Vladimir Uversky

1(226). Oldfield C.J., Meng J., Yang, J.Y., Yang, M.Q., Uversky V.N., Dunker A.K. (2008) Flexible nets: Disorder and induced fit in the associations of p53 and 14-3-3 with their partners. BMC Genomics. 9 (Suppl. 1), S1. (IF – 4.206).

2(227). Uversky V.N., Oldfield C.J., Dunker A.K. (2008) Intrinsically disordered proteins in human diseases: Introducing the D² concept. Ann. Rev. Biophys. Biomol. Structure. 37, 215-246. (IF – 17.524).

3(228). Dunker A.K., Uversky V.N. (2008) Signal transduction via unstructured protein conduits. Nature Chemical Biology. 4 (4), 229-230. (IF – 15.806).

4(229). Mohan A., Sullivan W.J. Jr., Radivojac P., Dunker A.K., Uversky V.N. (2008) Intrinsic disorder in pathogenic and non-pathogenic microbes: Discovering and analyzing the unfoldomes of early-branching eukaryotes. Molecular Biosystems. 4 (3),328 - 340. (IF – 3.825).

5(230). Prokhorov D.A., Timchenko A.A., Uversky V.N., Khristophorov V.S., Kihara H., Kimura K., Kutyshenko V.P. (2008) Dynamics of oligomer formation by denatured carbonic anhydrase II. Biochim. Biophys. Acta - Proteins and Proteomics. 1784 (5), 834-842. (IF – 2.773).

6(231). Tóth-Petróczy A., Mészáros B., Simon I., Dunker A.K., Uversky V.N., Fuxreiter M. (2008) Assessing conservation of disordered regions in proteins. The Open Proteomics Journal. 1 (1), 46-53.

7(232). Uversky V.N. (2008) Amyloidogenesis of natively unfolded proteins. Current Alzheimer Research. 5 (3), 260-287. (IF – 4.953).

8(233). Paliy O., Gargac S.M., Cheng Y., Uversky V.N., Dunker A.K. (2008) Protein disorder is positively correlated with gene expression in E. coli. Journal of Proteome Research. 7 (6), 2234–2245. (IF – 5.460).

9(234). De Biasio A., Guarnaccia C., Popovic M., Uversky V.N., Pintar P., Pongor S. (2008) Prevalence of intrinsic disorder in the intracellular region of human single-pass type I proteins: The case of the Notch ligand Delta-4. Journal of Proteome Research. 7 (6), 2496–2506. (IF – 5.460).

10(235). Singh V.K., Pacheco I., Uversky V.N., Smith S.P., MacLeod R.J., Jia Z. (2008) Intrinsically disordered human C/EBP homologous protein regulates biological activity of colon cancer cells during calcium stress. J. Mol. Biol. 380 (2), 313-326. (IF – 4.008).

11(236). Permyakov S.E., Bakunts A.G., Denesyuk A.I., Knyazeva E.L., Uversky V.N. Permyakov E.A. (2008) Apo-parvalbumin as an intrinsically disordered protein. PROTEINS Structure, Function, and Bioinformatics. 72 (3), 822-836. (IF – 2.813).

12(237). Rantalainen K., Uversky V.N., Permi P., Kalkkinen N., Dunker A.K., Mäkinen K. (2008) Potato virus A genome-linked protein VPg is an intrinsically disordered molten globule-like protein with a hydrophobic core. Virology. 377 (2),280-288. (IF – 3.305).

13(238). Xu M., Ermolenkov V.V., Uversky V.N., Lednev I.K. (2008) Hen egg white lysozyme fibrillation: A deep UV resonance Raman spectroscopic study. Journal of Biophotonics. 1 (3), 215-229. (IF – 4.240).

14(239). Dunker A.K., Oldfield, C.J., Meng J., Romero P., Yang, J.Y., Cheng J.W., Vacic V., Obradovic Z., Uversky V.N. (2008) The unfoldomics decade: An update on intrinsically disordered proteins. BMC Genomics. 9 (Suppl. 2), S1. (IF – 4.206).

15(240). Goh G.K.-M., Dunker A.K., Uversky V.N. (2008) Protein intrinsic disorder toolbox for comparative analysis of viral proteins. BMCGenomics. 9 (Suppl. 2), S4. (IF – 4.206).

16(241). Ren S., Uversky V.N., Chen Z., Dunker A.K., Obradovic Z. (2008) Short Linear Motifs recognized by SH2, SH3 and S/T Kinase domains are conserved in disordered protein regions. BMC Genomics. 9 (Suppl. 2), S26. (IF – 4.206).

17(242). Durand F., Dagkessamanskaia A., Martin-Yken H., Graille M., Van Tilbeurgh H., Uversky V.N., Francois J.M. (2008) Structure-function analysis of Knr4/Smi1, a newly member of intrinsically disordered proteins family, indispensable in the absence of a functional PKC1-SLT2 pathway in Saccharomyces cerevisiae. Yeast. 25 (8), 563-676. (IF – 1.626).

18(243). Stepanenko O.V., Verkhusha V.V, Kuznetsova I.M., Uversky V.N., Turoverov ?.?. (2008) Fluorescent proteins as biomarkers and biosensors: Throwing color lights on molecular and cellular processes. Current Protein and Peptide Science. 9 (4), 338-369. (IF – 3.854).

19(244). Meng X., Fink A.L., Uversky V.N. (2008) The effect of membranes on the in vitro fibrillation of an amyloidogenic light chain variable domain SMA. J. Mol. Biol. 381 (4), 989-999. (IF – 4.008).

20(245). Hu D., Qin Z., Xue B., Fink A.L., Uversky V.N. (2008) Effect of methionine oxidation on structural properties, conformational stability and aggregation of immunoglobulin light chain LEN. Biochemistry. 47 (33), 8665-8677. (IF – 3.226).

