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Лаборатория новых методов в биологии: некоторые публикации

Некоторые публикации лаборатории по тематике нативно разупорядоченных белков

  • Uversky, V.N., What does it mean to be natively unfolded? Eur. J. Biochem. 269, 2-12, 2002.
  • Uversky V.N., Cracking the folding code. Why do some proteins adopt partially folded conformations, whereas other don't? FEBS Letters 514, 181-183, 2002.
  • Uversky V.N., and Fink, A.L., The chicken-egg scenario of protein folding revisited. FEBS Letters 515, 79-83, 2002.
  • Uversky, V.N. Natively unfolded proteins: A point where biology waits for physics. Protein Sci. 11, 739-756, 2002.
  • Uversky V.N. Protein folding revisited. A polypeptide chain at the folding - misfolding - non-folding crossroads: Which way to go? Cell. Mol. Life Sci. 60, 9, 1852-1871, 2003.
  • Uversky V.N., Oldfield, C., Dunker, A.K. Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling. J. Mol. Recognit. 18, 5, 343-384, 2005.
  • Dunker A.K., Cortese M.S., Romero P., Iakoucheva L.M., Uversky V.N. Flexible nets: The roles of intrinsic disorder in protein interaction networks. FEBS Journal. 272, 20, 5129-5148, 2005.
  • Daughdrill G.W, Pielak G.J., Uversky V.N., Cortese M.S., Dunker A.K. Natively disordered proteins. In Protein Folding Handbook (Buchner J., and Kiefhaber T., eds.). Wiley-VCH, Verlag GmbH & Co. KGaA, Weinheim, Germany, pp.271-353, 2005.
  • Receveur-Br?chot V., Bourhis J.-M., Uversky V.N., Canard B., Longhi S. Assessing protein disorder and induced folding. POTEINS Structure, Function, and Bioinformatics. 62, 1, 24-45, 2006.
  • Radivojac P., Vucetic S., O'Connor T.R., Uversky V.N., Obradovic Z., Dunker A.K. Calmodulin regulation: Prediction and analysis of a disorder-dependent signaling mechanism. POTEINS Structure, Function, and Bioinformatics. 63, 2, 398-410, 2006.
  • Chen J.W., Romero P., Uversky V.N., Dunker A.K. Conservation of intrinsic disorder in protein domains and families: I. A database of conserved predicted disordered regions. Journal of Proteome Research. 5, 4, 879-887, 2006.
  • Chen J.W., Romero P., Uversky V.N., Dunker A.K. Conservation of intrinsic disorder in protein domains and families: II. Functions of conserved disorder. Journal of Proteome Research. 5, 4, 888-898, 2006.
  • Romero R., Zaidi S., Fang Y.Y., Uversky V.N., Radivojac P., Oldfield C.J., Cortese M.S., Sickmeier M., LeGall T., Obradovic Z., Dunker A.K. Functional profiling by alternative splicing and intrinsic protein disorder. Proc. Natl. Acad. Sci. USA. 103, 22, 8390-8395, 2006.
  • Liu J., Perumal N.B., Oldfield C.J., Su E.W., Uversky V.N., Dunker A.K. Intrinsic disorder in transcription factors. Biochemistry. 45, 22, 6773-6888, 2006.
  • Bhalla J., Storchan G.B., MacCarthy C.M., Uversky V.N., Tcherkasskaya O. Local flexibility in molecular function paradigm. Molecular and Cellular Proteomics. 5, 7, 1212-1223, 2006.
  • Haynes C., Ji F., Oldfield C.J., Klitgord N., Cusick M.E., Radivojac P., Uversky V.N., Vidal M., Iakoucheva L.M. Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes. PLoS Computational Biology. 2, 8, e100 (0001-0012), 2006.
  • Uversky V.N., Roman A., Oldfield C.J., Dunker A.K. Protein intrinsic disorder and human papillomaviruses: Increased amount of disorder in E6 and E7 oncoproteins from high risk HPVs. Journal of Proteome Research. 5, 8, 1829-1842, 2006.
  • Cheng Y., Le Gall T., Oldfield C.J., Dunker A.K., Uversky V.N. Abundance of intrinsic disorder in proteins associated with cardiovascular disease. Biochemistry. 45, 35, 10448-10460, 2006.
  • Mohan A., Radivojac P., Oldfield C.J., Vacic V., Cortese M.S., Dunker A.K., Uversky V.N. Analysis of molecular recognition features (MoRFs). J. Mol. Biol. 362, 5, 1043-1059, 2006.
  • Cheng Y., Le Gall, T., Oldfield C.J., Mueller J.P., Van Y.-Y., Romero P., Cortese M.S., Uversky V.N., Dunker A.K. Rational drug design via intrinsically disordered protein. Trends in Biotechnology. 24, 10, 435-442, 2006.
  • Oldfield C.J., Meng J., Yang, J.Y., Yang, M.Q., Uversky V.N., Dunker A.K. Flexible nets: Disorder and induced fit in the associations of p53 and 14-3-3 with their partners. BMC Genomics. 9 (Suppl. 1), S1, 2008.
  • Uversky V.N., Oldfield C.J., Dunker A.K. Intrinsically disordered proteins in human diseases: Introducing the D2 concept. Ann. Rev. Biophys. Biomol. Structure. 37, 215-246, 2008.
  • Dunker A.K., Uversky V.N. Signal transduction via unstructured protein conduits. Nature Chemical Biology. 4, 4, 229-230, 2008.
  • Mohan A., Sullivan W.J. Jr., Radivojac P., Dunker A.K., Uversky V.N. Intrinsic disorder in pathogenic and non-pathogenic microbes: Discovering and analyzing the unfoldomes of early-branching eukaryotes. Molecular Biosystems. 4, 3, 328 - 340, 2008.
  • T?th-Petr?czy A., M?sz?ros B., Simon I., Dunker A.K., Uversky V.N., Fuxreiter M. Assessing conservation of disordered regions in proteins. The Open Proteomics Journal. 1, 1, 46-53, 2008.
  • Uversky V.N. Amyloidogenesis of natively unfolded proteins. Current Alzheimer Research. 5, 3, 260-287, 2008.
  • Paliy O., Gargac S.M., Cheng Y., Uversky V.N., Dunker A.K. Protein disorder is positively correlated with gene expression in E. coli. Journal of Proteome Research. 7, 6, 2234-2245, 2008.
  • De Biasio A., Guarnaccia C., Popovic M., Uversky V.N., Pintar P., Pongor S. 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, 2008.
