Vladimir Uversky

Indiana University, USA

Vladimir N. Uversky received broad training, with the M.S. degree in physics, Leningrad State University, Russia, 1986, the Ph.D. degree from Moscow Institute of Technical Physics, 1991, and the D.S. degree in biophysics, Institute of Experimental and Theoretical Biophysics, Russian Academy of Sciences, 1998, and with pre- and postdoctoral research in structural biology, biochemistry, and biophysics (1991–1998, Institute of Protein Research, Russian Academy of Sciences). From 1985 until 1998, Dr. Uversky used a variety of biophysical and biochemical techniques to study molecular mechanisms of protein folding and to analyze structure and function of globular proteins. In 1998, he started to investigate protein misfolding. Working on protein folding-misfolding, Dr. Uversky found that many biologically active proteins do not have rigid structure and are often involved in human diseases. He is known for his work on structural characterization of partially folded proteins, for development of novel tools to study protein folding, misfolding and nonfolding, for studies on intrinsically disordered (or natively unfolded) proteins, and for a model of protein amyloidogenesis involving the premolten globular (disordered) state. While he continues to use biophysics and biochemistry, more recently Dr. Uversky has focused on the development and use of bioinformatics methods for the study of intrinsically disordered proteins.

Biography Updated on 1 October 2007

Articles in Scholarly Journals [Incomplete List]

  1. The Mysterious Unfoldome: Structureless, Underappreciated, Yet Vital Part of Any Given Proteome
    Journal of Biomedicine and Biotechnology, vol. 2010, no. 21, Article ID 568068, 14 pages, 2010
  2. Intrinsic disorder in Viral Proteins Genome-Linked: experimental and predictive analyses
    Virology Journal, vol. 6, no. 1, p. 23, 2009
  3. Close encounters of the third kind: disordered domains and the interactions of proteins
    BioEssays, vol. 31, no. 3, pp. 328–335, 2009
  4. Smoking and Parkinson's disease: Does nicotine affect α-synuclein fibrillation?
    Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics, vol. 1794, no. 2, pp. 282–290, 2009
  5. CDF it all: Consensus prediction of intrinsically disordered proteins based on various cumulative distribution functions
    FEBS Letters, vol. 583, no. 9, pp. 1469–1474, 2009
  6. At Low Concentrations, 3,4-Dihydroxyphenylacetic Acid (DOPAC) Binds Non-Covalently to α-Synuclein and Prevents Its Fibrillation
    Journal of Molecular Biology, vol. 388, no. 3, pp. 597–610, 2009
  7. Do viral proteins possess unique biophysical features?
    Trends in Biochemical Sciences, vol. 34, no. 2, pp. 53–59, 2009
  8. Exploring the Molecular Design of Protein Interaction Sites with Molecular Dynamics Simulations and Free Energy Calculations
    Biochemistry, vol. 48, no. 2, pp. 399–414, 2009
  9. Effect of Methionine Oxidation on the Structural Properties, Conformational Stability, and Aggregation of Immunoglobulin Light Chain LEN
    Biochemistry, vol. 47, no. 33, pp. 8665–8677, 2008
  10. Guiding Protein Aggregation with Macromolecular Crowding
    Biochemistry, vol. 47, no. 34, pp. 8993–9006, 2008
  11. Thioflavin T as a Molecular Rotor: Fluorescent Properties of Thioflavin T in Solvents with Different Viscosity
    The Journal of Physical Chemistry B, vol. 112, no. 49, pp. 15893–15902, 2008
  12. Protein Disorder Is Positively Correlated with Gene Expression in Escherichia coli
    Journal of Proteome Research, vol. 7, no. 6, pp. 2234–2245, 2008
  13. 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, vol. 7, no. 6, pp. 2496–2506, 2008
