Pinna LA - Search Results

1

Exploring the CK2 Paradox: Restless, Dangerous, Dispensable.

Franchin C, Borgo C, Zaramella S, Cesaro L, Arrigoni G, Salvi M, Pinna LA. Franchin C, et al. Among authors: pinna la. Pharmaceuticals (Basel). 2017 Jan 20;10(1):11. doi: 10.3390/ph10010011. Pharmaceuticals (Basel). 2017. PMID: 28117670 Free PMC article. Review.

2

Spleen protein tyrosine kinases TPK-IIB and CSK display different immunoreactivity and opposite specificities toward c-src-derived peptides.

Brunati AM, Allee G, Marin O, Donella-Deana A, Cesaro L, Bougeret C, Fagard R, Benarous R, Fischer S, Pinna LA. Brunati AM, et al. Among authors: pinna la. FEBS Lett. 1992 Nov 30;313(3):291-4. doi: 10.1016/0014-5793(92)81212-5. FEBS Lett. 1992. PMID: 1280230 Free article.

3

Linear and cyclic synthetic peptides related to the main autophosphorylation site of the Src tyrosine kinases as substrates and inhibitors of Lyn.

Ruzza P, Calderan A, Filippi B, Biondi B, Deana AD, Cesaro L, Pinna LA, Borin G. Ruzza P, et al. Among authors: pinna la. Int J Pept Protein Res. 1995 Jun;45(6):529-39. doi: 10.1111/j.1399-3011.1995.tb01316.x. Int J Pept Protein Res. 1995. PMID: 7558583

4

Phosphorylated residues as specificity determinants for an acidophilic protein tyrosine kinase. A study with src and cdc2 derived phosphopeptides.

Donella-Deana A, Marin O, Brunati AM, Cesaro L, Piutti C, Pinna LA. Donella-Deana A, et al. Among authors: pinna la. FEBS Lett. 1993 Sep 13;330(2):141-5. doi: 10.1016/0014-5793(93)80260-2. FEBS Lett. 1993. PMID: 7689979 Free article.

5

Isolation from spleen of a 57-kDa protein substrate of the tyrosine kinase Lyn. Identification as a protein related to protein disulfide-isomerase and localisation of the phosphorylation sites.

Donella-Deana A, James P, Staudenmann W, Cesaro L, Marin O, Brunati AM, Ruzzene M, Pinna LA. Donella-Deana A, et al. Among authors: pinna la. Eur J Biochem. 1996 Jan 15;235(1-2):18-25. doi: 10.1111/j.1432-1033.1996.00018.x. Eur J Biochem. 1996. PMID: 8631326 Free article.

6

Synthetic Tyr-phospho and non-hydrolyzable phosphonopeptides as PTKs and TC-PTP inhibitors.

Ruzza P, Deana AD, Calderan A, Pavanetto M, Cesaro L, Pinna LA, Borin G. Ruzza P, et al. Among authors: pinna la. Int J Pept Protein Res. 1995 Dec;46(6):535-46. doi: 10.1111/j.1399-3011.1995.tb01609.x. Int J Pept Protein Res. 1995. PMID: 8748714

7

Spontaneous autophosphorylation of Lyn tyrosine kinase at both its activation segment and C-terminal tail confers altered substrate specificity.

Donella-Deana A, Cesaro L, Ruzzene M, Brunati AM, Marin O, Pinna LA. Donella-Deana A, et al. Among authors: pinna la. Biochemistry. 1998 Feb 3;37(5):1438-46. doi: 10.1021/bi971332s. Biochemistry. 1998. PMID: 9477973

8

Linear and cyclic peptides as substrates for Lyn tyrosine kinase.

Ruzza P, Donella-Deana A, Calderan A, Zanotti G, Cesaro L, Pinna LA, Borin G. Ruzza P, et al. Among authors: pinna la. J Pept Sci. 1998 Feb;4(1):33-45. doi: 10.1002/(sici)1099-1387(199802)4:1<33::aid-psc127>3.0.co;2-y. J Pept Sci. 1998. PMID: 9523754

9

A multifunctional network of basic residues confers unique properties to protein kinase CK2.

Sarno S, Vaglio P, Cesaro L, Marin O, Pinna LA. Sarno S, et al. Among authors: pinna la. Mol Cell Biochem. 1999 Jan;191(1-2):13-9. Mol Cell Biochem. 1999. PMID: 10094387

10

CK2: a protein kinase in need of control.

Guerra B, Boldyreff B, Sarno S, Cesaro L, Issinger OG, Pinna LA. Guerra B, et al. Among authors: pinna la. Pharmacol Ther. 1999 May-Jun;82(2-3):303-13. doi: 10.1016/s0163-7258(98)00064-3. Pharmacol Ther. 1999. PMID: 10454208 Review.

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