Conservation of intrinsic disorder in protein domains and families: I. A database of conserved predicted disordered regions Journal of Proteome Research. 5 (4) 879-887.
165. 2006 Calmodulin regulation: Prediction and analysis of a disorder-dependent signaling mechanism. POTEINS Structure, Function, and Bioinformatics. 63 (2) 398-410
166. 2006 The role of quarternary structure in fluorescent protein stability Cytology (St. Petersburg). 47 (11) 1017-1027.
167. 2006 Early events in the fibrillation of monomeric insulin J. Biol. Chem. 280 (52) 42669-42675
168. 2005 Agrin modulates a-synuclein fibrillation and localizes to Lewy bodies in Parkinson’s disease brain Glycobiology. 15 (12) 1320-1331.
169. 2005 Protein interactions, aggregation and misfolding via AFM analyses. J. Mol. Biol. 354 (5) 1028-1042.
170. 2005 Improving solubility of Shewanella oneidensis MR-1 and Clostridium thermocellum JW-20 proteins expressed in Esherichia coli Journal of Proteome Research. 4 (6) 1942-1951
171. 2005 Comparing and combining predictors of mostly disordered proteins. Biochemistry. 44 (6) 1989-2000
172. 2005 Nitrated human a-synuclein: Structure and aggregation Mol. Brain Res. 134 (1) 84-102.
173. 2005 Conversion of human a-lactalbumin to an apo-like state in the complexes with basic poly-amino acids: towards understanding of the molecular mechanism of antitumor action of HAMLET J. Proteome Res. 4 (2) 564-569.
174. 2005 Flexible nets: The roles of intrinsic disorder in protein interaction networks. FEBS Journal. 272 (20) 5129-5148
175. 2005 Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling J. Mol. Recognit. 18 (5) 343-384
176. 2005 A GLYmmer of insight intro fibril formation Structure. 13 (8) 1090-1092
177. 2005 Structure-related statistical singularities along protein sequences: A correlation study. Journal of Chemical Information and Modeling. 45 (1) 183-189
178. 2005 Methionine oxidation, a-synuclein, and Parkinson’s disease Biochim. Biophys. Acta. 1703 (2) 157-169
179. 2005 Natively disordered proteins Protein Folding Handbook (Buchner J., Kiefhaber T, Eds.) Wiley-VCH, Verlag GmbH & Co. KGaA, Weinheim, Germany. pp.271-353
180. 2005 Pathways to amyloid fibril formation: Partially folded intermediates in fibrillation of unfolded proteins. Amyloid Proteins: The Beta Pleated Sheet Conformation and Disease (Sipe J.D., ed.) Wiley-VCH, Verlag GmbH & Co. KGaA, Weinheim, Germany. Pp. 247-265
181. 2005 Protein dissection enhances the amyloidogenic properties of a-lactalbumin. FEBS Journal. 272 (9) 2176-2188
182. 2005 Forcing the non-amyloidogenic b-synuclein to fibrillate Biochemistry. 44 (25) 9096-9107
183. 2005 Deep UV Raman spectroscopy is a powerful method for characterizing protein conformations at all stages of fibrillation process Biopolymers. 79 (1) 58-61
184. 2005 Domain coupling in a multimodular cellobiohydrolase CbhA from Clostridium thermocellum FEBS Letters. 579 (20) 4367-4373
185. 2005 How to "improve" nature: Study of electrostatic properties of the surface of a-lactalbumin. Protein Engineering, Design and Selection. 18 (9) 425-433
186. 2005 Coupled folding and binding with a-helix-forming molecular recognition elements. Biochemistry. 44 (37) 12454 - 12470
187. 2005 Uncovering the unfoldome: Enriching cell extracts for unstructured proteins by acid treatment. Journal of Proteome Research. 4 (5) 1610-1618
188. 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.
