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Volumn 7, Issue 1, 2012, Pages 44-51

Chasing phosphohistidine, an elusive sibling in the phosphoamino acid family

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; PHOSPHOAMINO ACID; PHOSPHOHISTIDINE; PHOSPHOHISTIDINE ANTIBODY; PHOSPHORYLTRIAZOLYLALANINE DERIVATIVE; PROTEIN HISTIDINE KINASE; THIOPHOSPHOHISTIDINE; UNCLASSIFIED DRUG;

EID: 84856158810     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb200445w     Document Type: Review
Times cited : (114)

References (86)
  • 2
    • 3543037572 scopus 로고    scopus 로고
    • Molecularly targeted therapy: Have the floodgates opened?
    • DOI 10.1634/theoncologist.9-4-357
    • Druker, B. J. (2004) Molecularly targeted therapy: Have the floodgates opened? Oncologist 9, 357-360 (Pubitemid 39014547)
    • (2004) Oncologist , vol.9 , Issue.4 , pp. 357-360
    • Druker, B.J.1
  • 3
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases - The major drug targets of the twenty-first century?
    • Cohen, P. (2002) Protein kinases - the major drug targets of the twenty-first century? Nat. Rev. Drug Discovery 1, 309-315 (Pubitemid 37361447)
    • (2002) Nature Reviews Drug Discovery , vol.1 , Issue.4 , pp. 309-315
    • Cohen, P.1
  • 4
    • 0000183819 scopus 로고
    • Identification of phosphohistidine in digests from a probable intermediate of oxidative phosphorylation
    • Boyer, P. D., Peter, J. B., Ebner, K. E., Deluca, M., and Hultquist, D. (1962) Identification of phosphohistidine in digests from a probable intermediate of oxidative phosphorylation J. Biol. Chem. 237, 3306-3308
    • (1962) J. Biol. Chem. , vol.237 , pp. 3306-3308
    • Boyer, P.D.1    Peter, J.B.2    Ebner, K.E.3    Deluca, M.4    Hultquist, D.5
  • 5
    • 0018580807 scopus 로고
    • An activity phosphorylating tyrosine in polyoma T antigen immunoprecipitates
    • Eckhart, W., Hutchinson, M. A., and Hunter, T. (1979) An activity phosphorylating tyrosine in polyoma T antigen immunoprecipitates Cell 18, 925-933 (Pubitemid 10172631)
    • (1979) Cell , vol.18 , Issue.4 , pp. 925-933
    • Eckhart, W.1    Hutchinson, M.A.2    Hunter, T.3
  • 6
    • 29244442913 scopus 로고    scopus 로고
    • Bacterial histidine kinase as signal sensor and transducer
    • DOI 10.1016/j.biocel.2005.08.018, PII S1357272505002608
    • Khorchid, A. and Ikura, M. (2006) Bacterial histidine kinase as signal sensor and transducer Int. J. Biochem. Cell Biol. 38, 307-312 (Pubitemid 41821879)
    • (2006) International Journal of Biochemistry and Cell Biology , vol.38 , Issue.3 , pp. 307-312
    • Khorchid, A.1    Ikura, M.2
  • 7
    • 79954505968 scopus 로고    scopus 로고
    • Receptor domains of two-component signal transduction systems
    • Perry, J., Koteva, K., and Wright, G. (2011) Receptor domains of two-component signal transduction systems Mol. BioSyst. 7, 1388-1398
    • (2011) Mol. BioSyst. , vol.7 , pp. 1388-1398
    • Perry, J.1    Koteva, K.2    Wright, G.3
  • 8
    • 33845260754 scopus 로고    scopus 로고
    • Focus on phosphohistidine
    • DOI 10.1007/s00726-006-0443-6, Special Issue: Focus on Biologically Active D-Amino Acids
    • Attwood, P. V., Piggott, M. J., Zu, X. L., and Besant, P. G. (2007) Focus on phosphohistidine Amino Acids 32, 145-156 (Pubitemid 44866582)
    • (2007) Amino Acids , vol.32 , Issue.1 , pp. 145-156
    • Attwood, P.V.1    Piggott, M.J.2    Zu, X.L.3    Besant, P.G.4
  • 9
    • 0037428893 scopus 로고    scopus 로고
    • Histidine kinases and histidine phosphorylated proteins in mammalian cell biology, signal transduction and cancer
    • DOI 10.1016/S0304-3835(02)00499-8
    • Steeg, P. S., Palmieri, D., Ouatas, T., and Salerno, M. (2003) Histidine kinases and histidine phosphorylated proteins in mammalian cell biology, signal transduction and cancer Cancer Lett. 190, 1-12 (Pubitemid 36106550)
    • (2003) Cancer Letters , vol.190 , Issue.1 , pp. 1-12
    • Steeg, P.S.1    Palmieri, D.2    Ouatas, T.3    Salerno, M.4
  • 11
    • 0037177222 scopus 로고    scopus 로고
    • Mammalian histidine kinases: Do they really exist?
