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Laboratory of new methods in biology: Some publications on natively disordered proteins

  • 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.
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