  14. Malleable machines take shape in eukaryotic transcriptional regulation
    Nature Chemical Biology, vol. 4, no. 12, Article ID nchembio.127, 9 pages, 2008
  15. Signal transduction via unstructured protein conduits
    Nature Chemical Biology, vol. 4, no. 4, Article ID nchembio0408-229, 1 pages, 2008
  16. Intrinsic disorder in pathogenic and non-pathogenic microbes: discovering and analyzing the unfoldomes of early-branching eukaryotes
    Molecular BioSystems, vol. 4, no. 4, p. 328, 2008
  17. Intrinsic disorder in scaffold proteins: Getting more from less
    Progress in Biophysics and Molecular Biology, vol. 98, no. 1, pp. 85–106, 2008
  18. Function and structure of inherently disordered proteins
    Current Opinion in Structural Biology, vol. 18, no. 6, pp. 756–764, 2008
  19. Potato virus A genome-linked protein VPg is an intrinsically disordered molten globule-like protein with a hydrophobic core
    Virology, vol. 377, no. 2, pp. 280–288, 2008
  20. Intrinsically Disordered Human C/EBP Homologous Protein Regulates Biological Activity of Colon Cancer Cells during Calcium Stress
    Journal of Molecular Biology, vol. 380, no. 2, pp. 313–326, 2008
  21. The Effect of Membranes on the In Vitro Fibrillation of an Amyloidogenic Light-Chain Variable-Domain SMA
    Journal of Molecular Biology, vol. 381, no. 4, pp. 989–999, 2008
  22. Structural Characteristics of α-Synuclein Oligomers Stabilized by the Flavonoid Baicalein☆
    Journal of Molecular Biology, vol. 383, no. 1, pp. 214–223, 2008
  23. Dynamics of oligomer formation by denatured carbonic anhydrase II
    Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics, vol. 1784, no. 5, pp. 834–842, 2008
  24. Apo‐parvalbumin as an intrinsically disordered protein
    Proteins: Structure, Function, and Bioinformatics, vol. 72, no. 3, pp. 822–836, 2008
  25. Understanding the role of Arg96 in structure and stability of green fluorescent protein
    Proteins: Structure, Function, and Bioinformatics, vol. 73, no. 3, pp. 539–551, 2008
  26. Structure-function analysis of Knr4/Smi1, a newly member of intrinsically disordered proteins family, indispensable in the absence of a functional PKC1-SLT2 pathway in Saccharomyces cerevisiae
    Yeast, vol. 25, no. 8, pp. 563–576, 2008
  27. Malleable Machines in Transcription Regulation: The Mediator Complex
    PLoS Computational Biology, vol. 4, no. 12, p. e1000243, 2008
  28. TOP-IDP-Scale: A New Amino Acid Scale Measuring Propensity for Intrinsic Disorder
    Protein and Peptide Letters, vol. 15, no. 9, pp. 956–963, 2008
  29. Concerted Action of Metals and Macromolecular Crowding on the Fibrillation of α-Synuclein
    Protein and Peptide Letters, vol. 15, no. 10, pp. 1079–1085, 2008
  30. Fluorescent Proteins as Biomarkers and Biosensors: Throwing Color Lights on Molecular and Cellular Processes
    Current Protein and Peptide Science, vol. 9, no. 4, pp. 338–369, 2008
  31. α-Synuclein Misfolding and Neurodegenerative Diseases
    Current Protein and Peptide Science, vol. 9, no. 5, pp. 507–540, 2008
  32. Amyloidogenesis of Natively Unfolded Proteins
    Current Alzheimer Research, vol. 5, no. 3, pp. 260–287, 2008
  33. BIOCHEMISTRY: Controlled Chaos
    Science, vol. 322, no. 5906, pp. 1340–1341, 2008
  34. Intrinsically Disordered Proteins in Human Diseases: Introducing the D 2 Concept
    Annual Review of Biophysics, vol. 37, no. 1, pp. 215–246, 2008
  35. Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners
    BMC Genomics, vol. 9, no. Suppl 1, p. S1, 2008
  36. The unfoldomics decade: an update on intrinsically disordered proteins
    BMC Genomics, vol. 9, no. Suppl 2, p. S1, 2008
  37. Short Linear Motifs recognized by SH2, SH3 and Ser/Thr Kinase domains are conserved in disordered protein regions