21(246). Munishkina L.A., Ahmad A., Fink A.L., Uversky V.N. (2008) Guiding protein aggregation with macromolecular crowding. Biochemistry. 47 (34), 8993-9006. (IF – 3.226).

22(247). Cortese M.S., Uversky V.N., Dunker A.K. (2008) Intrinsic disorder in scaffold proteins: Getting more from less. Progress in Biophysics & Molecular Biology. 98 (1), 85-106. (IF – 3.964).

23(248). Hong D.-P., Fink A.L., Uversky V.N. (2008) Structural characteristics of the a-synuclein oligomers stabilized by the flavonoid baicalein. J. Mol. Biol. 383 (1), 214-223. (IF – 4.008).

24(249). Stepanenko O.V., Verkhusha V.V., Shavlovsky M.M., Kuznetsova I.M., Uversky V.N., Turoverov K.K. (2008) Understanding the role of Arg96 in structure and stability of green fluorescent protein. PROTEINS Structure, Function, and Bioinformatics. 73 (3), 539-551. (IF – 2.813).

25(250). Uversky V.N. (2008) a-Synuclein misfolding and neurodegenerative diseases. Current Protein and Peptide Science. 9 (5), 507-540. (IF – 3.854).

26(251). Campen A., Williams R.M., Brown C.J., Uversky V.N., Dunker A.K. (2008) TOP-IDP-Scale: A new amino acid scale measuring propensity for intrinsic disorder. Protein and Peptide Letters. 15 (10) 1079-1085. (IF – 1.849).

27(252). Uversky V.N. (2008) Protein folding, misfolding and aggregation: Classical themes and novel approaches. Edited by Victor Muñoz. Book review. ChemBioChem. 9 (16), 2750-2751. (IF – 3.945).

28(253). Goh G.K.-M., Dunker A.K., Uversky V.N. (2008) A comparative analysis of viral matrix proteins using disorder predictors. Virology Journal. 5, 126. (IF – 2.546).

29(254). Fuxreiter M., Tompa P., Simon I., Uversky V.N., Hansen J.C., Asturias F.J. (2008) Malleable machines take shape in transcription regulation. Nature Chemical Biology. 4 (12), 728-737. (IF – 15.806).

30(255). Uversky V.N., Dunker A.K. (2008) Controlled chaos. Science. 322 (5906), 1340-1341. (IF – 31.377).

31(256). Munishkina L.A., Fink A.L., Uversky V.N. (2008) Concert action of metals and macromolecular crowding on the fibrillation of a-synuclein. Protein and Peptide Letters956-963. (IF – 1.849).. 15 (9),

32(257). Dunker A.K., Silman I., Uversky V.N., Sussman J.L. (2008) Function and structure of inherently disordered proteins. Current Opinion in Structural Biology. 18 (6), 756-764. (IF – 9.903).

33(258). Stsiapura V.I., Maskevich A.A., Kuzmitsky V.A., Uversky V.N., Kuznetsova I.M., Turoverov K.K. (2008) Thioflavin T as a molecular rotor. Fluorescent properties of thioflavin T in solvents with different viscosity. J. Phys. Chem. B. 112 (49), 15893-15902. (IF – 3.603)

34(259). Tóth-Petróczy A., Oldfield, C.J., Simon I., Takagi, Y., Dunker A.K., Uversky V.N., Fuxreiter M. (2008) Malleable machines in transcription regulation: The mediator complex. PLoS Comp. Biol. 4 (12), e1000243. (IF – 5.515).

 

1(260). Hong D.-P., Fink A.L., Uversky V.N. (2009) Smoking and Parkinson’s disease: Does nicotine affect a-synuclein fibrillation? Biochim. Biophys. Acta - Proteins and Proteomics. 1794 (2), 282–290. PMID: 19013262 (IF – 2.48). (IF – 2.773).

2(261). Liang S., Li L., Hsu W.-L., Zhou Y., Dunker A.K., Uversky V.N., Meroueh S.O. (2009) Exploring the molecular design of protein interaction sites with molecular dynamics simulations and free energy calculations. Biochemistry. 48 (2), 399-414. PMID: 19113835 (IF – 3.226).

3(262). Turoverov K.K., Uversky V.N., Kuznetsova I.M. (2009) Native globular and native partially or completely disordered proteins. Folding, supramolecular complex formation and aggregation. Cytology (St. Petersburg). 51 (3), 190-203. PMID: 19435273.

4(263). Tokuriki N., Oldfield C.J., Uversky V.N., Berezovsky I.N., Tawfik D.S. (2009) The biophysical uniqueness of viral proteins. Trends in Biochemical Sciences. 34(2), 53-59. PMID: 19062293 (IF – 11.572).

5(264). Hébrard E., Bessin Y., Michon T., Longhi S., Uversky V.N., Delalande F., Van Dorsselaer  A., Romero P., Walter J., Declerk N., Fargette D. (2009) Intrinsic disorder in viral proteins genome-linked: Experimental and predictive analyses. Virology Journal. 6, 23. PMID: 19220875 (IF – 2.435).

6(265). Tompa P., Fuxreiter M., Oldfield C.J., Simon I., Dunker A.K., Uversky V.N. (2009) Close encounters of the third kind: Disordered domains and the interactions of proteins. BioEssays. 31 (3), 328-335. PMID: 19260013 (IF – 5.125).

7(266). Uversky V.N. (2009) Neuropathology and neurochemistry of Parkinson’s disease: The never-ending story or the story with no beginning? Minerva Psichiatrica. 50 (1), 1-26.