  • 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.
  • Dunker A.K., Oldfield, C.J., Meng J., Romero P., Yang, J.Y., Cheng J.W., Vacic V., Obradovic Z., Uversky V.N. The unfoldomics decade: An update on intrinsically disordered proteins. BMC Genomics. 9 (Suppl. 2), S1, 2008.
  • Goh G.K.-M., Dunker A.K., Uversky V.N. Protein intrinsic disorder toolbox for comparative analysis of viral proteins. BMC Genomics. 9 (Suppl. 2), S4, 2008.
  • Ren S., Uversky V.N., Chen Z., Dunker A.K., Obradovic Z. Short Linear Motifs recognized by SH2, SH3 and S/T Kinase domains are conserved in disordered protein regions. BMC Genomics. 9 (Suppl. 2), S26, 2008.
  • Durand F., Dagkessamanskaia A., Martin-Yken H., Graille M., Van Tilbeurgh H., Uversky V.N., Francois J.M. 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, 2008.
  • Cortese M.S., Uversky V.N., Dunker A.K. Intrinsic disorder in scaffold proteins: Getting more from less. Progress in Biophysics & Molecular Biology. 98, 1, 85-106, 2008.
  • Dunker A.K., Silman I., Uversky V.N., Sussman J.L. Function and structure of inherently disordered proteins. Current Opinion in Structural Biology. 18, 6, 756-764, 2008.
  • H?brard E., Bessin Y., Michon T., Longhi S., Uversky V.N., Delalande F., Van Dorsselaer A., Romero P., Walter J., Declerk N., Fargette D. Intrinsic disorder in viral proteins genome-linked: Experimental and predictive analyses. Virology Journal. 6, 23, 2009.
  • Tompa P., Fuxreiter M., Oldfield C.J., Simon I., Dunker A.K., Uversky V.N. Close encounters of the third kind: Disordered domains and the interactions of proteins. BioEssays. 31, 3, 328-335, 2009.
  • Xue B., Oldfield C.J, Dunker A.K., Uversky V.N. CDF it all: Consensus prediction of intrinsically disordered proteins based on various cumulative distribution functions. FEBS Letters. 583, 6, 1469-1474, 2009.
  • Uversky V.N. Intrinsic disorder in proteins associated with neurodegenerative diseases. Frontiers in Bioscience. 14, 14, 5188-5238, 2009.
  • Goh G.K.-M., Dunker A.K., Uversky V.N., Protein intrinsic disorder and influenza virulence: The 1918 H1N1 and H5N1 viruses. Virology Journal. 6, 69, 2009.
  • Brocca S., ?amalikova M., Uversky V.N., Lotti M., Vanoni M., Alberghina A., Grandori R. Order propensity of an intrinsically disordered protein, the cyclin-dependent-kinase inhibitor Sic1. Proteins: Structure, Function, and Bioinformatics. 76, 3, 731-746, 2009.
  • Uversky V.N., Oldfield C.J, Midic U., Xie H., Vucetic S., Xue B., Iakoucheva L.M., Obradovic Z., Dunker A.K. Unfoldomics of human diseases: Linking protein intrinsic disorder with diseases. BMC Genomics. 10 (Suppl. 1), S7, 2009.
  • Midic U., Oldfield C.J., Dunker A.K., Obradovic Z., Uversky V.N. Protein disorder in the human diseasome: Unfoldomics of human genetic diseases. BMC Genomics. 10 (Suppl.1), S12, 2009.
  • He B., Wang K., Liu Y.-L., Xue B., Uversky V.N., Dunker A.K. Predicting intrinsic disorder in proteins: An overview. Cell Research. 19, 8, 929-949, 2009.
  • Midic U., Oldfield C.J., Dunker A.K., Obradovic Z., Uversky V.N. Unfoldomics of human genetic diseases: Illustrative examples of ordered and intrinsically disordered members of human diseasome. Protein and Peptide Letters. 16, 12, 1533-1547, 2009.
  • Xue B., Dunbrack R.L., Williams R.W., Dunker A.K., Uversky V.N. PONDR-FIT: A meta-predictor of intrinsically disordered amino acids. Biochim. Biophys. Acta - Proteins and Proteomics. 1804, 4, 996-1010, 2010.
  • Uversky V.N., Dunker A.K. Understanding protein non-folding. Biochim. Biophys. Acta - Proteins and Proteomics. 1804, 6, 1231-1264, 2010.
  • 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. 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, 2010.
  • Xue B., Hsu W., Lu H., Dunker A.K., Uversky V.N. SPA: Short peptide analyzer on intrinsic disorder status. Genes to Cells. 15, 6, 635-646, 2010.
  • Xue B., Williams R.W., Oldfield C.J., Dunker A.K., Uversky V.N. Archaic chaos: Intrinsically disordered proteins in Archaea. BMC Systems Biology. 4 (Suppl. 1) S1, 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. Targeting intrinsically disordered proteins in neurodegenerative and protein dysfunction diseases: Another illustration of the D2 concept. Expert Review of Proteomics. 7, 4, 543-564, 2010.
  • Uversky V.N. Conformational behavior of intrinsically disordered proteins: Effects of strong denaturants, temperature, pH, counter ions, and macromolecular crowding. In: Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation (Uversky V.N., Longhi S., Eds.) In The Wiley Series in Protein and Peptide Science (Uversky V.N. series Ed.), John Wiley & Sons, Inc, Hoboken, New Jersey, USA. pp. 547-568, 2010.
  • Uversky V.N., Cortese M.S, Tompa P., Csizmok V., Dunker A.K. Large-scale identification of intrinsically disordered proteins. In: Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation (Uversky V.N., Longhi S., Eds.) In The Wiley Series in Protein and Peptide Science (Uversky V.N. series Ed.), John Wiley & Sons, Inc, Hoboken, New Jersey, USA. pp. 671-693, 2010.
  • Uversky V.N. Flexible nets of malleable guardians: Intrinsically disordered chaperones in neurodegenerative diseases. Chemical Reviews, 2011, 111, 2, 2234-1166 PMID: 21086986.
  • Uversky V.N. Multitude of binding modes attainable by intrinsically disordered proteins: A portrait gallery of disorder-based complexes. Chemical Society Reviews, 2011, 40, 3, 1623-1634. DOI: 10.1039/C0CS00057D.
  • Uversky V.N. Intrinsically disordered proteins may escape unwanted interactions via functional misfolding. Biochim. Biophys. Acta - Proteins and Proteomics, 2011, 1814, 5, 693–712 PMID: 21440685.
