메뉴 건너뛰기




Volumn 120, Issue 1, 2015, Pages 20-27

Phosphohistidine phosphatase 1 (PHPT1) also dephosphorylates phospholysine of chemically phosphorylated histone H1 and polylysine

Author keywords

Histone H1; Phosphohistidine phosphatase; Phospholysine; Phospholysine phosphatase; PHP; PHPT1; Protein histidine phosphatase

Indexed keywords

ARGININE; FUCHSINE; HISTIDINE; HISTONE; LYSINE; MALACHITE GREEN; ORGANOPHOSPHORUS COMPOUND; PHOSPHATASE; PHOSPHO-L-ARGININE; PHOSPHOHISTIDINE; PHPT1 PROTEIN, HUMAN; POLYLYSINE; RECOMBINANT PROTEIN;

EID: 84924363716     PISSN: 03009734     EISSN: 20001967     Source Type: Journal    
DOI: 10.3109/03009734.2014.996720     Document Type: Article
Times cited : (17)

References (56)
  • 1
    • 0000183819 scopus 로고
    • Identification of phosphohistidine in digests from a probable intermediate of oxidative phosphorylation
    • Boyer PD, DeLuca M, Ebner KE, Hultquist DE, Peter JB. Identification of phosphohistidine in digests from a probable intermediate of oxidative phosphorylation. J Biol Chem. 1962; 237:PC3306-8.
    • (1962) J Biol Chem. , vol.237 , pp. PC3306-PC3308
    • Boyer, P.D.1    Deluca, M.2    Ebner, K.E.3    Hultquist, D.E.4    Peter, J.B.5
  • 2
    • 84856158810 scopus 로고    scopus 로고
    • Chasing phosphohistidine, an elusive sibling in the phosphoamino acid family
    • Kee JM, Muir TW. Chasing phosphohistidine, an elusive sibling in the phosphoamino acid family. ACS Chem Biol. 2012;7:44-51.
    • (2012) ACS Chem Biol. , vol.7 , pp. 44-51
    • Kee, J.M.1    Muir, T.W.2
  • 3
    • 84893609793 scopus 로고    scopus 로고
    • The involvement of transport proteins in transcriptional and metabolic regulations
    • Västermark Å, Saier MH Jr. The involvement of transport proteins in transcriptional and metabolic regulations. Curr Opin Microbiol. 2014;18:8-15.
    • (2014) Curr Opin Microbiol. , vol.18 , pp. 8-15
    • Västermark, A.1    Saier, M.H.2
  • 4
    • 84877015880 scopus 로고    scopus 로고
    • Determinants of specificity in twocomponent signal transduction
    • Podgornaia AI, Laub MT. Determinants of specificity in twocomponent signal transduction. Curr Opin Microbiol. 2013; 16:156-62.
    • (2013) Curr Opin Microbiol. , vol.16 , pp. 156-162
    • Podgornaia, A.I.1    Laub, M.T.2
  • 5
    • 0028829688 scopus 로고
    • Protein kinases and phosphatases that act on histidine, lysine, or arginine residues in eukaryotic proteins: A possible regulator of the mitogen-activated protein kinase cascade
    • Matthews HR. Protein kinases and phosphatases that act on histidine, lysine, or arginine residues in eukaryotic proteins: a possible regulator of the mitogen-activated protein kinase cascade. Pharmac Ther. 1995;67:323-50.
    • (1995) Pharmac Ther. , vol.67 , pp. 323-350
    • Matthews, H.R.1
  • 6
    • 66149112136 scopus 로고    scopus 로고
    • Reversible phosphorylation of histidine residues in proteins from vertebrates
    • Klumpp S, Krieglstein J. Reversible phosphorylation of histidine residues in proteins from vertebrates. Sci Signal. 2009;2:pe13.
    • (2009) Sci Signal. , vol.2 , pp. pe13
    • Klumpp, S.1    Krieglstein, J.2
  • 7
    • 84880521180 scopus 로고    scopus 로고
    • Histidine kinases from bacteria to humans
    • Attwood PV. Histidine kinases from bacteria to humans. Biochem Soc Trans. 2013;41:1023-8.