8(267).Zhou W., Gallagher A., Hong D.-P., Long C., Fink A.L., Uversky V.N. (2009) At low concentrations, 3,4-Dihydroxyphenylacetic acid (DOPAC) binds non-covalently to a-synuclein and prevents its fibrillation. J. Mol. Biol. 388 (3), 597-610. PMID: 19328209 (IF – 4.008).

9(268). Xue B., Oldfield C.J, Dunker A.K., Uversky V.N. (2009) CDF it all: Consensus prediction of intrinsically disordered proteins based on various cumulative distribution functions. FEBS Letters. 583 (6), 1469-1474. PMID: 19351533 (IF – 3.601).

10(269). Uversky V.N. (2009) Intrinsic disorder in proteins associated with neurodegenerative diseases. Frontiers in Bioscience. 14 (14), 5188-5238. PMID: 19482612 (IF – 3.736).

11(270). Munishkina L.A., Fink A.L., Uversky V.N. (2009) Accelerated fibrillation of human a-synuclein induced by the combined action of macromolecular crowding and factors inducing partial folding. Current Alzheimer Research. 6. PMID: 19519306 (IF – 4.971). (3), 252-260

12(271). Goh G.K.-M., Dunker A.K., Uversky V.N. (2009) Protein intrinsic disorder and influenza virulence: The 1918 H1N1 and H5N1 viruses. Virology Journal. 6, 69. PMID: 19493338 (IF – 2.435).

13(272). Brocca S., Šamalikova M., Uversky V.N., Lotti M., Vanoni M., Alberghina A., Grandori R. (2009) Order propensity of an intrinsically disordered protein, the cyclin-dependent-kinase inhibitor Sic1. Proteins: Structure, Function, and Bioinformatics. 76 (3), 731-746. PMID: 19280601 (IF – 2.813).

14(273). Uversky V.N., Oldfield C.J, Midic U., Xie H., Vucetic S., Xue B., Iakoucheva L.M., Obradovic Z., Dunker A.K. (2009) Unfoldomics of human diseases: Linking protein intrinsic disorder with diseases. BMC Genomics. 10 (Suppl. 1), S7. PMID: 19594884 (IF – 3.579)

15(274). Midic U., Oldfield C.J., Dunker A.K., Obradovic Z., Uversky V.N. (2009) Protein disorder in the human diseasome: Unfoldomics of human genetic diseases. BMC Genomics. 10 (Suppl.1), S12. PMID: 19594871 (IF – 3.579)

16(275). He B., Wang K., Liu Y.-L., Xue B., Uversky V.N., Dunker A.K. (2009) Predicting intrinsic disorder in proteins: An overview. Cell Research. 19 (8), 929-949. PMID: 19597536 (IF – 8.151).

17(276). Meng X., Munishkina L.A., Fink A.L., Uversky V.N. (2009) Molecular mechanisms underlying the flavanoid-induced inhibition of a-synuclein fibrillation. Biochemistry. 48 (34), 8206-8224. PMID: 19634918 (IF – 3.226).

18(277). Mohan A., Uversky V.N., Radivojac P. (2009) Influence of sequence changes and environment on intrinsically disordered proteins. PLoS Computational Biology. 5 (9), e1000497. PMID: 19730682 (IF – 5.759).

19(278). Permyakov S.E., Bakunts A.G., Permyakova M.E., Denesyuk A.I., Uversky V.N., Permyakov E.A. (2009) Metal-controlled interdomain cooperativity in parvalbumins. Cell Calcium. 46 (3), 163-175. PMID: 19651438 (IF – 4.288).

20(279). Kutyshenko V.P., Prokhorov D.A., Timchenko ?.?., Kudrevatykh Yu.?., Gushchina L.V., Khristoforov V.S., Filimonov V.V., Uversky V.N. (2009) Solution structure and dynamics of the chimeric SH3 domains, SHH- and SHA-“Bergeracs”. Biochim. Biophys. Acta - Proteins and Proteomics. 1794 (2009) 1813–1822. PMID: 19732853 (IF – 2.773).

21(280). Einarsdottir O., Uversky V.N. (2009). Anthony L. Fink (1943-2008): Scientist, Teacher and Artist. Current Protein and Peptide Science. 10 (5) 395-396. PMID: 19860703 (IF – 3.854).

22(281). Dunn B.M., Uversky V.N. (2009) Cryoenzymology: Enzyme action in slow motion. Current Protein and Peptide Science. 10 (5) 408-415. PMID: 19538150 (IF – 3.854).

23(282). Uversky V.N., Goto Y. (2009) Acid denaturation and anion-induced folding of globular proteins: Multitude of equilibium partially folded intermediates. Current Protein and Peptide Science. 10 (5) 447-455. PMID: 19538151 (IF – 3.854).

24(283). Seshadri S., Oberg K.A., Uversky V.N. (2009) Mechanisms and consequences of protein aggregation: The role of folding intermediates. Current Protein and Peptide Science. 10 (5) 456-463. PMID: 19538148 (IF – 3.854).

25(284). Uversky V.N., Eliezer D. (2009) Biophysics of Parkinson’s disease: Structure and aggregation of a-synuclein. Current Protein and Peptide Science. 10 (5) 483-499. PMID: 19538146 (IF – 3.854).

26(285). Midic U., Oldfield C.J., Dunker A.K., Obradovic Z., Uversky V.N. (2009) Unfoldomics of human genetic diseases: Illustrative examples of ordered and intrinsically disordered members of human diseasome. Protein and Peptide Letters. 16 (12) 1533-1547. PMID: 20001916 (IF – 1.849).

27(286). Xue B., Li L., Meroueh S.O., Uversky V.N., Dunker A.K. (2009) Analysis of structured and intrinsically disordered regions of integral transmembrane proteins. Molecular Biosystems. 5 (12) 1688-1702, PMID: 19585006 (IF – 3.859).  

