Russo Krauss I - Search Results

1

Identification of an active dimeric intermediate populated during the unfolding process of the cambialistic superoxide dismutase from Streptococcus mutans.

Merlino A, Russo Krauss I, Rossi B, Vergara A, De Vendittis A, Marco S, De Vendittis E, Sica F. Merlino A, et al. Among authors: russo krauss i. Biochimie. 2012 Mar;94(3):768-75. doi: 10.1016/j.biochi.2011.11.008. Epub 2011 Nov 28. Biochimie. 2012. PMID: 22155088

2

Structure and flexibility in cold-adapted iron superoxide dismutases: the case of the enzyme isolated from Pseudoalteromonas haloplanktis.

Merlino A, Russo Krauss I, Castellano I, De Vendittis E, Rossi B, Conte M, Vergara A, Sica F. Merlino A, et al. Among authors: russo krauss i. J Struct Biol. 2010 Dec;172(3):343-52. doi: 10.1016/j.jsb.2010.08.008. Epub 2010 Aug 21. J Struct Biol. 2010. PMID: 20732427

3

Structural and denaturation studies of two mutants of a cold adapted superoxide dismutase point to the importance of electrostatic interactions in protein stability.

Merlino A, Russo Krauss I, Castellano I, Ruocco MR, Capasso A, De Vendittis E, Rossi B, Sica F. Merlino A, et al. Among authors: russo krauss i. Biochim Biophys Acta. 2014 Mar;1844(3):632-40. doi: 10.1016/j.bbapap.2014.01.007. Epub 2014 Jan 17. Biochim Biophys Acta. 2014. PMID: 24440460

4

Crystallization and preliminary x-ray diffraction studies of a psychrophilic iron superoxide dismutase from Pseudoalteromonas haloplanktis.

Merlino A, Russo Krauss I, Castellano I, De Vendittis E, Vergara A, Sica F. Merlino A, et al. Among authors: russo krauss i. Protein Pept Lett. 2008;15(4):415-8. doi: 10.2174/092986608784246533. Protein Pept Lett. 2008. PMID: 18473957

5

Improving protein crystal quality by the without-oil microbatch method: crystallization and preliminary X-ray diffraction analysis of glutathione synthetase from Pseudoalteromonas haloplanktis.

Merlino A, Russo Krauss I, Albino A, Pica A, Vergara A, Masullo M, De Vendittis E, Sica F. Merlino A, et al. Among authors: russo krauss i. Int J Mol Sci. 2011;12(9):6312-9. doi: 10.3390/ijms12096312. Epub 2011 Sep 23. Int J Mol Sci. 2011. PMID: 22016660 Free PMC article.

6

Exploring the unfolding mechanism of γ-glutamyltranspeptidases: the case of the thermophilic enzyme from Geobacillus thermodenitrificans.

Pica A, Russo Krauss I, Castellano I, Rossi M, La Cara F, Graziano G, Sica F, Merlino A. Pica A, et al. Among authors: russo krauss i. Biochim Biophys Acta. 2012 Apr;1824(4):571-7. doi: 10.1016/j.bbapap.2012.01.014. Epub 2012 Jan 31. Biochim Biophys Acta. 2012. PMID: 22322192

7

High-resolution structures of two complexes between thrombin and thrombin-binding aptamer shed light on the role of cations in the aptamer inhibitory activity.

Russo Krauss I, Merlino A, Randazzo A, Novellino E, Mazzarella L, Sica F. Russo Krauss I, et al. Nucleic Acids Res. 2012 Sep;40(16):8119-28. doi: 10.1093/nar/gks512. Epub 2012 Jun 4. Nucleic Acids Res. 2012. PMID: 22669903 Free PMC article.

8

Effect of NaCl on the conformational stability of the thermophilic γ-glutamyltranspeptidase from Geobacillus thermodenitrificans: Implication for globular protein halotolerance.

Pica A, Russo Krauss I, Castellano I, La Cara F, Graziano G, Sica F, Merlino A. Pica A, et al. Among authors: russo krauss i. Biochim Biophys Acta. 2013 Jan;1834(1):149-57. doi: 10.1016/j.bbapap.2012.09.014. Epub 2012 Oct 2. Biochim Biophys Acta. 2013. PMID: 23036908

9

Dissecting the contribution of thrombin exosite I in the recognition of thrombin binding aptamer.

Pica A, Russo Krauss I, Merlino A, Nagatoishi S, Sugimoto N, Sica F. Pica A, et al. Among authors: russo krauss i. FEBS J. 2013 Dec;280(24):6581-8. doi: 10.1111/febs.12561. Epub 2013 Nov 1. FEBS J. 2013. PMID: 24128303 Free article.

10

Toward an antitumor form of bovine pancreatic ribonuclease: the crystal structure of three noncovalent dimeric mutants.

Merlino A, Russo Krauss I, Perillo M, Mattia CA, Ercole C, Picone D, Vergara A, Sica F. Merlino A, et al. Among authors: russo krauss i. Biopolymers. 2009 Dec;91(12):1029-37. doi: 10.1002/bip.21183. Biopolymers. 2009. PMID: 19280639

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