  • Xue B., Soeria-Atmadja D., Gustafsson M.G., Hammerling, U., Dunker A.K, Uversky V.N. Abundance and functional roles of intrinsic disorder in allergenic proteins and allergen representative peptides. Proteins: Structure, Function, and Bioinformatics, 2011, 79, 9, 2595-2606. PMD: 21732419.
  • Breydo L., Uversky V.N. Role of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases. Metallomics, 2011, 3, 11, 1163-1180. PMID: 21869995.
  • Xue B., Oldfield C.J., Van Y.Y., Dunker A.K., Uversky V.N. Protein intrinsic disorder and induced pluripotent stem cells. Molecular BioSystems, 2011, PMID: 21761058.
  • 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, 2011 PMID: 21922108.
  • Breydo L., Wu J.W., Uversky V.N. ?-Synuclein misfolding and Parkinson's disease. Biochim. Biophys. Acta – Molecular Basis of Diseases, 2011, PMID: 22024360.
  • 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, 2011, PMID: 22033837.
  • 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, 2011, 175, 2, 192-195 PMID: 21055425.
  • Hong D.-P., Han S., Fink A.L., Uversky V.N. Characterization of the non-fibrillar ?-synuclein oligomers. Protein and Peptide Letters, 2011, 18, 3, 230-240. PMID: 20858207.
  • Silva B.A., Einarsdottir, O., Fink A.L., Uversky V.N. Modulating ?-sinuclein misfolding and fibrillation in vitro by agrochemicals. Research and Reports in Biology, 2011, 2, 43-56. DOI: 10.2147/RRB.S16448.
  • Sigalov A.S., Uversky V.N. Protein disorder differentially occurs in the cytoplasmic signaling domains of cell receptors. Self/Nonself, 2011, 2, 1, 1-18.
  • Uversky V.N., Shah S., Gritsyna Yu., Hitchcock-DeGregori S.E., Kostyukova A.S. Systematic analysis of tropomodulin/tropomyosin interactions uncovers fine-tuned binding specificity of intrinsically disordered proteins. Journal of Molecular Recognition, 2011, 24, 4, 647-655. doi: 10.1002/jmr.1093. PMID: 21584876.
  • Uversky V.N. Intrinsically disordered proteins from A to Z. International Journal of Biochemistry and Cell Biology, 2011, 43, 8, 1090–1103. PMID: 21501695.
  • Mizianty M., Zhang T., Xue B., Zhou Y., Dunker A.K., Uversky V.N., Kurgan L. In-silico prediction of disorder content using hybrid sequence representation. BMC Bioinformatics, 2011, 12, 1, 245. PMID: 21682902.
  • Uversky, V.N, and Dunker, A.K. A multiparametric analysis of intrinsically disordered proteins: Looking at intrinsic disorder through compound eyes. Anal. Chem. (2012) 84, 5, 2096?2104.
  • Breydo, L., Wu, J.W., and Uversky, V.N. ?-Synuclein misfolding and Parkinson's disease. Biochim. Biophys. Acta – Molecular Basis of Diseases. (2012) 1822, 2, 261-285.
  • Disfani, F.M., Hsu, W.-L., Mizianty, M.J., Oldfield, C.J., Xue, B., Dunker, A.K., Uversky, V.N., and Kurgan, L. MoRFpred, a computational tool for sequence-based prediction and characterization of disorder-to-order transitioning binding sites in proteins. Bioinformatics (2012) 28, 12, i75-i83.
  • Sikirzhytski, V., Topilina, N.I, Takor, G.A., Higashiya, S., Welch, J.T., Uversky, V.N., and Lednev I.K. Fibrillation mechanism of a model intrinsically disordered protein revealed by 2D correlation deep UV resonance raman spectroscopy. Biomacromolecules (2012) 13, 5, 1503-1509.
  • Liu, J., Li, D.S., Dunker, A.K., and Uversky, V.N. Molecular profiling - an essential technology enabling personalized medicine in breast cancer. Current Drug Targets (2012) 13, 4, 541-554.
  • Xue, B., Mizianty, M., Kurgan, L., and Uversky, V.N. Protein intrinsic disorder as flexible armor and weapon of HIV-1. Cellular and Molecular Life Sciences (2012) 69, 8, 1211-1259.
  • Westerheide, S.D., Raynes, R., Powell, C., Xue, B., and Uversky, V.N. HSF transcription factor family, heat shock response, and protein intrinsic disorder. Current Protein and Peptide Science (2012) 13, 1, 86-103.
  • Uversky, V.N., Santambrogio, C., Brocca, S., and Grandori, R. Length-dependent compaction of intrinsically disordered proteins. FEBS Letters (2012) 586, 1, 70-73.
  • Johnson, D.E., Xue, B., Sickmeier, M.D., Meng, J., Cortese, M.S., Oldfield, C.J., Le Gall, T., Dunker, A.K., and Uversky V.N. High-throughput characterization of intrinsic disorder in proteins from the protein structure initiative. J. Struct. Biol. (2012) 180, 1, 201-215.
  • Adl, A.A., Nowzari-Dalini, A., Xue, X., Uversky, V.N., and Qian X. Accurate prediction of protein structural classes using functional domains and predicted secondary structure sequences. J. Biomol. Structure and Dynamics (2012) 29, 6, 623-633.
  • Zhang, T., Faraggi, E., Xue, B., Dunker, A.K., Uversky, V.N., and Zhou Y. Accurate prediction of short and long disordered regions by a single neural-network-based method. J. Biomol. Structure and Dynamics (2012) 29, 4, 799-813.
  • Melnik, B.S., Povarnitsyna, T.V., Glukhov, A.S., Melnik, T.N., and Uversky, V.N. SS-stabilizing proteins rationally: Intrinsic disorder-based design of stabilizing disulphide bridges in GFP. J. Biomol. Structure and Dynamics (2012) 29, 4, 817-824.
  • Ahmad, A., Burns, C.S., Fink, A.L., and Uversky, V.N. Peculiarities of the copper binding to ?-synuclein. J. Biomol. Structure and Dynamics (2012) 29, 4, 825-842.
  • Xue, B., Dunker, A.K., and Uversky, V.N. The roles of intrinsic disorder in orchestrating the Wnt pathway. J. Biomol. Structure and Dynamics (2012) 29, 5, 843-861.
  • Fedotoff, O., Mikheeva, L.M., Chait, A., Uversky, V.N., and Zaslavsky, B.Y. Influence of serum proteins on conformation of prostate-specific antigen. J. Biomol. Structure and Dynamics (2012) 29, 5, 1051-1064.
