Zerovnik E - Search Results

1

Calorimetric measurements of thermal denaturation of stefins A and B. Comparison to predicted thermodynamics of stefin-B unfolding.

Zerovnik E, Lohner K, Jerala R, Laggner P, Turk V. Zerovnik E, et al. Eur J Biochem. 1992 Nov 15;210(1):217-21. doi: 10.1111/j.1432-1033.1992.tb17411.x. Eur J Biochem. 1992. PMID: 1446674 Free article.

2

Denaturation of stefin B by GuHCl, pH and heat; evidence for molten globule intermediates.

Zerovnik E, Jerala R, Kroon-Zitko L, Turk V, Pain RH. Zerovnik E, et al. Biol Chem Hoppe Seyler. 1992 Jul;373(7):453-8. doi: 10.1515/bchm3.1992.373.2.453. Biol Chem Hoppe Seyler. 1992. PMID: 1515074

3

Intermediates in denaturation of a small globular protein, recombinant human stefin B.

Zerovnik E, Jerala R, Kroon-Zitko L, Pain RH, Turk V. Zerovnik E, et al. J Biol Chem. 1992 May 5;267(13):9041-6. J Biol Chem. 1992. PMID: 1577741 Free article.

4

Folding studies of the cysteine proteinase inhibitor--human stefin A.

Zerovnik E, Lenarcic B, Jerala R, Turk V. Zerovnik E, et al. Biochim Biophys Acta. 1991 Jul 12;1078(3):313-20. doi: 10.1016/0167-4838(91)90149-t. Biochim Biophys Acta. 1991. PMID: 1859820

5

Refolding of chicken cystatin and human stefin A studied by fast protein liquid chromatography (FPLC).

Zerovnik E, Kos J, Lenarcic B, Turk V. Zerovnik E, et al. Biol Chem Hoppe Seyler. 1990 May;371 Suppl:151-6. Biol Chem Hoppe Seyler. 1990. PMID: 2400575

6

Structural basis for the difference in thermodynamic properties between the two cysteine proteinase inhibitors human stefins A and B.

Jerala R, Zerovnik E, Lohner K, Turk V. Jerala R, et al. Among authors: zerovnik e. Protein Eng. 1994 Aug;7(8):977-84. doi: 10.1093/protein/7.8.977. Protein Eng. 1994. PMID: 7809037

7

The three-dimensional solution structure of human stefin A.

Martin JR, Craven CJ, Jerala R, Kroon-Zitko L, Zerovnik E, Turk V, Waltho JP. Martin JR, et al. Among authors: zerovnik e. J Mol Biol. 1995 Feb 17;246(2):331-43. doi: 10.1006/jmbi.1994.0088. J Mol Biol. 1995. PMID: 7869384

8

Compactness of the molten globule in comparison to unfolded states as observed by size-exclusion chromatography.

Zerovnik E, Jerala R, Poklar N, Kroon-Zitko L, Turk V. Zerovnik E, et al. Biochim Biophys Acta. 1994 Nov 16;1209(1):140-3. doi: 10.1016/0167-4838(94)90149-x. Biochim Biophys Acta. 1994. PMID: 7947976

9

Structural characterisation of human stefin A in solution and implications for binding to cysteine proteinases.

Martin JR, Jerala R, Kroon-Zitko L, Zerovnik E, Turk V, Waltho JP. Martin JR, et al. Among authors: zerovnik e. Eur J Biochem. 1994 Nov 1;225(3):1181-94. doi: 10.1111/j.1432-1033.1994.1181b.x. Eur J Biochem. 1994. PMID: 7957209 Free article.

10

Human cathepsin B is a metastable enzyme stabilized by specific ionic interactions associated with the active site.

Turk B, Dolenc I, Zerovnik E, Turk D, Gubensek F, Turk V. Turk B, et al. Among authors: zerovnik e. Biochemistry. 1994 Dec 13;33(49):14800-6. doi: 10.1021/bi00253a019. Biochemistry. 1994. PMID: 7993907

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