189. 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
190. 2004 Interactions between immunoglobulin-like and catalytic modules of Clostridium thermocellum cellulosomal CbhA affect fold and stability Biotechnology of Lignocellulose Degradation and Biomass Utilization. Proceedings of Mie Bioforum 2003, Ise-Shima, Japan, p. 199-205
191. 2004 Charge and hydrophobicity patterning along the sequence predicts the folding mechanism and aggregation of proteins: A computational approach J. Proteome Res. 3 (6) 1243-1253
192. 2004 Interactions between immunoglobulin-like and catalytic modules in Clostridium thermocellum cellulosomal cellobiohydrolase CbhA Protein Engineering, Design, and Selection. 17 (11) 759-769
193. 2004 Rifampicin inhibits a-synuclein fibrillation and disaggregates fibrils. Chem. Biol. 11 (11) 1513-1521
194. 2004 Conformational prerequisites for formation of amyloid fibrils from histones. J. Mol. Biol. 342 (4) 1305-1324
195. 2004 The effect of macromolecular crowding on protein aggregation and amyloid fibril formation. J. Mol. Recognit. 17 (5) 456-464
196. 2004 No need to be HAMLET or BAMLET to interact with histones. Binding of monomeric a-lactalbumin to histones and basic poly-amino acids. Biochemistry. 43(19) 5575-5582
197. 2004 Rrole of individual methionines in the fibrillation of methionine-oxidized a-synuclein. Biochemistry. 43(15) 4621-4633
198. 2004 Stimulation of insulin fibrillation by urea-induced intermediates. J. Biol. Chem. 279(15) 14999-15013.
199. 2004 Conformational constraints for the amyloid fibrillation: The importance of being unfolded Biochim. Biophys. Acta. 1698(2) 131-153
200. 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
201. 2004 The role of protein-water interactions and electrostatics in a-synuclein fibril formation Biochemistry. 43(11) 3289-3300
202. 2004 An analysis of environmental factors modulating fibrillation of a small neuroprotein a-synuclein. J. Undergrad. Chem. Res. 3(1) 21-25.
203. 2004 Adenylation-dependent conformation and unfolding pathways of the NAD+-dependent DNA ligase from the hyperthermophile Thermus scotoductus Biophys. J. 86(2) 1089-1104
204. 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
205. 2003 Polymeric aspects of protein folding Prot. Pept. Lett. 10 (3) 239-245
206. 2003 A protein-chameleon: Conformational plasticity of a-synuclein, a disordered protein involved in neurodegenerative disorders J. Biomol. Struct. Dyn. 21 (2) 211-234
207. 2003 Protein Structures: Kaleidoscope of Structural Properties and Functions Research Signpost, Trivandrum, Kerala, India (2003). (ISBN: 81-7736-177-5).
208. 2003 Structural base of the polyfunctional role of Caf1 protein in providing Yersinia pestis circulation in ecological systems of natural plague foci. Protein Structures: Kaleidoscope of Structural Properties and Functions. (Uversky V.N., Ed.). Research Signpost, Trivandrum, Kerala, India, pp. 373-404
209. 2003 Human soluble guanylate cyclase – Structure and function. Protein Structures: Kaleidoscope of Structural Properties and Functions. (Uversky V.N., Ed.) Research Signpost, Trivandrum, Kerala, India, pp. 299-324
210. 2003 Prothymosin a: A simple yet mysterious protein Protein Structures: Kaleidoscope of Structural Properties and Functions. (Uversky V.N., Ed.) Research Signpost, Trivandrum, Kerala, India, pp. 223-238
211. 2003 A rigidifying union: The role of ligands in protein structure and stability Recent Research Developments in Biophysics & Biochemistry (Pandalai S.G., Ed.). Transworld Research Network, Kerala, India, vol. 3, pp. 711-745
212. 2003 Certain metals trigger fibrillation of the methionine-oxidazed a-synuclein J. Biol. Chem. 278 (30) 27630–27635.
213. 2003 Partially folded intermediates in insulin fibrillation Biochemistry 42 (39) 11404-11416
214. 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
215. 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
216. 2003 Structural and functional adaptation to extreme temperatures in psychrophilic, mesophilic and thermophilic DNA ligases J. Biol. Chem. 278 (39) 37015-37023
217. 2003 Spectral properties of Thioflavine T and its complexes with amyloid fibrils. Journal of Applied Spectroscopy (Moscow) 70 (6) 765-773.
218. 2003 Ultraviolet illumination-induced reduction of a-lactalbumin disulfide bridges Proteins: Structure, Function and Genetics. 51 (4) 498-503.
219. 2003 Nitration inhibits fibrillation of human a-synuclein in vitro by formation of soluble oligomers FEBS Lett. 542 (1-3) 147-152
220. 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
221. 2003 Structural and functional properties of IL‑4d2, an alternative splice variant of human IL‑4. J. Proteome Res. 2 (3) 273-281.
