Uversky VN - Search Results

1

A new approach to artificial and modified proteins: theory-based design, synthesis in a cell-free system and fast testing of structural properties by radiolabels.

Chemeris VV, Dolgikh DA, Fedorov AN, Finkelstein AV, Kirpichnikov MP, Uversky VN, Ptitsyn OB. Chemeris VV, et al. Among authors: uversky vn. Protein Eng. 1994 Aug;7(8):1041-52. doi: 10.1093/protein/7.8.1041. Protein Eng. 1994. PMID: 7809031

2

Triple point mutation Asp10-->His, Asn101-->Asp, Arg148-->Ser in T4 phage lysozyme leads to the molten globule.

Uversky VN, Leontiev VV, Gudkov AT. Uversky VN, et al. Protein Eng. 1992 Dec;5(8):781-3. doi: 10.1093/protein/5.8.781. Protein Eng. 1992. PMID: 1287658

3

'All-or-none' mechanism of the molten globule unfolding.

Uversky VN, Semisotnov GV, Pain RH, Ptitsyn OB. Uversky VN, et al. FEBS Lett. 1992 Dec 7;314(1):89-92. doi: 10.1016/0014-5793(92)81468-2. FEBS Lett. 1992. PMID: 1451808 Free article.

4

Circularly permuted dihydrofolate reductase of E. coli has functional activity and a destabilized tertiary structure.

Protasova NYu, Kireeva ML, Murzina NV, Murzin AG, Uversky VN, Gryaznova OI, Gudkov AT. Protasova NYu, et al. Among authors: uversky vn. Protein Eng. 1994 Nov;7(11):1373-7. doi: 10.1093/protein/7.11.1373. Protein Eng. 1994. PMID: 7700869

5

Kinetic and equilibrium folding intermediates.

Ptitsyn OB, Bychkova VE, Uversky VN. Ptitsyn OB, et al. Among authors: uversky vn. Philos Trans R Soc Lond B Biol Sci. 1995 Apr 29;348(1323):35-41. doi: 10.1098/rstb.1995.0043. Philos Trans R Soc Lond B Biol Sci. 1995. PMID: 7770484

6

"Partly folded" state, a new equilibrium state of protein molecules: four-state guanidinium chloride-induced unfolding of beta-lactamase at low temperature.

Uversky VN, Ptitsyn OB. Uversky VN, et al. Biochemistry. 1994 Mar 15;33(10):2782-91. doi: 10.1021/bi00176a006. Biochemistry. 1994. PMID: 8130190

7

The molten globule is a third thermodynamical state of protein molecules.

Ptitsyn OB, Uversky VN. Ptitsyn OB, et al. Among authors: uversky vn. FEBS Lett. 1994 Mar 14;341(1):15-8. doi: 10.1016/0014-5793(94)80231-9. FEBS Lett. 1994. PMID: 8137915 Free article.

8

Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule.

Uversky VN. Uversky VN. Biochemistry. 1993 Dec 7;32(48):13288-98. doi: 10.1021/bi00211a042. Biochemistry. 1993. PMID: 8241185

9

Comparative stability of dihydrofolate reductase mutants in vitro and in vivo.

Leontiev VV, Uversky VN, Gudkov AT. Leontiev VV, et al. Among authors: uversky vn. Protein Eng. 1993 Jan;6(1):81-4. doi: 10.1093/protein/6.1.81. Protein Eng. 1993. PMID: 8433973

10

Further evidence on the equilibrium "pre-molten globule state": four-state guanidinium chloride-induced unfolding of carbonic anhydrase B at low temperature.

Uversky VN, Ptitsyn OB. Uversky VN, et al. J Mol Biol. 1996 Jan 12;255(1):215-28. doi: 10.1006/jmbi.1996.0018. J Mol Biol. 1996. PMID: 8568868

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