Vladimir N. Uversky

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 25 September 2007

Personal Home Page

http://www.biochemistry.iu.edu/body.cfm?id=6246&oTopID=3021

Articles in Scholarly Journals [Incomplete List]

  1. 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
  2. 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
  3. 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
  4. 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
  5. Recoverin as a Redox-Sensitive Protein
    Journal of Proteome Research, vol. 0, no. 0, pp. 0–0, 2007
  6. 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
  7. Characterization of Molecular Recognition Features, MoRFs, and Their Binding Partners
    Journal of Proteome Research, vol. 6, no. 6, pp. 2351–2366, 2007
  8. 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
  9. DisProt: the Database of Disordered Proteins
    Nucleic Acids Research, vol. 35, no. Database, pp. D786–D793, 2007
  10. Neuropathology, biochemistry, and biophysics of ?-synuclein aggregation
    Journal of Neurochemistry, vol. 0, no. 0, pp. 070710052154012–???, 2007
  11. Synuclein-  Targeting Peptide Inhibitor that Enhances Sensitivity of Breast Cancer Cells to Antimicrotubule Drugs
    Cancer Research, vol. 67, no. 2, pp. 626–633, 2007
  12. Composition Profiler: a tool for discovery and visualization of amino acid composition differences
    BMC Bioinformatics, vol. 8, no. 1, p. 211, 2007
  13. Intrinsic Disorder Is a Common Feature of Hub Proteins from Four Eukaryotic Interactomes
    PLoS Computational Biology, vol. 2, no. 8, p. e100, 2006
  14. Intrinsic Disorder and Functional Proteomics
    Biophysical Journal, vol. 92, no. 5, pp. 1439–1456, 2006
  15. Local Flexibility in Molecular Function Paradigm
    Molecular & Cellular Proteomics, vol. 5, no. 7, pp. 1212–1223, 2006
  16. 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
  17. 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
  18. Journal of Proteome Research, vol. 5, no. 4, pp. 879–887, 2006
  19. Journal of Proteome Research, vol. 5, no. 4, pp. 888–898, 2006
  20. Journal of Proteome Research, vol. 5, no. 8, pp. 1829–1842, 2006
  21. Journal of Proteome Research, vol. 5, no. 10, pp. 2505–2522, 2006
  22. Biochemistry, vol. 45, no. 38, pp. 11523–11531, 2006
  23. Biochemistry, vol. 45, no. 22, pp. 6873–6888, 2006
  24. Biochemistry, vol. 45, no. 35, pp. 10448–10460, 2006
  25. Biochemistry, vol. 45, no. 51, pp. 15731–15739, 2006
  26. Calmodulin signaling: Analysis and prediction of a disorder-dependent molecular recognition
    Proteins: Structure, Function, and Bioinformatics, vol. 63, no. 2, pp. 398–410, 2006
  27. 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
  28. Nanoimaging for protein misfolding and related diseases
    Journal of Cellular Biochemistry, vol. 99, no. 1, pp. 52–70, 2006
  29. Analysis of Molecular Recognition Features (MoRFs)
    Journal of Molecular Biology, vol. 362, no. 5, pp. 1043–1059, 2006
  30. Rational drug design via intrinsically disordered protein
    Trends in Biotechnology, vol. 24, no. 10, pp. 435–442, 2006
  31. Effects of nitration on the structure and aggregation of a-synuclein
    Molecular Brain Research, vol. 134, no. 1, pp. 84–102, 2005
  32. A GLYmmer of Insight into Fibril Formation
    Structure, vol. 13, no. 8, pp. 1090–1092, 2005
  33. Domain coupling in a multimodular cellobiohydrolase CbhA from
    FEBS Letters, vol. 579, no. 20, pp. 4367–4373, 2005
  34. Protein Interactions and Misfolding Analyzed by AFM Force Spectroscopy
    Journal of Molecular Biology, vol. 354, no. 5, pp. 1028–1042, 2005
  35. Methionine oxidation, ?-synuclein and Parkinson's disease
    Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics, vol. 1703, no. 2, pp. 157–169, 2005
  36. Assessing protein disorder and induced folding
    Proteins: Structure, Function, and Bioinformatics, vol. 62, no. 1, pp. 24–45, 2005