222. 2003 High Stability of Discosoma DsRed as Compared to Aequorea EGFP Biochemistry. 42 (26) 7879-7884
223. 2003 Structural reorganization leading to the transformation of LEN off-pathway soluble oligomers into fibril-prone specie Biochemistry. 42 (26) 8094-8104
224. 2003 Nuclear localization of a-synuclein and its interaction with histones Biochemistry. 42 (28) 8465-8471
225. 2003 Polycation-induced oligomerization and accelerated fibrillation of human a-synuclein in vitro. Protein Sci. 12 (4) 702-707.
226. 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
227. 2003 Conformational behavior and aggregation of human a-synuclein in organic solvents. Modeling the effect of membranes Biochemistry 42 (9) 2720-2730
228. 2003 Recoverin is a zinc-binding protein J. Proteome Res. 2 (1) 51-57.
229. 2003 Biophysical constraints for protein structure predictions. Tcherkasskaya O., Davidson E., Uversky V.N
230. 2003 Prediction of the association state of insulin using spectral parameters. J. Pharm. Sci. 92 (4) 847-858
231. 2002 Biophysical properties of human a-synuclein and its role in Parkinson’s disease Recent Research Developments in Proteins (Pandalai, S.G., Ed.). Transworld Research Network, Kerala, India, vol. 1, pp. 153-186
232. 2002 Capture of intermediates in protein unfolding-refolding reactions by the fluorescence diagram method Recent Research Developments in Biophysics (Pandalai S.G., Ed.). Transworld Research Network, Kerala, India, vol. 1, pp. 101-119
233. 2002 Conformational behavior of human a-synuclein is modulated by familial Parkinson’s disease point mutations A30P and A53T NeuroToxicology 23 (4-5) 553-567
234. 2002 Synergistic effects of pesticides and metals on the fibrillation of a-synuclein: Implications for Parkinson’s disease NeuroToxicology. 23 (4-5) 527-536
235. 2002 Conformational prerequisites for the a-lactabumin fibrillation Biochemistry 41 (41) 12546-12551
236. 2002 The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein. J. Biol. Chem. 277 (36) 33447-33455
237. 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
238. 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
239. 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
240. 2002 Unraveling multistate unfolding of rabbit muscle creatine kinase. Biochim. Biophys. Acta. 1596 (1), 129-146
241. 2002 Methionine oxidation inhibits fibrillation of human a-synuclein in vitro FEBS Lett. 517 (1-3), 239-244.
242. 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
243. 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
244. 2002 Effect of zinc and temperature on the conformation of the g subunit of retinal phosphodiesterase: A natively unfolded protein. J. Proteome Res. 1 (2), 149-159.
245. 2002 Accelerated a-synuclein fibrillation in crowded milieu. FEBS Lett. 515 (1-3) 99-103
246. 2002 The chicken-egg scenario of protein folding revisited FEBS Lett. 515 (1-3) 79-83.
247. 2002 Cracking the folding code: Why do some proteins adopt partially folded conformation, whereas other don’t? FEBS Lett. 514 (2-3) 181-183
248. 2002 Biophysical properties of the synucleins and their propensities to fibrillate: Inhibition of a-synuclein assembly by b- and g-synucleins. J. Biol. Chem. 277 (14), 11970-11978
249. 2002 Heparin and other glycosoamino-glycans stimulate the formation of amyloid fibrils from a-synuclein in vitro Biochemistry. 41 (5), 1502-1511.
250. 2002 Circular dichroism spectra of the molten globules. Biochim. Biophys. Acta. 1594 (1), 168-177.
251. 2002 The herbicide paraquate causes upregulation and aggregation of a-synuclein in mice. J. Biol. Chem. 277 (3), 1641-1644
252. 2002 Human a-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.
253. 2002 What does it mean to be natively unfolded? Review. Eur. J. Biochem. 269 (1), 2-12
254. 2002 Natively unfolded proteins: A point where biology waits for physics Protein Sci. 11 (4), 739-756
255. 2002 Minireview. Amino acid sequence determinants of a-synuclein aggregation: Putting together pieces of the puzzle FEBS Lett. 522 (1-3) 9-13
256. 2001 Human soluble guanylate cyclase. Functional expression, purification and structural characterization Arch. Biochem. Biophys. 388 (2), 185-197
257. 2001 effect of salts on the stability and folding of Staphylococcal nuclease Biochemistry 40 (7) 2113-2128
258. 2001 Secondary structure of homologous proteins, a-fetoprotein and serum albumin, from their circular dichroism and infrared spectra Prot. Pept. Lett. 8 (4), 297-302.