  • Xue, B., Dunker, A.K., and Uversky, V.N. Orderly order in protein intrinsic disorder distribution: Disorder in 3500 proteomes from viruses and the three domains of life. J. Biomol. Structure and Dynamics (2012) 30, 2, 131-142.
  • Uversky, V.N. Disordered competitive recruiter: Fast and foldable. J. Mol. Biol. (2012) 418, 5, 267-268.
  • Goh, G.K.-M., Dunker, A.K., and Uversky, V.N. Understanding viral transmission behavior via protein intrinsic disorder prediction: Coronaviruses. J. Pathogens. (2012) article ID 738590, doi:10.1155/2012/738590.
  • Kuznetsova, I.M., Sulatskaya, A.I., Uversky, V.N., and Turoverov, K.K. A new trend in experimental methodology for the analysis of the thioflavin T binding to amyloid fibrils. Mol. Neurobiol. (2012) 45, 3, 488-498.
  • Xue, B., Oldfield, C.J., Van, Y.Y., Dunker, A.K., and Uversky, V.N. Protein intrinsic disorder and induced pluripotent stem cells. Mol. BioSystems (2012) 8, 1, 134-150.
  • Zambelli, B., Cremades, N., Neyroz, P., Turano, P., Uversky, V.N., and Ciurli S. Insights in the (un)structural organization of Bacillus pasteurii UreG, an intrinsically disordered GTPase enzyme. Mol. BioSyst. (2012) 8, 1, 220-228.
  • Peng, Z., Mizianty, M.J., Xue, B., Kurgan, L., and Uversky V.N. More than just tails: Intrinsic disorder in histone proteins. Mol. Biosyst. (2012) 8, 7, 1886-1901.
  • Tipparaju, S.M., Li, X.-P., Kilfoil, P., Xue, B., Uversky, V.N., Bhatnagar, A., and Barski, O.A. Interactions between the C-terminus of Kv1.5 and Kv? regulate pyridine nucleotide-dependent changes in channel gating. Pflugers Archiv – Eur. J. Physiology. (2012) 463, 6, 799-181.
  • Hervas, R., Oroz, J., Galera-Prat, A., Goni, O., Valbuena, A., Vera, A., Gomez-Sicilia, A., Losada-Urzaiz, F., Uversky, V.N., Menendez, M., Laurents, D.V., Bruix, M., and Carrion-Vazquez, M. Common features at the start of the neurodegeneration cascade. PLoS Biology (2012) 10, 5, e1001335.
  • Vacic, V., Markwick, P.R.L., Oldfield, C.J., Zhao, X., Haynes, C., Uversky, V.N., and Iakoucheva, L.M. Disease-associated mutations disrupt functionally important regions of intrinsic protein disorder. PLoS Computational Biology (2012) 8, 10, e1002709.
  • Kuznetsova, I.M., Sulatskaya, A.I., Uversky, V.N., and Turoverov, K.K. Analyzing thioflavin T binding to amyloid fibrils by an equilibrium microdialysis-based technique. PLoS One (2012) 7, 2, e30724.
  • Singh, V.K., Rahman, M.N., Munro, M., Uversky, V.N., Smith, S., and Jia Z. Free cysteine modulates the conformation of human C/EBP homologous protein. PLoS One. (2012) 7, 4, e34680.
  • Xu, K., Uversky, V.N., and Xue, B. Local flexibility facilitates oxidization of buried methionine residues. Protein and Peptide Letters (2012)1 9, 6, 688-697.
  • Santner, A.A., Croy, C.H., Vasanwala, F.H., Uversky, V.N., Van, Y.Y., and Dunker, A.K. Sweeping away protein aggregation with entropic bristles: IDP fusions enhance soluble expression. Biochemistry (2012) 51, 37, 7250-7262.
  • Uversky, V.N. Intrinsically disordered proteins and novel strategies for drug discovery. Expert Opinion on Drug Discovery (2012) 7, 6, 475-488.
  • 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).
  • 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. (2012) 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. DOI: 10.1142/S0218339012400086 (IF – 0.570).
  • 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 – 8.278).
  • 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 – 3.733).
  • 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 – 3.733).
  • 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. PMID: 23361308.
  • Ribeiro M.C., Espinosa J., Islam S., Martinez O., Thanki J.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. 1 e2. PMID: 23638354.
  • 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. 288 (7) 4899-4907 PMID: 23271735 (IF – 4.651).
  • Xue B., Brown C.J., Dunker A.K., Uversky V.N. (2013) Intrinsically disordered regions of p53 family are highly diversified in evolution. Biochim. Biophys. Acta - Proteins and Proteomics. 1834 (4) 725-738. PMID: 23352836 (IF – 3.733).
  • 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. 22 (3) 258-273 PMID: 23233352 (IF – 2.735).
  • Sun X., Rikkerink E., Jones W.T., Uversky V. N. (2013) Multifarious roles of intrinsically disordered proteins in plant signalling and regulation. Plant Cell. 25 (1) 38-55. PMID: 23362206 (IF – 9.251).
  • Xue B., Jeffers V., Sullivan W.J., Jr., Uversky V.N. (2013) Protein intrinsic disorder in the acetylome of intracellular and extracellular Toxoplasma gondii. Molecular Biosystems. 9 (4) 645-657. PMID: 23403842 (IF – 3.350).
  • Uversky V.N. (2013) MultIDIMensionality of IDIMs: Intrinsic disorder in autoinhibition. Structure. 21 (3) 315-316. PMID: 23473663. (IF – 5.994).
  • Silva B.A., Breydo L., Uversky V.N. (2013) Targeting the chameleon: A focused look at -synuclein and its roles in neurodegeneration. Molecular Neurobiology. 47 (2) 446-459. PMID: 22940885 (IF – 5.471).
  • Silva B.A., Breydo L., Fink A.L., Uversky V.N. (2013) Agrochemicals, -synuclein, and Parkinson’s disease. Molecular Neurobiology. 47 (2) 598-612. PMID: 22933040. (IF – 5.471).
  • Ortiz J.F, MacDonald M., Masterson P., Uversky V.N., Siltberg-Liberles J. (2013) Rapid evolutionary dynamics of structural disorder as a potential driving force for biological divergence. Genome Biology and Evolution. 5 (3) 504-513. PMID: 23418179 (IF – 4.759).