28(287). 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. PMID: 19768526 (IF – 1.017)

 

1(288). Budantsev A.Yu., Uversky V.N., Kutyshenko V.P. (2010) Analysis of metabolites in apical area of Allium cepa roots by high resolution NMR spectroscopy. Protein and Peptide Letters. 17 (1) 86-91 (IF – 1.849).

2(289). 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, 14 pages. DOI:10.1155/2010/568068. PMID: 20011072 (IF – 1.750).

3(290). Frimpong A., Abzalimov R.R., Uversky V.N., Kaltashov I.A. (2010) Characterization of intrinsically disordered proteins with electrospray ionization mass spectrometry: Conformational heterogeneity of a-synuclein. Proteins: Structure, Function, and Bioinformatics. 78 (3) 714-722. PMID: 19847913 (IF – 2.813).

4(291). Zhou W., Long C., Fink A.L., Uversky V.N. (2010) 3,4-Dihydroxyphenylacetic acid (DOPAC) impairs interaction of a-synuclein with lipids. The Open Proteomics Journal. 3, 1-7. DOI:10.2174/1875039701003010001 .

5(292). Meng X., Munishkina L.A., Fink A.L., Uversky V.N. (2010) Effects of various flavanoids on the fibrillation of ?-synuclein. Parkinson’s Disease. Volume 2010, Article ID 650794, 16 pages DOI:10.4061/2010/650794.

6(293). Zhou W., Long C., Reaney S.H., Di Monte D.A., Fink A.L., Uversky V.N. (2010) Methionine oxidation stabilizes non-toxic oligomers of a-synuclein through strengthening the auto-inhibitory intra-molecular long-range interactions. Biochim. Biophys. Acta – Molecular Basis of Diseases. 1802 (3) 322–330. PMID: 20026206 (IF – 4.139).

7(294). Zhou W., Long C., Fink A.L., Uversky V.N. (2010) Calbindin-D_28K acts as a calcium-dependent chaperone suppressing α-synuclein fibrillation in vitro. Central European Journal of Biology. 15 (1) 11-20. DOI: 10.2478/s11535-009-0071-8 (IF – 0.915).

8(295). Xue B., Dunbrack R.L., Williams R.W., Dunker A.K., Uversky V.N. (2010) PONDR-FIT: A meta-predictor of intrinsically disordered amino acids. Biochim. Biophys. Acta - Proteins and Proteomics. 1804 (4) 996-1010. PMID: 20100603 (IF – 2.773).

9(296). Posokhova E., Uversky V.N., Martemyanov K.A. (2010) Proteomic identification of Hsc70 as a mediator of RGS9-2 degradation by the in vivo interactome analysis. J. Proteome Res. 9(3), 1510-1521. PMID: 20095651 (IF – 5.460).

10(297). Uversky V.N., Dunker A.K. (2010) Understanding protein non-folding. Biochim. Biophys. Acta - Proteins and Proteomics. 1804 (6) 1231–1264. PMID: 20117254 (IF – 2.773).

11(298). Sun X., Jones W.T., Harvey D., Edwards P., Pascal S, Kirk C., Considine T., Sheerin D.J., Rakonjac J., Oldfield C.J., Xue B., Dunker A.K., Uversky V.N. (2010) N-terminal domains of DELLA proteins are intrinsically unstructured proteins in the absence of interaction with GID1 GA receptors. J. Biol. Chem. 285 (15) 11557-11571. PMID: 20103592 (IF – 5.328).

12(299). Xue B., Hsu W., Lu H., Dunker A.K., Uversky V.N. (2010) SPA: Short peptide analyzer on intrinsic disorder status. Genes to Cells. 15 (6) 635-646. PMID: 20497238 (IF – 2.952).

13(300). Ghosh R.P., Nikitina T., Horowitz-Scherer R.A., Gierasch L.M., Uversky V.N., Hite K., Hansen J.C., Woodcock C.L. (2010)Unique physical properties and interactions of the domains of methylated DNA binding protein 2. Biochemistry. 49 (20) 4395-4410. PMID: 20405910 (IF – 3.226).

14(301). 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 (IF – 4.064).

15(302). Santner A., Uversky V.N. (2010) Metalloproteomics and metal toxicology of ?-synuclein. Metallomics. 2 (6), 378–392. DOI: 10.1039/b926659c (IF – 3.592).

16(303). Jorda J., Xue B., Uversky V.N., Kajava A.V. (2010) Protein tandem repeats: The more perfect the less structured. FEBS Journal. 277 (12) 2673-2682. PMID: 20491906 (IF – 3.129)

17(304). 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 (IF – 3.992).

18(305). Dagkessamanskaia A., Durand F., Uversky V.N., Binda M., Lopez F., El Azzouzi K., Francois J.M., Martin-Yken H. (2010) Functional dissection of an intrinsically disordered protein: Understanding the roles of different domains of Knr4 protein in protein-protein interactions. Protein Science. 19 (7) 1376-1385. PMID: 20506404 (IF – 2.937).

19(306). 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. PMID: 20100603 (IF – 1.849).

20(307). 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. PMID: 20653509 (IF – 3.570)

21(308). Uversky V.N. (2010) Mysterious oligomerization of the amyloidogenic proteins. FEBS Journal. 277 (14) 2940-2953. PMID: 20546306 (IF – 3.129).

22(309). Permyakov S.E., Khokhlova T.I., Uversky V.N., Permyakov E.A. (2010) Ca2⁺/Mg²⁺ selectivity of solitary helix-loop-helix Ca²⁺-binding motif: α-Lactalbumin and Ca²⁺-binding lysozyme cases. Proteins: Structure, Function, and Bioinformatics. 78 (12) 2609-2624. PMID: 20602456 (IF – 2.813).

