Vladimir Uversky F-4515-2011

Vladimir Uversky, PhD, DSc

Associate Professor, College of Medicine Molecular Medicine

Contact Info 12901 Bruce B. Downs Blvd. MDC07
Tampa FL 33612

Academic Email: vuversky@health.usf.edu

Academic Phone:(813) 974-5816

View My C.V.

Education

  • DSc, Biophysics, Russian Academy of Sciences, 1998
  • PhD, Biophysics, Moscow Institute of Technical Physics, 1991

Academic Philosophy

"Progress of modern science is defined by the collaboration and team-based research. Students should be prepared for the reality of team science. This goes in parallel with creativity, critical and integrative thinking, and interdisciplinarity."

Interdisciplinary and Emerging Signature Programs

  • Allergy, Immunology & Infectious Disease
  • Biomedical Engineering & Nanomedicine
  • Cancer Biology
  • Cardiovascular Sciences
  • Cellular and Molecular Biology
  • Metabolic Regulation and Disorders
  • Neurodegenerative Disease
  • Other

Research Interests

  • Our scientific interests are broadly defined as everything related to protein folding, misfolding and non-folding. However, the passion is definitely the field of protein non-folding , which is related to the discovery of intrinsically disordered proteins (IDPs), analysis of their abundance in nature, characterization of their exceptional structural and functional plasticity, understanding of their vital roles in various biological processes, and establishing their involvement in the pathogenesis of multiple human diseases. These and related aspects of IDPs are analyzed by a combination of a wide spectrum of computational, bioinformatics, and experimental approaches of modern protein biophysics. Due to the high abundance of IDPs in various proteomes, the exceptional structural and functional plasticity of these proteins, and their intimate relations to the maladies' pathogenesis, it is almost impossible to find an area of protein science where IDPs would not play a noticeable role.

Memberships

  • ASBMB (Member, 2012 - Present)
  • Biophysical Society (Member, 2006 - Present)