    • (2013) Biochem Soc Trans. , vol.41 , pp. 1023-1028
    • Attwood, P.V.1
  • 8
    • 0014547457 scopus 로고
    • Preparation of crystalline nucleoside diphosphate kinase from baker's yeast and identification of 1 [32P]phosphohistidine as the main phosphorylated product of an alkaline hydrolysate of enzyme incubated with adenosine [32P]triphosphate
    • Edlund B, Rask L, Olsson P, Wålinder O, Zetterqvist Ö, Engström L. Preparation of crystalline nucleoside diphosphate kinase from baker's yeast and identification of 1 [32P]phosphohistidine as the main phosphorylated product of an alkaline hydrolysate of enzyme incubated with adenosine [32P]triphosphate. Eur J Biochem. 1969;9:451-5.
    • (1969) Eur J Biochem. , vol.9 , pp. 451-455
    • Edlund, B.1    Rask, L.2    Olsson, P.3    Wålinder, O.4    Zetterqvist, O.5    Engström, L.6
  • 9
    • 0029154302 scopus 로고
    • Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium
    • Moréra S, Chiadmi M, LeBras G, Lascu I, Janin J. Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium. Biochemistry. 1995;34: 11062-70.
    • (1995) Biochemistry , vol.34 , pp. 11062-11070
    • Moréra, S.1    Chiadmi, M.2    Lebras, G.3    Lascu, I.4    Janin, J.5
  • 10
    • 0015243897 scopus 로고
    • Studies on a rat-liver cell-sap protein yielding 3 [32P]phosphohistidine after incubation with [32P]ATP and alkaline hydrolysis. Identification of the protein as ATP citrate lyase
    • Mårdh S, Ljungström O, Högstedt S, Zetterqvist Ö. Studies on a rat-liver cell-sap protein yielding 3 [32P]phosphohistidine after incubation with [32P]ATP and alkaline hydrolysis. Identification of the protein as ATP citrate lyase. Biochim Biophys Acta. 1971;251:419-26.
    • (1971) Biochim Biophys Acta , vol.251 , pp. 419-426
    • Mårdh, S.1    Ljungström, O.2    Högstedt, S.3    Zetterqvist, O.4
  • 11
    • 0022399331 scopus 로고
    • Phosphorus-31 nuclear magnetic resonance study of the active site phosphohistidine and regulatory phosphoserine residues of rat liver ATP citrate lyase
    • Williams SP, Sykes BD, Bridger WA. Phosphorus-31 nuclear magnetic resonance study of the active site phosphohistidine and regulatory phosphoserine residues of rat liver ATP citrate lyase. Biochemistry. 1985;24:5527-31.
    • (1985) Biochemistry , vol.24 , pp. 5527-5531
    • Williams, S.P.1    Sykes, B.D.2    Bridger, W.A.3
  • 13
    • 0013773646 scopus 로고
    • The association of readily-soluble bound phosphohistidine from mitochondria with succinate thiokinase
    • Mitchell RA, Butler LG, Boyer PD. The association of readily-soluble bound phosphohistidine from mitochondria with succinate thiokinase. Biochem Biophys Res Commun. 1964;16:545-50.
    • (1964) Biochem Biophys Res Commun. , vol.16 , pp. 545-550
    • Mitchell, R.A.1    Butler, L.G.2    Boyer, P.D.3
  • 14
    • 0013872353 scopus 로고
    • The preparation and characterization of 1 phosphohistidine and 3 phosphohistidine
    • Hultquist DE, Moyer RW, Boyer PD. The preparation and characterization of 1 phosphohistidine and 3 phosphohistidine. Biochemistry. 1966;5:322-31.
    • (1966) Biochemistry , vol.5 , pp. 322-331
    • Hultquist, D.E.1    Moyer, R.W.2    Boyer, P.D.3
  • 15
    • 0034705332 scopus 로고    scopus 로고
    • Phosphorylated and dephosphorylated structures of pig heart, GTP specific succinyl CoA synthetase
    • Fraser ME, James MNG, Bridger WA, Wolodko WT. Phosphorylated and dephosphorylated structures of pig heart, GTP specific succinyl CoA synthetase. J Mol Biol. 2000;299:1325-39.
    • (2000) J Mol Biol. , vol.299 , pp. 1325-1339
    • Fraser, M.E.1    James, M.N.G.2    Bridger, W.A.3    Wolodko, W.T.4
  • 17
    • 79960127921 scopus 로고    scopus 로고
    • Phosphorylation of basic amino acid residues in proteins: Important but easily missed
    • Cies̈la J, Fra{ogonek}czyk T, Rode W. Phosphorylation of basic amino acid residues in proteins: important but easily missed. Acta Biochim Pol. 2011;58:137-47.