23(310). 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. PMID: 20547696 (IF – 6.747).

24(311). Uversky V.N. (2010) Seven lessons from one IDP structural analysis. Structure. 18 (9) 1069-1071. DOI: 10.1016/j.str.2010.08.003. PMID: 20826332 (IF – 5.904).

25(312). Xue B., Dunker A.K., Uversky V.N. (2010) Retro-MoRFs: Identifying protein binding sites by normal and reverse alignment and intrinsic disorder prediction. International Journal of Molecular Sciences. 11(10), 3725-3747. doi:10.3390/ijms11103725 (IF – 1.387).

26(313). Yamada J., 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. (2010) A bimodal distribution of two distinct categories of intrinsically-disordered structures with separate functions in FG nucleoporins. Molecular and Cellular Proteomics. 9 2205-2224. PMID: 20214631 (IF – 8.791). (10)

27(314). Sulatskaya A.I., Maskevich A.A., Kuznetsova I.M, Uversky V.N., Turoverov K.K. (2010) Fluorescence quantum yield of thioflavin T in rigid environment when ultrafast intramolecular twisting is restricted. PLoS One. 5 (10) e15385. doi:10.1371/journal.pone.0015385 (IF – 4.351).

28(315). Dunker A.K., Uversky V.N. (2010) Drugs for “protein clouds”: Targeting intrinsically disordered transcription factors. Current Opinion in Pharmacology. 10 (6) 782-788. PMID: 20889377 (IF – 7.259).

1(316). Dixon S.E., Bhatti M.M., Uversky V.N., Dunker A.K., Sullivan W.J. Jr. (2011) Regions of intrinsic disorder help identify a novel nuclear localization signal in Toxoplasma gondii histone acetyltransferase TgGCN5-B. Molecular and Biochemical Parasitology. 175 (2) 192-195 PMID: 21055425 (IF – 2.939).

2(317). Uversky V.N. (2011) Flexible nets of malleable guardians: Intrinsically disordered chaperones in neurodegenerative diseases. Chemical Reviews. 111 (2) 2234-1166 PMID: 21086986 (IF – 35.957).

3(318). Uversky V.N. (2011) Multitude of binding modes attainable by intrinsically disordered proteins: A portrait gallery of disorder-based complexes. Chemical Society Reviews. 40 (3) 1623-1634. DOI: 10.1039/C0CS00057D(IF – 20.086).

4(319). Hong D.-P., Han S., Fink A.L., Uversky V.N. (2011) Characterization of the non-fibrillar α-synuclein oligomers. Protein and Peptide Letters. 18 (3) 230-240.PMID: 20858207 (IF – 1.849).

5(320). Silva B.A., Einarsdottir, O., Fink A.L., Uversky V.N. (2011) Modulating ?-sinuclein misfolding and fibrillation in vitro by agrochemicals. Research and Reports in Biology. 2 43-56. DOI: 10.2147/RRB.S16448.

6(321). Sigalov A.S., Uversky V.N. (2011) Protein disorder differentially occurs in the cytoplasmic signaling domains of cell receptors. Self/Nonself. 2 (1) 55-72. PMID: 21776336

7(322). Uversky V.N. (2011) Intrinsically disordered proteins may escape unwanted interactions via functional misfolding. Biochim. Biophys. Acta - Proteins and Proteomics. 1814 (5) 693–712 PMID: 21440685  (IF – 2.773).

8(323). Uversky V.N., Shah S., Gritsyna Yu., Hitchcock-DeGregori S.E.,Kostyukova A.S. (2011) Systematic analysis of tropomodulin/tropomyosin interactions uncovers fine-tuned binding specificity of intrinsically disordered proteins. JournalofMolecularRecognition. 24 (4) 647-655. doi: 10.1002/jmr.1093. PMID: 21584876 (IF – 2.776).

9(324). Rochman M., Taher L., Kurahashi T., Cherukuri S., Uversky V.N., Landsman D., Ovcharenko I., Bustin M. (2011) Effects of HMGN variants on the cellular transcriptionprofile. Nucleic Acid Research. 39 (10) 4076-4087. PMID: 21278158 (IF – 7.479).

10(325). Uversky V.N. (2011) Intrinsically disordered proteins from A to Z. International Journal of Biochemistry and Cell Biology. 43 (8) 1090–1103. PMID: 21501695 (IF – 4.956)

11(326). Permyakov S.E., Ismailov R.G., Xue B., Denesyuk A.I., Uversky V.N., Permyakov E.A. (2011) Intrinsic disorder in S100 proteins. Molecular BioSystems. 7 (7), 2164 – 2180. PMID: 21528128 (IF – 3.859)

12(327).  Mizianty M., Zhang T., Xue B., Zhou Y., Dunker A.K., Uversky V.N., Kurgan L. (2011) In-silico prediction of disorder content using hybrid sequence representation. BMC Bioinformatics. 12 (1) 245. PMID: 21682902 (IF – 3.428).

13(328). Xue B., Soeria-Atmadja D., Gustafsson M.G., Hammerling, U., Dunker A.K, Uversky V.N. (2011) Abundance and functional roles of intrinsic disorder in allergenic proteins and allergen representative peptides. Proteins: Structure, Function, and Bioinformatics. 79 (9) 2595-2606. PMID: 21732419 (IF – 3.085).

14(329). Melnik T.N., Povarnitsyna T.V, Glukhov A.S, Uversky V.N., Melnik B.S. (2011) Sequential melting of two hydrophobic clusters within the GFP-cycle3. Biochemistry. 50 (36) 7735-7744. PMID: 21823681 (IF – 3.226).