    BMC Genomics, vol. 9, no. Suppl 2, p. S26, 2008
  38. Protein intrinsic disorder toolbox for comparative analysis of viral proteins
    BMC Genomics, vol. 9, no. Suppl 2, p. S4, 2008
  39. A comparative analysis of viral matrix proteins using disorder predictors
    Virology Journal, vol. 5, no. 1, p. 126, 2008
  40. Synuclein-  Targeting Peptide Inhibitor that Enhances Sensitivity of Breast Cancer Cells to Antimicrotubule Drugs
    Cancer Research, vol. 67, no. 2, pp. 626–633, 2007
  41. Composition Profiler: a tool for discovery and visualization of amino acid composition differences
    BMC Bioinformatics, vol. 8, no. 1, p. 211, 2007
  42. Neuropathology, biochemistry, and biophysics of ?-synuclein aggregation
    Journal of Neurochemistry, vol. 0, no. 0, pp. 070710052154012–???, 2007
  43. DisProt: the Database of Disordered Proteins
    Nucleic Acids Research, vol. 35, no. Database, pp. D786–D793, 2007
  44. Nanoimaging in protein-misfolding and -conformational diseases
    Nanomedicine, vol. 2, no. 5, pp. 615–643, 2007
  45. 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, vol. 27, no. 51, pp. 14117–14127, 2007
  46. Functional Anthology of Intrinsic Disorder. 1. Biological Processes and Functions of Proteins with Long Disordered Regions
    Journal of Proteome Research, vol. 0, no. 0, pp. 0–0, 2007
  47. Functional Anthology of Intrinsic Disorder. 2. Cellular Components, Domains, Technical Terms, Developmental Processes, and Coding Sequence Diversities Correlated with Long Disordered Regions
    Journal of Proteome Research, vol. 0, no. 0, pp. 0–0, 2007
  48. Functional Anthology of Intrinsic Disorder. 3. Ligands, Post-Translational Modifications, and Diseases Associated with Intrinsically Disordered Proteins
    Journal of Proteome Research, vol. 0, no. 0, pp. 0–0, 2007
  49. Spectral Properties of Thioflavin T in Solvents with Different Dielectric Properties and in a Fibril-Incorporated Form
    Journal of Proteome Research, vol. 6, no. 4, pp. 1392–1401, 2007
  50. Recoverin as a Redox-Sensitive Protein
    Journal of Proteome Research, vol. 0, no. 0, pp. 0–0, 2007
  51. Attachment of LcrV from Yersinia pestis at Dual Binding Sites to Human TLR-2 and Human IFN-? Receptor
    Journal of Proteome Research, vol. 6, no. 6, pp. 2222–2231, 2007
  52. Characterization of Molecular Recognition Features, MoRFs, and Their Binding Partners
    Journal of Proteome Research, vol. 6, no. 6, pp. 2351–2366, 2007
  53. Multiple aromatic side chains within a disordered structure are critical for transcription and transforming activity of EWS family oncoproteins
    Proceedings of the National Academy of Sciences, vol. 104, no. 2, pp. 479–484, 2007
  54. A Computational Investigation of Allostery in the Catabolite Activator Protein
    Journal of the American Chemical Society, vol. 129, no. 50, pp. 15668–15676, 2007
  55. Mining α-Helix-Forming Molecular Recognition Features with Cross Species Sequence Alignments
    Biochemistry, vol. 46, no. 47, pp. 13468–13477, 2007
  56. Biochemistry, vol. 45, no. 38, pp. 11523–11531, 2006
  57. Biochemistry, vol. 45, no. 22, pp. 6873–6888, 2006
  58. Biochemistry, vol. 45, no. 35, pp. 10448–10460, 2006
  59. Biochemistry, vol. 45, no. 51, pp. 15731–15739, 2006
  60. Journal of Proteome Research, vol. 5, no. 4, pp. 879–887, 2006
  61. Journal of Proteome Research, vol. 5, no. 4, pp. 888–898, 2006
  62. Journal of Proteome Research, vol. 5, no. 8, pp. 1829–1842, 2006
  63. Journal of Proteome Research, vol. 5, no. 10, pp. 2505–2522, 2006
  64. Alternative splicing in concert with protein intrinsic disorder enables increased functional diversity in multicellular organisms