  37. Lysozyme fibrillation: Deep UV Raman spectroscopic characterization of protein structural transformation
    Biopolymers, vol. 79, no. 1, pp. 58–61, 2005
  38. 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
  39. Biochemistry, vol. 44, no. 6, pp. 1989–2000, 2005
  40. Biochemistry, vol. 44, no. 25, pp. 9096–9107, 2005
  41. Biochemistry, vol. 44, no. 37, pp. 12454–12470, 2005
  42. Journal of Chemical Information and Modeling, vol. 45, no. 1, pp. 183–189, 2005
  43. Journal of Proteome Research, vol. 4, no. 2, pp. 564–569, 2005
  44. Journal of Proteome Research, vol. 4, no. 6, pp. 1942–1951, 2005
  45. Journal of Proteome Research, vol. 4, no. 5, pp. 1610–1618, 2005
  46. Agrin binds  -synuclein and modulates  -synuclein fibrillation
    Glycobiology, vol. 15, no. 12, pp. 1320–1331, 2005
  47. Protein dissection enhances the amyloidogenic properties of alpha-lactalbumin
    FEBS Journal, vol. 272, no. 9, pp. 2176–2188, 2005
  48. Flexible nets. The roles of intrinsic disorder in protein interaction networks
    FEBS Journal, vol. 272, no. 20, pp. 5129–5148, 2005
  49. Early Events in the Fibrillation of Monomeric Insulin
    Journal of Biological Chemistry, vol. 280, no. 52, pp. 42669–42675, 2005
  50. 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
  51. 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
  52. Stimulation of Insulin Fibrillation by Urea-induced Intermediates
    Journal of Biological Chemistry, vol. 279, no. 15, pp. 14999–15013, 2004
  53. 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
  54. Journal of Proteome Research, vol. 3, no. 3, pp. 485–494, 2004
  55. Biochemistry, vol. 43, no. 11, pp. 3289–3300, 2004
  56. Biochemistry, vol. 43, no. 19, pp. 5575–5582, 2004
  57. Biochemistry, vol. 43, no. 15, pp. 4621–4633, 2004
  58. Biochemistry, vol. 43, no. 47, pp. 14913–14923, 2004
  59. The effect of macromolecular crowding on protein aggregation and amyloid fibril formation
    Journal of Molecular Recognition, vol. 17, no. 5, pp. 456–464, 2004
  60. Rifampicin Inhibits ?-Synuclein Fibrillation and Disaggregates Fibrils
    Chemistry & Biology, vol. 11, no. 11, pp. 1513–1521, 2004
  61. 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
  62. 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
  63. Conformational Prerequisites for Formation of Amyloid Fibrils from Histones
    Journal of Molecular Biology, vol. 342, no. 4, pp. 1305–1324, 2004
  64. 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
  65. Prediction of the association state of insulin using spectral parameters
    Journal of Pharmaceutical Sciences, vol. 92, no. 4, pp. 847–858, 2003
  66. Ultraviolet illumination-induced reduction of ?-lactalbumin disulfide bridges
    Proteins: Structure, Function, and Genetics, vol. 51, no. 4, pp. 498–503, 2003
  67. 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
  68. Biochemistry, vol. 42, no. 9, pp. 2720–2730, 2003
  69. Biochemistry, vol. 42, no. 28, pp. 8465–8471, 2003
  70. Biochemistry, vol. 42, no. 26, pp. 7879–7884, 2003
  71. Biochemistry, vol. 42, no. 26, pp. 8094–8104, 2003
  72. Biochemistry, vol. 42, no. 39, pp. 11404–11416, 2003
  73. 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
  74. Journal of Proteome Research, vol. 2, no. 1, pp. 37–42, 2003
  75. Journal of Proteome Research, vol. 2, no. 1, pp. 51–57, 2003
  76. Journal of Proteome Research, vol. 2, no. 3, pp. 273–281, 2003
  77. 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
  78. Polycation-induced oligomerization and accelerated fibrillation of human alpha-synuclein in vitro
    Protein Science, vol. 12, no. 4, pp. 702–707, 2003
  79. 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
  80. Certain Metals Trigger Fibrillation of Methionine-oxidized  -Synuclein
    Journal of Biological Chemistry, vol. 278, no. 30, pp. 27630–27635, 2003
  81. 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