15(330). Sun X., Xue B., Jones W.T., Rikkerink E., Dunker A.K., Uversky V. N. (2011) 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) 205-223. PMID: 21732203 (IF – 4.149).

16(331). Liu J., Jolly R.A., Smith A.K., Searfoss G.H, Goldstein K.M., Uversky V.N., Dunker A.K., Li S., Thomas C.E., Wei T. (2011) Predictive Power Estimation Algorithm (PPEA) - a new algorithm to reduce overfitting for genomic biomarker discovery. PLoS One. 6 (9) e24233. PMID: 21935387 (IF – 4.351).

17(332). Breydo L., Uversky V.N. (2011) Role of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases. Metallomics. 3 (11) 1163-1180. PMID: 21869995 (IF – 3.592).

18(333). Peysselon F., Xue B., Uversky V.N., Ricard-Blum S. (2011) Intrinsic disorder in the extracellular matrix. Molecular BioSystems. 7 (12) 3353-3365. PMID: 22009114 (IF – 3.859)

19(334). Melnik B.S., Molochkov N.V., Prokhorov D.A., Uversky V.N., Kutyshenko V.P. (2011) Molecular mechanisms of the anomalous thermal aggregation of green fluorescent protein. Biochim. Biophys. Acta - Proteins and Proteomics. 1814 (12) 1930–1939. PMID: 21816236 (IF – 2.773).

20(335). Kutyshenko V.P., Molchanov M., Beskaravayny P., Uversky V.N., Timchenko M.A. (2011) Analyzing and mapping sweat metabolomics by high-resolution NMR spectroscopy. PLoS One. 6 (12) e28824. doi:10.1371/journal.pone.0028824 (IF – 4.351).

1(336). Xue B., Oldfield C.J., Van Y.Y., Dunker A.K., Uversky V.N. (2012) Protein intrinsic disorder and induced pluripotent stem cells. Molecular BioSystems. 8 (1) 134-150. PMID: 21761058. (IF – 3.825).

2(337). Zambelli B., Cremades N., Neyroz P., Turano P., Uversky V.N., Ciurli S. (2012) Insights in the (un)structural organization of Bacillus pasteurii UreG, an intrinsically disordered GTPase enzyme. Molecular BioSystems. 8 (1) 220-228. PMID: 21922108. (IF – 3.825).

3(338). Breydo L., Wu J.W., Uversky V.N. (2012) α-Synuclein misfolding and Parkinson's disease. Biochim. Biophys. Acta – Molecular Basis of Diseases. 1822 (2) 261-285. PMID: 22024360. (IF – 5.387).

4(339). Hsu W.-L., Oldfield C.J., Meng J., Huang F., Xue B., Uversky V.N., Romero P., Dunker A.K. (2012) Intrinsic protein disorder and protein-protein interactions. Pacific Symposium on Biocomputing. 116-127. PMID: 22174268.

5(340). Huang F., Oldfield C.J., Meng J., Hsu W.-L., Xue B., Uversky V.N., Romero P., Dunker A.K. (2012) Subclassifying disordered proteins by the CH-CDF plot method. Pacific Symposium on Biocomputing. 128-139. PMID: 22174269.

6(341). Zhang T., Faraggi, E., Xue B., Dunker A.K., Uversky V.N., Zhou Y. (2012) Accurate prediction of short and long disordered regions by a single neural-network-based method. Journal of Biomolecular Structure and Dynamics. 29 (4) 799-813. PMID: 22208280. (IF – 4.986).

7(342). Melnik B.S., Povarnitsyna T.V., Glukhov A.S., Melnik T.N., Uversky V.N. (2012) SS-stabilizing proteins rationally: Intrinsic disorder-based design of stabilizing disulphide bridges in GFP. Journal of Biomolecular Structure and Dynamics. 29 (4) 817-824. PMID: 22208281. (IF – 4.986).

8(343). Ahmad A., Burns C.S., Fink A.L., Uversky V.N. (2012) Peculiarities of the copper binding to a-synuclein. Journal of Biomolecular Structure and Dynamics. 29 (4) 825-842. PMID: 22208282. (IF – 4.986).

9(344). Uversky V.N., Santambrogio C., Brocca S., Grandori R. (2012) Length-dependent compaction of intrinsically disordered proteins. FEBS Letters. 586 (1) 70-73. PMID: 22138473. (IF – 3.538).

10(345). Xue B., Dunker A.K., Uversky V.N. (2012) The roles of intrinsic disorder in orchestrating the Wnt pathway. Journal of Biomolecular Structure and Dynamics. 29 (5) 843-861. PMID: 22292947. (IF – 4.986).

11(346). Fedotoff O., Mikheeva L.M., Chait A., Uversky V.N., Zaslavsky B.Y. (2012) Influence of serum proteins on conformation of prostate-specific antigen. Journal of Biomolecular Structure and Dynamics. 29 (5) 1051-1064. PMID: 22292959. (IF – 4.986).

12(347). Uversky V.N. (2012) Intrinsically disordered proteins: A focused look at the fuzzy subjects. Current Protein and Peptide Science. 13 (1) 2-5 PMID: 22455660.  (IF – 2.886).

13(348). Westerheide S.D., Raynes R., Powell C., Xue B., Uversky V.N. (2012) HSF transcription factor family, heat shock response, and protein intrinsic disorder. Current Protein and Peptide Science. 13 (1) 86-103. PMID: 22044151. (IF – 2.886).

14(349). Kuznetsova I.M., Sulatskaya A.I., Uversky V.N., Turoverov K.K. (2012) An equilibrium microdialysis-based methodology for the analysis of Thioflavin T binding to amyloid fibrils. PLoS One. 7 (2) e30724. PMID: 22383971. (IF – 4.092).