    • DOI 10.1021/bi012021r
    • Tan, E., Besant, P., and Attwood, P. (2002) Mammalian histidine kinases: do they REALLY exist? Biochemistry 41, 3843-3851 (Pubitemid 34251021)
    • (2002) Biochemistry , vol.41 , Issue.12 , pp. 3843-3851
    • Tan, E.1    Besant, P.G.2    Attwood, P.V.3
  • 12
    • 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, H. (1995) 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 Pharmacol. Ther. 67, 323-350
    • (1995) Pharmacol. Ther. , vol.67 , pp. 323-350
    • Matthews, H.1
  • 15
    • 0027198334 scopus 로고
    • Guanine nucleotide-specific phosphate transfer by guanine nucleotide- binding regulatory protein β-subunits. Characterization of the phosphorylated amino acid
    • Wieland, T., Nürnberg, B., Ulibarri, I., Kaldenberg-Stasch, S., Schultz, G., and Jakobs, K. H. (1993) Guanine nucleotide-specific phosphate transfer by guanine nucleotide-binding regulatory protein β-subunits. Characterization of the phosphorylated amino acid J. Biol. Chem. 268, 18111-18118 (Pubitemid 23260331)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.24 , pp. 18111-18118
    • Wieland, T.1    Nurnberg, B.2    Ulibarri, I.3    Kaldenberg-Stasch, S.4    Schultz, G.5    Jakobs, K.H.6
  • 16
    • 0037470147 scopus 로고    scopus 로고
    • Activation of heterotrimeric G proteins by a high energy phosphate transfer via nucleoside diphosphate kinase (NDPK) B and Gβ subunits. Complex formation of NDPK B with Gβγ dimers and phosphorylation of his-266 in Gβ
    • DOI 10.1074/jbc.M210304200
    • Cuello, F., Schulze, R. A., Heemeyer, F., Meyer, H. E., Lutz, S., Jakobs, K. H., Niroomand, F., and Wieland, T. (2003) Activation of heterotrimeric G proteins by a high energy phosphate transfer via nucleoside diphosphate kinase (NDPK) B and Gβ subunits. Complex formation of NDPK B with Gβ? dimers and phosphorylation of His-266 in Gβ J. Biol. Chem. 278, 7220-7226 (Pubitemid 36800722)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.9 , pp. 7220-7226
    • Cuello, F.1    Schulze, R.A.2    Heemeyer, F.3    Meyer, H.E.4    Lutz, S.5    Jakobs, K.H.6    Niroomand, F.7    Wieland, T.8
  • 18
    • 0037098278 scopus 로고    scopus 로고
    • Identification and characterization of a novel protein histidine kinase in the islet β cell: Evidence for its regulation by mastoparan, an activator of G-proteins and insulin secretion
    • DOI 10.1016/S0006-2952(02)01025-0, PII S0006295202010250
    • Kowluru, A. (2002) Identification and characterization of a novel protein histidine kinase in the islet beta cell: evidence for its regulation by mastoparan, an activator of G-proteins and insulin secretion Biochem. Pharmacol. 63, 2091-2100 (Pubitemid 34756674)
    • (2002) Biochemical Pharmacology , vol.63 , Issue.12 , pp. 2091-2100
    • Kowluru, A.1
  • 19
    • 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
    • DOI 10.1016/j.molcel.2006.11.012, PII S1097276506007830
    • Srivastava, S., Li, Z., Ko, K., Choudhury, P., Albaqumi, M., Johnson, A. K., Yan, Y., Backer, J. M., Unutmaz, D., Coetzee, W. A., and Skolnik, E. Y. (2006) 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 24, 665-675 (Pubitemid 44839222)
    • (2006) Molecular Cell , vol.24 , Issue.5 , pp. 665-675
    • Srivastava, S.1    Li, Z.2    Ko, K.3    Choudhury, P.4    Albaqumi, M.5    Johnson, A.K.6    Yan, Y.7    Backer, J.M.8    Unutmaz, D.9    Coetzee, W.A.10    Skolnik, E.Y.11