  82. 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
  83. Polymeric Aspects of Protein Folding: a Brief Overview
    Protein and Peptide Letters, vol. 10, no. 3, pp. 239–245, 2003
  84. 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
  85. 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
  86. 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
  87. The Saccharomyces cerevisiae Nucleoporin Nup2p Is a Natively Unfolded Protein
    Journal of Biological Chemistry, vol. 277, no. 36, pp. 33447–33455, 2002
  88. 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
  89. Natively unfolded proteins: A point where biology waits for physics
    Protein Science, vol. 11, no. 4, pp. 739–756, 2002
  90. What does it mean to be natively unfolded?
    European Journal of Biochemistry, vol. 269, no. 1, pp. 2–12, 2002
  91. Journal of Proteome Research, vol. 1, no. 2, pp. 149–159, 2002
  92. Journal of Proteome Research, vol. 1, no. 4, pp. 307–315, 2002
  93. 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
  94. The chicken–egg scenario of protein folding revisited
    FEBS Letters, vol. 515, no. 1-3, pp. 79–83, 2002
  95. Accelerated a-synuclein fibrillation in crowded milieu
    FEBS Letters, vol. 515, no. 1-3, pp. 99–103, 2002
  96. Methionine oxidation inhibits fibrillation of human a-synuclein in vitro
    FEBS Letters, vol. 517, no. 1-3, pp. 239–244, 2002
  97. Amino acid determinants of a-synuclein aggregation: putting together pieces of the puzzle
    FEBS Letters, vol. 522, no. 1-3, pp. 9–13, 2002
  98. 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
  99. 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
  100. 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
  101. 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
  102. 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
  103. Biochemistry, vol. 41, no. 5, pp. 1502–1511, 2002
  104. Biochemistry, vol. 41, no. 41, pp. 12546–12551, 2002
  105. Biochemistry, vol. 40, no. 7, pp. 2113–2128, 2001
  106. Biochemistry, vol. 40, no. 20, pp. 6036–6046, 2001
  107. Biochemistry, vol. 40, no. 20, pp. 6076–6084, 2001
  108. Biochemistry, vol. 40, no. 28, pp. 8397–8409, 2001
  109. Biochemistry, vol. 40, no. 38, pp. 11604–11613, 2001
  110. 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
  111. Denatured collapsed states in protein folding: Example of apomyoglobin
    Proteins: Structure, Function, and Genetics, vol. 44, no. 3, pp. 244–254, 2001
  112. Human Soluble Guanylate Cyclase: Functional Expression, Purification and Structural Characterization
    Archives of Biochemistry and Biophysics, vol. 388, no. 2, pp. 185–197, 2001
  113. 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
  114. Trimethylamine-N-oxide-induced folding of a-synuclein
    FEBS Letters, vol. 509, no. 1, pp. 31–35, 2001
  115. 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
  116. 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
  117. Evidence for a Partially Folded Intermediate in alpha -Synuclein Fibril Formation
    Journal of Biological Chemistry, vol. 276, no. 14, pp. 10737–10744, 2001
  118. Is Congo Red an Amyloid-specific Dye?
    Journal of Biological Chemistry, vol. 276, no. 25, pp. 22715–22721, 2001
  119. 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
  120. 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
  121. 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
  122. 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
  123. 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
  124. Why are ?natively unfolded? proteins unstructured under physiologic conditions?
    Proteins: Structure, Function, and Genetics, vol. 41, no. 3, pp. 415–427, 2000
  125. 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
  126. Structure and stability of recombinant protein depend on the extra N-terminal methionine residue: S6 permutein from direct and fusion expression systems
    Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol. 1432, no. 2, pp. 324–332, 1999
  127. Fine tuning the N-terminus of a calcium binding protein: ?-lactalbumin
    Proteins: Structure, Function, and Genetics, vol. 37, no. 1, pp. 65–72, 1999
  128. Biochemistry, vol. 38, no. 46, pp. 15352–15359, 1999
  129. Association-induced folding of globular proteins
    Proceedings of the National Academy of Sciences, vol. 95, no. 10, pp. 5480–5483, 1998
  130. Anion-induced folding of Staphylococcal nuclease: characterization of multiple equilibrium partially folded intermediates
    Journal of Molecular Biology, vol. 278, no. 4, pp. 879–894, 1998
  131. Self-association of 8-anilino-1-naphthalene-sulfonate molecules: spectroscopic characterization and application to the investigation of protein folding
    Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol. 1388, no. 1, pp. 133–142, 1998
  132. Can grafting of an octapeptide improve the structure of a de novo protein?
    FEBS Letters, vol. 425, no. 1, pp. 101–104, 1998
  133. Hyperphosphorylation induces structural modification of tau-protein
    FEBS Letters, vol. 439, no. 1-2, pp. 21–25, 1998
  134. Ligand-free form of human a-fetoprotein: evidence for the molten globule state
    FEBS Letters, vol. 410, no. 2-3, pp. 280–284, 1997
  135. S6 permutein shows that the unusual target topology is not responsible for the absence of rigid tertiary structure in de novo protein albebetin
    FEBS Letters, vol. 414, no. 2, pp. 243–246, 1997
  136. Conformational transitions provoked by organic solvents in -lactoglobulin: can a molten globule like intermediate be induced by the decrease in dielectric constant?
    Folding and Design, vol. 2, no. 3, pp. 163–172, 1997
  137. Biochemistry, vol. 36, no. 44, pp. 13638–13645, 1997
  138. Macromolecules, vol. 30, no. 24, pp. 7427–7434, 1997
  139. Biochemistry, vol. 35, no. 19, pp. 6058–6063, 1996
  140. The de novo protein with grafted biological function: transferring of interferon blast-transforming activity to albebetin
    "Protein Engineering, Design and Selection", vol. 9, no. 2, pp. 195–201, 1996
  141. All-or-none solvent-induced transitions between native, molten globule and unfolded states in globular proteins
    Folding and Design, vol. 1, no. 2, pp. 117–122, 1996
  142. Further Evidence on the Equilibrium “Pre-molten Globule State”: Four-state Guanidinium Chloride-induced Unfolding of Carbonic Anhydrase B at Low Temperature
    Journal of Molecular Biology, vol. 255, no. 1, pp. 215–228, 1996
  143. Use of fluorescence decay times of 8-ANS-protein complexes to study the conformational transitions in proteins which unfold through the molten globule state
    Biophysical Chemistry, vol. 60, no. 3, pp. 79–88, 1996
  144. 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, vol. 364, no. 2, pp. 165–167, 1995
  145. Kinetic and Equilibrium Folding Intermediates
    Philosophical Transactions of the Royal Society B: Biological Sciences, vol. 348, no. 1323, pp. 35–41, 1995
  146. Macromolecules, vol. 28, no. 22, pp. 7519–7524, 1995
  147. Biochemistry, vol. 33, no. 10, pp. 2782–2791, 1994
  148. Biochemistry, vol. 32, no. 48, pp. 13288–13298, 1993
  149. Introduction of Ca2+-binding amino-acid sequence into the T4 lysozyme
    Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol. 1162, no. 1-2, pp. 84–88, 1993
  150. 'All-or-none' mechanism of the molten globule unfolding
    FEBS Letters, vol. 314, no. 1, pp. 89–92, 1992
  151. Study of the ?molten globule? intermediate state in protein folding by a hydrophobic fluorescent probe
    Biopolymers, vol. 31, no. 1, pp. 119–128, 1991
  152. Two slow stages in refolding of bovine carbonic anhydrase B are due to proline isomerization
    Journal of Molecular Biology, vol. 213, no. 3, pp. 561–568, 1990