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1
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0028838971
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Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling
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of outstanding interest. This is an excellent, comprehensive review of the role of kinases and phosphatases in cellular signaling.
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Hunter T. Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. of outstanding interest Cell. 80:1995;225-236 This is an excellent, comprehensive review of the role of kinases and phosphatases in cellular signaling.
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(1995)
Cell
, vol.80
, pp. 225-236
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Hunter, T.1
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2
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0029349221
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Control and activity of type-1 serine/threonine protein phosphatase during the cell cycle
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Ludlow JW, Nelson DA. Control and activity of type-1 serine/threonine protein phosphatase during the cell cycle. Semin Cancer Biol. 6:1995;195-202.
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Semin Cancer Biol
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, pp. 195-202
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Ludlow, J.W.1
Nelson, D.A.2
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3
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0027143725
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Protein serine/threonine phosphatases: Structure, regulation, and functions in cell growth
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Mumby MC, Walter G. Protein serine/threonine phosphatases: structure, regulation, and functions in cell growth. Physiol Rev. 4:1993;673-699.
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Physiol Rev
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Mumby, M.C.1
Walter, G.2
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4
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0029598482
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The role of calcineurin in immune system responses
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Kincaid RL. The role of calcineurin in immune system responses. J Allergy Clin Immunol. 96:1995;1170-1177.
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J Allergy Clin Immunol
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Kincaid, R.L.1
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5
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0025893168
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Calcineurin is a common target of cyclophilin - Cyclosporin A and FKBP - FK506 complexes
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Liu J, Farmer J Jr, Lane WS, Friedman J, Weissman I, Schreiber SL. Calcineurin is a common target of cyclophilin - cyclosporin A and FKBP - FK506 complexes. Cell. 66:1991;807-815.
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Cell
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Liu, J.1
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Friedman, J.4
Weissman, I.5
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7
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0028929331
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Synaptic desensitization of NMDA receptors by calcineurin
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Tong G, Shepherd D, Jahr CE. Synaptic desensitization of NMDA receptors by calcineurin. Science. 267:1995;1510-1512.
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Science
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Tong, G.1
Shepherd, D.2
Jahr, C.E.3
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8
-
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0029094754
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Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1
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of outstanding interest. The X-ray structure, at 2.1 Å resolution, of rabbit muscle PP1 with the toxin microcystin bound at the active site is described. The structure reveals the dimetal active site and the positions of conserved residues and suggests the basis for catalysis in this family of enzymes.
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Goldberg J, Huang H-b, Kwon Y-g, Greengard P, Nairn AC, Kuriyan J. Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. of outstanding interest Nature. 376:1995;745-753 The X-ray structure, at 2.1 Å resolution, of rabbit muscle PP1 with the toxin microcystin bound at the active site is described. The structure reveals the dimetal active site and the positions of conserved residues and suggests the basis for catalysis in this family of enzymes.
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(1995)
Nature
, vol.376
, pp. 745-753
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Goldberg, J.1
Huang H-b2
Kwon Y-g3
Greengard, P.4
Nairn, A.C.5
Kuriyan, J.6
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9
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0029583122
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Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate
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of outstanding interest. The structure of human PP1 at 2.5 Å resolution is described. The identities and positions of the bound metal ions were determined. Tungstate was bound at the active site, indicating the probable structure of the enzyme - product complex.
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Egloff M-P, Cohen PTW, Reinemer P, Barford D. Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate. of outstanding interest J Mol Biol. 254:1995;942-959 The structure of human PP1 at 2.5 Å resolution is described. The identities and positions of the bound metal ions were determined. Tungstate was bound at the active site, indicating the probable structure of the enzyme - product complex.
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(1995)
J Mol Biol
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Egloff M-P1
Cohen, P.T.W.2
Reinemer, P.3
Barford, D.4
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10
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0029133116
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X-ray structure of calcineurin inhibited by the immunophilin - Immunosuppressant FKBP - FK506 complex
-
of outstanding interest. The structure of a fragment of bovine PP2b with a drug - immunophilin complex bound at 2.5 Å resolution is described. The location of the binding of FKBP - FK506 and a description of the binding interactions is given. A mechanism of inhibition by FKBP-FK506 involving steric hindrance is proposed. Phosphate is bound at the active site. The roles of active site residues and the possible catalytic mechanism are presented.