    • (2011) Acta Biochim Pol. , vol.58 , pp. 137-147
    • Cies̈la, J.1    Frączyk, T.2    Rode, W.3
  • 18
    • 84880561371 scopus 로고    scopus 로고
    • Attempting to rewrite history: Challenges with the analysis of histidine phosphorylated peptides
    • Gonzalez Sanchez MB, Lanucara F, Helm M, Eyers CE. Attempting to rewrite history: challenges with the analysis of histidine phosphorylated peptides. Biochem Soc Trans. 2013;41:1089-95.
    • (2013) Biochem Soc Trans. , vol.41 , pp. 1089-1095
    • Gonzalez Sanchez, M.B.1    Lanucara, F.2    Helm, M.3    Eyers, C.E.4
  • 19
    • 84921272425 scopus 로고    scopus 로고
    • A phosphohistidine proteomics strategy based on elucidation of a unique gas-phase phosphopeptide fragmentation mechanism
    • Oslund RC, Kee JM, Couvillon AD, Bhatia VN, Perlman DH, Muir TW. A phosphohistidine proteomics strategy based on elucidation of a unique gas-phase phosphopeptide fragmentation mechanism. J Am Chem Soc. 2014; 136:12899-911.
    • (2014) J Am Chem Soc. , vol.136 , pp. 12899-12911
    • Oslund, R.C.1    Kee, J.M.2    Couvillon, A.D.3    Bhatia, V.N.4    Perlman, D.H.5    Muir, T.W.6
  • 20
    • 0036411843 scopus 로고    scopus 로고
    • Identification and characterization of a mammalian 14-kDa phosphohistidine phosphatase
    • Ek P, Pettersson G, Ek B, Gong F, Li J-P, Zetterqvist Ö. Identification and characterization of a mammalian 14-kDa phosphohistidine phosphatase. Eur J Biochem. 2002;269: 5016-23.
    • (2002) Eur J Biochem. , vol.269 , pp. 5016-5023
    • Ek, P.1    Pettersson, G.2    Ek, B.3    Gong, F.4    Li, J.-P.5    Zetterqvist Ö.6
  • 24
    • 61449218994 scopus 로고    scopus 로고
    • Solution structure and catalytic mechanism of human protein histidine phosphatase 1
    • Gong W, Li Y, Cui G, Hu J, Fang H, Jin C, et al. Solution structure and catalytic mechanism of human protein histidine phosphatase 1. Biochem J. 2009;418:337-44.
    • (2009) Biochem J. , vol.418 , pp. 337-344
    • Gong, W.1    Li, Y.2    Cui, G.3    Hu, J.4    Fang, H.5    Jin, C.6
  • 27
    • 33751513093 scopus 로고    scopus 로고
    • Histidine phosphorylation of the potassium channel KCa3.1 by nucleoside diphosphate kinase B is required for activation of KCa3.1 and CD4 T cells
    • Srivastava S, Li Z, Ko K, Choudhury P, Albaqumi M, Johnson AK, et al. Histidine phosphorylation of the potassium channel KCa3.1 by nucleoside diphosphate kinase B is required for activation of KCa3.1 and CD4 T cells. Mol Cell. 2006;24:665-75.
    • (2006) Mol Cell. , vol.24 , pp. 665-675
    • Srivastava, S.1    Li, Z.2    Ko, K.3    Choudhury, P.4    Albaqumi, M.5    Johnson, A.K.6
  • 28
    • 55749083563 scopus 로고    scopus 로고
    • Protein histidine phosphatase 1 negatively regulates CD4 T cells by inhibiting the K+ channel KCa3
    • Srivastava S, Zhdanova O, Di L, Li Z, Albaqumi M, Wulff H, et al. Protein histidine phosphatase 1 negatively regulates CD4 T cells by inhibiting the K+ channel KCa3. Proc Natl Acad Sci USA. 2008;105:14442-6.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14442-14446
    • Srivastava, S.1    Zhdanova, O.2    Di, L.3    Li, Z.4    Albaqumi, M.5    Wulff, H.6
  • 29
    • 84907814413 scopus 로고    scopus 로고
    • Regulation of the epthelial Ca2+ channel TRPV5 by reversible histidine phosphorylation mediated by NDPK B and PHPT1
    • Cai X, Srivastava S, Surindran S, Li Z, Skolnik EY. Regulation of the epthelial Ca2+ channel TRPV5 by reversible histidine phosphorylation mediated by NDPK B and PHPT1. Mol Biol Cell. 2014;25:1244-50.