  • 20
    • 30044440424 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate indirectly activates KCa3.1 via 14 amino acids in the carboxy terminus of KCa3.1
    • DOI 10.1091/mbc.E05-08-0763
    • Srivastava, S., Choudhury, P., Li, Z., Liu, G., Nadkarni, V., Ko, K., Coetzee, W. A., and Skolnik, E. Y. (2006) Phosphatidylinositol 3-phosphate indirectly activates KCa3.1 via 14 amino acids in the carboxy terminus of KCa3.1 Mol. Biol. Cell 17, 146-154 (Pubitemid 43049469)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.1 , pp. 146-154
    • Srivastava, S.1    Choudhury, P.2    Li, Z.3    Liu, G.4    Nadkarni, V.5    Ko, K.6    Coetzee, W.A.7    Skolnik, E.Y.8
  • 21
    • 0029101744 scopus 로고
    • Phosphorylation of ATP-citrate lyase by nucleoside diphosphate kinase
    • Wagner, P. D. and Vu, N. D. (1995) Phosphorylation of ATP-citrate lyase by nucleoside diphosphate kinase J. Biol. Chem. 270, 21758-21764
    • (1995) J. Biol. Chem. , vol.270 , pp. 21758-21764
    • Wagner, P.D.1    Vu, N.D.2
  • 22
    • 0016266268 scopus 로고
    • Occurrence and distribution of acid-labile histone phosphates in regenerating rat liver
    • Chen, C. C., Smith, D. L., Bruegger, B. B., Halpern, R. M., and Smith, R. A. (1974) Occurrence and distribution of acid-labile histone phosphates in regenerating rat liver Biochemistry 13, 3785-3789
    • (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
  • 23
    • 0017752240 scopus 로고
    • Phosphorylation of nuclear proteins in rat regenerating liver
    • Chen, C. C., Bruegger, B. B., Kern, C. W., Lin, Y. C., Halpern, R. M., and Smith, R. A. (1977) Phosphorylation of nuclear proteins in rat regenerating liver Biochemistry 16, 4852-4855 (Pubitemid 8220978)
    • (1977) Biochemistry , vol.16 , Issue.22 , pp. 4852-4855
    • Chen, C.C.1    Bruegger, B.B.2    Kern, C.W.3
  • 24
    • 0019876092 scopus 로고
    • Characterization of chemical and enzymatic acid-labile phosphorylation of histone H4 using phosphorus-31 nuclear magnetic resonance
    • Fujitaki, J. M., Fung, G., Oh, E. Y., and Smith, R. A. (1981) Characterization of chemical and enzymatic acid-labile phosphorylation of histone H4 using phosphorus-31 nuclear magnetic resonance Biochemistry 20, 3658-3664
    • (1981) Biochemistry , vol.20 , pp. 3658-3664
    • Fujitaki, J.M.1    Fung, G.2    Oh, E.Y.3    Smith, R.A.4
  • 25
    • 0037870267 scopus 로고    scopus 로고
    • Nucleoside diphosphate kinases in mammalian signal transduction systems: Recent development and perspective
    • DOI 10.1023/A:1023489722460
    • Kimura, N., Shimada, N., Ishijima, Y., Fukuda, M., Takagi, Y., and Ishikawa, N. (2003) Nucleoside diphosphate kinases in mammalian signal transduction systems: recent development and perspective J. Bioenerg. Biomembr. 35, 41-47 (Pubitemid 36667579)
    • (2003) Journal of Bioenergetics and Biomembranes , vol.35 , Issue.1 , pp. 41-47
    • Kimura, N.1    Shimada, N.2    Ishijima, Y.3    Fukuda, M.4    Takagi, Y.5    Ishikawa, N.6
  • 27
    • 0022399331 scopus 로고
    • Phosphorus-31 nuclear magnetic resonance study of the active site phosphohistidine and regulatory phosphoserine residues of rat liver ATP-citrate lyase
    • DOI 10.1021/bi00341a037