-
Griffith JP, Kim JL, Kim EE, Sintchak MD, Thomson JA, Fitzgibbon MJ, Fleming MA, Caron PR, Hsiao K, Navia MA. X-ray structure of calcineurin inhibited by the immunophilin - immunosuppressant FKBP - FK506 complex. of outstanding interest Cell. 82:1995;507-522 The structure of a fragment of bovine PP2b with a drug - immunophilin complex bound at 2.5 Å resolution is described. The location of the binding of FKBP - FK506 and a description of the binding interactions is given. A mechanism of inhibition by FKBP-FK506 involving steric hindrance is proposed. Phosphate is bound at the active site. The roles of active site residues and the possible catalytic mechanism are presented.
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(1995)
Cell
, vol.82
, pp. 507-522
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Griffith, J.P.1
Kim, J.L.2
Kim, E.E.3
Sintchak, M.D.4
Thomson, J.A.5
Fitzgibbon, M.J.6
Fleming, M.A.7
Caron, P.R.8
Hsiao, K.9
Navia, M.A.10
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11
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0028848524
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Crystal structures of human calcineurin and the human FKBP12 - FK506-calcineurin complex
-
of outstanding interest. The structure, at 2.1 Å resolution, of full-length human calcineurin is reported. The autoinhibitory sequence is bound at the active site but does not appear to mimic the interactions of a substrate. A large part of the carboxy-terminal portion of the protein, including the calmodulin-binding domain, is disordered. The complex of full-length calcineurin with FKBP - FK506 shows that the autoinhibitory segment is displaced from the active site. The structural basis for noncompetitive inhibition by FKBP - FK506 is discussed.
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Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, et al. Crystal structures of human calcineurin and the human FKBP12 - FK506-calcineurin complex. of outstanding interest Nature. 378:1995;641-644 The structure, at 2.1 Å resolution, of full-length human calcineurin is reported. The autoinhibitory sequence is bound at the active site but does not appear to mimic the interactions of a substrate. A large part of the carboxy-terminal portion of the protein, including the calmodulin-binding domain, is disordered. The complex of full-length calcineurin with FKBP - FK506 shows that the autoinhibitory segment is displaced from the active site. The structural basis for noncompetitive inhibition by FKBP - FK506 is discussed.
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(1995)
Nature
, vol.378
, pp. 641-644
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Kissinger, C.R.1
Parge, H.E.2
Knighton, D.R.3
Lewis, C.T.4
Pelletier, L.A.5
Tempczyk, A.6
Kalish, V.J.7
Tucker, K.D.8
Showalter, R.E.9
Moomaw, E.W.10
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12
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0020565637
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Protein phosphatases: Properties and role in cellular regulation
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Ingebritsen TS, Cohen P. Protein phosphatases: properties and role in cellular regulation. Science. 221:1983;331-338.
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Science
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Ingebritsen, T.S.1
Cohen, P.2
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13
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0029870187
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Multiple structural elements define the specificity of recombinant human inhibitor-1 as a protein phosphatase-1 inhibitor
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Endo S, Zhou X, Connor J, Wang B, Shenolikar S. Multiple structural elements define the specificity of recombinant human inhibitor-1 as a protein phosphatase-1 inhibitor. Biochemistry. 35:1996;5220-5228.
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Biochemistry
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Endo, S.1
Zhou, X.2
Connor, J.3
Wang, B.4
Shenolikar, S.5
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14
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0029349353
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Flicking the switches: Phosphorylation of serine/threonine protein phosphatases
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of special interest. This is a recent review of the functional and regulatory effects of phosphorylation of Ser/Thr phosphatases.