    Proceedings of the National Academy of Sciences, vol. 103, no. 22, pp. 8390–8395, 2006
  65. Nanoimaging for protein misfolding and related diseases
    Journal of Cellular Biochemistry, vol. 99, no. 1, pp. 52–70, 2006
  66. Calmodulin signaling: Analysis and prediction of a disorder-dependent molecular recognition
    Proteins: Structure, Function, and Bioinformatics, vol. 63, no. 2, pp. 398–410, 2006
  67. Role of lysine versus arginine in enzyme cold-adaptation: Modifying lysine to homo-arginine stabilizes the cold-adapted a-amylase fromPseudoalteramonas haloplanktis
    Proteins: Structure, Function, and Bioinformatics, vol. 64, no. 2, pp. 486–501, 2006
  68. Analysis of Molecular Recognition Features (MoRFs)
    Journal of Molecular Biology, vol. 362, no. 5, pp. 1043–1059, 2006
  69. Rational drug design via intrinsically disordered protein
    Trends in Biotechnology, vol. 24, no. 10, pp. 435–442, 2006
  70. Intrinsic Disorder Is a Common Feature of Hub Proteins from Four Eukaryotic Interactomes
    PLoS Computational Biology, vol. 2, no. 8, p. e100, 2006
  71. Intrinsic Disorder and Functional Proteomics
    Biophysical Journal, vol. 92, no. 5, pp. 1439–1456, 2006
  72. Local Flexibility in Molecular Function Paradigm
    Molecular & Cellular Proteomics, vol. 5, no. 7, pp. 1212–1223, 2006
  73. The Disordered Amino-Terminus of SIMPL Interacts with Members of the 70-kDa Heat-Shock Protein Family
    DNA and Cell Biology, vol. 25, no. 12, pp. 704–714, 2006
  74. Agrin binds  -synuclein and modulates  -synuclein fibrillation
    Glycobiology, vol. 15, no. 12, pp. 1320–1331, 2005
  75. Protein dissection enhances the amyloidogenic properties of alpha-lactalbumin
    FEBS Journal, vol. 272, no. 9, pp. 2176–2188, 2005
  76. Flexible nets. The roles of intrinsic disorder in protein interaction networks
    FEBS Journal, vol. 272, no. 20, pp. 5129–5148, 2005
  77. Early Events in the Fibrillation of Monomeric Insulin
    Journal of Biological Chemistry, vol. 280, no. 52, pp. 42669–42675, 2005
  78. How to improve nature: study of the electrostatic properties of the surface of  -lactalbumin
    Protein Engineering Design and Selection, vol. 18, no. 9, pp. 425–433, 2005
  79. A GLYmmer of Insight into Fibril Formation
    Structure, vol. 13, no. 8, pp. 1090–1092, 2005
  80. Protein Interactions and Misfolding Analyzed by AFM Force Spectroscopy
    Journal of Molecular Biology, vol. 354, no. 5, pp. 1028–1042, 2005
  81. Effects of nitration on the structure and aggregation of a-synuclein
    Molecular Brain Research, vol. 134, no. 1, pp. 84–102, 2005
  82. Lysozyme fibrillation: Deep UV Raman spectroscopic characterization of protein structural transformation
    Biopolymers, vol. 79, no. 1, pp. 58–61, 2005
  83. Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
    Journal of Molecular Recognition, vol. 18, no. 5, pp. 343–384, 2005
  84. Assessing protein disorder and induced folding
    Proteins: Structure, Function, and Bioinformatics, vol. 62, no. 1, pp. 24–45, 2005
  85. Domain coupling in a multimodular cellobiohydrolase CbhA from
    FEBS Letters, vol. 579, no. 20, pp. 4367–4373, 2005
  86. Methionine oxidation, ?-synuclein and Parkinson's disease
    Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics, vol. 1703, no. 2, pp. 157–169, 2005
  87. Journal of Proteome Research, vol. 4, no. 6, pp. 1942–1951, 2005
  88. Journal of Proteome Research, vol. 4, no. 5, pp. 1610–1618, 2005
  89. Journal of Proteome Research, vol. 4, no. 2, pp. 564–569, 2005
  90. Journal of Chemical Information and Modeling, vol. 45, no. 1, pp. 183–189, 2005
  91. Biochemistry, vol. 44, no. 25, pp. 9096–9107, 2005