15(350). Uversky V.N, Dunker A.K. (2012) A multiparametric analysis of intrinsically disordered proteins: Looking at intrinsic disorder through compound eyes. Analytical Chemistry. 84 (5) 2096−2104. PMID: 22242801. (IF – 5.856).

16(351). Liu J., Li D.S., Dunker A.K., Uversky V.N. (2012) Molecular profiling - an essential technology enabling personalized medicine in breast cancer. Current Drug Targets. 13(4) 541-554. PMID: 22250651. (IF – 3.553).

17(352). Xue B., Mizianty M., Kurgan L., Uversky V.N. (2012) Protein intrinsic disorder as flexible armor and weapon of HIV-1. Cellular and Molecular Life Sciences. 69 (8) 1211-1259. PMID: 22033837. (IF – 6.570).

18(353). Xu K., Uversky V.N., Xue B. (2012) Local flexibility facilitates oxidization of buried methionine residues. Protein and Peptide Letters. 19 (6) 688-697 PMID: 22519542  (IF – 1.942).

19(354). Singh V.K., Rahman M.N., Munro M., Uversky V.N., Smith S., Jia Z. (2012) Free cysteine modulates the conformation of human C/EBP homologous protein. PLoS One. 7 (4) e34680.PMID: 22496840. (IF – 4.092).

20(355). Uversky V.N. (2012) Disordered competitive recruiter: Fast and foldable. Journal of Molecular Biology. 418 (5) 267-268. PMID: 22381408. (IF – 4.001).

21(356). Adl A.A., Nowzari-Dalini A., Xue X., Uversky V.N, Qian X. (2012) Accurate prediction of protein structural classes using functional domains and predicted secondary structure sequences. Journal of Biomolecular Structure and Dynamics. 29 (6) 623-633. PMID: 22545993. (IF – 4.986).

22(357). Xue B., Dunker A.K., Uversky V.N. (2012) Orderly order in protein intrinsic disorder distribution: Disorder in 3500 proteomes from viruses and the three domains of life. Journal of Biomolecular Structure and Dynamics. 30 (2) 131-142. (IF – 4.986).

23(358). Sikirzhytski V., Topilina N.I, Takor G.A., Higashiya S., Welch J.T., Uversky V.N., Lednev I.K. (2012) Fibrillation mechanism of a model intrinsically disordered protein revealed by 2D correlation deep UV resonance raman spectroscopy. Biomacromolecules. 13 (5) 1503-1509. PMID: 22515261 (IF – 5.479).

24(358). Tipparaju S.M., Li X.-P., Kilfoil P., Xue B., Uversky V.N., Bhatnagar A., Barski O.A. (2012) 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) 799-181. PMID: 22426702. (IF – 4.463).

25(360). Hervás R., Oroz J., Galera-Prat A., Goñi O.,Valbuena A., Vera A., Gómez-Sicilia A., Losada-Urzáiz F., Uversky V.N., Menéndez M., Laurents D.V., Bruix M., Carrión-Vázquez M. (2012) Common features at the start of the neurodegeneration cascade. PLoS Biology. 10 (5) e1001335. PMID: 22666178 (IF – 11.452).

26(361). Peng Z., Mizianty M.J., Xue B., Kurgan L., Uversky V.N. (2012) More than just tails: Intrinsic disorder in histone proteins. Molecular Biosystems. 8 (7) 1886 – 1901. PMID: 22543956 (IF – 3.534).

27(362). Uversky V.N. (2012) Intrinsically disordered proteins and novel strategies for drug discovery. Expert Opinion on Drug Discovery. 7 (6) 475-488. PMID: 22559227 (IF – 2.116).

28(363). Disfani F.M., Hsu W.-L., Mizianty M.J., Oldfield C.J., Xue B., Dunker A.K., Uversky V.N., Kurgan L. (2012) MoRFpred, a computational tool for sequence-based prediction and characterization of disorder-to-order transitioning binding sites in proteins. Bioinformatics. 28 (12) i75-i83. PMID: (IF – 5.468).

29(364). Kuznetsova I.M., Sulatskaya A.I., Uversky V.N., Turoverov K.K. (2012) A new trend in experimental methodology for the analysis of the thioflavin T binding to amyloid fibrils. Molecular Neurobiology. 45 (3) 488-498 PMID: 22592269. (IF – 5.735).

30(365). Sulatskaya A.I., Povarova O.I., Kuznetsova I.M., Uversky V.N., Turoverov K.K. (2012) Binding stoichiometry and affinity of fluorescent dyes to proteins in different structural states. Methods in Molecular Biology. 895441-460. PMID: 22760333.

31(366). Uversky V.N. (2012) Size-exclusion chromatography in structural analysis of intrinsically disordered proteins. Methods in Molecular Biology. 386, 179-194. PMID: 22821524.

32(367). Neyroz P., Ciurli S., Uversky V.N. (2012) Denaturant-induced conformational transitions in intrinsically disordered proteins. Methods in Molecular Biology. 386, 197-213. PMID: 22821525.

33(368). Santner A.A., Croy C.H., Vasanwala F.H., Uversky V.N., Van Y.Y., Dunker A.K. (2012) Sweeping away protein aggregation with entropic bristles: IDP fusions enhance soluble expression. Biochemistry. 51 (37) 7250-7262.PMID: 22924672. (IF – 3.422).

34(369). Johnson D.E., Xue B., Sickmeier M.D., Meng J., Cortese M.S., Oldfield C.J., Le Gall T., Dunker A.K., Uversky V.N. (2012) High-throughput characterization of intrinsic disorder in proteins from the protein structure initiative. Journal of Structural Biology. 180 (1) 201-215. PMID: 22651963. (IF – 3.406).