  • Wood M., Rae G.M., Wu R.M., Walton E.F., Xue B., Hellens R.P., Uversky V.N. (2013) Actinidia DRM1 – An intrinsically disordered protein whose mRNA expression is inversely correlated with spring bud break in kiwifruit. PLOS ONE. 8 (3) e57354. PMID: 23516402 (IF – 3.730).
  • 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. (2013) What’s in a name? Why these proteins are intrinsically disordered. Intrinsically Disordered Proteins. 1 (1) e24157.
  • 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. 27 (4) 1450-1459. PMID: 23271055 (IF – 5.704).
  • Theillet F.-X., Kalmar L., Tompa P., Han K.-H., Dunker A.K. Selenko P., A.K. Dunker, Daughdrill G.W., Uversky V.N. (2013) 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.
  • Uversky V.N. (2013) Unusual biophysics of intrinsically disordered proteins. Biochim. Biophys. Acta - Proteins and Proteomics. 1834 (5) 932-951. PMID: 23269364 (IF –3.733).
  • Azia A., Uversky V.N., Horovitz A., Unger, R. (2013) The effects of mutations on protein function: A comparative study of three databases of mutations in humans. Israel Journal of Chemistry. 53 (3-4) 217 – 226. (IF – 3.025).
  • Uversky V.N. (2013) The alphabet of intrinsic disorder. II. Various roles of glutamic acids in ordered and intrinsically disordered proteins. Intrinsically Disordered Proteins. 1 (1) e24684.
  • Uversky V.N. (2013) Intrinsic disorder-based protein interactions and their modulators. Current Pharmaceutical Design. 42 (23) 4191 – 4213. PMID: 23170892 (IF – 3.311).
  • Xue B., Romero P.R., Noutsou M., Maurice M.M., Rüdiger S.G.D., William A.M. Jr., Mizianty M.J., Kurgan L., Uversky V.N., Dunker A.K. (2013) Stochastic machines as a colocalization mechanism for scaffold protein function. FEBS Letters. 587 (11) 1587-1591. PMID: 23603389 (IF – 3.582).
  • Uversky V.N. (2013) A decade and a half of protein intrinsic disorder: Biology still waits for physics. Protein Science. 22 (6) 693-724. PMID: 23553817 (IF – 2.735).
  • Lapteva Y.S., Uversky V.N., Permyakov S.E. (2013) Sequence microheterogeneity of parvalbumin, the major fish allergen. Biochim. Biophys. Acta - Proteins and Proteomics. 1834 (8) 1607-1614. PMID: 23632315 (IF – 3.733).
  • Uversky V.N. (2013) The most important thing is the tail: Multitudinous functionalities of intrinsically disordered protein termini. FEBS Letters. 587 (13) 1891-1901. PMID: 23665034 (IF – 3.582).
  • Yan J., Mizianty M., Filipow P.L., Uversky V.N., Kurgan L. (2013) RAPID: fast and accurate sequence-based prediction of intrinsic disorder content on proteomic scale. Biochim. Biophys. Acta – Proteins and Proteomics. 1834 (8) 1671-1680 PMID: 23732563 (IF –3.3733).
  • Bhat-Nakshatri P., Song E.-K., Collins N.R., Uversky V.N., Dunker A.K., O’Malley B.W., Geistlinger T.R., Carroll J.S., Brown M., Nakshatri H. (2012) Interplay between estrogen receptor and akt in estradiol-induced alternative splicing. BMC Medical Genomics. 6 21 PMID: 23758675 (IF – 3.807).
  • Malaney P., Pathak, R.R., Xue B., Uversky V.N., Davé V. (2013) Intrinsic disorder in PTEN and its interactome confers structural plasticity and functional versatility. Scientific Reports. 3 2035. PMID: 23783762 (IF – 2.927).
  • Kutyshenko V.P., Beskaravayny P.M., Paskevich S.I., Prokhorov D.A., Uversky V.N. (2013) Looking at microbe metabolism by high-resolution 2H-NMR spectroscopy. PeerJ. 1 e101. PMID: 23871835.
  • Testa L., Brocca S., Santambrogio C., D’Urzo A., Habchi J., Longhi S., Uversky V.N, Grandori R. (2013) Extracting structural information from charge-state distributions of intrinsically disordered proteins by non-denaturing electrospray-ionization mass spectrometry. Intrinsically Disordered Proteins. 1 (1) e25068.
  • Xue B., Uversky V.N. (2013) Structural characterizations of phosphorylatable residues in trans-membrane proteins from Arabidopsis thaliana. Intrinsically Disordered Proteins. 1 (1) e25713.
  • Uversky V.N. (2013) Digested disorder: Quarterly intrinsic disorder digest (January/February/ March, 2013) Intrinsically Disordered Proteins. 1 (1) e25496.
  • Williams R.W., Xue B., Uversky V.N., Dunker A.K. (2012) Distribution and cluster analysis of predicted intrinsically disordered protein Pfam domains. Intrinsically Disordered Proteins. 1 (1) e25724.
  • Uversky V.N. (2013) Hypothesis: The unfolding power of protein dielectricity. Intrinsically Disordered Proteins. 1 (1) e25725.
  • Choi U.B., Kazi R., Stenzoski N., Wollmuth L., Uversky V.N., Bowen M. E. (2013) Modulating the intrinsic disorder in the cytoplasmic domain alters the biological activity of the N-methyl D-aspartate-sensitive glutamate receptor. Journal of Biological Chemistry. 288 (31) 22506-22515. PMID: 23782697 (IF – 4.651).
  • Peng Z., Xue B., Kurgan L., Uversky V.N. (2013) Resilience of death: Intrinsic disorder in proteins involved in the programmed cell death. Cell Death and Differentiation. 20 (9) 1257-1267. PMID: 23764774 (IF – 8.371).
  • Shivu B., Li J., Oberg K.A., Seshadri S., Uversky V.N., Fink A.L. (2013) Distinct -sheet structure in protein aggregates determined by ATR-FTIR spectroscopy. Biochemistry. 52 (31) 5176–5183. PMID: 23837615 (IF – 3.377)
  • Hedlund R., Uversky V.N. (2013) Understanding the molecular mechanisms underlying complex cancer genome rearrangements. Intrinsically Disordered Proteins. 1 (2) e25954.
  • Uversky V.N. (2013) Under-folded proteins: Conformational ensembles and their roles in protein folding, function and pathogenesis. Biopolymers. 99 (11) 870-997. PMID: 23754493 (IF – 2.879).