  92. Biochemistry, vol. 44, no. 37, pp. 12454–12470, 2005
  93. Biochemistry, vol. 44, no. 6, pp. 1989–2000, 2005
  94. Biochemistry, vol. 43, no. 47, pp. 14913–14923, 2004
  95. Biochemistry, vol. 43, no. 11, pp. 3289–3300, 2004
  96. Biochemistry, vol. 43, no. 19, pp. 5575–5582, 2004
  97. Biochemistry, vol. 43, no. 15, pp. 4621–4633, 2004
  98. Charge and Hydrophobicity Patterning along the Sequence Predicts the Folding Mechanism and Aggregation of Proteins: A Computational Approach
    Journal of Proteome Research, vol. 3, no. 6, pp. 1243–1253, 2004
  99. Journal of Proteome Research, vol. 3, no. 3, pp. 485–494, 2004
  100. Conformational constraints for amyloid fibrillation: the importance of being unfolded
    Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics, vol. 1698, no. 2, pp. 131–153, 2004
  101. Rifampicin Inhibits ?-Synuclein Fibrillation and Disaggregates Fibrils
    Chemistry & Biology, vol. 11, no. 11, pp. 1513–1521, 2004
  102. Neurotoxicant-induced animal models of Parkinson?s disease: understanding the role of rotenone, maneb and paraquat in neurodegeneration
    Cell and Tissue Research, vol. 318, no. 1, pp. 225–241, 2004
  103. The effect of macromolecular crowding on protein aggregation and amyloid fibril formation
    Journal of Molecular Recognition, vol. 17, no. 5, pp. 456–464, 2004
  104. Conformational Prerequisites for Formation of Amyloid Fibrils from Histones
    Journal of Molecular Biology, vol. 342, no. 4, pp. 1305–1324, 2004
  105. Adenylation-Dependent Conformation and Unfolding Pathways of the NAD+-Dependent DNA Ligase from the Thermophile Thermus scotoductus
    Biophysical Journal, vol. 86, no. 2, pp. 1089–1104, 2004
  106. Interactions between immunoglobulin-like and catalytic modules in Clostridium thermocellum cellulosomal cellobiohydrolase CbhA
    Protein Engineering Design and Selection, vol. 17, no. 11, pp. 759–769, 2004
  107. Stimulation of Insulin Fibrillation by Urea-induced Intermediates
    Journal of Biological Chemistry, vol. 279, no. 15, pp. 14999–15013, 2004
  108. Certain Metals Trigger Fibrillation of Methionine-oxidized  -Synuclein
    Journal of Biological Chemistry, vol. 278, no. 30, pp. 27630–27635, 2003
  109. Structural and Functional Adaptations to Extreme Temperatures in Psychrophilic, Mesophilic, and Thermophilic DNA Ligases
    Journal of Biological Chemistry, vol. 278, no. 39, pp. 37015–37023, 2003
  110. Cofactor Binding Modulates the Conformational Stabilities and Unfolding Patterns of NAD+-dependent DNA Ligases from Escherichia coli and Thermus scotoductus
    Journal of Biological Chemistry, vol. 278, no. 50, pp. 49945–49953, 2003
  111. Polycation-induced oligomerization and accelerated fibrillation of human alpha-synuclein in vitro
    Protein Science, vol. 12, no. 4, pp. 702–707, 2003
  112. Polymeric Aspects of Protein Folding: a Brief Overview
    Protein and Peptide Letters, vol. 10, no. 3, pp. 239–245, 2003
  113. Nitration inhibits fibrillation of human a-synuclein in vitro by formation of soluble oligomers
    FEBS Letters, vol. 542, no. 1-3, pp. 147–152, 2003
  114. Prediction of the association state of insulin using spectral parameters
    Journal of Pharmaceutical Sciences, vol. 92, no. 4, pp. 847–858, 2003
  115. Ultraviolet illumination-induced reduction of ?-lactalbumin disulfide bridges
    Proteins: Structure, Function, and Genetics, vol. 51, no. 4, pp. 498–503, 2003
  116. Natively unfolded C-terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin
    Proteins: Structure, Function, and Genetics, vol. 53, no. 4, pp. 855–Na, 2003
  117. Protein folding revisited. A polypeptide chain at the folding ? misfolding ? nonfolding cross-roads: which way to go?