259. 2001 Probing the mechanism of insulin fibril formation with insulin mutants Biochemistry 40 (28), 8397-8409.
260. 2001 Pesticides directly accelerate the rate of a-synuclein fibril formation: A possible factor in Parkinson’s disease. FEBS Lett. 500 (3), 105-108
261. 2001 Denatured collapsed states in protein folding: Example of apomyoglobin Proteins: Structure Function and Genetics. 44, 244-254
262. 2001 Is Congo red an amyloid specific dye . Biol. Chem. 276 (25), 22715-22721
263. 2001 Structural and functional similarity between Yersinia pestis capsular protein Caf1 and human interleukin-1b. Biochemistry 40 (20), 6076-6084
264. 2001 The effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism Biochemistry 40 (20), 6036-6046
265. 2001 Evidence for a partially-folded intermediate in a-synuclein fibrillation J. Biol. Chem. 276 (14), 10737-10744
266. 2001 Role of conformational changes in the activation and inhibition of human soluble guanylate cyclase. J. Inorg. Biochem. 87 (4), 267-276
267. 2001 Mutating aspartate in the calcium-binding site of a-lactalbumin: Effects on the protein stability and cation binding Protein Engineering 14 (10) 785-789.
268. 2001 Trimethylamin-N-oxide-induced folding of a-synuclein. FEBS Lett. 509 (1), 31-35
269. 2001 Metal-triggered structural transformations, aggregation and fibril formation of human a-synuclein. A possible molecular link between Parkinson’s disease and heavy metal exposure J. Biol. Chem. 276 (47), 44284-44296
270. 2001 Stabilization of partially folded conformation during a-synuclein oligomerization in both purified and cytosolic preparations J. Biol. Chem. 276 (47), 43495-43498.
271. 2001 Partially folded conformations in the unfolding pathway of bovine carbonic anhydrase B: A fluorescence study ChemBioChem 2, 813-821
272. 2001 Effect of familial Parkinson’s disease point mutations A30P and A53T on the structural properties, aggregation and fibrillation of human a-synuclein Biochemistry 40 (38), 11604-11613
273. 2000 Understanding the contribution of individual tryptophan residues to intrinsic lysozyme fluorescence Prot. Pept. Lett. 7 (6), 411-420
274. 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
275. 2000 Multi-state fluorescence in proteins with multiple tryptophan residues: Apomyoglobin natural variants and site directed mutants. J. Biol. Chem. 275 (46), 36285-36194
276. 2000 Why are “natively unfolded” proteins unstructured under the physiological conditions? Proteins: Structure, Function and Genetics. 42 (3), 415-427
277. 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
278. 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
279. 2000 Zn2+-mediated structure formation and compaction of the "natively unfolded" human prothymosin a Biochem. Biophys. Res. Comun. 267, 663-668
280. 2000 Structure and Function of a-Fetoprotein: A biophysical overview Biochim. Biophys. Acta 1480 (1-2), 41-56
281. 1999 Fine tuning the N-terminus of a calcium binding protein: a-lactalbumin. Proteins. Structure Function and Genetics. 37, 65-72
282. 1999 Protein deposits as the molecular basis of amyloidosis. II. Localized amyloidosis and neurodegenerative disordres Med. Sci. Monitor. 5 (6), 1238-1254
283. 1999 A multiparametric approach to studies of self-organization of globular proteins Biochemistry (Moscow). 64, 250-266.
284. 1999 Protein deposits as the molecular basis of amyloidosis. Part I. Systemic amyloidoses Med. Sci. Monitor. 5 (5), 1001-1012
285. 1999 Association of partially-folded intermediates of Staphylococcal nuclease induces structure and stability. Protein Sci. 8, 161-173
286. 1999 Studies on ANS fluorescence: I. Effect of self-association on structural properties of the dye Cytology (St. Petersburg). 41, 173-182
287. 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
288. 1999 Unusual combination of the distorted structure and frozen internal mobility in inactivated actin. Prot. Pept. Let. 6, 73-78
289. 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
290. 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
291. 1999 Effect of self-association on structural organization of partially-folded proteins: Inactivated actin. Biophys. J. 77, 2788-2800
292. 1999 Transient dimer in the refolding kinetics of cytochrome c characterized by small angle X-ray scattering. Biochemistry. 38 (46), 15352-15359
293. 1999 Natively unfolded" human prothymosin a adopts partially-folded conformation at acidic pH Biochemistry. 38 (45), 15009-15016.
