Marin O - Search Results

1

Phosphorylation and activation of the atypical kinase p53-related protein kinase (PRPK) by Akt/PKB.

Facchin S, Ruzzene M, Peggion C, Sartori G, Carignani G, Marin O, Brustolon F, Lopreiato R, Pinna LA. Facchin S, et al. Among authors: marin o. Cell Mol Life Sci. 2007 Oct;64(19-20):2680-9. doi: 10.1007/s00018-007-7179-7. Cell Mol Life Sci. 2007. PMID: 17712528 Free PMC article.

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: marin o. 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

Phosphorylation of the phosphatase modulator subunit (inhibitor-2) by casein kinase-1. Identification of the phosphorylation sites.

Agostinis P, Marin O, James P, Hendrix P, Merlevede W, Vandenheede JR, Pinna LA. Agostinis P, et al. Among authors: marin o. FEBS Lett. 1992 Jun 29;305(2):121-4. doi: 10.1016/0014-5793(92)80877-j. FEBS Lett. 1992. PMID: 1319929 Free article.

4

Selective effect of poly(lysine) on the enhancement of the lyn tyrosine protein kinase activity. Increased specificity toward src peptides.

Donella-Deana A, Marin O, Brunati AM, Pinna LA. Donella-Deana A, et al. Among authors: marin o. Eur J Biochem. 1992 Mar 15;204(3):1159-63. doi: 10.1111/j.1432-1033.1992.tb16742.x. Eur J Biochem. 1992. PMID: 1372554 Free article.

5

The consensus sequences for cdc2 kinase and for casein kinase-2 are mutually incompatible. A study with peptides derived from the beta-subunit of casein kinase-2.

Marin O, Meggio F, Draetta G, Pinna LA. Marin O, et al. FEBS Lett. 1992 Apr 13;301(1):111-4. doi: 10.1016/0014-5793(92)80221-2. FEBS Lett. 1992. PMID: 1451779 Free article.

6

The comparative efficiencies of the Ser(P)-, Thr(P)- and Tyr(P)-residues as specificity determinants for casein kinase-1.

Meggio F, Perich JW, Marin O, Pinna LA. Meggio F, et al. Among authors: marin o. Biochem Biophys Res Commun. 1992 Feb 14;182(3):1460-5. doi: 10.1016/0006-291x(92)91898-z. Biochem Biophys Res Commun. 1992. PMID: 1540189

7

The effect of polylysine on casein-kinase-2 activity is influenced by both the structure of the protein/peptide substrates and the subunit composition of the enzyme.

Meggio F, Boldyreff B, Marin O, Marchiori F, Perich JW, Issinger OG, Pinna LA. Meggio F, et al. Among authors: marin o. Eur J Biochem. 1992 May 1;205(3):939-45. doi: 10.1111/j.1432-1033.1992.tb16860.x. Eur J Biochem. 1992. PMID: 1577011 Free article.

8

Role of phosphorylated aminoacyl residues in generating atypical consensus sequences which are recognized by casein kinase-2 but not by casein kinase-1.

Perich JW, Meggio F, Reynolds EC, Marin O, Pinna LA. Perich JW, et al. Among authors: marin o. Biochemistry. 1992 Jun 30;31(25):5893-7. doi: 10.1021/bi00140a027. Biochemistry. 1992. PMID: 1610832

9

Peptides reproducing the phosphoacceptor sites of pp60c-src as substrates for TPK-IIB, a splenic tyrosine kinase devoid of autophosphorylation activity.

Marin O, Donella-Deana A, Brunati AM, Fischer S, Pinna LA. Marin O, et al. J Biol Chem. 1991 Sep 25;266(27):17798-803. J Biol Chem. 1991. PMID: 1717442 Free article.

10

Role of the beta subunit of casein kinase-2 on the stability and specificity of the recombinant reconstituted holoenzyme.

Meggio F, Boldyreff B, Marin O, Pinna LA, Issinger OG. Meggio F, et al. Among authors: marin o. Eur J Biochem. 1992 Feb 15;204(1):293-7. doi: 10.1111/j.1432-1033.1992.tb16636.x. Eur J Biochem. 1992. PMID: 1740140 Free article.

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