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Brautigan DL. Flicking the switches: phosphorylation of serine/threonine protein phosphatases. of special interest Semin Cancer Biol. 6:1995;211-217 This is a recent review of the functional and regulatory effects of phosphorylation of Ser/Thr phosphatases.
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Semin Cancer Biol
, vol.6
, pp. 211-217
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Brautigan, D.L.1
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15
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0028832251
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Identification of a new family of protein phosphatase 2A regulatory subunits
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McCright B, Virshup DM. Identification of a new family of protein phosphatase 2A regulatory subunits. J Biol Chem. 270:1995;26123-26128.
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(1995)
J Biol Chem
, vol.270
, pp. 26123-26128
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McCright, B.1
Virshup, D.M.2
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16
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0028931302
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Purification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney
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Li M, Guo H, Damuni Z. Purification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney. Biochemistry. 34:1995;1988-1996.
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Biochemistry
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Li, M.1
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17
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0021916862
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The protein phosphatases involved in cellular regulation
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Pelech S, Cohen P. The protein phosphatases involved in cellular regulation. Eur J Biochem. 148:1985;245-251.
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Eur J Biochem
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Pelech, S.1
Cohen, P.2
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18
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0001018554
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Calcineurin: A calcium- and calmodulin-binding protein of the nervous sytem
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Klee CB, Crouch TH, Krinks MH. Calcineurin: a calcium- and calmodulin-binding protein of the nervous sytem. Proc Natl Acad Sci USA. 76:1979;6270-6273.
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Klee, C.B.1
Crouch, T.H.2
Krinks, M.H.3
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19
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0343096255
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Characterization of a cDNA clone encoding the calmodulin-binding domain of mouse brain calcineurin
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Kincaid RL, Nightingale MS, Martin BM. Characterization of a cDNA clone encoding the calmodulin-binding domain of mouse brain calcineurin. Proc Natl Acad Sci USA. 85:1988;8983-8987.
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Proc Natl Acad Sci USA
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Kincaid, R.L.1
Nightingale, M.S.2
Martin, B.M.3
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20
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0030048096
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Identification of a physical interaction between calcineurin and nuclear factor of activated T cells (NFATp)
-
of special interest. This report provides evidence that a putative physiological substrate for PP2b, NFATp (nuclear factor of activated T cells), forms a stable complex with the enzyme in both the phosphorylated and dephosphorylated forms.
-
Wesselborg S, Fruman DA, Sagoo JK, Bierer BE, Burakoff SJ. Identification of a physical interaction between calcineurin and nuclear factor of activated T cells (NFATp). of special interest J Biol Chem. 271:1996;1274-1277 This report provides evidence that a putative physiological substrate for PP2b, NFATp (nuclear factor of activated T cells), forms a stable complex with the enzyme in both the phosphorylated and dephosphorylated forms.
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(1996)
J Biol Chem
, vol.271
, pp. 1274-1277
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Wesselborg, S.1
Fruman, D.A.2
Sagoo, J.K.3
Bierer, B.E.4
Burakoff, S.J.5
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21
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15844416253
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Calcineurin binds the transcription factor NFAT1 and reversibly regulates its activity
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of special interest. These researchers show that the phosphorylation state of NFATp in vivo is strongly dependent on the level of PP2b activity and can be isolated as a complex with the phosphatase in T-cell lysates.
-
Loh C, Shaw KT-Y, Carew J, Viola JPB, Luo C, Perrino B, Rao A. Calcineurin binds the transcription factor NFAT1 and reversibly regulates its activity. of special interest J Biol Chem. 271:1996;10884-10891 These researchers show that the phosphorylation state of NFATp in vivo is strongly dependent on the level of PP2b activity and can be isolated as a complex with the phosphatase in T-cell lysates.
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(1996)
J Biol Chem
, vol.271
, pp. 10884-10891
-
-
Loh, C.1
Shaw KT-Y2
Carew, J.3
Viola, J.P.B.4
Luo, C.5
Perrino, B.6
Rao, A.7
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22
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0029640070
-
Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site
-
of outstanding interest. The structure of the Zn/Fe-containing purple acid phosphatase from kidney bean at 2.9 Å resolution. The metal-binding residues and the structural motif that position them are similar to those subsequently found in the Ser/Thr phosphatases.