    • Williams, S., Sykes, B., and Bridger, W. (1985) Phosphorus-31 nuclear magnetic-resonance study of the active-site phosphohistidine and regulatory phosphoserine residues of rat-liver ATP-citrate lyase Biochemistry 24, 5527-5531 (Pubitemid 16228834)
    • (1985) Biochemistry , vol.24 , Issue.20 , pp. 5527-5531
    • Williams, S.P.1    Sykes, B.D.2    Bridger, W.A.3
  • 28
    • 1842582072 scopus 로고    scopus 로고
    • Histidine 167 Is the Phosphate Acceptor in Glucose-6-phosphatase-β Forming a Phosphohistidine Enzyme Intermediate during Catalysis
    • DOI 10.1074/jbc.M313271200
    • Ghosh, A., Shieh, J.-J., Pan, C.-J., and Chou, J. Y. (2004) Histidine 167 is the phosphate acceptor in glucose-6-phosphatase-β forming a phosphohistidine enzyme intermediate during catalysis J. Biol. Chem. 279, 12479-12483 (Pubitemid 38445817)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12479-12483
    • Ghosh, A.1    Shieh, J.-J.2    Pan, C.-J.3    Chou, J.Y.4
  • 29
    • 0021354642 scopus 로고
    • Evidence for two catalytic sites on 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase. Dynamics of substrate exchange and phosphoryl enzyme formation
    • Pilkis, S. J., Regen, D. M., Stewart, H. B., Pilkis, J., Pate, T. M., and El-Maghrabi, M. R. (1984) Evidence for two catalytic sites on 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase. Dynamics of substrate exchange and phosphoryl enzyme formation J. Biol. Chem. 259, 949-958 (Pubitemid 14192449)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.2 , pp. 949-958
    • Pilkis, S.J.1    Regen, D.M.2    Stewart, H.B.3
  • 30
    • 0014866943 scopus 로고
    • Evidence for a phosphohistidine protein intermediate in the phosphoglycerate mutase reaction
    • Rose, Z. B. (1970) Evidence for a phosphohistidine protein intermediate in the phosphoglycerate mutase reaction Arch. Biochem. Biophys. 140, 508-513
    • (1970) Arch. Biochem. Biophys. , vol.140 , pp. 508-513
    • Rose, Z.B.1
  • 33
    • 0017902284 scopus 로고
    • Isolation of γ-phosphohistidine from a phosphoryl-enzyme intermediate of human prostatic acid phosphatase
    • Ostrowski, W. (1978) Isolation of ?-phosphohistidine from a phosphoryl-enzyme intermediate of human prostatic acid-phosphatase Biochim. Biophys. Acta 526, 147-153 (Pubitemid 8401888)
    • (1978) Biochimica et Biophysica Acta , vol.526 , Issue.1 , pp. 147-153
    • Ostrowski, W.1
  • 37
    • 33645050656 scopus 로고    scopus 로고
    • Two-component signal transduction in human fungal pathogens
    • Kruppa, M. and Calderone, R. (2006) Two-component signal transduction in human fungal pathogens FEMS Yeast Res. 6, 149-159
    • (2006) FEMS Yeast Res. , vol.6 , pp. 149-159
    • Kruppa, M.1    Calderone, R.2
  • 38
    • 4644309634 scopus 로고    scopus 로고
    • Plant two-component systems: Principles, functions, complexity and cross talk
    • DOI 10.1007/s00425-004-1316-4
    • Grefen, C. and Harter, K. (2004) Plant two-component systems: principles, functions, complexity and cross talk Planta 219, 733-742 (Pubitemid 39282937)
    • (2004) Planta , vol.219 , Issue.5 , pp. 733-742
    • Grefen, C.1    Harter, K.2
  • 39
    • 0015898333 scopus 로고
    • New histone kinases in nuclei of rat tissues
    • Smith, D. L., Bruegger, B. B., Halpern, R. M., and Smith, R. A. (1973) New histone kinases in nuclei of rat tissues Nature 246, 103-104
    • (1973) Nature , vol.246 , pp. 103-104