Recent Publications

  • Na I, DeForte S, Stojanovski BM, Ferreira GC, Uversky VN. Molecular dynamics analysis of the structural and dynamic properties of the functionally enhanced hepta-variant of mouse 5-aminolevulinate synthase. Journal of biomolecular structure & dynamics. : 1-14, 2017. http://www.ncbi.nlm.nih.gov/pubmed/27928941
  • Ghag G, Holler CJ, Taylor G, Kukar TL, Uversky VN, Rangachari V. Disulfide bonds and disorder in granulin-3: An unusual handshake between structural stability and plasticity. Protein science : a publication of the Protein Society. 26(9) : 1759-1772, 2017. http://www.ncbi.nlm.nih.gov/pubmed/28608407
  • Yacoub HA, Sadek MA, Uversky VN. On the potential of using peculiarities of the protein intrinsic disorder distribution in mitochondrial cytochrome b to identify the source of animal meats. Intrinsically disordered proteins. 5(1) : e1264350, 2017. http://www.ncbi.nlm.nih.gov/pubmed/28331777
  • Sormanni P, Piovesan D, Heller GT, Bonomi M, Kukic P, Camilloni C, Fuxreiter M, Dosztanyi Z, Pappu RV, Babu MM, Longhi S, Tompa P, Dunker AK, Uversky VN, Tosatto SC, Vendruscolo M. Simultaneous quantification of protein order and disorder. Nature chemical biology. 13(4) : 339-342, 2017. http://www.ncbi.nlm.nih.gov/pubmed/28328918
  • DeForte S, Uversky VN. Quarterly intrinsic disorder digest (April-May-June, 2014). Intrinsically disordered proteins. 5(1) : e1287505, 2017. http://www.ncbi.nlm.nih.gov/pubmed/28321370
  • Falchi M, Varricchio L, Martelli F, Marra M, Picconi O, Tafuri A, Girelli G, Uversky VN, Migliaccio AR. The Calreticulin control of human stress erythropoiesis is impaired by JAK2V617F in polycythemia vera. Experimental hematology. , 2017. http://www.ncbi.nlm.nih.gov/pubmed/28232234
  • Redington JM, Breydo L, Uversky VN. When Good Goes Awry: The Aggregation of Protein Therapeutics. Protein and peptide letters. , 2017. http://www.ncbi.nlm.nih.gov/pubmed/28190397
  • Fonin AV, Silonov SA, Sitdikova AK, Kuznetsova IM, Uversky VN, Turoverov KK. Structure and Conformational Properties of d-Glucose/d-Galactose-Binding Protein in Crowded Milieu. Molecules (Basel, Switzerland). 22(2) , 2017. http://www.ncbi.nlm.nih.gov/pubmed/28178192
  • Ferreira LA, Uversky VN, Zaslavsky BY. Effects of the Hofmeister series of sodium salts on the solvent properties of water. Physical chemistry chemical physics : PCCP. 19(7) : 5254-5261, 2017. http://www.ncbi.nlm.nih.gov/pubmed/28150000
  • Kathiriya JJ, Pathak RR, Bezginov A, Xue B, Uversky VN, Tillier ER, Davé V. Data on evolution of intrinsically disordered regions of the human kinome and contribution of FAK1 IDRs to cytoskeletal remodeling. Data in brief. 10: 315-324, 2017. http://www.ncbi.nlm.nih.gov/pubmed/28004021
  • Uversky VN, Tu YN, Nwogu O, Butler SN, Ramsamooj M, Blanck G. High-level intrinsic disorder explains the universality of CLIP binding to diverse MHC class II variants. Cellular & molecular immunology. , 2017. http://www.ncbi.nlm.nih.gov/pubmed/28757614
  • Uversky VN, El-Baky NA, El-Fakharany EM, Sabry A, Mattar EH, Uversky AV, Redwan EM. Functionality of intrinsic disorder in tumor necrosis factor-α and its receptors. The FEBS journal. , 2017. http://www.ncbi.nlm.nih.gov/pubmed/28746777
  • Palombo M, Bonucci A, Etienne E, Ciurli S, Uversky VN, Guigliarelli B, Belle V, Mileo E, Zambelli B. The relationship between folding and activity in UreG, an intrinsically disordered enzyme. Scientific reports. 7(1) : 5977, 2017. http://www.ncbi.nlm.nih.gov/pubmed/28729736
  • Novikova OD, Chistyulin DK, Khomenko VA, Sidorin EV, Kim NY, Sanina NM, Portnyagina OY, Solov'eva TF, Uversky VN, Shnyrov VL. Peculiarities of thermal denaturation of OmpF porin from Yersinia ruckeri. Molecular bioSystems. 13(9) : 1854-1862, 2017. http://www.ncbi.nlm.nih.gov/pubmed/28726924
  • Du Z, Uversky VN. Functional roles of intrinsic disorder in CRISPR-associated protein Cas9. Molecular bioSystems. 13(9) : 1770-1780, 2017. http://www.ncbi.nlm.nih.gov/pubmed/28692085
  • Baker JD, Shelton LB, Zheng D, Favretto F, Nordhues BA, Darling A, Sullivan LE, Sun Z, Solanki PK, Martin MD, Suntharalingam A, Sabbagh JJ, Becker S, Mandelkow E, Uversky VN, Zweckstetter M, Dickey CA, Koren J, Blair LJ. Human cyclophilin 40 unravels neurotoxic amyloids. PLoS biology. 15(6) : e2001336, 2017. http://www.ncbi.nlm.nih.gov/pubmed/28654636
  • DeForte S, Uversky VN. Not an exception to the rule: the functional significance of intrinsically disordered protein regions in enzymes. Molecular bioSystems. 13(3) : 463-469, 2017. http://www.ncbi.nlm.nih.gov/pubmed/28098335
  • Dentovskaya SV, Platonov ME, Svetoch TE, Kopylov PK, Kombarova TI, Ivanov SA, Shaikhutdinova RZ, Kolombet LV, Chauhan S, Ablamunits VG, Motin VL, Uversky VN, Anisimov AP. Two Isoforms of Yersinia pestis Plasminogen Activator Pla: Intraspecies Distribution, Intrinsic Disorder Propensity, and Contribution to Virulence. PloS one. 11(12) : e0168089, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27936190
  • Uversky VN, Redwan EM. Erythropoietin and co.: intrinsic structure and functional disorder. Molecular bioSystems. 13(1) : 56-72, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27833947
  • Uversky VN, Shah SP, Gritsyna Y, Hitchcock-DeGregori SE, Kostyukova AS. Systematic analysis of tropomodulin/tropomyosin interactions uncovers fine-tuned binding specificity of intrinsically disordered proteins. Journal of Molecular Recognition : JMR. 24(4) : 647-55, 2016. http://www.ncbi.nlm.nih.gov/pubmed/21584876
  • Bürgi J, Xue B, Uversky VN, van der Goot FG. Intrinsic Disorder in Transmembrane Proteins: Roles in Signaling and Topology Prediction. PloS ONE. 11(7) : e0158594, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27391701
  • Kutyshenko VP, Mikoulinskaia GV, Molochkov NV, Prokhorov DA, Taran SA, Uversky VN. Structure and dynamics of the retro-form of the bacteriophage T5 endolysin. Biochimica et Biophysica Acta. 1864(10) : 1281-1291, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27376687
  • Luna-Martínez OD, Vidal-Limón A, Villalba-Velázquez MI, Sánchez-Alcalá R, Garduño-Juárez R, Uversky VN, Becerril B. Simple approach for ranking structure determining residues. Peer J. 4: e2136, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27366642
  • Gusella GL, Teixeira A, Aberg J, Uversky VN, Mosoian A. Prothymosin-α Variants Elicit Anti-HIV-1 Response via TLR4 Dependent and Independent Pathways. PloS ONE. 11(6) : e0156486, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27310139
  • Redwan EM, El-Baky NA, Al-Hejin AM, Baeshen MN, Almehdar HA, Elsaway A, Gomaa AB, Al-Masaudi SB, Al-Fassi FA, AbuZeid IE, Uversky VN. Significant antibacterial activity and synergistic effects of camel lactoferrin with antibiotics against methicillin-resistant Staphylococcus aureus (MRSA). Research in Microbiology. 167(6) : 480-91, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27130281
  • Stepanenko OV, Roginskii DO, Stepanenko OV, Kuznetsova IM, Uversky VN, Turoverov KK. Structure and stability of recombinant bovine odorant-binding protein: I. Design and analysis of monomeric mutants. Peer J. 4: e1933, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27114880
  • Stepanenko OV, Roginskii DO, Stepanenko OV, Kuznetsova IM, Uversky VN, Turoverov KK. Structure and stability of recombinant bovine odorant-binding protein: III. Peculiarities of the wild type bOBP unfolding in crowded milieu. Peer J. 4: e1642, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27114858
  • Stepanenko OV, Roginskii DO, Stepanenko OV, Kuznetsova IM, Uversky VN, Turoverov KK. Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms. Peer J. 4: e1574, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27114857
  • Whelan JN, Reddy KD, Uversky VN, Teng MN. Functional correlations of respiratory syncytial virus proteins to intrinsic disorder. Molecular BioSystems. 12(5) : 1507-26, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27062995
  • Polanco C, Buhse T, Uversky VN. Structure and function relationships of proteins based on polar profile: a review. Acta Biochimica Polonica. 63(2) : 229-33, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27059018
  • Polanco C, Castañón-González JA, Buhse T, Uversky VN, Amkie RZ. Classifying lipoproteins based on their polar profiles. Acta Biochimica Polonica. 63(2) : 235-41, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27059017
  • Wang C, Uversky VN, Kurgan L. Disordered nucleiome: Abundance of intrinsic disorder in the DNA- and RNA-binding proteins in 1121 species from Eukaryota, Bacteria and Archaea. Proteomics. 16(10) : 1486-98, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27037624
  • Ferreira LA, da Silva NR, Wlodarczyk SR, Loureiro JA, Madeira PP, Teixeira JA, Uversky VN, Zaslavsky BY. Interrelationship between partition behavior of organic compounds and proteins in aqueous dextran-polyethylene glycol and polyethylene glycol-sodium sulfate two-phase systems. Journal of Chromatography. A. 1443: 21-5, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27016118
  • Redwan EM, Linjawi MH, Uversky VN. Looking at the carcinogenicity of human insulin analogues via the intrinsic disorder prism. Scientific Reports. 6: 23320, 2016. http://www.ncbi.nlm.nih.gov/pubmed/26983499
  • Yacoub HA, El-Hamidy SM, Mahmoud MM, Baeshen MN, Almehdar HA, Uversky VN, Redwan EM, Al-Maghrabi OA, Elazzazy AM. Biocidal activity of chicken defensin-9 against microbial pathogens. Biochemistry and Cell Biology = Biochimie et biologie cellulaire. 94(2) : 176-87, 2016. http://www.ncbi.nlm.nih.gov/pubmed/26914652
  • Stojanovski BM, Breydo L, Uversky VN, Ferreira GC. Murine erythroid 5-aminolevulinate synthase: Truncation of a disordered N-terminal extension is not detrimental for catalysis. Biochimica et Biophysica acta. 1864(5) : 441-52, 2016. http://www.ncbi.nlm.nih.gov/pubmed/26854603
  • Platonov ME, Svetoch TE, Evseeva VV, Knyazeva AI, Dentovskaya SV, Motin VL, Uversky VN, Anisimov AP. Polymorphism of the Cysteine Protease YopT from Yersinia pestis. Protein and Peptide Letters. 23(4) : 379-85, 2016. http://www.ncbi.nlm.nih.gov/pubmed/26845766
  • Reddy KD, Malipeddi J, DeForte S, Pejaver V, Radivojac P, Uversky VN, Deschenes RJ. Physicochemical sequence characteristics that influence S-palmitoylation propensity. Journal of Biomolecular Structure & Dynamics. : 1-14, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27498722
  • Javadi S, Yousefi R, Hosseinkhani S, Tamaddon AM, Uversky VN. Protective effects of carnosine on dehydroascorbate-induced structural alteration and opacity of lens crystallins: Important implications of carnosine pleiotropic functions to combat cataractogenesis. Journal of Biomolecular Structure & Dynamics. : 1-61, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27472261
  • Landau KS, Na I, Schenck RO, Uversky VN. Unfoldomics of prostate cancer: on the abundance and roles of intrinsically disordered proteins in prostate cancer. Asian Journal of Andrology. , 2016. http://www.ncbi.nlm.nih.gov/pubmed/27453073
