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Лаборатория новых методов в биологии

Некоторые публикации лаборатории по тематике нативно разупорядоченных белков

  • 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).
  • Goh G.K.M., Dunker A.K., Uversky V.N. (2015) Detection of links between Ebola nucleocapsid and virulence using disorder analysis. Molecular Biosystems. 11 (8) 2337-2344. PMID: 26086270. (IF – 3.210).
  • Kutyshenko V.P., Beskaravayny P., Uversky V.N. (2015) “In-plant” NMR: Analysis of the intact plant Vesicularia dubyana by high resolution NMR spectroscopy. Molecules. 20 (3) 4359-4368 PMID: 25759953 (IF – 2.416).
  • Dolan P.T., Roth A.P., Sun R., Dunker A.K., Uversky V.N., LaCount D.J. (2015) Intrinsic disorder mediates hepatitis C virus core – host cell protein interactions. Protein Science. 24 (2) 221-235. PMID: 25424537 (IF – 2.854).
  • Ferreira L., Fedotoff O., Uversky V.N., Zaslavsky B.Y. (2015) Effects of osmolytes on protein-solvent interactions in crowded environment: Study of sucrose and trehalose effects on different proteins by solvent interaction analysis. RSC Advances. 5 (34) 27154-27162. PMID: (IF – 3.708).
  • Prokhorov D.A., Mikoulinskaia G.V., Molochkov N.V., Uversky V.N., Kutyshenko V.P. (2015) High-resolution NMR structure of a Zn+2-containing form of the bacteriophage T5 L-alanyl-D-glutamate peptidase. RSC Advances. 5 (51) 41041-41049. PMID: (IF – 3.708).