    • Smith, D.L.1    Bruegger, B.B.2    Halpern, R.M.3    Smith, R.A.4
  • 40
    • 0016288110 scopus 로고
    • Characterization of protein kinases forming acid-labile histone phosphates in Walker-256 carcinosarcoma cell nuclei
    • Smith, D. L., Chen, C. C., Bruegger, B. B., Holtz, S. L., Halpern, R. M., and Smith, R. A. (1974) Characterization of protein kinases forming acid-labile histone phosphates in Walker-256 carcinosarcoma cell nuclei Biochemistry 13, 3780-3785
    • (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
  • 41
    • 0025800420 scopus 로고
    • Purification of a protein histidine kinase from the yeast Saccharomyces cerevisiae. The first member of this class of protein kinases
    • Huang, J. M., Wei, Y. F., Kim, Y. H., Osterberg, L., and Matthews, H. R. (1991) Purification of a protein histidine kinase from the yeast Saccharomyces cerevisiae. The first member of this class of protein kinases J. Biol. Chem. 266, 9023-9029
    • (1991) J. Biol. Chem. , vol.266 , pp. 9023-9029
    • Huang, J.M.1    Wei, Y.F.2    Kim, Y.H.3    Osterberg, L.4    Matthews, H.R.5
  • 42
    • 0033986924 scopus 로고    scopus 로고
    • Detection of a mammalian histone H4 kinase that has yeast histidine kinase-like enzymic activity
    • DOI 10.1016/S1357-2725(99)00119-3, PII S1357272599001193
    • Besant, P. and Attwood, P. (2000) Detection of a mammalian histone H4 kinase that has yeast histidine kinase-like enzymic activity Int. J. Biochem. Cell Biol. 32, 243-253 (Pubitemid 30001826)
    • (2000) International Journal of Biochemistry and Cell Biology , vol.32 , Issue.2 , pp. 243-253
    • Besant, P.G.1    Attwood, P.V.2
  • 43
    • 8844230284 scopus 로고    scopus 로고
    • Histone H4 histidine kinase displays the expression pattern of a liver oncodevelopmental marker
    • DOI 10.1093/carcin/bgh222
    • Tan, E., Besant, P. G., Zu, X. L., Turck, C. W., Bogoyevitch, M. A., Lim, S. G., Attwood, P. V., and Yeoh, G. C. (2004) Histone H4 histidine kinase displays the expression pattern of a liver oncodevelopmental marker Carcinogenesis 25, 2083-2088 (Pubitemid 39534844)
    • (2004) Carcinogenesis , vol.25 , Issue.11 , pp. 2083-2088
    • Tan, E.1    Besant, P.G.2    Zu, X.L.3    Turck, C.W.4    Bogoyevitch, M.A.5    Lim, S.G.6    Attwood, P.V.7    Yeoh, G.C.8
  • 44
    • 0036411843 scopus 로고    scopus 로고
    • Identification and characterization of a mammalian 14-kDa phosphohistidine phosphatase
    • DOI 10.1046/j.1432-1033.2002.03206.x
    • Ek, P., Pettersson, G., Ek, B., Gong, F., Li, J. P., and Zetterqvist, O. (2002) Identification and characterization of a mammalian 14-kDa phosphohistidine phosphatase Eur. J. Biochem. 269, 5016-5023 (Pubitemid 35279015)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.20 , pp. 5016-5023
    • Ek, P.1    Pettersson, G.2    Ek, B.3    Gong, F.4    Li, J.-P.5    Zetterqvist, O.6
  • 47
    • 0027279242 scopus 로고
    • Protein phosphatases 1, 2A, and 2C are protein histidine phosphatases
    • Kim, Y., Huang, J., Cohen, P., and Matthews, H. R. (1993) Protein phosphatases 1, 2A, and 2C are protein histidine phosphatases J. Biol. Chem. 268, 18513-18518 (Pubitemid 23273783)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.25 , pp. 18513-18518
    • Kim, Y.1    Huang, J.2    Cohen, P.3    Matthews, H.R.4
  • 48
    • 0029034416 scopus 로고