  • Hu Q, Uversky VN, Huang M, Kang H, Xu F, Liu X, Lian L, Liang Q, Jiang H, Liu A, Zhang C, Pan-Montojo F, Zhu S. Baicalein inhibits α-synuclein oligomer formation and prevents progression of α-synuclein accumulation in a rotenone mouse model of Parkinson's disease. Biochimica et Biophysica Acta. 1862(10) : 1883-1890, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27425033
  • Na I, Meng F, Kurgan L, Uversky VN. Autophagy-related intrinsically disordered proteins in intra-nuclear compartments. Molecular BioSystems. , 2016. http://www.ncbi.nlm.nih.gov/pubmed/27377881
  • Breydo L, Kurouski D, Rasool S, Milton S, Wu JW, Uversky VN, Lednev IK, Glabe CG. Structural differences between amyloid beta oligomers. Biochemical and Biophysical Research Communications. 477(4) : 700-5, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27363332
  • Permyakov EA, Uversky VN, Permyakov SE. Interleukin-11: A Multifunctional Cytokine with Intrinsically Disordered Regions. Cell Biochemistry and Biophysics. , 2016. http://www.ncbi.nlm.nih.gov/pubmed/27334537
  • Yacoub HA, Elazzazy AM, Mahmoud MM, Baeshen MN, Al-Maghrabi OA, Alkarim S, Ahmed ES, Almehdar HA, Uversky VN. Chicken cathelicidins as potent intrinsically disordered biocides with antimicrobial activity against infectious pathogens. Developmental and Comparative Immunology. 65: 8-24, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27328070
  • Mattar EH, Almehdar HA, Uversky VN, Redwan EM. Virucidal activity of human α- and β-defensins against hepatitis C virus genotype 4. Molecular BioSystems. , 2016. http://www.ncbi.nlm.nih.gov/pubmed/27327492
  • Uversky VN. Protein intrinsic disorder-based liquid-liquid phase transitions in biological systems: Complex coacervates and membrane-less organelles. Advances in Colloid and Interface Science. , 2016. http://www.ncbi.nlm.nih.gov/pubmed/27291647
  • Permyakov EA, Permyakov SE, Breydo L, Redwan EM, Almehdar HA, Uversky VN. Disorder in Milk Proteins: α-Lactalbumin. Part C. Peculiarities of Metal Binding. Current Protein & Peptide Science. , 2016. http://www.ncbi.nlm.nih.gov/pubmed/27238572
  • Fonin AV, Uversky VN, Kuznetsova IM, Turoverov KK. [Protein Folding and Stability in the Presence of Osmolytes]. Biofizika. 61(2) : 222-30, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27192822
  • Redington JM, Breydo L, Almehdar HA, Redwan EM, Uversky VN. α-Lactalbumin: Of camels and cows. Protein and Peptide Letters. , 2016. http://www.ncbi.nlm.nih.gov/pubmed/27184498
  • Kutyshenko VP, Prokhorov DA, Mikoulinskaia GV, Molochkov NV, Paskevich SI, Uversky VN. Evidence for the residual tertiary structure in the urea-unfolded form of bacteriophage T5 endolysin. Journal of Biomolecular Structure & Dynamics. : 1-8, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27109308
  • Na I, Kong MJ, Straight S, Pinto JR, Uversky VN. Troponins, intrinsic disorder, and cardiomyopathy. Biological Chemistry. 397(8) : 731-51, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27074551
  • Ferreira LA, Breydo L, Reichardt C, Uversky VN, Zaslavsky BY. Effects of osmolytes on solvent features of water in aqueous solutions. Journal of Biomolecular Structure & Dynamics. : 1-14, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27026414
  • Zaslavsky BY, Uversky VN, Chait A. Analytical applications of partitioning in aqueous two-phase systems: Exploring protein structural changes and protein-partner interactions in vitro and in vivo by solvent interaction analysis method. Biochimica et Biophysica Acta. 1864(5) : 622-44, 2016. http://www.ncbi.nlm.nih.gov/pubmed/26923390
  • Uversky VN, Permyakov SE, Breydo L, Redwan EM, Almehdar HA, Permyakov EA. Disorder in Milk Proteins: α-Lactalbumin. Part B. A Multifunctional Whey Protein Acting as an Oligomeric Molten Globular "Oil Container" in the Anti-Tumorigenic Drugs, Liprotides. Current Protein & Peptide Science. 17(6) : 612-28, 2016. http://www.ncbi.nlm.nih.gov/pubmed/26916155
  • Uversky VN. Dancing Protein Clouds: The Strange Biology and Chaotic Physics of Intrinsically Disordered Proteins. The Journal of Biological Chemistry. 291(13) : 6681-8, 2016. http://www.ncbi.nlm.nih.gov/pubmed/26851286
  • Ferreira LA, Povarova OI, Stepanenko OV, Sulatskaya AI, Madeira PP, Kuznetsova IM, Turoverov KK, Uversky VN, Zaslavsky BY. Effects of low urea concentrations on protein-water interactions. Journal of Biomolecular Structure & Dynamics. : 1-12, 2016. http://www.ncbi.nlm.nih.gov/pubmed/26726130
  • Kazakov AS, Sokolov AS, Vologzhannikova AA, Permyakova ME, Khorn PA, Ismailov RG, Denessiouk KA, Denesyuk AI, Rastrygina VA, Baksheeva VE, Zernii EY, Zinchenko DV, Glazatov VV, Uversky VN, Mirzabekov TA, Permyakov EA, Permyakov SE. Interleukin-11 binds specific EF-hand proteins via their conserved structural motifs. Journal of Biomolecular Structure & Dynamics. : 1-14, 2016. http://www.ncbi.nlm.nih.gov/pubmed/26726132
  • Zaslavsky BY, Uversky VN, Chait A. Solvent interaction analysis as a proteomic approach to structure-based biomarker discovery and clinical diagnostics. Expert Review of Proteomics. 13(1) : 9-17, 2016. http://www.ncbi.nlm.nih.gov/pubmed/26558960
  • Meng F, Na I, Kurgan L, Uversky V, N. Compartmentalization and functionality of nuclear disorder: Intrinsic disorder and protein-protein interactions in intra-nuclear compartments. International Journal of Molecular Sciences. 17(1) : 24, 2016.
  • Kuznetsova I, M, Sulatskaya A, I, Maskevich A, A, Uversky V, N, Turoverov K, K. High fluorescence anisotropy of thioflavin T in aqueous solution results from its molecular rotor nature. Analytical Chemistry. 88(1) : 718-724, 2016.
  • Breydo L, Newland B, Zhang H, Rosser A, Werner C, Uversky V, Wang W. A hyperbranched dopa-containing peg-based polymer inhibits α-synuclein fibrillation: A simple alternative to functionalized dendrimers. Biochemical and Biophysical Research Communications. 469(4) : 830-835, 2016.
  • DeForte S, Uversky V, N. Intrinsically disordered proteins in PubMed: What can the tip of the iceberg tell us about what lies below? RSC Advances.. 6(14) : 11513-11521, 2016.
  • Ferreira L, Madeira P, P, Breydo L, Reichardt C, Uversky V, N, Zaslavsky B, Y. Role of solvent properties of aqueous media in macromolecular crowding effects. Journal of Biomolecular Structure and Dynamics. 34(1) : 92-103, 2016.
  • Kuznetsova I, M, Povarova O, I, Uversky V, N, Turoverov K, K. The native globular actin has a thermodynamically unstable, quasi-stationary structure with some elements of intrinsic disorder. FEBS Journal. 283(3) : 438-445, 2016.
  • Yan J, Dunker A, K, Uversky V, N, Kurgan L. Molecular recognition features (MoRFs) in three domains of life. Molecular BioSystems.. 12(3) : 697-710, 2016.
  • DeForte S, Uversky V, N. Resolving the ambiguity: Making sense of intrinsic disorder when PDB structures disagree. Protein Science.. 25(3) : 676-688, 2016.
  • Breydo L, Morgan D, Uversky V, N. Pseudocatalytic antiaggregation activity of antibodies: Immu-noglobulins can influence protein aggregation at substoichiometric concentrations. Molecular Neurobiology. 53(3) : 1949-1958, 2016.
  • Sales A, E, Breydo L, Porto T, S, Porto A, L, F, Uversky V, N. Hydrophobicity-dependent effects of polymers on different protein conformations. RSC Advances. 6(49) : 42971-42983, 2016.
  • Al-Jiffri O, H, Alsharif F, M, Al-Jiffri E, H, Uversky V, N. Intrinsic disorder in biomarkers of insulin resistance, hypoadiponectinemia, and endothelial dysfunction among the type 2 diabetic patients. Intrinsically Disorded Proteins. 4(1) : e1171278-92, 2016.
  • Goh G, K, M, Dunker A, K, Uversky V, N. Correlation between the flavivirus virulence and levels of intrinsic disorder in shell proteins: Protective roles vs. immune evasion. Molecular Bio-systems.. 12(6) : 1881-1891, 2016.
  • Ferreira L, Loureiro J, Gomes J, Uversky V, N, Madeira P, Zaslavsky B. Why physico-chemical properties of aqueous solutions of various compounds are linearly interrelated. Journal of Molecular Liqids. 221(9) : 116-123, 2016.
  • Lobbens E, S, Breydo L, Skamris T, Vestergaard B, Jäger A, K, Jørgensen L, Uversky V, N, van de We-ert M. Mechanistic study of the inhibitory activity of Geum urbanum extract against α-synuclein fi-brillation. Biochim. Biophys. Acta – Proteins and Proteomics. 1864(9) : 1160-1169, 2016.
  • Uversky V, N, Dunker A, K. Understanding protein non-folding. Biochim. Biophys. Acta - Proteins and Proteomics.. 1804(6) : 1231-1264, 2016.
  • Klionsky DJ Abdelmohsen K Abe A Abedin MJ Abeliovich H Acevedo Arozena A et al. Guidelines for the use and interpre-tation of assays for monitoring autophagy (3rd edition). Autophagy.. 12(1) : 1-222, 2016.
  • DeForte S, Reddy K, D, Uversky V, N. Digested disorder, issue #5: Quarterly intrinsic disorder digest (January-February-March, 2014). Intrinsically Disordered Proteins. 4(1) : 1-15, 2016.
  • Uversky V, N. Paradoxes and wonders of intrinsic disorder: Complexity of simplicity. Intrinsically Disordered Proteins.. 4(1) : 1-9, 2016.
  • Mattar E, H, Almehdar H, A, Yacoub H, A, Uversky V, N, Redwan E, M. Antimicrobial potentials and structural disorder of human and animal defensins. Cytokine and Growth Factor Reviews.. 28: 95-111, 2016.
  • Uversky V, N. (Intrinsically disordered) splice variants in the proteome: Implications for novel drug discovery. Genes & Genomics. 38(7) : 577-594, 2016.
  • Hu G, Wu Z, Wang K, Uversky V, N, Kurgan L. Untapped potential of disordered proteins in cur-rent druggable human proteome. Current Drug Targets.. 17(10) : 1198-1205, 2016.
  • Shaban H, Na I, Kislichkina AA, Dentovskaya SV, Anisimov AP, Uversky VN. Effect of natural polymorphism on structure and function of the Yersinia pestis outer membrane porin F (OmpF protein): a computational study. Journal of biomolecular structure & dynamics. : 1-16, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27593697
  • Yacoub HA, El-Hamidy SM, Mahmoud MM, Baeshen MN, Almehdar HA, Uversky VN, Redwan EM, Al-Maghrabi OA, Elazzazy AM. Corrigendum: Biocidal activity of chicken defensin-9 against microbial pathogens. Biochemistry and cell biology = Biochimie et biologie cellulaire. 94(4) : 379, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27471878
  • Kopylov PKh, Platonov ME, Ablamunits VG, Kombarova TI, Ivanov SA, Kadnikova LA, Somov AN, Dentovskaya SV, Uversky VN, Anisimov AP. Yersinia pestis Caf1 Protein: Effect of Sequence Polymorphism on Intrinsic Disorder Propensity, Serological Cross-Reactivity and Cross-Protectivity of Isoforms. PloS one. 11(9) : e0162308, 2016. http://www.ncbi.nlm.nih.gov/pubmed/27606595
  • da Silva NR, Ferreira LA, Madeira PP, Teixeira JA, Uversky VN, Zaslavsky BY. Effect of sodium chloride on solute-solvent interactions in aqueous polyethylene glycol-sodium sulfate two-phase systems. Journal of Chromatography. A. 1425: 51-61, 2015. http://www.ncbi.nlm.nih.gov/pubmed/26615710
  • DeForte S, Reddy K, D, Uversky V, N. Digested disorder, issue #4: Quarterly intrinsic disorder digest (October-November-December, 2013). Intrinsically Disordered Proteins.. 3(1) : 1-10, 2015.