294. 1999 Effect of hyperphosphorylation on structural properties of tau-protein Cytology (St. Petersburg). 41, 540-549.
295. 1999 The a-fetoprotein molecule has one or two rigid domains depending on the protein purification procedure Prot. Pept. Lett.. 6 (4), 237-244.
296. 1999 A new scheme of the human a-fetoprotein isolation Russian J. Bioorganic Chemistry. 25, 412-417
297. 1999 Inactivated actin, an aggregate composed of partially-folded monomers, has an overall native-like packing density. Pro. Pept. Lett. 6, 173-178
298. 1999 Do protein molecules have a native-like topology in the pre-molten globule state? Biochemistry (Moscow). 64, 552-555
299. 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
300. 1998 Influence of a biologically active interferon fragment on the carrier de novo protein structure. Biofizika 43 (3), 384-391
301. 1998 Hyperphospho-rylation induces structural modification of tau-protein FEBS Lett. 439, 21-25
302. 1998 a-Fetoprotein structure depends on the protein purification procedure: Further evidence on the structure forming role of the ligands Prot. Pept. Lett. 5, 295-301
303. 1998 Anion-induced folding of Staphylococcal nuclease: Characterization of multiple partially folded intermediates J. Mol. Biol. 278, 879-894
304. 1998 Can grafting of an octapeptide improve the structure of a de novo protein? FEBS Letters 425, 101-104
305. 1998 Association-induced folding in globular proteins Proc. Natl. Acad. Sci. U.S.A. 95, 5480-5483
306. 1998 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.
307. 1998 Pre-molten globule state in the random copolymer consisting of hydrophobic and hydrophilic amino acid residues Mol. Biol. (Moscow) 32, 550-556
308. 1998 Diversity of denatured forms of globular proteins. II. Structural properties of A-forms. Mol. Biol. (Moscow) 32, 488-497.
309. 1998 Diversity of denatured forms of globular proteins. I. Anion-induced folding of staphylococcal nuclease. Mol. Biol. (Moscow) 32, 482-487
310. 1998 Effect of natural ligands on structural properties and conformational stability of proteins (Review). Biochemistry (Moscow) 63, 420-433
311. 1998 Decrease of dielectric constant transforms the protein molecule into the molten globule state. Biochemistry (Moscow) 63, 448-455
312. 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
313. 1998 Structural properties of staphylococcal nuclease in oligomeric A-forms Biochemistry (Moscow) 63, 463-469
314. 1998 Structural effect of association on protein molecules in partially folded intermediates. Biochemistry (Moscow) 63, 456-462
315. 1998 How many molten globule states there exist? Biofizika (Moscow) 43, 416-421
316. 1997 Diversity of compact forms of denatured globular proteins Protein and Peptide Letters 4, 355-367.
317. 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.
318. 1997 Sequential compactization of random copolymer of hydrophilic and hydrophobic amino acid residues Macromolecules 30, 7427-7434
319. 1997 Rigidity of human a-fetoprotein structure is under the ligand control Biochemistry 44, 13638-13645
320. 1997 Human a-fetoprotein is in the molten globule state under conditions modelling protein environment near the membrane surface Protein and Peptide Letters 4, 243-249
321. 1997 Ligand-free form of human a-fetoprotein: Evidence for the molten globule state. FEBS Letters 410, 280-284
322. 1997 Coformational transitions provoked by organic solvents in b-lactoglobulin: Can a molten globule-like intermediate be induced by the decrease in dielectric constant? Folding & Design 2, 163-173
323. 1997 Comparison of structural properties of homologous proteins Human serum albumin and alpha-fetoprotein. Mol. Biol. (Moscow) 31, 1128-1133
324. 1996 Three-stage equilibrium unfolding of small globular proteins by strong denaturants: I. Carbonic anhydrase B Mol. Biol. (Moscow) 30, 1124-1134.
325. 1996 Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface. Biochemistry 35, 6058-6063.