  • Kutyshenko V.P., Prokhorov D.A., Timchenko М.А., Kudrevatykh Yu.А., Gushchina L.V., Filimonov V.V., Uversky V.N. (2014) Dancing retro: Solution structure and micelle interactions of the retro-SH3-domain, retro-SHH-“Bergerac”. Journal of Biomolecular Structure and Dynamics. 32 (2) 257-272. PMID: 23527530 (IF – 2.983).
  • Lee C., Kalmar L., Xue B., Tompa P., Daughdrill G.W., Uversky V.N., Han K.H. (2014) Contribution of proline to the pre-structuring tendency of transient helical secondary structure elements in intrinsically disordered proteins. Biochim. Biophys. Acta – General Subjects. 1840 (3) 993-1003. PMID: 24211251 (IF – 3.829).
  • Breydo L., Reddy K.D., Piai A., Felli I.C., Pierattelli R., Uversky V.N. (2014) The crowd you’re in with: Effects of different types of crowding agents on protein aggregation. Biochim. Biophys. Acta – Proteins and Proteomics. 1844 (2) 346-357, PMID: 24252314 (IF –3.191).
  • Uversky V.N. (2014) The triple power of D3: Protein intrinsic disorder in degenerative diseases. Frontiers in Bioscience. 19 (1) 181-258, PMID: 24389181 (IF – 4.249).
  • Varadi M., Kosol S., Lebrun P., Valentini E., Blackledge M., Dunker A.K., Felli I.C., Forman-Kay J., Kriwacki R.W., Pierattelli R., Sussman J., Svergun D., Uversky V.N., Vendruscolo M., Wishart D., Wright P.E., Tompa P. (2014) pE-DB: the database of structural ensembles of intrinsically disordered and denatured proteins. Nucleic Acids Research. 42 (1) D326-D335. PMID: 24174539 (IF – 8.808).
  • Ferreira L., Fan X., Mikheeva L.M, Madeira P.P., Kurgan L., Uversky V.N., Zaslavsky B.Y. (2014) Structural features important for differences in protein partitioning in aqueous dextran-polyethylene glycol two-phase systems of different ionic composition. Biochim. Biophys. Acta –Proteins and Proteomics. 1844 (3) 694-704. PMID: 24442277 (IF –3.191).
  • Madeira P.P., Bessa A., Álvares-Ribeiro L.M., Aires-Barros M.R., Rodrigues A.E., Uversky V.N., Zaslavsky B.Y. (2014) Amino acid-water interactions study: A new amino acid scale. Journal of Biomolecular Structure and Dynamics. 32 (6) 959-968. PMID: 23781980 (IF – 2.983).
  • Xue B., Uversky V.N. (2014) 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. PMID: 24184279 (IF – 3.959).
  • Mizianty M., Uversky V.N., Kurgan L. (2014) Prediction of intrinsic disorder in proteins using MFDp2. Methods in Molecular Biology. 1137 147-162. PMID: 24573480
  • Na I., Reddy K.D., Breydo L., Xue B., Uversky V.N. (2014) A putative role of the Sup35p C-terminal domain in the cytoskeleton organization during the yeast mitosis. Molecular BioSystems. 10 (4) 925-940. PMID: 24549315 (IF – 3.183).
  • Xue B., Ganti K., Rabionet A., Banks L., Uversky V.N. (2014) Disordered interactome of human papillomavirus. Current Pharmaceutical Design. 20 (8) 1274 - 1292. PMID: 23713779 (IF – 3.288).
  • Peng Z., Oldfield, C.J., Xue B., Mizianty M.J., Dunker A.K. Kurgan L., Uversky V.N. (2014) A creature with hundred of waggly tails: Intrinsically disordered proteins in the ribosome. Cellular and Molecular Life Sciences. 71 (8) 1477-1504. PMID: 23942625 (IF – 5.856).
  • DeForte S., Reddy K.D., Uversky V.N. (2013) Digested disorder, issue #2: Quarterly intrinsic disorder digest (April-May-June, 2013). Intrinsically Disordered Proteins. 1 (1) e27454.
  • Reddy K.D., DeForte S., Uversky V.N. (2014) Digested disorder, issue #3: Quarterly intrinsic disorder digest (July-August-September, 2013). Intrinsically Disordered Proteins. 2 e27833.
  • Peng Z., Sakai Y., Kurgan L., Sokolowski B., Uversky V.N. (2014) Intrinsic disorder in the BK channel and its interactome. PLOS ONE. 9 (4) e94331 PMID: 24727949 (IF – 3.534).
  • Fan X., Dolan P.T., Xue B., LeCount D.J., Kurgan L., Uversky V.N. (2014) The intrinsic disorder status of the human hepatitis C virus proteome. Molecular BioSystems. 10 (6) 1345-1363 PMID: 24752801 (IF – 3.183).
  • Butler C., Lucas O., Wuchty S., Xue B., Uversky V.N., White M. (2014) Identifying novel cell cycle proteins in Apicomplexa parasites through co-expression decision analysis. PLOS ONE. 9 (5) e97625. PMID: 24841368 (IF – 3.534).
  • Rae G.M., Uversky V.N., David K., Wood M. (2014) DRM1 and DRM2 expression regulation: potential role of splice variants in response to stress and environmental factors in Arabidopsis thaliana. Molecular Genetics and Genomics. 289 (3) 317-332. PMID: 24442277 (IF – 2.831).
  • Popelka H., Uversky V.N., Klionsky D.J. (2014) Identification of Atg3 as an intrinsically disordered polypeptide yields insights into the molecular dynamics of autophagy-related proteins in yeast. Autophagy. 10 (6) 1093-1104. PMID: 24879155 (IF – 11.423).
  • Kovacs G.G., Breydo L., Green R., Kis V., Puska G., Lőrincz P., Perju-Dumbrava L., Giera R., Pirker W., Lutz M., Lachmann I., Budka H., Uversky V.N., Molnár K., László L. (2014) Intracellular processing of disease-associated -synuclein in the human brain resembles spreading of prions in prion disease. Neurobiology of Disease. 69C 76-92. PMID: 24878508 (IF – 5.202).
  • Redwan E.M., EL-Fakharany E.M., Uversky V.N., Linjawi M.H. (2014) Screening the antiinfectivity potentials of native N- and C-lobes derived from the camel lactoferrin against hepatitis C virus. BMC Complement. Altern. Med. 14 (1) 219. PMID: 24993815 (IF – 1.877).
