Perich JW - Search Results

1

Phosphotyrosine specifies the phosphorylation by protein kinase CK2 of a peptide reproducing the activation loop of the insulin receptor protein tyrosine kinase.

Marin O, Meggio F, Perich JW, Pinna LA. Marin O, et al. Among authors: perich jw. Int J Biochem Cell Biol. 1996 Sep;28(9):999-1005. doi: 10.1016/1357-2725(96)00049-0. Int J Biochem Cell Biol. 1996. PMID: 8930123

2

Phosphotyrosine as a specificity determinant for casein kinase-2, a growth related Ser/Thr-specific protein kinase.

Meggio F, Perich JW, Reynolds EC, Pinna LA. Meggio F, et al. Among authors: perich jw. FEBS Lett. 1991 Feb 25;279(2):307-9. doi: 10.1016/0014-5793(91)80174-2. FEBS Lett. 1991. PMID: 1705898 Free article.

3

A synthetic beta-casein phosphopeptide and analogues as model substrates for casein kinase-1, a ubiquitous, phosphate directed protein kinase.

Meggio F, Perich JW, Reynolds EC, Pinna LA. Meggio F, et al. Among authors: perich jw. FEBS Lett. 1991 Jun 3;283(2):303-6. doi: 10.1016/0014-5793(91)80614-9. FEBS Lett. 1991. PMID: 2044770 Free article.

4

Synthetic fragments of beta-casein as model substrates for liver and mammary gland casein kinases.

Meggio F, Perich JW, Meyer HE, Hoffmann-Posorske E, Lennon DP, Johns RB, Pinna LA. Meggio F, et al. Among authors: perich jw. Eur J Biochem. 1989 Dec 22;186(3):459-64. doi: 10.1111/j.1432-1033.1989.tb15229.x. Eur J Biochem. 1989. PMID: 2606100 Free article.

5

Partially dephosphorylated phosphopeptide AcSer(P)-Ser(P)-Ser(P) is an excellent substrate for casein kinase-2.

Meggio F, Perich JW, Johns RB, Pinna LA. Meggio F, et al. Among authors: perich jw. FEBS Lett. 1988 Sep 12;237(1-2):225-8. doi: 10.1016/0014-5793(88)80206-0. FEBS Lett. 1988. PMID: 3169237 Free article.

6

Specificity of T-cell protein tyrosine phosphatase toward phosphorylated synthetic peptides.

Ruzzene M, Donella-Deana A, Marin O, Perich JW, Ruzza P, Borin G, Calderan A, Pinna LA. Ruzzene M, et al. Among authors: perich jw. Eur J Biochem. 1993 Jan 15;211(1-2):289-95. doi: 10.1111/j.1432-1033.1993.tb19897.x. Eur J Biochem. 1993. PMID: 7678807 Free article.

7

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: perich jw. 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

8

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: perich jw. 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.

9

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. Biochemistry. 1992 Jun 30;31(25):5893-7. doi: 10.1021/bi00140a027. Biochemistry. 1992. PMID: 1610832

10

Phosphorylation of src-phosphopeptides by casein kinases-1 and -2: favourable effect of phosphotyrosine.

Perich JW, Meggio F, Kitas EA, Valerio RM, Johns RB, Pinna LA. Perich JW, et al. Biochem Biophys Res Commun. 1990 Jul 31;170(2):635-42. doi: 10.1016/0006-291x(90)92139-q. Biochem Biophys Res Commun. 1990. PMID: 1696474

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