-
Sträter N, Klabunde T, Tucker P, Witzel H, Krebs B. Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site. of outstanding interest Science. 268:1995;1489-1492 The structure of the Zn/Fe-containing purple acid phosphatase from kidney bean at 2.9 Å resolution. The metal-binding residues and the structural motif that position them are similar to those subsequently found in the Ser/Thr phosphatases.
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(1995)
Science
, vol.268
, pp. 1489-1492
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Sträter, N.1
Klabunde, T.2
Tucker, P.3
Witzel, H.4
Krebs, B.5
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23
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0028053053
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Conservation analysis and structure prediction of the protein serine/threonine phosphatases
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Barton GJ, Cohen PTW, Barford D. Conservation analysis and structure prediction of the protein serine/threonine phosphatases. Eur J Biochem. 220:1994;225-237.
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Eur J Biochem
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Barton, G.J.1
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Barford, D.3
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24
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Conserved sequence pattern in a wide variety of phosphoesterases
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Koonin EV. Conserved sequence pattern in a wide variety of phosphoesterases. Protein Sci. 3:1994;356-358.
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Protein Sci
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Koonin, E.V.1
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25
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Mutational analysis of a Ser/Thr phosphatase. Identification of residues important in phosphoesterase substrate binding and catalysis
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Zhuo S, Clemens JC, Stone RL, Dixon JE. Mutational analysis of a Ser/Thr phosphatase. Identification of residues important in phosphoesterase substrate binding and catalysis. J Biol Chem. 269:1994;26234-26238.
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J Biol Chem
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Zhuo, S.1
Clemens, J.C.2
Stone, R.L.3
Dixon, J.E.4
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26
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0021134292
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The calmodulin-dependent activation and deactivation of the phosphoprotein phosphatase, calcineurin, and the effect of nucleotides, pyrophosphate, and divalent metal ions. Identification of calcineurin as a Zn and Fe metalloenzyme
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King MM, Huang CY. The calmodulin-dependent activation and deactivation of the phosphoprotein phosphatase, calcineurin, and the effect of nucleotides, pyrophosphate, and divalent metal ions. Identification of calcineurin as a Zn and Fe metalloenzyme. J Biol Chem. 259:1984;8847-8856.
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King, M.M.1
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0028886436
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Evidence that calcineurin accommodates an active site binuclear metal center
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Yu L, Haddy A, Rusnak F. Evidence that calcineurin accommodates an active site binuclear metal center. J Am Chem Soc. 117:1995;10147-10148.
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Yu, L.1
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Mechanistic aspects of the low-molecular-weight phosphatase activity of the calmodulin-activated phosphatase, calcineurin
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Martin B, Graves DJ. Mechanistic aspects of the low-molecular-weight phosphatase activity of the calmodulin-activated phosphatase, calcineurin. J Biol Chem. 261:1986;14545-14550.
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Isotope effects on the mechanism of calcineurin catalysis: Kinetic solvent isotope and isotope exchange studies
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Martin BL, Graves DJ. Isotope effects on the mechanism of calcineurin catalysis: kinetic solvent isotope and isotope exchange studies. Biochim Biophys Acta. 1206:1994;136-142.
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Martin, B.L.1
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Mueller EG, Crowder MW, Averill BA, Knowles JR. Purple acid phosphatase: A diiron enzyme that catalyzes a direct phospho group transfer to water. J Am Chem Soc. 115:1993;2974-2975.
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Mueller, E.G.1
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Averill, B.A.3
Knowles, J.R.4
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0026019625
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Structural basis for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I: A two metal ion mechanism
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Beese LS, Steitz TA. Structural basis for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism. EMBO J. 10:1991;25-33.
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Derbyshire V, Grindley NDF, Joyce CM. The 3'-5' exonuclease of DNA polymerase 1 of Escherichia coli: contribution of each amino acid at the active site to the reaction. EMBO J. 10:1991;17-24.
