Uversky VN - Search Results

1

Polymorphism of the Cysteine Protease YopT from Yersinia pestis.

Platonov ME, Svetoch TE, Evseeva VV, Knyazeva AI, Dentovskaya SV, Motin VL, Uversky VN, Anisimov AP. Platonov ME, et al. Among authors: uversky vn. Protein Pept Lett. 2016;23(4):379-85. doi: 10.2174/0929866523666160204124259. Protein Pept Lett. 2016. PMID: 26845766

2

Attachment of LcrV from Yersinia pestis at dual binding sites to human TLR-2 and human IFN-gamma receptor.

Abramov VM, Khlebnikov VS, Vasiliev AM, Kosarev IV, Vasilenko RN, Kulikova NL, Khodyakova AV, Evstigneev VI, Uversky VN, Motin VL, Smirnov GB, Brubaker RR. Abramov VM, et al. Among authors: uversky vn. J Proteome Res. 2007 Jun;6(6):2222-31. doi: 10.1021/pr070036r. Epub 2007 Apr 19. J Proteome Res. 2007. PMID: 17441749

3

Unfoldomics of human genetic diseases: illustrative examples of ordered and intrinsically disordered members of the human diseasome.

Midic U, Oldfield CJ, Dunker AK, Obradovic Z, Uversky VN. Midic U, et al. Among authors: uversky vn. Protein Pept Lett. 2009;16(12):1533-47. doi: 10.2174/092986609789839377. Protein Pept Lett. 2009. PMID: 20001916 Review.

4

Local flexibility facilitates oxidization of buried methionine residues.

Xu K, Uversky VN, Xue B. Xu K, et al. Among authors: uversky vn. Protein Pept Lett. 2012 Jun 1;19(6):688-97. doi: 10.2174/092986612800494084. Protein Pept Lett. 2012. PMID: 22519542

5

Disorder in milk proteins: caseins, intrinsically disordered colloids.

Redwan EM, Xue B, Almehdar HA, Uversky VN. Redwan EM, et al. Among authors: uversky vn. Curr Protein Pept Sci. 2015;16(3):228-42. doi: 10.2174/1389203716666150224145900. Curr Protein Pept Sci. 2015. PMID: 25714333 Review.

6

Disorder in milk proteins: structure, functional disorder, and biocidal potentials of lactoperoxidase.

Almehdar HA, El-Fakharany EM, Uversky VN, Redwan EM. Almehdar HA, et al. Among authors: uversky vn. Curr Protein Pept Sci. 2015;16(4):352-65. doi: 10.2174/1389203716666150316114956. Curr Protein Pept Sci. 2015. PMID: 25772156 Review.

7

Pliability of protein complexes and complexity of protein pliability.

Uversky VN, Oldfield CJ. Uversky VN, et al. FEBS Lett. 2015 Sep 14;589(19 Pt A):2431-2. doi: 10.1016/j.febslet.2015.08.035. Epub 2015 Aug 29. FEBS Lett. 2015. PMID: 26325593 Free article. No abstract available.

8

Disorder in Milk Proteins: α-Lactalbumin. Part B. A Multifunctional Whey Protein Acting as an Oligomeric Molten Globular "Oil Container" in the Anti-Tumorigenic Drugs, Liprotides.

Uversky VN, Permyakov SE, Breydo L, Redwan EM, Almehdar HA, Permyakov EA. Uversky VN, et al. Curr Protein Pept Sci. 2016 Jul 15;17(6):612-28. doi: 10.2174/1389203717666151203003151. Curr Protein Pept Sci. 2016. PMID: 26916155 Review.

9

Disorder in Milk Proteins: α -Lactalbumin. Part A. Structural Properties and Conformational Behavior.

Permyakov EA, Permyakov SE, Breydo L, Redwan EM, Almehdar HA, Uversky VN. Permyakov EA, et al. Among authors: uversky vn. Curr Protein Pept Sci. 2016;17(4):352-67. doi: 10.2174/138920371704160405001222. Curr Protein Pept Sci. 2016. PMID: 26956441 Review.

10

α-Lactalbumin: Of Camels and Cows.

Redington JM, Breydo L, Almehdar HA, Redwan EM, Uversky VN. Redington JM, et al. Among authors: uversky vn. Protein Pept Lett. 2016;23(12):1072-1080. doi: 10.2174/0929866523666160517123738. Protein Pept Lett. 2016. PMID: 27184498

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