    • (2014) Mol Biol Cell. , vol.25 , pp. 1244-1250
    • Cai, X.1    Srivastava, S.2    Surindran, S.3    Li, Z.4    Skolnik, E.Y.5
  • 30
    • 79952202394 scopus 로고    scopus 로고
    • Reversible histidine phosphorylation in mammalian cells: A teeter totter formed by nucleoside diphosphate kinase and protein histidine phosphatase 1
    • Wieland T, Hippe HJ, Ludwig K, Zhou XB, Korth M, Klumpp S. Reversible histidine phosphorylation in mammalian cells: a teeter totter formed by nucleoside diphosphate kinase and protein histidine phosphatase 1. Methods Enzymol. 2010;471:379-402.
    • (2010) Methods Enzymol. , vol.471 , pp. 379-402
    • Wieland, T.1    Hippe, H.J.2    Ludwig, K.3    Zhou, X.B.4    Korth, M.5    Klumpp, S.6
  • 31
    • 71549168985 scopus 로고    scopus 로고
    • 14 kDa phosphohistidine phosphatase and its role inhuman lung cancer cell migration and invasion
    • Xu A, Hao J, Zhang Z, Tian T, Jiang S, Hao J, et al. 14 kDa phosphohistidine phosphatase and its role inhumanlung cancer cell migration and invasion. Lung Cancer. 2010;67:48-56.
    • (2010) Lung Cancer. , vol.67 , pp. 48-56
    • Xu, A.1    Hao, J.2    Zhang, Z.3    Tian, T.4    Jiang, S.5    Hao, J.6
  • 32
    • 84878594159 scopus 로고    scopus 로고
    • A novel high throughput invasion screen identifies host actin regulators for efficient cell entry by Toxoplasma gondii
    • Gaji RY, Huynh MH, Carruthers VB. A novel high throughput invasion screen identifies host actin regulators for efficient cell entry by Toxoplasma gondii. PLoS One. 2013;8:e64693.
    • (2013) PLoS One. , vol.8 , pp. e64693
    • Gaji, R.Y.1    Huynh, M.H.2    Carruthers, V.B.3
  • 33
    • 84864709677 scopus 로고    scopus 로고
    • 14-kDa phosphohistidine phosphatase plays an important role in hepatocellular carcinoma cell proliferation
    • Han SX, Wang LJ, Zhao J, Zhang Y, Li M, Zhou X, et al. 14-kDa phosphohistidine phosphatase plays an important role in hepatocellular carcinoma cell proliferation. Oncol Lett. 2012;4:658-64.
    • (2012) Oncol Lett. , vol.4 , pp. 658-664
    • Han, S.X.1    Wang, L.J.2    Zhao, J.3    Zhang, Y.4    Li, M.5    Zhou, X.6
  • 34
    • 71649115175 scopus 로고    scopus 로고
    • Chemical phosphorylation of histidine containing peptides based on the sequence of histone H4 and their dephosphorylation by protein histidine phosphatase
    • Attwood PV, Ludwig K, Bergander K, Besant PG, Adina-Zada A, Krieglstein J, et al. Chemical phosphorylation of histidine containing peptides based on the sequence of histone H4 and their dephosphorylation by protein histidine phosphatase. Biochim Biophys Acta. 2010;1804:199-205.
    • (2010) Biochim Biophys Acta. , vol.1804 , pp. 199-205
    • Attwood, P.V.1    Ludwig, K.2    Bergander, K.3    Besant, P.G.4    Adina-Zada, A.5    Krieglstein, J.6
  • 35
    • 79960671630 scopus 로고    scopus 로고
    • A screening method for phosphohistidine phosphatase 1 activity
    • Beckman Sundh U, Ek B, Zetterqvist Ö, Ek P. A screening method for phosphohistidine phosphatase 1 activity. Ups J Med Sci. 2011;116:161-8.