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A medicinal chemistry evaluation of the autoinhibitory domain of calcineurin
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Rivetna MN, Salowe SP, Tolman RL, Jones AB. A medicinal chemistry evaluation of the autoinhibitory domain of calcineurin. Biorg Med Chem Lett. 5:1995;1147-1150.
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Rivetna, M.N.1
Salowe, S.P.2
Tolman, R.L.3
Jones, A.B.4
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34
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0028950664
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Inhibition of specific binding of okadaic acid to protein phosphatase 2A by microcystin-LR, calyculin-A, and tautomycin: Method of analysis of interactions of tight-binding ligands with target protein
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Takai A, Sasaki K, Nagai H, Mieskes G, Isobe M, Isono K, Yasumoto T. Inhibition of specific binding of okadaic acid to protein phosphatase 2A by microcystin-LR, calyculin-A, and tautomycin: method of analysis of interactions of tight-binding ligands with target protein. Biochem J. 306:1995;657-665.
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Takai, A.1
Sasaki, K.2
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Mieskes, G.4
Isobe, M.5
Isono, K.6
Yasumoto, T.7
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35
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0028298882
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A mutant of protein phosphatase-1 that exhibits altered toxin sensitivity
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Zhang Z, Zhao S, Long F, Zhang L, Bai G, Shima H, Nagao M, Lee EYC. A mutant of protein phosphatase-1 that exhibits altered toxin sensitivity. J Biol Chem. 269:1994;16997-17000.
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Zhang, Z.1
Zhao, S.2
Long, F.3
Zhang, L.4
Bai, G.5
Shima, H.6
Nagao, M.7
Lee, E.Y.C.8
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36
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0030065764
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Tyrosine-272 is involved in the inhibition of protein phosphatase-1 by multiple toxins
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of special interest. Evidence for active site binding by exogenous inhibitors of PP1.
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Zhang L, Zhang Z, Long F, Lee EYC. Tyrosine-272 is involved in the inhibition of protein phosphatase-1 by multiple toxins. of special interest Biochemistry. 35:1996;1606-1611 Evidence for active site binding by exogenous inhibitors of PP1.
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Biochemistry
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Zhang, L.1
Zhang, Z.2
Long, F.3
Lee, E.Y.C.4
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The latch region of calcineurin B is involved in both immunosuppressant-immunophilin complex docking and phsophatase activation
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Milan D, Griffith J, Su M, Price ER, McKeon F. The latch region of calcineurin B is involved in both immunosuppressant-immunophilin complex docking and phsophatase activation. Cell. 79:1994;437-447.
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Milan, D.1
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Kawamura A, Su MS-S. Interaction of FKBP12 - FK506 with calcineurin A at the B subunit-binding domain. J Biol Chem. 270:1995;15463-15466.
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Kawamura, A.1
Su MS-S2
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Targets of immunophilin - Immunosuppressant complexes are distinct highly conserved regions of calcineurin A
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Cardenas ME, Muir RS, Breuder T, Heitman J. Targets of immunophilin - immunosuppressant complexes are distinct highly conserved regions of calcineurin A. EMBO J. 14:1995;2772-2783.
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Cardenas, M.E.1
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40
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0028175752
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Cyclophilin residues that affect noncompetitive inhibition of the protein serine phosphatase activity of calcineurin by the cyclophilin - Cyclosporin A complex
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Etzkorn FA, Chang Z, Stolz LA, Walsh CT. Cyclophilin residues that affect noncompetitive inhibition of the protein serine phosphatase activity of calcineurin by the cyclophilin - cyclosporin A complex. Biochemistry. 33:1994;2380-2388.
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Etzkorn, F.A.1
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0027202187
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Expression, purification, crystallization, and biochemical characterization of a recombinant protein phosphatase
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Zhuo S, Clemens JC, Hakes DJ, Barford D, Dixon JE. Expression, purification, crystallization, and biochemical characterization of a recombinant protein phosphatase. J Biol Chem. 268:1993;17754-17761.
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