  • Permyakov SE, Permyakov EA, Uversky VN. Intrinsically disordered caldesmon binds calmodulin via the "buttons on a string" mechanism. Peer J. 3: e1265, 2015. http://www.ncbi.nlm.nih.gov/pubmed/26417545
  • da Silva NR, Ferreira LA, Madeira PP, Teixeira JA, Uversky VN, Zaslavsky BY. Analysis of partitioning of organic compounds and proteins in aqueous polyethylene glycol-sodium sulfate aqueous two-phase systems in terms of solute-solvent interactions. Journal of Chromatography. A. 1415: 1-10, 2015. http://www.ncbi.nlm.nih.gov/pubmed/26342872
  • Fratz EJ, Clayton J, Hunter GA, Ducamp S, Breydo L, Uversky VN, Deybach JC, Gouya L, Puy H, Ferreira GC. Human Erythroid 5-Aminolevulinate Synthase Mutations Associated with X-Linked Protoporphyria Disrupt the Conformational Equilibrium and Enhance Product Release. Biochemistry. 54(36) : 5617-31, 2015. http://www.ncbi.nlm.nih.gov/pubmed/26300302
  • Wu Z, Hu G, Yang J, Peng Z, Uversky VN, Kurgan L. In various protein complexes, disordered protomers have large per-residue surface areas and area of protein-, DNA- and RNA-binding interfaces. FEBS letters. 589(19 Pt A) : 2561-9, 2015. http://www.ncbi.nlm.nih.gov/pubmed/26297830
  • Meng F, Badierah RA, Almehdar HA, Redwan EM, Kurgan L, Uversky VN. Unstructural biology of the Dengue virus proteins. The FEBS Journal. 282(17) : 3368-94, 2015. http://www.ncbi.nlm.nih.gov/pubmed/26096987
  • Petrovich A, Borne A, Uversky VN, Xue B. Identifying Similar Patterns of Structural Flexibility in Proteins by Disorder Prediction and Dynamic Programming. International Journal of Molecular Sciences. 16(6) : 13829-49, 2015. http://www.ncbi.nlm.nih.gov/pubmed/26086829
  • Goh GK, Dunker AK, Uversky VN. Detection of links between Ebola nucleocapsid and virulence using disorder analysis. Molecular BioSystems. 11(8) : 2337-44, 2015. http://www.ncbi.nlm.nih.gov/pubmed/26086270
  • Goh GK, Dunker AK, Uversky VN. Shell disorder, immune evasion and transmission behaviors among human and animal retroviruses. Molecular BioSystems. 11(8) : 2312-23, 2015. http://www.ncbi.nlm.nih.gov/pubmed/26080321
  • Ferreira LA, Cole JT, Reichardt C, Holland NB, Uversky VN, Zaslavsky BY. Solvent Properties of Water in Aqueous Solutions of Elastin-Like Polypeptide. International Journal of Molecular Sciences. 16(6) : 13528-47, 2015. http://www.ncbi.nlm.nih.gov/pubmed/26075870
  • Breydo L, Sales AE, Frege T, Howell MC, Zaslavsky BY, Uversky VN. Effects of Polymer Hydrophobicity on Protein Structure and Aggregation Kinetics in Crowded Milieu. Biochemistry. 54(19) : 2957-66, 2015. http://www.ncbi.nlm.nih.gov/pubmed/25919930
  • Kutyshenko VP, Beskaravayny P, Uversky VN. "In-plant" NMR: analysis of the intact plant Vesicularia dubyana by high resolution NMR spectroscopy. Molecules (Basel, Switzerland). 20(3) : 4359-68, 2015. http://www.ncbi.nlm.nih.gov/pubmed/25759953
  • Sluchanko NN, Uversky VN. Hidden disorder propensity of the N-terminal segment of universal adapter protein 14-3-3 is manifested in its monomeric form: Novel insights into protein dimerization and multifunctionality. Biochimica et Biophysica Acta. 1854(5) : 492-504, 2015. http://www.ncbi.nlm.nih.gov/pubmed/25747569
  • Breydo L, Sales AE, Ferreira L, Fedotoff O, Shevelyova MP, Permyakov SE, Kroeck KG, Permyakov EA, Zaslavsky BY, Uversky VN. Effects of osmolytes on protein-solvent interactions in crowded environment: Analyzing the effect of TMAO on proteins in crowded solutions. Archives of Biochemistry and Biophysics. 570: 66-74, 2015. http://www.ncbi.nlm.nih.gov/pubmed/25712220
  • Ferreira LA, Madeira PP, Uversky AV, Uversky VN, Zaslavsky BY. Responses of proteins to different ionic environment are linearly interrelated. Journal of Chromatography. A. 1387: 32-41, 2015. http://www.ncbi.nlm.nih.gov/pubmed/25708470
  • Polanco C, Samaniego JL, Uversky VN, Castañón-González JA, Buhse T, Leopold-Sordo M, Madero-Arteaga A, Morales-Reyes A, Tavera-Sierra L, González-Bernal JA, Arias-Estrada M. Identification of proteins associated with amyloidosis by polarity index method. Acta Biochimica Polonica. 62(1) : 41-55, 2015. http://www.ncbi.nlm.nih.gov/pubmed/25669158
  • Uversky VN. Hot, Hotter, and Hottest Trends in α-Synuclein Research. Current Protein & Peptide Science. 16(8) : 682-7, 2015. http://www.ncbi.nlm.nih.gov/pubmed/26554087
  • Uversky VN. Biophysical Methods to Investigate Intrinsically Disordered Proteins: Avoiding an "Elephant and Blind Men" Situation. Advances in Experimental Medicine and Biology. 870: 215-60, 2015. http://www.ncbi.nlm.nih.gov/pubmed/26387104
  • Uversky VN, Oldfield CJ. Pliability of protein complexes and complexity of protein pliability. FEBS letters. 589(19 Pt A) : 2431-2, 2015. http://www.ncbi.nlm.nih.gov/pubmed/26325593
  • Breydo L, Uversky VN. Structural, morphological, and functional diversity of amyloid oligomers. FEBS letters. 589(19 Pt A) : 2640-8, 2015. http://www.ncbi.nlm.nih.gov/pubmed/26188543
  • El-Baky NA, Uversky VN, Redwan EM. Human consensus interferons: Bridging the natural and artificial cytokines with intrinsic disorder. Cytokine & Growth Factor Reviews. 26(6) : 637-45, 2015. http://www.ncbi.nlm.nih.gov/pubmed/26169931
  • Uversky VN. Protein Misfolding in Lipid-Mimetic Environments. Advances in Experimental Medicine and Biology. 855: 33-66, 2015. http://www.ncbi.nlm.nih.gov/pubmed/26149925
  • Uversky VN. The multifaceted roles of intrinsic disorder in protein complexes. FEBS letters. 589(19 Pt A) : 2498-506, 2015. http://www.ncbi.nlm.nih.gov/pubmed/26073257
  • Uversky VN. Intrinsically disordered proteins and their (disordered) proteomes in neurodegenerative disorders. Frontiers in Aging Neuroscience. 7: 18, 2015. http://www.ncbi.nlm.nih.gov/pubmed/25784874
  • Almehdar HA, El-Fakharany EM, Uversky VN, Redwan EM. Disorder in milk proteins: structure, functional disorder, and biocidal potentials of lactoperoxidase. Current Protein & Peptide Science. 16(4) : 352-65, 2015. http://www.ncbi.nlm.nih.gov/pubmed/25772156
  • Redwan EM, Xue B, Almehdar HA, Uversky VN. Disorder in milk proteins: caseins, intrinsically disordered colloids. Current Protein & Peptide Science. 16(3) : 228-42, 2015. http://www.ncbi.nlm.nih.gov/pubmed/25714333
  • Uversky VN. Functional roles of transiently and intrinsically disordered regions within proteins. The FEBS journal. 282(7) : 1182-9, 2015. http://www.ncbi.nlm.nih.gov/pubmed/25631540
  • Kuznetsova IM, Zaslavsky BY, Breydo L, Turoverov KK, Uversky VN. Beyond the excluded volume effects: mechanistic complexity of the crowded milieu. Molecules (Basel, Switzerland). 20(1) : 1377-409, 2015. http://www.ncbi.nlm.nih.gov/pubmed/25594347
  • Uversky V, N, Kuznetsova I, M, Turoverov K, K, Zaslavsky B, Y. Hypothesis: Intrinsically disor-dered proteins as crucial constituents of cellular aqueous two phase systems and coacervates. FEBS Letters.. 5(1) : 15-22, 2015.
  • Peng Z, Yan J, Fan X, Mizianty M, J, Xue B, Uversky V, N, Kurgan L. Exceptionally abundant exceptions: Comprehensive characterization of intrinsic disorder in a thousand proteomes from all domains of life. Cellular and Molecular Life Sciences.. 72(1) : 137-151, 2015.
  • Portillo A, Zhang Y, Breydo L, Uversky V, N, Lyubchenko Y, L. Role of monomer arrangement in the amyloid self-assembly. Biochim. Biophys. Acta – Proteins and Proteomics.. 1854(3) : 218-228, 2015.
  • Dolan P, T, Roth A, P, Sun R, Dunker A, K, Uversky V, N, LaCount D, J. Intrinsic disorder mediates hepatitis C virus core – host cell protein interactions. Protein Science.. 24(2) : 221-235, 2015.
  • Ferreira L, Fedotoff O, Uversky V, N, Zaslavsky B, Y. Effects of osmolytes on protein-solvent in-teractions in crowded environment: Study of sucrose and trehalose effects on different proteins by solvent interaction analysis. RSC Advances.. 5(34) : 27154-27162, 2015.
  • Lopes F, C, Dobrovolska O, Guerra R, R, Broll V, Zambelli B, Musiani F, Uversky V, N, Carlini C, R, Ciurli S. Pleable biocide: Disordered nature of Jaburetox, an insectidal peptide derived from the jack bean (Canavalia ensiformis) urease. FEBS Journal. 282(6) : 1043-1064, 2015.
  • Malaney P, Uversky V, N, Dave V. Identification of intrinsically disordered regions in PTEN and delineation of its function via a network approach. Methods.. 77(78) : 69-74, 2015.
  • Frege T, Uversky V, N. Intrinsically disordered proteins in the nucleus of human cells. Biochemistry & Biophysics Reports.. 1(1) : 33-51, 2015.
  • Kutyshenko V, P, Budantsev A, Uversky V, N. Analysis of seasonal changes in plants by high-resolution NMR spectroscopy: Looking at the aqueous extracts from different plant tissues. Journal of Nature and Science.. 1(5) : e88, 2015.
  • Prokhorov D, A, Mikoulinskaia G, V, Molochkov N, V, Uversky V, N, Kutyshenko V, P. High-resolution NMR structure of a Zn+2-containing form of the bacteriophage T5 L-alanyl-D-glutamate peptidase. RSC Advances.. 5(51) : 41041-41049, 2015.
  • Dobrinski K, P, Drenberg C, D, Buttermore S, T, Mohamed M, Uversky V, N, Hoffman M, S, Nicosia S, V, Kruk P, A. Increased high mobility group protein A2/SMAD3 relates to ovarian cancer progres-sion. Journal of Gynecology Research.. 1(1) : 1-13, 2015.
  • Ferreira L, Madeira P, P, Uversky V, N, Zaslavsky B, Y. Analyzing the effects of protecting osmo-lytes on solute-water interactions by solvatochromic comparison method: I. Small organic compounds. RSC Advances. 5(74) : 59812-59822, 2015.
  • Ferreira L, Fan X, Madeira P, P, Kurgan L, Uversky V, N, Zaslavsky B, Y. Analyzing the effects of protecting osmolytes on solute-water interactions by solvatochromic comparison method: II. Small globular proteins. RSC Advances.. 5(73) : 59780-59791, 2015.
  • Redwan E, M, Almehdar H, A, EL-Fakharany E, M, Baig A, -W, K, Uversky V, N. Potential antiviral activities of camel, bovine, and human lactoperoxidases against hepatitis C virus genotype 4. RSC Advances. 5(74) : 60441-60452, 2015.
  • Suvorov A, Dukhovlinov I, Leontieva G, Kramskaya T, Koroleva I, Grabovskaya K, Fedorova E, Chernyaeva E, Klimov N, Orlov A, Uversky V, N. Chimeric protein PSPF, a potential vaccine for prevention Streptococcus pneumoniae infections. Journal of Vaccines & Vaccination.. 6(6) : 304-311, 2015.
  • Uversky V, N. Proteins without unique 3D structures: Biotechnological applications of intrinsically unstable/disordered proteins. Biotechnology Journal. 10(3) : 356-366, 2015.
  • Uversky V, N. Unreported intrinsic disorder in proteins: Disorder emergency room. Intrinsically Dis-ordered Proteins.. 3(1) : 1-15, 2015.
  • Uversky V, N. The intrinsic disorder alphabet: III. Dual personality of serine. Intrinsically Disordered Proteins. 3(1) : 1-21, 2015.
  • Povarova OI, Gagarskaia YA, Uversky VN, Kuznetsova IM, Turoverov KK. [GLOBULAR ACTIN IS THE PARTIALLY INTRINSICALLY DISORDERED PROTEIN WITH QUASI-STATIONARY STRUCTURE]. Tsitologiia. 57(7) : 467-79, 2015. http://www.ncbi.nlm.nih.gov/pubmed/26591059