    • (2011) Ups J Med Sci. , vol.116 , pp. 161-168
    • Beckman Sundh, U.1    Ek, B.2    Zetterqvist, O.3    Ek, P.4
  • 36
    • 0034238106 scopus 로고    scopus 로고
    • Synthesis of [32P]phosphoramidate for use as a low molecular weight phosphodonor reagent
    • Buckler DR, Stock AM. Synthesis of [32P]phosphoramidate for use as a low molecular weight phosphodonor reagent. Anal Biochem. 2000;283:222-7.
    • (2000) Anal Biochem. , vol.283 , pp. 222-227
    • Buckler, D.R.1    Stock, A.M.2
  • 37
    • 0010991082 scopus 로고
    • Isolation of a homogenous lysine-rich histone from calf thymus
    • de Nooij EH, Westenbrink HGK. Isolation of a homogenous lysine-rich histone from calf thymus. Biochim Biophys Acta. 1962;62:608-9.
    • (1962) Biochim Biophys Acta. , vol.62 , pp. 608-609
    • De Nooij, E.H.1    Westenbrink, H.G.K.2
  • 38
    • 78650881098 scopus 로고    scopus 로고
    • Electron capture dissociation mass spectrometric analysis of lysine phosphorylated peptides
    • Kowalewska K, Stefanowicz P, Ruman T, Fra{ogonek}czyk T, Rode W, Szewczuk Z. Electron capture dissociation mass spectrometric analysis of lysine phosphorylated peptides. Biosci Rep. 2010;30:433-43.
    • (2010) Biosci Rep. , vol.30 , pp. 433-443
    • Kowalewska, K.1    Stefanowicz, P.2    Ruman, T.3    Frączyk, T.4    Rode, W.5    Szewczuk, Z.6
  • 39
    • 58149289691 scopus 로고    scopus 로고
    • Histone H1 and its isoforms: Contribution to chromatin structure and function
    • Happel N, Doenecke D. Histone H1 and its isoforms: contribution to chromatin structure and function. Gene. 2009; 431:1-12.
    • (2009) Gene , vol.431 , pp. 1-12
    • Happel, N.1    Doenecke, D.2
  • 40
    • 33846488609 scopus 로고    scopus 로고
    • Mass spectrometric mapping of linker histone H1 variants reveals multiple acetylations, methylations, and phosphorylation as well as differences between cell culture and tissue
    • Wis̈niewski JR, Zougman A, Krüger S, Mann M. Mass spectrometric mapping of linker histone H1 variants reveals multiple acetylations, methylations, and phosphorylation as well as differences between cell culture and tissue. Mol Cell Proteomics. 2007;6:72-87.
    • (2007) Mol Cell Proteomics. , vol.6 , pp. 72-87
    • Wis̈niewski, J.R.1    Zougman, A.2    Krüger, S.3    Mann, M.4
  • 42
    • 0016288110 scopus 로고
    • Characterization of protein kinases forming acid labile histone phosphates in Walker 256 carcinosarcoma cell nuclei
    • Smith DL, Chen CC, Bruegger BB, Holtz SL, Halpern RM, Smith RA. Characterization of protein kinases forming acid labile histone phosphates in Walker 256 carcinosarcoma cell nuclei. Biochemistry. 1974;13:3780-5.
    • (1974) Biochemistry , vol.13 , pp. 3780-3785
    • Smith, D.L.1    Chen, C.C.2    Bruegger, B.B.3    Holtz, S.L.4    Halpern, R.M.5    Smith, R.A.6
  • 43
    • 0016266268 scopus 로고
    • Occurrence and distribution of acid labile histone phosphates in regenerating rat liver
    • Chen CC, Smith DL, Bruegger BB, Halpern RM, Smith RA. Occurrence and distribution of acid labile histone phosphates in regenerating rat liver. Biochemistry. 1974;13:3785-9.
    • (1974) Biochemistry , vol.13 , pp. 3785-3789
    • Chen, C.C.1    Smith, D.L.2    Bruegger, B.B.3    Halpern, R.M.4    Smith, R.A.5
  • 45
    • 0020474065 scopus 로고
    • Isolation and purification of a new 105 kDa protein kinase from rat liver nuclei
    • Sikorska M, Whitfield JF. Isolation and purification of a new 105 kDa protein kinase from rat liver nuclei. Biochim Biophys Acta. 1982;703:171-9.
