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107 related items for PubMed ID: 7559654

  • 1. The yeast immunophilin Fpr3 is a physiological substrate of the tyrosine-specific phosphoprotein phosphatase Ptp1.
    Wilson LK, Benton BM, Zhou S, Thorner J, Martin GS.
    J Biol Chem; 1995 Oct 20; 270(42):25185-93. PubMed ID: 7559654
    [Abstract] [Full Text] [Related]

  • 2. Casein kinase II catalyzes tyrosine phosphorylation of the yeast nucleolar immunophilin Fpr3.
    Wilson LK, Dhillon N, Thorner J, Martin GS.
    J Biol Chem; 1997 May 16; 272(20):12961-7. PubMed ID: 9148902
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  • 3. A novel FK506- and rapamycin-binding protein (FPR3 gene product) in the yeast Saccharomyces cerevisiae is a proline rotamase localized to the nucleolus.
    Benton BM, Zang JH, Thorner J.
    J Cell Biol; 1994 Nov 16; 127(3):623-39. PubMed ID: 7525596
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  • 5. The in vivo tyrosine phosphorylation level of yeast immunophilin Fpr3 is influenced by the LMW-PTP Ltp1.
    Magherini F, Gamberi T, Paoli P, Marchetta M, Biagini M, Raugei G, Camici G, Ramponi G, Modesti A.
    Biochem Biophys Res Commun; 2004 Aug 20; 321(2):424-31. PubMed ID: 15358193
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  • 7. Intramolecular regulation of protein tyrosine phosphatase SH-PTP1: a new function for Src homology 2 domains.
    Pei D, Lorenz U, Klingmüller U, Neel BG, Walsh CT.
    Biochemistry; 1994 Dec 27; 33(51):15483-93. PubMed ID: 7528537
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  • 9. Purification of FKBP-70, a novel immunophilin from Saccharomyces cerevisiae, and cloning of its structural gene, FPR3.
    Manning-Krieg UC, Henríquez R, Cammas F, Graff P, Gavériaux S, Movva NR.
    FEBS Lett; 1994 Sep 19; 352(1):98-103. PubMed ID: 7925954
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  • 10. Expression of the Stp1 LMW-PTP and inhibition of protein CK2 display a cooperative effect on immunophilin Fpr3 tyrosine phosphorylation and Saccharomyces cerevisiae growth.
    Marchetta M, Gamberi T, Sarno S, Magherini F, Raugei G, Camici G, Pinna LA, Modesti A.
    Cell Mol Life Sci; 2004 May 19; 61(10):1176-84. PubMed ID: 15141303
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  • 12. Redundant Regulation of Cdk1 Tyrosine Dephosphorylation in Saccharomyces cerevisiae.
    Kennedy EK, Dysart M, Lianga N, Williams EC, Pilon S, Doré C, Deneault JS, Rudner AD.
    Genetics; 2016 Mar 19; 202(3):903-10. PubMed ID: 26715668
    [Abstract] [Full Text] [Related]

  • 13. G-protein beta gamma subunits mediate specific phosphorylation of the protein-tyrosine phosphatase SH-PTP1 induced by lysophosphatidic acid.
    Gaits F, Li RY, Bigay J, Ragab A, Ragab-Thomas MF, Chap H.
    J Biol Chem; 1996 Aug 16; 271(33):20151-5. PubMed ID: 8798377
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  • 14. Saccharomyces cerevisiae Yak1p protein kinase autophosphorylates on tyrosine residues and phosphorylates myelin basic protein on a C-terminal serine residue.
    Kassis S, Melhuish T, Annan RS, Chen SL, Lee JC, Livi GP, Creasy CL.
    Biochem J; 2000 Jun 01; 348 Pt 2(Pt 2):263-72. PubMed ID: 10816418
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  • 15. Molecular characterization of a FKBP-type immunophilin from higher plants.
    Luan S, Kudla J, Gruissem W, Schreiber SL.
    Proc Natl Acad Sci U S A; 1996 Jul 09; 93(14):6964-9. PubMed ID: 8692927
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  • 16. Tyrosine versus serine/threonine phosphorylation by protein kinase casein kinase-2. A study with peptide substrates derived from immunophilin Fpr3.
    Marin O, Meggio F, Sarno S, Cesaro L, Pagano MA, Pinna LA.
    J Biol Chem; 1999 Oct 08; 274(41):29260-5. PubMed ID: 10506183
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  • 17. Mutations in a protein tyrosine phosphatase gene (PTP2) and a protein serine/threonine phosphatase gene (PTC1) cause a synthetic growth defect in Saccharomyces cerevisiae.
    Maeda T, Tsai AY, Saito H.
    Mol Cell Biol; 1993 Sep 08; 13(9):5408-17. PubMed ID: 8395005
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  • 18. VHR and PTP1 protein phosphatases exhibit remarkably different active site specificities toward low molecular weight nonpeptidic substrates.
    Chen L, Montserat J, Lawrence DS, Zhang ZY.
    Biochemistry; 1996 Jul 23; 35(29):9349-54. PubMed ID: 8755712
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  • 19. Differential functions of the two Src homology 2 domains in protein tyrosine phosphatase SH-PTP1.
    Pei D, Wang J, Walsh CT.
    Proc Natl Acad Sci U S A; 1996 Feb 06; 93(3):1141-5. PubMed ID: 8577729
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  • 20. Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals.
    Klingmüller U, Lorenz U, Cantley LC, Neel BG, Lodish HF.
    Cell; 1995 Mar 10; 80(5):729-38. PubMed ID: 7889566
    [Abstract] [Full Text] [Related]

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