326. 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
327. 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
328. 1996 All-or-none solvent-induced transitions between native, molten globule and unfolded states in globular proteins Folding & Design, 1, 117-122
329. 1996 The de novo protein with grafted biological function: transferring of interferon blast-transformong activity to albebetin Protein Engineering 9, 195-201
330. 1996 Synthetic polyamino acids and polypeptides. Preparation by the N-carboxyanhydride method. Bioorgan. Khim. (Moscow) 22(8), 563-574.
331. 1996 Kinetic and equilibrium folding intermediates Protein Folding (Dobson, C.M., Fersht A.R., Eds.). Cambridge University Press, Cambridge, New York, Melbourne, pp. 35-41
332. 1996 Protein engineering of de nojo protein with predesigned structure ans activity. Applied Biochemistry and Biotechnology Protein Engineering 61, 85-96
333. 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
334. 1996 Stabilization of alpha-fetoprotein structure by sucrose. Bioorgan. Chem. (Moscow) 22, 408-414
335. 1996 Three-stage equilibrium unfolding of small globular proteins by strong denaturants: II. b-Lactamase and general model Mol. Biol. (Moscow) 30, 1135-1143
336. 1995 Structural properties of a-fetoprotein from human cord serum: the protein molecule at low pH possesses all the properties of the molten globule FEBS Letters 364, 165-167
337. 1995 Kinetic and equilibrium folding intermediates Phil. Trans. R. Soc. Lond. 348, 35-41.
338. 1995 Structural properties of ribosomal protein S8 from extreme thermophile Thermus thermophilus. Russian J. Bioorganic Chemistry 21, 423-428.
339. 1995 “Pre-molten globule” - a new equilibrium state of protein molecules FASEB Journal 9, A1469
340. 1995 “Domain” coil-globule transition in homopolimers Macromolecules 28, 7519-7524
341. 1994 Circularly permuted dihydrofolate reductase of E.coli has functional activity and a destabilized tertiary structure Protein Engineering 7, 1373-1377
342. 1994 Permyakov E.A., Gripas A.F., Mitin Y.V. (1994) Fluorescence monitoring of the solid phase peptide synthesis. “Peptides 1994”, H.L.S. Maia, Ed., ESCOM, Leiden, pp.177-178
343. 1994 Gel-permeation chromatography as a unique instrument for quantitative and qualitative analysis of protein denaturation and unfolding Int. J. Bio-Chromatography 1, 103-114
344. 1994 A Quartz reaction-cuvette for fluorescent monitoring of the solid phase peptide synthesis. Bioorgan. Khimia (Moscow) 20, 635-644
345. 1994 “Partly folded” state, a new equilibrium state of protein molecules: Four-state guanidinium chloride-induced unfolding of b-lactamase at low temperature Biochemistry 33, 2782-2791
346. 1994 The molten globule is a third thermodinamical state of protein molecules FEBS Letters 341, 15-18
347. 1994 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 7, 1041-1052
348. 1993 Comparative stability of dihydrofolate reductase mutants in vitro and in vivo Protein Engineering 6, 81-84
349. 1993 Unfolding of the molten globule by strong denaturants follows the "all-or-none" principle Biophysics (Moscow) 38, 31-39
350. 1993 Effect of point amino acid replacements on the stability of phage T4 lysozyme. I. Asn101-Asp replacement Biophysics (Moscow) 38, 619-622
351. 1993 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) 38, 623-627
352. 1993 Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule Biochemistry 32, 13288-13298
353. 1993 Introduction of Ca2+-binding amino-acid sequence into the T4 Lysozyme. Biochim. Biophys. Acta 1162, 84-88
354. 1992 Triple point mutation Asp10-His, Asn101-Asp, Arg148-Ser in T4 phage lysozyme leads to the molten globule. Protein Engineering 5, 781-783
355. 1992 “All-or-none” mechasnism of the molten globule unfolding FEBS Letters 314, 89-92
356. 1991 Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers 13, 119-128
357. 1991 Cementing the folding community The Biochemist 13, No.3, 9
358. 1990 Two slow stages in refolding of bovine carbonic anhydrase B are due to proline isomerization J. Mol. Biol. 213, 561-568
359. 1989 Two-stage equilibrium unfolding of carbonic anhydrase B by strong denaturants Mol. Biol (Moscow) 23, 683-692
360. 1987 Study on the effect of Mn2+ and Mg2+ ions on DNA conformation Mol. Biol (Moscow) 21, 140-146


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