    Cellular and Molecular Life Sciences (CMLS), vol. 60, no. 9, pp. 1852–1871, 2003
  118. Journal of Proteome Research, vol. 2, no. 1, pp. 37–42, 2003
  119. Journal of Proteome Research, vol. 2, no. 1, pp. 51–57, 2003
  120. Journal of Proteome Research, vol. 2, no. 3, pp. 273–281, 2003
  121. Disorder in the nuclear pore complex: The FG repeat regions of nucleoporins are natively unfolded
    Proceedings of the National Academy of Sciences, vol. 100, no. 5, pp. 2450–2455, 2003
  122. Calcium and domain interactions contribute to the thermostability of domains of the multimodular cellobiohydrolase, CbhA, a subunit of the Clostridium thermocellum cellulosome
    Biochemical Journal, vol. 372, no. 1, p. 151, 2003
  123. Biochemistry, vol. 42, no. 9, pp. 2720–2730, 2003
  124. Biochemistry, vol. 42, no. 28, pp. 8465–8471, 2003
  125. Biochemistry, vol. 42, no. 26, pp. 7879–7884, 2003
  126. Biochemistry, vol. 42, no. 26, pp. 8094–8104, 2003
  127. Biochemistry, vol. 42, no. 39, pp. 11404–11416, 2003
  128. Biochemistry, vol. 41, no. 5, pp. 1502–1511, 2002
  129. Biochemistry, vol. 41, no. 41, pp. 12546–12551, 2002
  130. What does it mean to be natively unfolded?
    European Journal of Biochemistry, vol. 269, no. 1, pp. 2–12, 2002
  131. The Herbicide Paraquat Causes Up-regulation and Aggregation of alpha -Synuclein in Mice. PARAQUAT AND alpha -SYNUCLEIN
    Journal of Biological Chemistry, vol. 277, no. 3, pp. 1641–1644, 2002
  132. Journal of Proteome Research, vol. 1, no. 2, pp. 149–159, 2002
  133. Journal of Proteome Research, vol. 1, no. 4, pp. 307–315, 2002
  134. Cracking the folding code. Why do some proteins adopt partially folded conformations, whereas other don't?
    FEBS Letters, vol. 514, no. 2-3, pp. 181–183, 2002
  135. The chicken–egg scenario of protein folding revisited
    FEBS Letters, vol. 515, no. 1-3, pp. 79–83, 2002
  136. Accelerated a-synuclein fibrillation in crowded milieu
    FEBS Letters, vol. 515, no. 1-3, pp. 99–103, 2002
  137. Methionine oxidation inhibits fibrillation of human a-synuclein in vitro
    FEBS Letters, vol. 517, no. 1-3, pp. 239–244, 2002
  138. Amino acid determinants of a-synuclein aggregation: putting together pieces of the puzzle
    FEBS Letters, vol. 522, no. 1-3, pp. 9–13, 2002
  139. Conformational Behavior of Human a-Synuclein is Modulated by Familial Parkinson's Disease Point Mutations A30P and A53T
    NeuroToxicology, vol. 23, no. 4-5, pp. 553–567, 2002
  140. Synergistic Effects of Pesticides and Metals on the Fibrillation of a-Synuclein: Implications for Parkinson's Disease
    NeuroToxicology, vol. 23, no. 4-5, pp. 527–536, 2002
  141. Native-like secondary structure of molten globules
    Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol. 1594, no. 1, pp. 168–177, 2002
  142. Unraveling multistate unfolding of rabbit muscle creatine kinase
    Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol. 1596, no. 1, pp. 138–155, 2002
  143. Human a-fetoprotein as a Zn2+-binding protein. Tight cation binding is not accompanied by global changes in protein structure and stability
    Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, vol. 1586, no. 1, pp. 1–10, 2002
  144. Natively unfolded proteins: A point where biology waits for physics
    Protein Science, vol. 11, no. 4, pp. 739–756, 2002
  145. Elucidation of the Molecular Mechanism during the Early Events in Immunoglobulin Light Chain Amyloid Fibrillation. EVIDENCE FOR AN OFF-PATHWAY OLIGOMER AT ACIDIC pH
    Journal of Biological Chemistry, vol. 277, no. 15, pp. 12666–12679, 2002
  146. Effect of Association State and Conformational Stability on the Kinetics of Immunoglobulin Light Chain Amyloid Fibril Formation at Physiological pH
    Journal of Biological Chemistry, vol. 277, no. 15, pp. 12657–12665, 2002
  147. Biophysical Properties of the Synucleins and Their Propensities to Fibrillate. INHIBITION OF alpha -SYNUCLEIN ASSEMBLY BY beta - AND gamma -SYNUCLEINS