    • (1982) Biochim Biophys Acta. , vol.703 , pp. 171-179
    • Sikorska, M.1    Whitfield, J.F.2
  • 46
    • 67650608424 scopus 로고    scopus 로고
    • Immunohistochemical localization of phosphohistidine phosphatase PHPT1 in mouse and human tissues
    • Zhang XQ, Beckman Sundh U, Jansson L, Zetterqvist Ö, Ek P. Immunohistochemical localization of phosphohistidine phosphatase PHPT1 in mouse and human tissues. Ups JMed Sci. 2009;114:65-72.
    • (2009) Ups JMed Sci. , vol.114 , pp. 65-72
    • Zhang, X.Q.1    Beckman Sundh, U.2    Jansson, L.3    Zetterqvist, O.4    Ek, P.5
  • 47
    • 84986849651 scopus 로고
    • The effect of phosphorylation of the histidyl residue in the tetrapeptide Gly Gly His Ala. Changes of chemical shift and pK values in 1H and 31P NMR spectra
    • Kalbitzer HR, Rösch P. The effect of phosphorylation of the histidyl residue in the tetrapeptide Gly Gly His Ala. Changes of chemical shift and pK values in 1H and 31P NMR spectra. Org Magn Resonance. 1981;17:88-91.
    • (1981) Org Magn Resonance , vol.17 , pp. 88-91
    • Kalbitzer, H.R.1    Rösch, P.2
  • 48
    • 84977796802 scopus 로고    scopus 로고
    • Nucleoside diphosphate kinase as protein histidine kinase
    • [Epub ahead of print]
    • Attwood PV, Wieland T. Nucleoside diphosphate kinase as protein histidine kinase. Naunyn Schmiedebergs Arch Pharmacol. 2014. [Epub ahead of print].
    • (2014) Naunyn Schmiedebergs Arch Pharmacol
    • Attwood, P.V.1    Wieland, T.2
  • 49
    • 0032817262 scopus 로고    scopus 로고
    • Bovine liver phosphoamidase as a protein histidine/lysine phosphatase
    • Hiraishi H, Yokoi F, Kumon A. Bovine liver phosphoamidase as a protein histidine/lysine phosphatase. J Biochem. 1999; 126:368-74.
    • (1999) J Biochem. , vol.126 , pp. 368-374
    • Hiraishi, H.1    Yokoi, F.2    Kumon, A.3
  • 51
    • 84871720353 scopus 로고    scopus 로고
    • P-N bond protein phosphatases
    • Attwood PV. P-N bond protein phosphatases. Biochim Biophys Acta. 2013;1834:470-8.
    • (2013) Biochim Biophys Acta. , vol.1834 , pp. 470-478
    • Attwood, P.V.1
  • 52
    • 0032518191 scopus 로고    scopus 로고
    • 3-Phosphohistidine and 6-phospholysine are substrates of a 56 kDa inorganic pyrophosphatase from bovine liver
    • Hiraishi H, Yokoi F, Kumon A. 3-Phosphohistidine and 6-phospholysine are substrates of a 56 kDa inorganic pyrophosphatase from bovine liver. Arch Biochem Biophys. 1998;349: 381-7.
    • (1998) Arch Biochem Biophys. , vol.349 , pp. 381-387
    • Hiraishi, H.1    Yokoi, F.2    Kumon, A.3
  • 53
    • 0037971250 scopus 로고    scopus 로고
    • Molecular cloning of a cDNA for the human phospholysine phosphohistidine inorganic pyrophosphate phosphatase
    • Yokoi F, Hiraishi H, Izuhara K. Molecular cloning of a cDNA for the human phospholysine phosphohistidine inorganic pyrophosphate phosphatase. J Biochem. 2003; 133:607-14.
    • (2003) J Biochem. , vol.133 , pp. 607-614
    • Yokoi, F.1    Hiraishi, H.2    Izuhara, K.3
  • 54
    • 0027494437 scopus 로고
    • Phosphohistidine and phospholysine phosphatase activities in the rat: Potential protein lysine and protein histidine phosphatases?
    • Wong C, Faiola B, Wu W, Kennely J. Phosphohistidine and phospholysine phosphatase activities in the rat: potential protein lysine and protein histidine phosphatases? Biochem J. 1993;296:293-6.
    • (1993) Biochem J. , vol.296 , pp. 293-296
    • Wong, C.1    Faiola, B.2    Wu, W.3    Kennely, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.