  • Breydo L, Reddy KD, Piai A, Felli IC, Pierattelli R, Uversky VN. The crowd you're in with: Effects of different types of crowding agents on protein aggregation. Biochimica et Biophysica Acta. 1844(2) : 346-57, 2014. http://www.ncbi.nlm.nih.gov/pubmed/24252314
  • Kuznetsova I, M, Zaslavsky B, Y, Breydo L, Turoverov K, K, Uversky V, N. Beyond the excluded volume effects: Mechanistic complexity of crowded milieu. Molecules.. 20(1) : 1377-1409, 2014.
  • Varadi M, Kosol S, Lebrun P, Valentini E, Blackledge M, Dunker AK, Felli IC, Forman-Kay JD, Kriwacki RW, Pierattelli R, Sussman J, Svergun DI, Uversky VN, Vendruscolo M, Wishart D, Wright PE, Tompa P. pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins. Nucleic Acids Research. 42(1) : D326-35, 2014. http://www.ncbi.nlm.nih.gov/pubmed/24174539
  • Kutyshenko VP, Prokhorov DA, Molochkov NV, Sharapov MG, Kolesnikov I, Uversky VN. Dancing retro: solution structure and micelle interactions of the retro-SH3-domain, retro-SHH-'Bergerac'. Journal of Biomolecular Structure & dynamics. 32(2) : 257-72, 2014. http://www.ncbi.nlm.nih.gov/pubmed/23527530
  • Ferreira L, Fan X, Mikheeva LM, Madeira PP, Kurgan L, Uversky VN, Zaslavsky BY. Structural features important for differences in protein partitioning in aqueous dextran-polyethylene glycol two-phase systems of different ionic composition. Biochimica et Biophysica Acta. , 2014. http://www.ncbi.nlm.nih.gov/pubmed/24486798
  • Rae GM, Uversky VN, David K, Wood M. DRM1 and DRM2 expression regulation: potential role of splice variants in response to stress and environmental factors in Arabidopsis. Molecular Genetics and Genomics : MGG. , 2014. http://www.ncbi.nlm.nih.gov/pubmed/24442277
  • Uversky VN. The triple power of D³: protein intrinsic disorder in degenerative diseases. Frontiers in Bioscience (Landmark edition). 19: 181-258, 2014. http://www.ncbi.nlm.nih.gov/pubmed/24389181
  • Stojanovski BM, Breydo L, Hunter GA, Uversky VN, Ferreira GC. Catalytically active alkaline molten globular enzyme: Effect of pH and temperature on the structural integrity of 5-aminolevulinate synthase. Biochimica et Biophysica Acta. 1844(12) : 2145-54, 2014. http://www.ncbi.nlm.nih.gov/pubmed/25240868
  • Kathiriya JJ, Pathak RR, Clayman E, Xue B, Uversky VN, Davé V. Presence and utility of intrinsically disordered regions in kinases. Molecular BioSystems. 10(11) : 2876-88, 2014. http://www.ncbi.nlm.nih.gov/pubmed/25099472
  • Sun X, Greenwood DR, Templeton MD, Libich DS, McGhie TK, Xue B, Yoon M, Cui W, Kirk CA, Jones WT, Uversky VN, Rikkerink EH. The intrinsically disordered structural platform of the plant defence hub protein RPM1-interacting protein 4 provides insights into its mode of action in the host-pathogen interface and evolution of the nitrate-induced domain protein family. The FEBS Journal. 281(17) : 3955-79, 2014. http://www.ncbi.nlm.nih.gov/pubmed/25039985
  • Redwan EM, El-Fakharany EM, Uversky VN, Linjawi MH. Screening the anti infectivity potentials of native N- and C-lobes derived from the camel lactoferrin against hepatitis C virus. BMC Complementary and Alternative Medicine. 14: 219, 2014. http://www.ncbi.nlm.nih.gov/pubmed/24993815
  • Angelani CR, Curto LM, Cabanas IS, Caramelo JJ, Uversky VN, Delfino JM. Toward a common aggregation mechanism for a β-barrel protein family: insights derived from a stable dimeric species. Biochimica et Biophysica Acta. 1844(9) : 1599-607, 2014. http://www.ncbi.nlm.nih.gov/pubmed/24929115
  • Pejaver V, Hsu WL, Xin F, Dunker AK, Uversky VN, Radivojac P. The structural and functional signatures of proteins that undergo multiple events of post-translational modification. Protein Science : A publication of the Protein Society. 23(8) : 1077-93, 2014. http://www.ncbi.nlm.nih.gov/pubmed/24888500
  • Popelka H, Uversky VN, Klionsky DJ. Identification of Atg3 as an intrinsically disordered polypeptide yields insights into the molecular dynamics of autophagy-related proteins in yeast. Autophagy. 10(6) : 1093-104, 2014. http://www.ncbi.nlm.nih.gov/pubmed/24879155
  • Kovacs GG, Breydo L, Green R, Kis V, Puska G, Lőrincz P, Perju-Dumbrava L, Giera R, Pirker W, Lutz M, Lachmann I, Budka H, Uversky VN, Molnár K, László L. Intracellular processing of disease-associated α-synuclein in the human brain suggests prion-like cell-to-cell spread. Neurobiology of Disease. 69: 76-92, 2014. http://www.ncbi.nlm.nih.gov/pubmed/24878508
  • Butler CL, Lucas O, Wuchty S, Xue B, Uversky VN, White M. Identifying novel cell cycle proteins in Apicomplexa parasites through co-expression decision analysis. PloS ONE. 9(5) : e97625, 2014. http://www.ncbi.nlm.nih.gov/pubmed/24841368
  • Fan X, Xue B, Dolan PT, LaCount DJ, Kurgan L, Uversky VN. The intrinsic disorder status of the human hepatitis C virus proteome. Molecular BioSystems. 10(6) : 1345-63, 2014. http://www.ncbi.nlm.nih.gov/pubmed/24752801
  • Na I, Reddy KD, Breydo L, Xue B, Uversky VN. A putative role of the Sup35p C-terminal domain in the cytoskeleton organization during yeast mitosis. Molecular BioSystems. 10(4) : 925-40, 2014. http://www.ncbi.nlm.nih.gov/pubmed/24549315
  • Redwan EM, Uversky VN, El-Fakharany EM, Al-Mehdar H. Potential lactoferrin activity against pathogenic viruses. Comptes Rendus Biologies. 337(10) : 581-95, 2014. http://www.ncbi.nlm.nih.gov/pubmed/25282173
  • Uversky VN. Introduction to intrinsically disordered proteins (IDPs). Chemical Reviews. 114(13) : 6557-60, 2014. http://www.ncbi.nlm.nih.gov/pubmed/25004990
  • Uversky VN, Davé V, Iakoucheva LM, Malaney P, Metallo SJ, Pathak RR, Joerger AC. Pathological unfoldomics of uncontrolled chaos: intrinsically disordered proteins and human diseases. Chemical Reviews. 114(13) : 6844-79, 2014. http://www.ncbi.nlm.nih.gov/pubmed/24830552
  • Xue B, Blocquel D, Habchi J, Uversky AV, Kurgan L, Uversky VN, Longhi S. Structural disorder in viral proteins. Chemical Reviews. 114(13) : 6880-911, 2014. http://www.ncbi.nlm.nih.gov/pubmed/24823319
  • van der Lee R, Buljan M, Lang B, Weatheritt RJ, Daughdrill GW, Dunker AK, Fuxreiter M, Gough J, Gsponer J, Jones DT, Kim PM, Kriwacki RW, Oldfield CJ, Pappu RV, Tompa P, Uversky VN, Wright PE, Babu MM. Classification of intrinsically disordered regions and proteins. Chemical Reviews. 114(13) : 6589-631, 2014. http://www.ncbi.nlm.nih.gov/pubmed/24773235
  • Habchi J, Tompa P, Longhi S, Uversky VN. Introducing protein intrinsic disorder. Chemical Reviews. 114(13) : 6561-88, 2014. http://www.ncbi.nlm.nih.gov/pubmed/24739139
  • Fuxreiter M, Tóth-Petróczy Á, Kraut DA, Matouschek A, Matouschek AT, Lim RY, Xue B, Kurgan L, Uversky VN. Disordered proteinaceous machines. Chemical Reviews. 114(13) : 6806-43, 2014. http://www.ncbi.nlm.nih.gov/pubmed/24702702
  • Jakob U, Kriwacki R, Uversky VN. Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function. Chemical Reviews. 114(13) : 6779-805, 2014. http://www.ncbi.nlm.nih.gov/pubmed/24502763
  • Uversky VN. Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators. Frontiers in Molecular Biosciences. 1: 6, 2014. http://www.ncbi.nlm.nih.gov/pubmed/25988147
  • Xue B, Uversky V, N. Intrinsic disorder in proteins involved in the innate anti-viral immunity: Another flexible side of a molecular arms race. Journal of Molecular Biology.. 426(6) : 1322-1350, 2014.
  • Mizianty M, Uversky V, N, Kurgan L. Prediction of intrinsic disorder in proteins using MFDp2. Methods in Molecular Biology. 1137: 147-162, 2014.
  • Peng Z, Sakai Y, Kurgan L, Sokolowski B, Uversky V, N. Intrinsic disorder in the BK channel and its interactome. PLOS ONE. 9(4) : e94331, 2014.
  • Abramov V, Khlebnikov V, Kosarev I, Bairamova G, Vasilenko R, Suzina N, Machulin A, Sakulin V, Kulikova N, Vasilenko N, Karlyshev A, Uversky V, N, Chikindas M, Melnikov V. Probiotic properties of Lactobacillus crispatus 2029: homeostatic interaction with cervicovaginal epithelial cells and antagonistic activity to genitourinary pathogens. Probiotics Antimicrob. Proteins. 6(34) : 165-176, 2014.
  • Huang F, Oldfield C, J, Xue B, Hsu W, Meng J, Liu X, Shen L, Romero P, Uversky V, N, Dunker A, K. Improving protein order-disorder classification using charge hydropathy plots. BMC Bioinformatics (Suppl 17). 15: S4, 2014.
  • Reddy K, D, DeForte S, Uversky V, N. Digested disorder, issue #3: Quarterly intrinsic disorder digest (July-August-September, 2014). Intrinsically Disordered Proteins.. 2: e27833, 2014.
  • Xue B, Ganti K, Rabionet A, Banks L, Uversky V, N. Disordered interactome of human papillomavirus. Current Pharmaceutical Design. 20(8) : 1274-1292, 2014.
  • Povarova O, I, Uversky V, N, Kuznetsova I, M, Turoverov K, K. Actinous enigma or enigmatic actin: Folding, unfolding, misfolding, and nonfolding of most abundant eukaryotic protein. Intrinsically Disordered Proteins.. 2: e34500, 2014.
  • Uversky V, N. Unreported intrinsic disorder in proteins: Building connections to the literature on IDPs. Intrinsically Disordered Proteins.. 2: e36409, 2014.
  • Albar A, H, Almehdar H, A, Uversky V, N, Redwan E, M. Structural heterogeneity and multifunc-tionality of lactoferrin. Current Protein and Peptide Science.. 15(8) : 778-797, 2014.
  • Turoverov K, K, Kuznetsova I, M, Uversky V, N. What macromolecular crowding can do to a protein. International Journal of Molecular Sciences.. 15(12) : 23090-23140, 2014.
  • Uversky V, N, Kuznetsova I, M, Turoverov K, K, Zaslavsky B, Y. Hypothesis: Intrinsically disordered proteins as crucial constituents of cellular aqueous two phase systems and coacervates. FEBS Letters.. 589(1) : 15-22, 2014.
  • Lee C, Kalmar L, Xue B, Tompa P, Daughdrill GW, Uversky VN, Han KH. Contribution of proline to the pre-structuring tendency of transient helical secondary structure elements in intrinsically disordered proteins. Biochimica et Biophysica Acta. 1840(3) : 993-1003, 2014. http://www.ncbi.nlm.nih.gov/pubmed/24211251
  • Uversky AV, Xue B, Peng Z, Kurgan L, Uversky VN. On the intrinsic disorder status of the major players in programmed cell death pathways. F1000Research. 2: 190, 2013. http://www.ncbi.nlm.nih.gov/pubmed/24358900
  • Goh GK, Dunker AK, Uversky V. Prediction of Intrinsic Disorder in MERS-CoV/HCoV-EMC Supports a High Oral-Fecal Transmission. PLoS Currents. 5, 2013. http://www.ncbi.nlm.nih.gov/pubmed/24270586
  • Xue B, Uversky VN. Intrinsic Disorder in Proteins Involved in the Innate Antiviral Immunity: Another Flexible Side of a Molecular Arms Race. Journal of Molecular Biology. , 2013. http://www.ncbi.nlm.nih.gov/pubmed/24184279
  • Breydo L, Mikheeva LM, Madeira PP, Zaslavsky BY, Uversky VN. Solvent interaction analysis of intrinsically disordered proteins in aqueous two-phase systems. Molecular BioSystems. 9(12) : 3068-79, 2013. http://www.ncbi.nlm.nih.gov/pubmed/24072065
  • Malaney P, Uversky VN, Davé V. The PTEN Long N-tail is intrinsically disordered: increased viability for PTEN therapy. Molecular BioSystems. 9(11) : 2877-88, 2013. http://www.ncbi.nlm.nih.gov/pubmed/24056727