  • Angelani C.R., Curto L.M., Cabanas I.S., Caramelo J.J., Uversky V.N., Delfino J.M. (2014) Toward a common aggregation mechanism for a β-barrel protein family: Insights derived from a stable dimeric species. Biochim. Biophys. Acta – Proteins and Proteomics. 1844 (9) 1599-1607 PMID: 24929115 (IF – 3.191).
  • Uversky V.N. (2014) Introduction to intrinsically disordered proteins (IDPs). Chemical Reviews. 114 (13) 6557-6560. PMID: 25004990 (IF – 45.661).
  • Habchi J., Tompa P., Longhi S., Uversky V.N. (2014) Introducing protein intrinsic disorder phenomenon. Chemical Reviews. 114 (13) 6561-6588. PMID: 24739139 (IF – 45.661).
  • van der Lee R., Buljan M., Lang B., Weatheritt R.J., Daughdrill G.W., Dunker A.K., Fuxreiter M., Gough J., Gsponer J., Jones D.T., Kim P.M., Kriwacki R.W., Oldfield C.J., Pappu R., Tompa P., Uversky V.N., Wright P.E., Babu M.M. (2014) Classification of intrinsically disorded proteins and regions. Chemical Reviews. 114 (13) 6589-6631. PMID: 24773235 (IF – 45.661).
  • Jacob U., Kriwacki R., Uversky V.N. (2014) Conditionally and transiently disordered proteins: Awakening cryptic disorder to regulate protein function. Chemical Reviews. 114 (13) 6779-6805. PMID: 24502763 (IF – 45.661).
  • Fuxreiter M., Tóth-Petróczy A., Kraut D.A., Lim R.Y.H., Matouschek A., Xue B., Kurgan L., Uversky V.N. (2014) Disordered proteinaceous machines. Chemical Reviews. 114 (13) 6806-6843. PMID: 24702702 (IF – 45.661).
  • Uversky V.N., Davé V., Eliezer D., Iakoucheva L., Malaney P., Metallo S., Pathak, R.R., Joerger A.C. (2014) Pathological unfoldomics of uncontrolled chaos: Intrinsically disordered proteins and human diseases. Chemical Reviews. 114 (13) 6844-6879. PMID: 24830552 (IF – 45.661).
  • Xue B., Blocquel D., Habchi J., Uversky A.V., Kurgan L., Uversky V.N., Longhi S. (2014) Structural and functional disorder in viral proteins. Chemical Reviews. 114 (13) 6880-6911. PMID: 24823319 (IF – 45.661).
  • Povarova O.I., Uversky V.N., Kuznetsova I.M., Turoverov K.K. (2014) Actinous enigma or enigmatic actin: Folding, unfolding, misfolding, and nonfolding of most abundant eukaryotic protein. Intrinsically Disordered Proteins. 2 e34500.
  • Pejaver V., Hsu W.-L., Xin F., Dunker A.K. Uversky V.N., Radivojac P. (2014) Structural and functional aspects of concerted regulation by posttranslational modifications. Protein Science. 23 (8) 1077-1093. PMID: 24888500 (IF – 2.861).
  • Uversky V.N. (2014) Wrecked regulation of intrinsically disordered proteins in diseases: Pathogenicity of deregulated regulators. Frontiers in Molecular Biosciences: Protein Folding, Misfolding and Degradation. 1 (article 6) 1-24.
  • Sun X., Templeton M.D., Greenwood D.R., Libich D.S., McGhie T.K., Xue B., Yoon M., Cui W., Kirk C.A., Jones W.T., Uversky V.N., Rikkerink E.H.A. (2014) The intrinsically disordered structural platform of the plant defense hub protein RIN4 provides insights into its mode of action in the host-pathogen interface and evolution of the NOI protein family. FEBS J. 281 (17) 3955-3979. PMID: 25039985 (IF – 3.986).
  • Redwan E.M., Uversky V.N., El-Fakharany E.M., Al-Mehdar H. (2014) Potential lactoferrin activity against pathogenic viruses. Comptes Rendus Biologies. 337 (1) 581-595. PMID: 25282173 (IF – 1.681).
  • Kathiriya J., Pathak, R.R., Clayman E., Xue B., Uversky V.N., Davé V. (2014) Presence and utility of intrinsically disordered regions in kinases. Molecular BioSystems. 10 (11) 2876-2888. PMID: 25099472 (IF –3.183).
  • Uversky V.N. (2014) Unreported intrinsic disorder in proteins: Building connections to the literature on IDPs. Intrinsically Disordered Proteins. 2 e36409.
  • Stojanovski B., Breydo L., Hunter G.A., Uversky V.N., Ferreira G.C. (2014) Catalytically active alkaline molten globular enzyme: Effect of pH and temperature on the structural integrity of 5-aminolevulinate synthase. Biochim. Biophys. Acta – Proteins and Proteomics. 1844 (12) 2145-2154. PMID: 25240868 (IF –3.191).
  • 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. (2014) Probiotic properties of Lactobacillus crispatus 2029: homeostatic interaction with cervicovaginal epithelial cells and antagonistic activity to genitourinary pathogens. Probiotics Antimicrob. Proteins. 6 (3-4) 165-176. PMID: 25028263.
  • Huang F., Oldfield C.J., Xue B., Hsu W., Meng J., Liu X., Shen L., Romero P., Uversky V.N., Dunker A.K. (2014) Improving protein order-disorder classification using charge hydropathy plots. BMC Bioinformatics. 15 (Suppl 17) S4. (IF – 2.687).
  • Murina VN, Selivanova OM, Mikhaylina AO, Kazakov AS, Nikonova EY,Lekontseva NV, Tishchenko SV, Nikulin AD. Supramolecular organization of Hfq-like proteins. Biochemistry (Mosc). 2015;v.80, N4, p.441-448. doi: 10.1134/S0006297915040070.
  • Permyakov, E.A., Permyakov, S.E., Breydo, L., Redwan, E.M., Almehdar, H.A., Uversky, V.N. (2015) Disorder in milk proteins: α-Lactalbumin, a multifunctional whey protein acting as an oligomeric molten globular “oil container” in the anti-tumorigenic drugs, liprotides. Current Protein & Peptide Science.
  • Polanco C., Samaniego J.L., Uversky V.N., Castañón-González J.A., Buhse T., Leopold-Sordo M., Madero-Arteaga A., Morales-Reyes A., Tavera-Sierra L., González-Bernal J.A., Arias-Estrada M. (2015) Identification of proteins associated with amyloidosis by polarity index method. Acta Biochimica Polonica. 62 (1) 41-55. PMID: 25669158 (IF – 1.143).