    • Protein histidine phosphatase activity in rat liver and spinach leaves
    • Matthews, H. R. and MacKintosh, C. (1995) Protein histidine phosphatase activity in rat liver and spinach leaves FEBS Lett. 364, 51-54
    • (1995) FEBS Lett. , vol.364 , pp. 51-54
    • Matthews, H.R.1    MacKintosh, C.2
  • 49
    • 0013872353 scopus 로고
    • The preparation and characterization of 1-phosphohistidine and 3-phosphohistidine
    • Hultquist, D. E., Moyer, R. W., and Boyer, P. D. (1966) The preparation and characterization of 1-phosphohistidine and 3-phosphohistidine Biochemistry 5, 322-331
    • (1966) Biochemistry , vol.5 , pp. 322-331
    • Hultquist, D.E.1    Moyer, R.W.2    Boyer, P.D.3
  • 50
    • 0033577726 scopus 로고    scopus 로고
    • Phosphofurylalanine, a stable analog of phosphohistidine
    • DOI 10.1016/S0960-894X(99)00209-7, PII S0960894X99002097
    • Schenkels, C., Erni, B., and Reymond, J. L. (1999) Phosphofurylalanine, a stable analog of phosphohistidine Bioorg. Med. Chem. Lett. 9, 1443-1446 (Pubitemid 29232224)
    • (1999) Bioorganic and Medicinal Chemistry Letters , vol.9 , Issue.10 , pp. 1443-1446
    • Schenkels, C.1    Erni, B.2    Reymond, J.-L.3
  • 51
    • 38149048499 scopus 로고    scopus 로고
    • Histidine phosphorylation in biological systems
    • Puttick, J., Baker, E., and Delbaere, L. (2008) Histidine phosphorylation in biological systems Biochim. Biophys. Acta 1784, 100-105
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 100-105
    • Puttick, J.1    Baker, E.2    Delbaere, L.3
  • 52
    • 0017686350 scopus 로고    scopus 로고
    • Nomenclature of phosphorus-containing compounds of biochemical importance (Recommendations 1976)
    • IUPAC-IUB Commission on Biochemical Nomenclature (1977).
    • IUPAC-IUB Commission on Biochemical Nomenclature (1977) Nomenclature of phosphorus-containing compounds of biochemical importance (Recommendations 1976), Proc. Natl. Acad. Sci. U.S.A. 74, 2222-2230.
    • Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 2222-2230
  • 54
    • 0014411498 scopus 로고
    • The preparation and characterization of phosphorylated derivatives of histidine
    • Hultquist, D. E. (1968) The preparation and characterization of phosphorylated derivatives of histidine Biochim. Biophys. Acta 153, 329-340
    • (1968) Biochim. Biophys. Acta , vol.153 , pp. 329-340
    • Hultquist, D.E.1
  • 55
    • 0025935237 scopus 로고
    • Chemical properties and separation of phosphoamino acids by thin-layer chromatography and/or electrophoresis
    • Duclos, B., Marcandier, S., and Cozzone, A. J. (1991) Chemical properties and separation of phosphoamino acids by thin-layer chromatography and/or electrophoresis Methods Enzymol. 210, 10-21
    • (1991) Methods Enzymol. , vol.210 , pp. 10-21
    • Duclos, B.1    Marcandier, S.2    Cozzone, A.J.3
  • 56
    • 79952199067 scopus 로고    scopus 로고
    • Histidine phosphorylation in histones and in other mammalian proteins
    • Besant, P. G. and Attwood, P. V. (2010) Histidine phosphorylation in histones and in other mammalian proteins Methods Enzymol. 471, 403-426
    • (2010) Methods Enzymol. , vol.471 , pp. 403-426
    • Besant, P.G.1    Atwood, P.V.2
  • 57
    • 0027163002 scopus 로고
    • The involvement of the arginine 17 residue in the active site of the histidine-containing protein, HPr, of the phosphoenolpyruvate:sugar phosphotransferase system of Escherichia coli
