Main

Fields of interest:

• Intrinsically disordered proteins
• protein folding
• protein misfolding
• protein aggregation
• amyloid fibril
• partially folded protein
• protein function
• protein structure
• bioinformatics
• protein conformation diseases

Recent publications:

Uversky V.N. (2010) The mysterious unfoldome: Structureless, underappreciated, yet a vital part of any given proteome. Journal of Biomedicine and Biotechnology. Vol. 2010, Article ID 568068, DOI:10.1155/2010/568068.

Uversky V.N., Dunker A.K. (2010) Understanding protein non-folding. Biochim. Biophys. Acta - Proteins and Proteomics. 1804 (6) 1231–1264.

Xue B., Williams R.W., Oldfield C.J., Dunker A.K., Uversky V.N. (2010) Archaic chaos: Intrinsically disordered proteins in Archaea. BMC Systems Biology. 4 (Suppl. 1) S1. doi:10.1186/1752-0509-4-S1-S1

Santner A., Uversky V.N. (2010) Metalloproteomics and metal toxicology of a-synuclein. Metallomics. 2, 378–392. DOI: 10.1039/b926659c.

Turoverov K.K., Kuznetsova I.M., Uversky V.N. (2010) The protein kingdom extended: Ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation. Progress in Biophysics & Molecular Biology. 102 (2-3) 73-84. PMID: 20097220.

Xue B., Williams R.W., Oldfield C.J., Goh G.K.-M., Dunker A.K., Uversky V.N. (2010) Viral disorder or disordered viruses: Do viral proteins possess unique features? Protein and Peptide Letters. 17 (8) 932-951.

Uversky V.N. (2010) Targeting intrinsically disordered proteins in neurodegenerative and protein dysfunction diseases: Another illustration of the D2 concept. Expert Review of Proteomics. 7 (4) 543-564.

Uversky V.N. (2010) Mysterious oligomerization of the amyloidogenic proteins. FEBS Journal. 277 (14) 2940-2953.

Erkizan H.V., Uversky V.N., Toretsky J.A. (2010) Oncogenic partnerships: EWS-FLI1 protein interactions initiate key pathways of Ewing's sarcoma. Clinical Cancer Research. 16 (16) 4077-4083.

Uversky V.N. (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.