35(370). Vacic V., Markwick P.R.L., Oldfield C.J.,Zhao X., Haynes C., Uversky V.N., Iakoucheva L.M. (2012) Disease-associated mutations disrupt functionally important regions of intrinsic protein disorder. PLoS Computational Biology. 8 (10) e1002709. PMID: 23055912. (IF – 5.215).

36(371). Goh G.K.-M., Dunker A.K., Uversky V.N. (2012) Understanding viral transmission behavior via protein intrinsic disorder prediction: Coronaviruses. Journal of Pathogens. 2012, article ID 738590. PMID: 23097708.

37(372). Kirilyuk A., Shimoj M., Catania J., Sahu F., Giordano A., Albanese C., Mocchetti I., Uversky V.N., Avantaggiati M.L. (2012) An intrinsically disordered region of the acetyltransferase p300 with similarity to prion-like domains plays a role in aggregation. PLOS ONE. 7 (11) e48243 PMID: 23133622 (IF – 4.092).

1(373). Oates M., Romero P., Ishida T., Ghalwash M., Mizianty M.J., Xue B., Dosztanyi Z., Uversky V.N., Obradovic Z., Kurgan L., Dunker A.K., Gough J. (2013) D²P²: Database of disordered protein predictions. Nucleic Acids Research. 41 (D1) D508-D516. PMID: 23203878 (IF – 8.026).

2(374). Oldfield C.J, Xue B., Van Y.Y., Ulrich E.L., Markley J.L., Dunker A.K., Uversky V.N. (2013) Utilization of protein intrinsic disorder knowledge in structural proteomics. Biochim. Biophys. Acta - Proteins and Proteomics. 1834 (2) 487-498. PMID: 23232152 (IF – 3.635).

3(375). Zaslavsky A., Madeira P., Breydo L., Uversky V.N., Chait A., Zaslavsky B.Y. (2013) High throughput characterization of structural differences between closely related proteins in solution. Biochim. Biophys. Acta - Proteins and Proteomics. 1834 (2) 583-592. PMID: 23174655 (IF – 3.635).

4(376). Dunker A.K., Uversky V.N. (2013) The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure. F1000 Biology Reports. 5 1.

5(377).Silva B.A., Breydo L., Uversky V.N. (2013) Targeting the chameleon: A focused look at a-synuclein and its roles in neurodegeneration. Molecular Neurobiology. In press. PMID: 22940885 (IF – 5.735).

6(378). Silva B.A., Breydo L., Fink A.L., Uversky V.N. (2013) Agrochemicals, a-synuclein, and Parkinson’s disease. Molecular Neurobiology. In press. PMID: 22933040. (IF – 5.735).

7(379). Uversky V.N. (2013) Intrinsic disorder-based protein interactions and their modulators. Current Pharmaceutical Design. In press. PMID: 23170892 (IF – 3.807).

8(380). Hsu W.-L., Oldfield C.J., Xue B., Meng J., Huang F., Romero P., Uversky V.N., Dunker A.K. (2013) Exploring the binding diversity of intrinsically disordered proteins involved in one-to-many signaling. Protein Science. In press PMID: 23233352 (IF – 2.798).

9(381). 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. (2013) 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. In press (IF – 0.570).

10(382). Ribeiro M.C., Espinosa J., Islam S., Martinez O., Jamnadas Thanki J., Mazariegos S., Nguyen T., Larina M., Xue B., Uversky V.N. (2013) Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerivisiae spliceosome. PeerJ. In press

11(384). Jinwal U.K., Akoury E., Abisambra J.F., O'Leary J.C. 3rd, Thompson A.D., Blair L.J., Jin Y., Bacon J., Nordhues B.A., Cockman M., Zhang J., Li P., Zhang B., Borysov S., Uversky V.N., Biernat J., Mandelkow E., Gestwicki J.E., Zweckstetter M., Dickey C.A. (2013) Imbalance of Hsp70 family variants fosters tau accumulation. FASEB Journal. In press PMID: 23271055 (IF – 5.712).

12(383). Uversky V.N. (2013) Unusual biophysics of intrinsically disordered proteins. Biochim. Biophys. Acta - Proteins and Proteomics. In press PMID: 23269364 (IF –3.635).

13(385). Xue B., Ganti K., Rabionet A., Banks L., Uversky V.N. (2013) Disordered interactome of human papillomavirus. Current Pharmaceutical Design. In press (IF – 3.807)

14(386). Sun X., Rikkerink E., Jones W.T., Uversky V. N. (2013) Multifarious roles of intrinsically disordered proteins in plant signalling and regulation. Plant Cell. In press (IF – 10.224).

15(387). Kutyshenko V.P., Prokhorov D.A., Timchenko ?.?., Kudrevatykh Yu.?., Gushchina L.V., Filimonov V.V., Uversky V.N. (2013) Dancing retro: Solution structure and micelle interactions of the retro-SH3-domain, retro-SHH-“Bergerac”. Journal of Biomolecular Structure and Dynamics. In press (IF – 4.986).

16(388). Moroz N., Novak S.M., Azevedo R., Colpan M., Uversky V.N., Gregorio C.C., Kostyukova A.S. (2012) Alteration of tropomyosin-binding properties of tropomodulin1 affects its capping ability and localization in skeletal myocytes. Journal of Biological Chemistry. In press PMID: 23271735 (IF – 4.773)

17(389). Xue B., Jeffers V., Sullivan W.J., Jr., Uversky V.N. (2012) Protein intrinsic disorder in the acetylome of intracellular and extracellular Toxoplasma gondii. In press (IF – 3.825).

18(390). Xue B., Brown C.J., Biochim. Biophys. Acta - Proteins and Proteomics. In press (IF – 3.635).Dunker A.K., Uversky V.N. (2013) Intrinsically disordered regions of p53 family are highly diversified in evolution.