  • Uversky V.N. (2015) Protein misfolding in lipid-mimetic environments. Advances in Experimental Medicine and Biology. 855, 33-66. PMID: 26149925. (IF – 1.958).
  • Uversky V.N. (2015) Biophysical methods to investigate intrinsically disordered proteins: Avoiding an "elephant and blind men" situation. Advances in Experimental Medicine and Biology. 870 215-260. PMID: 26387104
  • Portillo A., Zhang Y., Breydo L., Uversky V.N., Lyubchenko Y.L. (2015) Role of monomer arrangement in the amyloid self-assembly. Biochim. Biophys. Acta – Proteins and Proteomics. 1854 (3) 218–228. PMID: 25542374 (IF – 2.747).
  • Sluchanko N.N., Uversky V.N. (2015) 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. Biochim. Biophys. Acta – Proteins and Proteomics. 1854 (5) 492-504. PMID: 25747569. (IF – 2.747).
  • Frege T., Uversky V.N. (2015) Intrinsically disordered proteins in the nucleus of human cells. Biochemistry & Biophysics Reports. 1 (1) 33-51.
  • Breydo L., Sales A.E., Frege T., Howell M., Ferreira L.A., Zaslavsky B.Y., Uversky V.N. (2015) Effects of polymer hydrophobicity on protein structure and aggregation kinetics in crowded milieu. Biochemistry. 54 (19) 2957-2966. PMID: 25919930. (IF – 3.015).
  • Uversky V.N. (2015) Proteins without unique 3D structures: Biotechnological applications of intrinsically unstable/disordered proteins. Biotechnology Journal. 10 (3) 356-366. PMID: 25287424 (IF – 3.490).
  • Peng Z., Yan, J., Fan X., Mizianty M.J., Xue B., Uversky V.N., Kurgan L. (2015) 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. PMID: 24939692 (IF – 5.808).
  • Uversky V.N. (2015) Hot, hotter, and hottest trends in α-synuclein research. Current Protein and Peptide Science. 16 (8) 682-687. (IF – 3.154).
  • Almehdar H.A., El-Fakharany E.M., Uversky V.N., Redwan E.M. (2015) Disorder in milk proteins: Structure, functional disorder, and biocidal potentials of lactoperoxidase. Current Protein and Peptide Science. 16 (4) 352-365. PMID: 25772156. (IF – 3.154).
  • Lopes F.C., Dobrovolska O., Guerra R.R., Broll V., Zambelli B., Musiani F., Uversky V.N., Carlini C.R., Ciurli S. (2015) Pleable biocide: Disordered nature of Jaburetox, an insectidal peptide derived from the jack bean (Canavalia ensiformis) urease. FEBS Journal. 282 (6) 1043-1064. PMID: 25605001 (IF – 4.001).
  • Uversky V.N., Kuznetsova I.M., Turoverov K.K., Zaslavsky B.Y. (2015) Hypothesis: Intrinsically disordered proteins as crucial constituents of cellular aqueous two phase systems and coacervates. FEBS Letters. 589 (1) 15-22. PMID: 25436423 (IF – 3.169).
  • Uversky V.N. Oldfield C.J. (2015) Pliability of protein complexes and complexity of protein pliability. FEBS Letters. 589 (19, part A), 2431-2432. PMID: 26325593. (IF – 3.169).
  • Uversky V.N. (2015) The multifaceted roles of intrinsic disorder in protein complexes. FEBS Letters. 589 (19, part A), 2498-2506. PMID: 26073257. (IF – 3.169).
  • Wu Z., Hu G., Yang J., Peng Z., Uversky V.N., Kurgan L. (2015) In various protein complexes, disordered protomers have large per-residue surface areas and areas of protein-, DNA- and RNA-binding interfaces. FEBS Letters. 589 (19, part A), 2561-2569. PMID: 26297830. (IF – 3.169).
  • Breydo L., Uversky V.N. (2015) Structural, morphological, and functional diversity of amyloid oligomers. FEBS Letters. 589 (19, part A), 2640-2648. PMID: 26188543. (IF – 3.347).
  • Uversky V.N. (2015) Intrinsically disordered proteins and their (disordered) proteomes in neurodegenerative disorders. Front. Aging Neurosci. 7, article 18, 1-6. doi: 10.3389/fnagi.2015.00018 PMID: 25784874. (IF – 4.000).
  • DeForte S., Reddy K.D., Uversky V.N. (2015) Digested disorder, issue #4: Quarterly intrinsic disorder digest (October-November-December, 2013). Intrinsically Disordered Proteins. 3 (1) 1-10. DOI: 10.4161/21690707.2014.984569.
  • Uversky V.N. (2015) The intrinsic disorder alphabet: III. Dual personality of serine. Intrinsically Disordered Proteins. 3 (1) 1-21. DOI: 10.1080/21690707.2015.1027032.
  • Uversky V.N. (2015) Paradoxes and wonders of intrinsic disorder: Prevalence of exceptionality. Intrinsically Disordered Proteins. 3 (1) 1-3. DOI: 10.1080/21690707.2015.1065029.
  • Ferreira L.A., Cole J.T., Reichardt C., Holland N.B., Uversky V.N., Zaslavsky B.Y. (2015) Effect of elastin-like polypeptide on solvent properties of aqueous media. International Journal of Molecular Sciences. 16 (6) 13528-13547. PMID: 26075870 (IF – 2.862).
  • Petrovich A., Borne A., Uversky V.N., Xue B. (2015) Identifying similar patterns of structural flexibility in proteins by disorder prediction and dynamic programming. International Journal of Molecular Sciences. 16 (6) 13829-13849. PMID: 26086829. (IF – 2.862).
  • Ferreira L., Madeira P.P., Uversky A.V., Uversky V.N., Zaslavsky B.Y. (2015) Responses of proteins to different ionic environment are linearly interrelated. Journal of Chromatography A. 1387 32-41. PMID: 25708470. (IF – 4.169).
  • Kutyshenko V.P., Budantsev A., Uversky V.N. (2015) 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.
  • Malaney, P., Uversky V.N., Dave V. (2015) Identification of intrinsically disordered regions in PTEN and delineation of its function via a network approach. Methods. 77-78 69-74. PMID: 25449897. (IF – 3.645).
  • Goh G.K.M., Dunker A.K., Uversky V.N. (2014) Shell disorder, immune evasion and transmission behavior among animal and human retroviruses. Molecular Biosystems. 11 (8) 2312-2323. PMID: 26080321. (IF – 3.210).
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