  • Marín M, Uversky VN, Ott T. Intrinsic disorder in pathogen effectors: protein flexibility as an evolutionary hallmark in a molecular arms race. The Plant Cell. 25(9) : 3153-7, 2013. http://www.ncbi.nlm.nih.gov/pubmed/24038649
  • Na I, Redmon D, Kopa M, Qin Y, Xue B, Uversky VN. Ordered disorder of the astrocytic dystrophin-associated protein complex in the norm and pathology. PloS ONE. 8(8) : e73476, 2013. http://www.ncbi.nlm.nih.gov/pubmed/24014171
  • Blair LJ, Nordhues BA, Hill SE, Scaglione KM, O'Leary JC, Fontaine SN, Breydo L, Zhang B, Li P, Wang L, Cotman C, Paulson HL, Muschol M, Uversky VN, Klengel T, Binder EB, Kayed R, Golde TE, Berchtold N, Dickey CA. Accelerated neurodegeneration through chaperone-mediated oligomerization of tau. The Journal of Clinical Investigation. 123(10) : 4158-69, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23999428
  • Peng Z, Oldfield CJ, Xue B, Mizianty MJ, Dunker AK, Kurgan L, Uversky VN. A creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome. Cellular and Molecular Life Sciences : CMLS. , 2013. http://www.ncbi.nlm.nih.gov/pubmed/23942625
  • Ferreira L, Madeira PP, Mikheeva L, Uversky VN, Zaslavsky B. Effect of salt additives on protein partition in polyethylene glycol-sodium sulfate aqueous two-phase systems. Biochimica et Biophysica Acta. 1834(12) : 2859-66, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23920121
  • Uversky VN. The UBE2E proteins as conjugating dispersers: extending function with extended extensions. Journal of Molecular Biology. 425(22) : 4067-70, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23871835
  • Kutyshenko VP, Beskaravayny PM, Molchanov MV, Paskevich SI, Prokhorov DA, Uversky VN. Looking at microbial metabolism by high-resolution (2)H-NMR spectroscopy. PeerJ. 1: e101, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23862103
  • Shivu B, Seshadri S, Li J, Oberg KA, Uversky VN, Fink AL. Distinct β-sheet structure in protein aggregates determined by ATR-FTIR spectroscopy. Biochemistry. 52(31) : 5176-83, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23837615
  • Malaney P, Pathak RR, Xue B, Uversky VN, Davé V. Intrinsic disorder in PTEN and its interactome confers structural plasticity and functional versatility. Scientific Reports. 3: 2035, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23783762
  • Choi UB, Kazi R, Stenzoski N, Wollmuth LP, Uversky VN, Bowen ME. Modulating the intrinsic disorder in the cytoplasmic domain alters the biological activity of the N-methyl-D-aspartate-sensitive glutamate receptor. The Journal of Biological Chemistry. 288(31) : 22506-15, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23782697
  • Madeira PP, Bessa A, Alvares-Ribeiro L, Raquel Aires-Barros M, Rodrigues AE, Uversky VN, Zaslavsky BY. Amino acid/water interactions study: a new amino acid scale. Journal of Biomolecular Structure & Dynamics. , 2013. http://www.ncbi.nlm.nih.gov/pubmed/23781980
  • Peng Z, Xue B, Kurgan L, Uversky VN. Resilience of death: intrinsic disorder in proteins involved in the programmed cell death. Cell Death and Differentiation. 20(9) : 1257-67, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23764774
  • Bhat-Nakshatri P, Song EK, Collins NR, Uversky VN, Dunker AK, O'Malley BW, Geistlinger TR, Carroll JS, Brown M, Nakshatri H. Interplay between estrogen receptor and AKT in estradiol-induced alternative splicing. BMC Medical Genomics. 6: 21, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23758675
  • Uversky VN. Under-folded proteins: Conformational ensembles and their roles in protein folding, function, and pathogenesis. Biopolymers. 99(11) : 870-87, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23754493
  • Yan J, Mizianty MJ, Filipow PL, Uversky VN, Kurgan L. RAPID: fast and accurate sequence-based prediction of intrinsic disorder content on proteomic scale. Biochimica et Biophysica Acta. 1834(8) : 1671-80, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23732563
  • Xue B, Ganti K, Rabionet A, Banks L, Uversky VN. Disordered Interactome of Human Papillomavirus. Current Pharmaceutical Design. , 2013. http://www.ncbi.nlm.nih.gov/pubmed/23713779
  • Uversky VN. The most important thing is the tail: multitudinous functionalities of intrinsically disordered protein termini. FEBS Letters. 587(13) : 1891-901, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23665034
  • Coelho Ribeiro Mde L, Espinosa J, Islam S, Martinez O, Thanki JJ, Mazariegos S, Nguyen T, Larina M, Xue B, Uversky VN. Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerevisiae spliceosome. PeerJ. 1: e2, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23638354
  • Lapteva YS, Uversky VN, Permyakov SE. Sequence microheterogeneity of parvalbumin, the major fish allergen. Biochimica et Biophysica Acta. 1834(8) : 1607-14, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23632315
  • Xue B, Romero PR, Noutsou M, Maurice MM, Rüdiger SG, William AM, Mizianty MJ, Kurgan L, Uversky VN, Dunker AK. Stochastic machines as a colocalization mechanism for scaffold protein function. FEBS Letters. 587(11) : 1587-91, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23603389
  • Uversky VN. A decade and a half of protein intrinsic disorder: biology still waits for physics. Protein Science : A publication of the Protein Society. 22(6) : 693-724, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23553817
  • Wood M, Rae GM, Wu RM, Walton EF, Xue B, Hellens RP, Uversky VN. Actinidia DRM1--an intrinsically disordered protein whose mRNA expression is inversely correlated with spring budbreak in kiwifruit. PloS ONE. 8(3) : e57354, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23516402
  • Uversky VN. MultIDIMensionality of IDIMs: intrinsic disorder in autoinhibition. Structure (London, England : 1993). 21(3) : 315-6, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23473663
  • Ortiz JF, MacDonald ML, Masterson P, Uversky VN, Siltberg-Liberles J. Rapid evolutionary dynamics of structural disorder as a potential driving force for biological divergence in flaviviruses. Genome Biology and Evolution. 5(3) : 504-13, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23418179
  • Xue B, Jeffers V, Sullivan WJ, Uversky VN. Protein intrinsic disorder in the acetylome of intracellular and extracellular Toxoplasma gondii. Molecular BioSystems. 9(4) : 645-57, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23403842
  • Sun X, Rikkerink EH, Jones WT, Uversky VN. Multifarious roles of intrinsic disorder in proteins illustrate its broad impact on plant biology. The Plant Cell. 25(1) : 38-55, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23362206
  • Uversky VN, Dunker AK. The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure. F1000 Biology Reports. 5: 1, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23361308
  • Xue B, Brown CJ, Dunker AK, Uversky VN. Intrinsically disordered regions of p53 family are highly diversified in evolution. Biochimica et Biophysica Acta. 1834(4) : 725-38, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23352836
  • Moroz NA, Novak SM, Azevedo R, Colpan M, Uversky VN, Gregorio CC, Kostyukova AS. Alteration of tropomyosin-binding properties of tropomodulin-1 affects its capping ability and localization in skeletal myocytes. The Journal of Biological Chemistry. 288(7) : 4899-907, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23271735
  • Jinwal UK, Akoury E, Abisambra JF, O'Leary JC, Thompson AD, Blair LJ, Jin Y, Bacon J, Nordhues BA, Cockman M, Zhang J, Li P, Zhang B, Borysov S, Uversky VN, Biernat J, Mandelkow E, Gestwicki JE, Zweckstetter M, Dickey CA. Imbalance of Hsp70 family variants fosters tau accumulation. FASEB Journal : Official publication of the Federation of American Societies for Experimental Biology. 27(4) : 1450-9, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23271055
  • Uversky VN. Unusual biophysics of intrinsically disordered proteins. Biochimica et Biophysica Acta. 1834(5) : 932-51, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23269364
  • Hsu WL, Oldfield CJ, Xue B, Meng J, Huang F, Romero P, Uversky VN, Dunker AK. Exploring the binding diversity of intrinsically disordered proteins involved in one-to-many binding. Protein Science : A publication of the Protein Society. 22(3) : 258-73, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23233352
  • Oldfield CJ, Xue B, Van YY, Ulrich EL, Markley JL, Dunker AK, Uversky VN. Utilization of protein intrinsic disorder knowledge in structural proteomics. Biochimica et Biophysica Acta. 1834(2) : 487-98, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23232152
  • Oates ME, Romero P, Ishida T, Ghalwash M, Mizianty MJ, Xue B, Dosztányi Z, Uversky VN, Obradovic Z, Kurgan L, Dunker AK, Gough J. D²P²: database of disordered protein predictions. Nucleic acids research. 41(Database issue) : D508-16, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23203878
  • Zaslavsky A, Madeira P, Breydo L, Uversky VN, Chait A, Zaslavsky B. High throughput characterization of structural differences between closely related proteins in solution. Biochimica et Biophysica Acta. 1834(2) : 583-92, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23174655
  • Uversky VN. Intrinsic disorder-based protein interactions and their modulators. Current Pharmaceutical Design. 19(23) : 4191-213, 2013. http://www.ncbi.nlm.nih.gov/pubmed/23170892
  • Silva BA, Breydo L, Uversky VN. Targeting the chameleon: a focused look at α-synuclein and its roles in neurodegeneration. Molecular Neurobiology. 47(2) : 446-59, 2013. http://www.ncbi.nlm.nih.gov/pubmed/22940885
  • Silva BA, Breydo L, Fink AL, Uversky VN. Agrochemicals, α-synuclein, and Parkinson's disease. Molecular Neurobiology. 47(2) : 598-612, 2013. http://www.ncbi.nlm.nih.gov/pubmed/22933040
  • Ribeiro M, C, Espinosa J, Islam S, Martinez O, Thanki J, J, Mazariegos S, Nguyen T, Larina M, Xue B, Uversky V, N. Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerivisiae spliceosome. PeerJ. 1: e2, 2013.
  • Azia A, Uversky V, N, Horovitz A, Unger R. The effects of mutations on protein function: A comparative study of three databases of mutations in humans. Israel Journal of Chemistry.. 53(3) : 217-226, 2013.
  • Xue B, Uversky V, N. Structural characterizations of phosphorylatable residues in trans-membrane proteins from Arabidopsis thaliana. Intrinsically Disordered Proteins. 1(1) : e25713, 2013.
  • Williams R, W, Xue B, Uversky V, N, Dunker A, K. Distribution and cluster analysis of predicted intrinsically disordered protein Pfam domains. Intrinsically Disordered Proteins.. 1(1) : e25724, 2013.
  • Uversky V, N. Hypothesis: The unfolding power of protein dielectricity. Intrinsically Disordered Proteins. 1(1) : e25725, 2013.
  • Uversky A, V, Xue B, Peng Z, Kurgan L, Uversky V, N. On The Intrinsic Disorder Status Of The Major Players In The Programmed Cell Death Pathways. F1000research.. 2: 190, 2013.
  • Silva B, A, Einarsdottir O, Fink A, L, Uversky V, N. Biophysical Characterization Of α-Synuclein And Rotenone Interaction. Biomolecules.. 3(3) : 703-732, 2013.
