Battistutta R - Search Results

1

Crystal structure and refolding properties of the mutant F99S/M153T/V163A of the green fluorescent protein.

Battistutta R, Negro A, Zanotti G. Battistutta R, et al. Proteins. 2000 Dec 1;41(4):429-37. doi: 10.1002/1097-0134(20001201)41:4<429::aid-prot10>3.0.co;2-d. Proteins. 2000. PMID: 11056031

2

One substrate many enzymes virtual screening uncovers missing genes of carnitine biosynthesis in human and mouse.

Malatesta M, Fornasier E, Di Salvo ML, Tramonti A, Zangelmi E, Peracchi A, Secchi A, Polverini E, Giachin G, Battistutta R, Contestabile R, Percudani R. Malatesta M, et al. Among authors: battistutta r. Nat Commun. 2024 Apr 13;15(1):3199. doi: 10.1038/s41467-024-47466-3. Nat Commun. 2024. PMID: 38615009 Free PMC article.

3

Crystal structure of the B subunit of Escherichia coli heat-labile enterotoxin carrying peptides with anti-herpes simplex virus type 1 activity.

Matković-Calogović D, Loregian A, D'Acunto MR, Battistutta R, Tossi A, Palù G, Zanotti G. Matković-Calogović D, et al. Among authors: battistutta r. J Biol Chem. 1999 Mar 26;274(13):8764-9. J Biol Chem. 1999. PMID: 10085117 Free article.

4

Susceptibility of the prion protein to enzymic phosphorylation.

Negro A, Meggio F, Bertoli A, Battistutta R, Sorgato MC, Pinna LA. Negro A, et al. Among authors: battistutta r. Biochem Biophys Res Commun. 2000 May 10;271(2):337-41. doi: 10.1006/bbrc.2000.2628. Biochem Biophys Res Commun. 2000. PMID: 10799298

5

Structure at 1.44 A resolution of an N-terminally truncated form of the rat serum complement C3d fragment.

Zanotti G, Bassetto A, Battistutta R, Folli C, Arcidiaco P, Stoppini M, Berni R. Zanotti G, et al. Among authors: battistutta r. Biochim Biophys Acta. 2000 May 23;1478(2):232-8. doi: 10.1016/s0167-4838(00)00040-6. Biochim Biophys Acta. 2000. PMID: 10825534

6

The replacement of ATP by the competitive inhibitor emodin induces conformational modifications in the catalytic site of protein kinase CK2.

Battistutta R, Sarno S, De Moliner E, Papinutto E, Zanotti G, Pinna LA. Battistutta R, et al. J Biol Chem. 2000 Sep 22;275(38):29618-22. doi: 10.1074/jbc.M004257200. J Biol Chem. 2000. PMID: 10882732 Free article.

7

The crystal structure of the complex of Zea mays alpha subunit with a fragment of human beta subunit provides the clue to the architecture of protein kinase CK2 holoenzyme.

Battistutta R, Sarno S, De Moliner E, Marin O, Issinger OG, Zanotti G, Pinna LA. Battistutta R, et al. Eur J Biochem. 2000 Aug;267(16):5184-90. doi: 10.1046/j.1432-1327.2000.01587.x. Eur J Biochem. 2000. PMID: 10931203 Free article.

8

Structural features underlying selective inhibition of protein kinase CK2 by ATP site-directed tetrabromo-2-benzotriazole.

Battistutta R, De Moliner E, Sarno S, Zanotti G, Pinna LA. Battistutta R, et al. Protein Sci. 2001 Nov;10(11):2200-6. doi: 10.1110/ps.19601. Protein Sci. 2001. PMID: 11604527 Free PMC article.

9

Structure of two iron-binding proteins from Bacillus anthracis.

Papinutto E, Dundon WG, Pitulis N, Battistutta R, Montecucco C, Zanotti G. Papinutto E, et al. Among authors: battistutta r. J Biol Chem. 2002 Apr 26;277(17):15093-8. doi: 10.1074/jbc.M112378200. Epub 2002 Feb 8. J Biol Chem. 2002. PMID: 11836250 Free article.

10

Toward the rational design of protein kinase casein kinase-2 inhibitors.

Sarno S, Moro S, Meggio F, Zagotto G, Dal Ben D, Ghisellini P, Battistutta R, Zanotti G, Pinna LA. Sarno S, et al. Among authors: battistutta r. Pharmacol Ther. 2002 Feb-Mar;93(2-3):159-68. doi: 10.1016/s0163-7258(02)00185-7. Pharmacol Ther. 2002. PMID: 12191608 Review.

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