    Journal of Biological Chemistry, vol. 277, no. 14, pp. 11970–11978, 2002
  148. The Saccharomyces cerevisiae Nucleoporin Nup2p Is a Natively Unfolded Protein
    Journal of Biological Chemistry, vol. 277, no. 36, pp. 33447–33455, 2002
  149. Evidence for a Partially Folded Intermediate in alpha -Synuclein Fibril Formation
    Journal of Biological Chemistry, vol. 276, no. 14, pp. 10737–10744, 2001
  150. Is Congo Red an Amyloid-specific Dye?
    Journal of Biological Chemistry, vol. 276, no. 25, pp. 22715–22721, 2001
  151. Metal-triggered Structural Transformations, Aggregation, and Fibrillation of Human alpha -Synuclein. A POSSIBLE MOLECULAR LINK BETWEEN PARKINSON'S DISEASE AND HEAVY METAL EXPOSURE
    Journal of Biological Chemistry, vol. 276, no. 47, pp. 44284–44296, 2001
  152. Stabilization of Partially Folded Conformation during alpha -Synuclein Oligomerization in Both Purified and Cytosolic Preparations
    Journal of Biological Chemistry, vol. 276, no. 47, pp. 43495–43498, 2001
  153. Mutating aspartate in the calcium-binding site of  -lactalbumin: effects on the protein stability and cation binding
    Protein Engineering Design and Selection, vol. 14, no. 10, pp. 785–789, 2001
  154. Secondary Structure of the Homologous Proteins, A A-Fetoprotein and Serum Albumin, from their Circular Dichroism and Infrared Spectra
    Protein and Peptide Letters, vol. 8, no. 4, pp. 297–302, 2001
  155. Role of conformational changes in the heme-dependent regulation of human soluble guanylate cyclase
    Journal of Inorganic Biochemistry, vol. 87, no. 4, pp. 267–276, 2001
  156. Pesticides directly accelerate the rate of a-synuclein fibril formation: a possible factor in Parkinson's disease
    FEBS Letters, vol. 500, no. 3, pp. 105–108, 2001
  157. Trimethylamine-N-oxide-induced folding of a-synuclein
    FEBS Letters, vol. 509, no. 1, pp. 31–35, 2001
  158. Denatured collapsed states in protein folding: Example of apomyoglobin
    Proteins: Structure, Function, and Genetics, vol. 44, no. 3, pp. 244–254, 2001
  159. Human Soluble Guanylate Cyclase: Functional Expression, Purification and Structural Characterization
    Archives of Biochemistry and Biophysics, vol. 388, no. 2, pp. 185–197, 2001
  160. Biochemistry, vol. 40, no. 7, pp. 2113–2128, 2001
  161. Biochemistry, vol. 40, no. 20, pp. 6036–6046, 2001
  162. Biochemistry, vol. 40, no. 20, pp. 6076–6084, 2001
  163. Biochemistry, vol. 40, no. 28, pp. 8397–8409, 2001
  164. Biochemistry, vol. 40, no. 38, pp. 11604–11613, 2001
  165. Multisite Fluorescence in Proteins with Multiple Tryptophan Residues. APOMYOGLOBIN NATURAL VARIANTS AND SITE-DIRECTED MUTANTS
    Journal of Biological Chemistry, vol. 275, no. 46, pp. 36285–36294, 2000
  166. Zn2+-Mediated Structure Formation and Compaction of the “Natively Unfolded” Human Prothymosin a
    Biochemical and Biophysical Research Communications, vol. 267, no. 2, pp. 663–668, 2000
  167. Why are ?natively unfolded? proteins unstructured under physiologic conditions?
    Proteins: Structure, Function, and Genetics, vol. 41, no. 3, pp. 415–427, 2000
  168. Point amino acid substitutions in the Ca2+-binding sites of recoverin: II. The unusual behavior of the protein upon the binding of calcium ions
    Russian Journal of Bioorganic Chemistry, vol. 26, no. 3, pp. 152–156, 2000
  169. Structure and function of a-fetoprotein: a biophysical overview
    Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol. 1480, no. 1-2, pp. 41–56, 2000
  170. Effects of mutations in the calcium-binding sites of recoverin on its calcium affinity: evidence for successive filling of the calcium binding sites
    Protein Engineering Design and Selection, vol. 13, no. 11, pp. 783–790, 2000
  171. Effect of Self-Association on the Structural Organization of Partially Folded Proteins: Inactivated Actin
    Biophysical Journal, vol. 77, no. 5, pp. 2788–2800, 1999
  172. Fine tuning the N-terminus of a calcium binding protein: ?-lactalbumin
    Proteins: Structure, Function, and Genetics, vol. 37, no. 1, pp. 65–72, 1999
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