  • Silva B, A, Breydo L, Uversky V, N. Targeting the chameleon: A focused look at α-synuclein and its roles in neurodegeneration. Molecular Neurobiology.. 47(2) : 446-459, 2013.
  • Silva B, A, Breydo L, Fink A, L, Uversky V, N. Agrochemicals, α-synuclein, and Parkinson’s disease. Molecular Neurobiology. 47(2) : 598-612, 2013.
  • Dunker A, K, Babu M, Barbar E, Blackledge M, Bondos S, E, Dosztányi Z, Dyson H, J, Forman-Kay J, Fuxreiter M, Gsponer J, Han K, -H, Jones D, T, Longhi S, Metallo S, J, Nishikawa K, Nussinov R, Obradovic Z, Pappu R, Rost B, Selenko P, Subramaniam V, Sussman J, L, Tompa P, Uversky V, N. What’s in a name? Why these proteins are intrinsically disordered. Intrinsically Disordered Proteins.. 1(1) : e24157, 2013.
  • Theillet F, -X, Kalmar L, Tompa P, Han K, -H, Dunker A, K, Selenko P, A, K, Dunker Daughdrill G, W, Uversky V, N. The alphabet of intrinsic disorder. I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins. Intrinsically Disordered Proteins.. 1(1) : e24360, 2013.
  • Uversky V, N. Unusual biophysics of intrinsically disordered proteins. Biochim. Biophys. Acta Proteins and Proteomics. 1834(5) : 932-951, 2013.
  • Uversky V, N. The alphabet of intrinsic disorder. II. Various roles of glutamic acids in ordered and intrinsically disordered proteins. Intrinsically Disordered Proteins.. 1(1) : e24684, 2013.
  • Uversky V, N. Intrinsic disorder-based protein interactions and their modulators. Pharmaceutical Design. 42(23) : 4191-4213, 2013.
  • Testa L, Brocca S, Santambrogio C, D’Urzo A, Habchi J, Longhi S, Uversky V, N, Grandori R. Extracting structural information from charge-state distributions of intrinsically disordered proteins by non-denaturing electrospray-ionization mass spectrometry. Intrinsically Disordered Proteins.. 1(1) : e25068, 2013.
  • Uversky V, N. Digested disorder: Quarterly intrinsic disorder digest (January/February/ March, 2013) Intrinsically Disordered Proteins.. 1(1) : e25496, 2013.
  • Hedlund R, Uversky V, N. Understanding the molecular mechanisms underlying complex cancer genome rearrangements. Intrinsically Disordered Proteins.. 1(2) : e25954, 2013.
  • Hedlund R, Uversky V, N. Understanding the molecular mechanisms underlying complex cancer genome rearrangements. Intrinsically Disordered Proteins.. 1(2) : e25954, 2013.
  • Uversky V, N. Disorder in the lifetime of a protein. Intrinsically Disordered Proteins. : e26782, 2013.
  • DeForte S, Reddy K, D, Uversky V, N. Digested disorder, issue #2: Quarterly intrinsic disorder digest (April-May-June, 2013). Intrinsically Disordered Proteins. 1(1) : e27454, 2013.
  • Permyakov E, A, Uversky V, N. The use of protein engineering methods for studies of calcium binding proteins. Proteomics Research Journal.. 4: 1-2, 2013.
  • Xue B, Oldfield C, J, Van Y, Y, Dunker A, K, Uversky V, N. Protein intrinsic disorder and induced pluripotent stem cells. Molecular BioSystems.. 8(1) : 134-150, 2012.
  • Uversky VN, Dunker AK. Multiparametric analysis of intrinsically disordered proteins: looking at intrinsic disorder through compound eyes. Analytical Chemistry. 84(5) : 2096-104, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22242801
  • Hsu W, -L, Oldfield C, J, Meng J, Huang F, Xue B, Uversky V, N, Romero P, Dunker A, K. Intrinsic protein disorder and protein-protein interactions. Pacific Symposium on Biocomputing. : 116-127, 2012.
  • Huang F, Oldfield C, J, Meng J, Hsu W, -L, Xue B, Uversky V, N, Romero P, Dunker A, K. Subclassifying disordered proteins by the CH-CDF plot method. Pacific Symposium on Biocomputing.. : 128-139, 2012.
  • Melnik B, S, Povarnitsyna T, V, Glukhov A, S, Melnik T, N, Uversky V, N. SS-stabilizing proteins rationally: Intrinsic disorder-based design of stabilizing disulphide bridges in GFP. Journal of Biomolecular Structure and Dynamics.. 29(4) : 817-824, 2012.
  • Uversky V, N, Santambrogio C, Brocca S, Grandori R. Length-dependent compaction of intrinsically disordered proteins. FEBS Letters.. 586(1) : 70-73, 2012.
  • Howell M, Green R, Killeen A, Wedderburn L, Picascio V, Rabionet A, Peng Z, Mizianty M, J, Larina M, Xue B, Kurgan L, Uversky V, N. Not that rigid midgets and not so flexible giants: On the abundance and roles of intrinsic disorder in short and long proteins. Journal of Biological Systems.. 20(4) : 471-511, 2012.
  • Westerheide S, D, Raynes R, Powell C, Xue B, Uversky V, N. HSF transcription factor family, heat shock response, and protein intrinsic disorder. Current Protein and Peptide Science.. 13(1) : 86-103, 2012.
  • Xue B, Mizianty M, Kurgan L, Uversky V, N. Protein intrinsic disorder as flexible armor and weapon of HIV-1. Cellular and Molecular Life Sciences.. 69(8) : 1211-1259, 2012.
  • Kirilyuk A, Shimoji M, Catania J, Sahu G, Pattabiraman N, Giordano A, Albanese C, Mocchetti I, Toretsky JA, Uversky VN, Avantaggiati ML. An intrinsically disordered region of the acetyltransferase p300 with similarity to prion-like domains plays a role in aggregation. PloS ONE. 7(11) : e48243, 2012. http://www.ncbi.nlm.nih.gov/pubmed/23133622
  • Goh GK, Dunker AK, Uversky VN. Understanding Viral Transmission Behavior via Protein Intrinsic Disorder Prediction: Coronaviruses. Journal of Pathogens. 2012: 738590, 2012. http://www.ncbi.nlm.nih.gov/pubmed/23097708
  • Vacic V, Markwick PR, Oldfield CJ, Zhao X, Haynes C, Uversky VN, Iakoucheva LM. Disease-associated mutations disrupt functionally important regions of intrinsic protein disorder. PLoS Computational Biology. 8(10) : e1002709, 2012. http://www.ncbi.nlm.nih.gov/pubmed/23055912
  • Santner AA, Croy CH, Vasanwala FH, Uversky VN, Van YY, Dunker AK. Sweeping away protein aggregation with entropic bristles: intrinsically disordered protein fusions enhance soluble expression. Biochemistry. 51(37) : 7250-62, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22924672
  • Xue B, Dunker AK, Uversky VN. Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life. Journal of Biomolecular Structure & Dynamics. 30(2) : 137-49, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22702725
  • Disfani FM, Hsu WL, Mizianty MJ, Oldfield CJ, Xue B, Dunker AK, Uversky VN, Kurgan L. MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins. Bioinformatics (Oxford, England). 28(12) : i75-83, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22689782
  • Hervás R, Oroz J, Galera-Prat A, Goñi O, Valbuena A, Vera AM, Gómez-Sicilia A, Losada-Urzáiz F, Uversky VN, Menéndez M, Laurents DV, Bruix M, Carrión-Vázquez M. Common features at the start of the neurodegeneration cascade. PLoS Biology. 10(5) : e1001335, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22666178
  • Johnson DE, Xue B, Sickmeier MD, Meng J, Cortese MS, Oldfield CJ, Le Gall T, Dunker AK, Uversky VN. High-throughput characterization of intrinsic disorder in proteins from the Protein Structure Initiative. Journal of Structural Biology. 180(1) : 201-15, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22651963
  • Kuznetsova IM, Sulatskaya AI, Uversky VN, Turoverov KK. A new trend in the experimental methodology for the analysis of the thioflavin T binding to amyloid fibrils. Molecular Neurobiology. 45(3) : 488-98, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22592269
  • Ahmadi Adl A, Nowzari-Dalini A, Xue B, Uversky VN, Qian X. Accurate prediction of protein structural classes using functional domains and predicted secondary structure sequences. Journal of Biomolecular Structure & Dynamics. 29(6) : 623-33, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22545993
  • Peng Z, Mizianty MJ, Xue B, Kurgan L, Uversky VN. More than just tails: intrinsic disorder in histone proteins. Molecular BioSystems. 8(7) : 1886-901, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22543956
  • Xu K, Uversky VN, Xue B. Local flexibility facilitates oxidization of buried methionine residues. Protein and Peptide Letters. 19(6) : 688-97, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22519542
  • Sikirzhytski V, Topilina NI, Takor GA, Higashiya S, Welch JT, Uversky VN, Lednev IK. Fibrillation mechanism of a model intrinsically disordered protein revealed by 2D correlation deep UV resonance Raman spectroscopy. Biomacromolecules. 13(5) : 1503-9, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22515261
  • Singh VK, Rahman MN, Munro K, Uversky VN, Smith SP, Jia Z. Free cysteine modulates the conformation of human C/EBP homologous protein. PloS ONE. 7(4) : e34680, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22496840
  • Tipparaju SM, Li XP, Kilfoil PJ, Xue B, Uversky VN, Bhatnagar A, Barski OA. Interactions between the C-terminus of Kv1.5 and Kvβ regulate pyridine nucleotide-dependent changes in channel gating. Pflügers Archiv : European journal of physiology. 463(6) : 799-818, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22426702
  • Kuznetsova IM, Sulatskaya AI, Uversky VN, Turoverov KK. Analyzing thioflavin T binding to amyloid fibrils by an equilibrium microdialysis-based technique. PloS ONE. 7(2) : e30724, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22383971
  • Fedotoff O, Mikheeva LM, Chait A, Uversky VN, Zaslavsky BY. Influence of serum proteins on conformation of prostate-specific antigen. Journal of Biomolecular Structure & Dynamics. 29(5) : 1051-64, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22292959
  • Xue B, Dunker AK, Uversky VN. The roles of intrinsic disorder in orchestrating the Wnt-pathway. Journal of Biomolecular Structure & Dynamics. 29(5) : 843-61, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22292947
  • Ahmad A, Burns CS, Fink AL, Uversky VN. Peculiarities of copper binding to alpha-synuclein. Journal of Biomolecular Structure & Dynamics. 29(4) : 825-42, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22208282
  • Zhang T, Faraggi E, Xue B, Dunker AK, Uversky VN, Zhou Y. SPINE-D: accurate prediction of short and long disordered regions by a single neural-network based method. Journal of Biomolecular Structure & Dynamics. 29(4) : 799-813, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22208280
  • Breydo L, Wu JW, Uversky VN. Α-synuclein misfolding and Parkinson's disease. Biochimica et Biophysica Acta. 1822(2) : 261-85, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22024360
  • Uversky VN. Intrinsically disordered proteins and novel strategies for drug discovery. Expert Opinion on Drug Discovery. 7(6) : 475-88, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22559227
  • Uversky VN. Editorial: intrinsically disordered proteins: a focused look at fuzzy subjects. Current Protein & Peptide Science. 13(1) : 2-5, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22455660
  • Uversky VN. Disordered competitive recruiter: fast and foldable. Journal of Molecular Biology. 418(5) : 267-8, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22381408
  • Liu J, Li S, Dunker AK, Uversky VN. Molecular profiling: an essential technology enabling personalized medicine in breast cancer. Current Drug Targets. 13(4) : 541-54, 2012. http://www.ncbi.nlm.nih.gov/pubmed/22250651
  • Zambelli B, Cremades N, Neyroz P, Turano P, Uversky V, N, Ciurli S. Insights in the (un)structural organization of Bacillus pasteurii UreG, an intrinsically disordered GTPase enzyme. Molecular BioSystems.. 8(1) : 220-228, 2012.
  • Hong D, -P, Han S, Fink A, L, Uversky V, N. Characterization of the non-fibrillar α-synuclein oligomers. Protein and Peptide Letters.. 18(3) : 230-240, 2011.
  • Silva B, A, Einarsdottir O, Fink A, L, Uversky V, N. Modulating α-sinuclein misfolding and fibrillation in vitro by agrochemicals. Research and Reports in Biology.. 2: 43-56, 2011.
  • Sigalov A, S, Uversky V, N. Protein disorder differentially occurs in the cytoplasmic signaling domains of cell receptors. Self/Nonself.. 2(1) : 55-72, 2011.
  • Uversky VN. Flexible nets of malleable guardians: intrinsically disordered chaperones in neurodegenerative diseases. Chemical Reviews. 111(2) : 1134-66, 2011. http://www.ncbi.nlm.nih.gov/pubmed/21086986
  • Uversky VN. Multitude of binding modes attainable by intrinsically disordered proteins: a portrait gallery of disorder-based complexes. Chemical Society Reviews. 40(3) : 1623-34, 2011. http://www.ncbi.nlm.nih.gov/pubmed/21049125
  • Kutyshenko VP, Molchanov M, Beskaravayny P, Uversky VN, Timchenko MA. Analyzing and mapping sweat metabolomics by high-resolution NMR spectroscopy. PloS ONE. 6(12) : e28824, 2011. http://www.ncbi.nlm.nih.gov/pubmed/22194922
  • Peysselon F, Xue B, Uversky VN, Ricard-Blum S. Intrinsic disorder of the extracellular matrix. Molecular BioSystems. 7(12) : 3353-65, 2011. http://www.ncbi.nlm.nih.gov/pubmed/22009114
  • Liu J, Jolly RA, Smith AT, Searfoss GH, Goldstein KM, Uversky VN, Dunker K, Li S, Thomas CE, Wei T. Predictive Power Estimation Algorithm (PPEA)--a new algorithm to reduce overfitting for genomic biomarker discovery. PloS ONE. 6(9) : e24233, 2011. http://www.ncbi.nlm.nih.gov/pubmed/21935387
  • Melnik TN, Povarnitsyna TV, Glukhov AS, Uversky VN, Melnik BS. Sequential melting of two hydrophobic clusters within the green fluorescent protein GFP-cycle3. Biochemistry. 50(36) : 7735-44, 2011. http://www.ncbi.nlm.nih.gov/pubmed/21823681
  • Melnik BS, Molochkov NV, Prokhorov DA, Uversky VN, Kutyshenko VP. Molecular mechanisms of the anomalous thermal aggregation of green fluorescent protein. Biochimica et Biophysica Acta. 1814(12) : 1930-9, 2011. http://www.ncbi.nlm.nih.gov/pubmed/21816236
  • Xue B, Soeria-Atmadja D, Gustafsson MG, Hammerling U, Dunker AK, Uversky VN. Abundance and functional roles of intrinsic disorder in allergenic proteins and allergen representative peptides. Proteins. 79(9) : 2595-606, 2011. http://www.ncbi.nlm.nih.gov/pubmed/21732419
  • Sun X, Xue B, Jones WT, Rikkerink E, Dunker AK, Uversky VN. A functionally required unfoldome from the plant kingdom: intrinsically disordered N-terminal domains of GRAS proteins are involved in molecular recognition during plant development. Plant Molecular Biology. 77(3) : 205-23, 2011. http://www.ncbi.nlm.nih.gov/pubmed/21732203
  • Mizianty MJ, Zhang T, Xue B, Zhou Y, Dunker AK, Uversky VN, Kurgan L. In-silico prediction of disorder content using hybrid sequence representation. BMC Bioinformatics. 12: 245, 2011. http://www.ncbi.nlm.nih.gov/pubmed/21682902
  • Permyakov SE, Ismailov RG, Xue B, Denesyuk AI, Uversky VN, Permyakov EA. Intrinsic disorder in S100 proteins. Molecular BioSystems. 7(7) : 2164-80, 2011. http://www.ncbi.nlm.nih.gov/pubmed/21528128
  • Rochman M, Taher L, Kurahashi T, Cherukuri S, Uversky VN, Landsman D, Ovcharenko I, Bustin M. Effects of HMGN variants on the cellular transcription profile. Nucleic Acids Research. 39(10) : 4076-87, 2011. http://www.ncbi.nlm.nih.gov/pubmed/21278158
  • Breydo L, Uversky VN. Role of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases. Metallomics : Integrated biometal science. 3(11) : 1163-80, 2011. http://www.ncbi.nlm.nih.gov/pubmed/21869995
  • Uversky VN. Intrinsically disordered proteins from A to Z. The International Journal of Biochemistry & Cell Biology. 43(8) : 1090-103, 2011. http://www.ncbi.nlm.nih.gov/pubmed/21501695
  • Uversky VN. Intrinsically disordered proteins may escape unwanted interactions via functional misfolding. Biochimica et Biophysica Acta. 1814(5) : 693-712, 2011. http://www.ncbi.nlm.nih.gov/pubmed/21440685
  • Dixon S, E, Bhatti M, M, Uversky V, N, Dunker A, K, Sullivan W, J, Jr. 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, 2011.
  • Uversky V, N. The mysterious unfoldome: Structureless, underappreciated, yet a vital part of any given proteome. Journal of Biomedicine and Biotechnology.. 2010, 2010.
  • Yamada Y, Phillips J, L, Patel S, Goldfien G, Calestagne-Morelli A, Huang H, Reza R, Acheson J, Krishnan V, V, Newsam S, Gopinathan A, Lau E, Y, Colvin M, E, Uversky V, N, Rexach M, F. Distinct categories of natively unfolded structures with separate functions in FG nucleoporins. Molecular and Cellular Proteomics.. 9(10) : 2205-2224, 2010.
  • Turoverov K, K, Kuznetsova I, M, Uversky V, N. Protein kingdom extended: Ordered and intrinsically disordered proteins, their folding, non-folding, supramolecular complex formation and aggregation. Progress in Biophysics & Molecular Biology.. 102(23) : 73-84, 2010.
  • Xue B, Williams R, W, Oldfield C, J, Goh G, K, -M, Dunker A, K, Uversky V, N. Viral disorder or disordered viruses: Do viral proteins possess unique features? Protein and Peptide Letters.. 17(8) : 932-951, 2010.
  • Uversky V, N. Mysterious oligomerization of the amyloidogenic proteins. FEBS Journal. 277(14) : 2940-2953, 2010.
  • Xue B, Dunker AK, Uversky VN. Retro-MoRFs: identifying protein binding sites by normal and reverse alignment and intrinsic disorder prediction. International Journal of Molecular Sciences. 11(10) : 3725-47, 2010. http://www.ncbi.nlm.nih.gov/pubmed/21152297
  • Sulatskaya AI, Maskevich AA, Kuznetsova IM, Uversky VN, Turoverov KK. Fluorescence quantum yield of thioflavin T in rigid isotropic solution and incorporated into the amyloid fibrils. PloS ONE. 5(10) : e15385, 2010. http://www.ncbi.nlm.nih.gov/pubmed/21048945
  • Permyakov SE, Khokhlova TI, Uversky VN, Permyakov EA. Analysis of Ca2+/Mg2+ selectivity in alpha-lactalbumin and Ca(2+)-binding lysozyme reveals a distinct Mg(2+)-specific site in lysozyme. Proteins. 78(12) : 2609-24, 2010. http://www.ncbi.nlm.nih.gov/pubmed/20602456
  • Jorda J, Xue B, Uversky VN, Kajava AV. Protein tandem repeats - the more perfect, the less structured. The FEBS Journal. 277(12) : 2673-82, 2010. http://www.ncbi.nlm.nih.gov/pubmed/20553501
  • Xue B, Williams RW, Oldfield CJ, Dunker AK, Uversky VN. Archaic chaos: intrinsically disordered proteins in Archaea. BMC systems biology. 4 Suppl 1: S1, 2010. http://www.ncbi.nlm.nih.gov/pubmed/20522251
  • Dagkessamanskaia A, Durand F, Uversky VN, Binda M, Lopez F, El Azzouzi K, Francois JM, Martin-Yken H. Functional dissection of an intrinsically disordered protein: understanding the roles of different domains of Knr4 protein in protein-protein interactions. Protein Science : A publication of the Protein Society. 19(7) : 1376-85, 2010. http://www.ncbi.nlm.nih.gov/pubmed/20506404
  • Xue B, Hsu WL, Lee JH, Lu H, Dunker AK, Uversky VN. SPA: Short peptide analyzer of intrinsic disorder status of short peptides. Genes to Cells : Devoted to molecular & cellular mechanisms. 15(6) : 635-46, 2010. http://www.ncbi.nlm.nih.gov/pubmed/20497238
  • Ghosh RP, Nikitina T, Horowitz-Scherer RA, Gierasch LM, Uversky VN, Hite K, Hansen JC, Woodcock CL. Unique physical properties and interactions of the domains of methylated DNA binding protein 2. Biochemistry. 49(20) : 4395-410, 2010. http://www.ncbi.nlm.nih.gov/pubmed/20405910
  • Budantsev AY, Uversky VN, Kutyshenko VP. Analysis of the metabolites in apical area of Allium cepa roots by high resolution NMR spectroscopy method. Protein and Peptide Letters. 17(1) : 86-91, 2010. http://www.ncbi.nlm.nih.gov/pubmed/20214631
  • Sun X, Jones WT, Harvey D, Edwards PJ, Pascal SM, Kirk C, Considine T, Sheerin DJ, Rakonjac J, Oldfield CJ, Xue B, Dunker AK, Uversky VN. N-terminal domains of DELLA proteins are intrinsically unstructured in the absence of interaction with GID1/gibberellic acid receptors. The Journal of Biological Chemistry. 285(15) : 11557-71, 2010. http://www.ncbi.nlm.nih.gov/pubmed/20103592
  • Xue B, Dunbrack RL, Williams RW, Dunker AK, Uversky VN. PONDR-FIT: a meta-predictor of intrinsically disordered amino acids. Biochimica et Biophysica Acta. 1804(4) : 996-1010, 2010. http://www.ncbi.nlm.nih.gov/pubmed/20100603
  • Santner A, Uversky VN. Metalloproteomics and metal toxicology of α-synuclein. Metallomics : Integrated biometal science. 2(6) : 378-92, 2010. http://www.ncbi.nlm.nih.gov/pubmed/21072383
  • Dunker AK, Uversky VN. Drugs for 'protein clouds': targeting intrinsically disordered transcription factors. Current Opinion in Pharmacology. 10(6) : 782-8, 2010. http://www.ncbi.nlm.nih.gov/pubmed/20889377
  • Uversky VN. Seven lessons from one IDP structural analysis. Structure (London, England : 1993). 18(9) : 1069-71, 2010. http://www.ncbi.nlm.nih.gov/pubmed/20826332
  • Uversky VN. Targeting intrinsically disordered proteins in neurodegenerative and protein dysfunction diseases: another illustration of the D(2) concept. Expert Review of Proteomics. 7(4) : 543-64, 2010. http://www.ncbi.nlm.nih.gov/pubmed/20653509
  • Uversky VN, Dunker AK. Understanding protein non-folding. Biochimica et Biophysica Acta. 1804(6) : 1231-64, 2010. http://www.ncbi.nlm.nih.gov/pubmed/20117254
  • Frimpong AK, Abzalimov RR, Uversky VN, Kaltashov IA. Characterization of intrinsically disordered proteins with electrospray ionization mass spectrometry: conformational heterogeneity of alpha-synuclein. Proteins. 78(3) : 714-22, 2010. http://www.ncbi.nlm.nih.gov/pubmed/19847913
  • Zhou W, Long C, Reaney SH, Di Monte DA, Fink AL, Uversky VN. Methionine oxidation stabilizes non-toxic oligomers of alpha-synuclein through strengthening the auto-inhibitory intra-molecular long-range interactions. Biochimica et Biophysica Acta. 1802(3) : 322-30, 2010. http://www.ncbi.nlm.nih.gov/pubmed/20026206
  • Zhou W, Long C, Fink A, L, Uversky V, N. 3, 4-Dihydroxyphenylacetic acid (DOPAC) impairs interaction of α-synuclein’s with lipids. The Open Proteomics Journal. 3: 1-7, 2010.
  • Zhou W, Long C, Fink A, L, Uversky V, N. Calbindin-D28K acts as a calcium-dependent chaperone suppressing α-synuclein fibrillation in vitro. Central European Journal of Biology.. 15(1) : 11-20, 2010.
  • Posokhova E, Uversky V, N, Martemyanov K, A. 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, 2010.
  • Santner A, Uversky V, N. Metalloproteomics and metal toxicology of -synuclein. Metallomics.. 2: 378-392, 2010.
  • Meng X, Munishkina LA, Fink AL, Uversky VN. Molecular mechanisms underlying the flavonoid-induced inhibition of alpha-synuclein fibrillation. Biochemistry. 48(34) : 8206-24, 2009. http://www.ncbi.nlm.nih.gov/pubmed/19634918