    • Anderson, J., Pullen, K., Georges, F., Klevit, R., and Waygood, E. (1993) The involvement of the arginine-17 residue in the active-site of the histidine-containing protein, HPr, of the phosphoenolpyruvate-sugar phosphotransferase system of Escherichia coli J. Biol. Chem. 268, 12325-12333 (Pubitemid 23182384)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.17 , pp. 12325-12333
    • Anderson, J.W.1    Pullen, K.2    Georges, F.3    Klevit, R.E.4    Waygood, E.B.5
  • 58
    • 70449731054 scopus 로고    scopus 로고
    • Detection and analysis of protein histidine phosphorylation
    • Besant, P. and Attwood, P. (2009) Detection and analysis of protein histidine phosphorylation Mol. Cell. Biochem. 329, 93-106
    • (2009) Mol. Cell. Biochem. , vol.329 , pp. 93-106
    • Besant, P.1    Attwood, P.2
  • 59
  • 60
    • 0031047030 scopus 로고    scopus 로고
    • Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR
    • DOI 10.1021/bi961663p
    • Zhou, H. and Dahlquist, F. W. (1997) Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR Biochemistry 36, 699-710 (Pubitemid 27110950)
    • (1997) Biochemistry , vol.36 , Issue.4 , pp. 699-710
    • Zhou, H.1    Dahlquist, F.W.2
  • 62
    • 0017364905 scopus 로고
    • 31P nuclear magnetic resonance studies on the phosphocarrier protein HPr, phosphohistidines and phosphorylated HPr
    • 31P-nuclear-magnetic-resonance studies on the phosphocarrier protein HPr, phosphohistidines and phosphorylated HPr Eur. J. Biochem. 75, 287-296 (Pubitemid 8080839)
    • (1977) European Journal of Biochemistry , vol.75 , Issue.1 , pp. 287-296
    • Gassner, M.1    Stehlik, D.2    Schrecker, O.3
  • 64
    • 0242438103 scopus 로고    scopus 로고
    • Detection of histidine kinases via a filter-based assay and reverse-phase thin-layer chromatographic phosphoamino acid analysis
    • DOI 10.1016/j.ab.2003.08.035
    • Tan, E. L., Zu, X. L., Yeoh, G. C., Besant, P. G., and Attwood, P. V. (2003) Detection of hisidine kinases via a filter-based assay and reverse-phase thin-layer chromatographic phosphoamino acid analysis Anal. Biochem. 323, 122-126 (Pubitemid 37393365)
    • (2003) Analytical Biochemistry , vol.323 , Issue.1 , pp. 122-126
    • Tan, E.1    Zu, X.L.2    Yeoh, G.C.3    Besant, P.G.4    Attwood, P.V.5
  • 65
    • 0025114462 scopus 로고
    • A filter-based protein kinase assay selective for alkali-stable protein phosphorylation and suitable for acid-labile protein phosphorylation
    • Wei, Y. F. and Matthews, H. R. (1990) A filter-based protein kinase assay selective for alkali-stable protein phosphorylation and suitable for acid-labile protein phosphorylation Anal. Biochem. 190, 188-192 (Pubitemid 20371952)
    • (1990) Analytical Biochemistry , vol.190 , Issue.2 , pp. 188-192
    • Wei, Y.-F.1    Matthews, H.R.2
  • 66
    • 0024830776 scopus 로고
    • Phosphorus-31 nuclear magnetic resonance of phosphoproteins
    • DOI 10.1016/0076-6879(89)77015-4
    • Vogel, H. J. (1989) Phosphorus-31 nuclear magnetic resonance of phosphoproteins Methods Enzymol. 177, 263-282 (Pubitemid 20041580)
    • (1989) Methods in Enzymology , vol.177 , pp. 263-282
    • Vogel, H.J.1
  • 67
    • 78449241676 scopus 로고    scopus 로고
    • Detection and identification of protein-phosphorylation sites in histidines through HNP correlation patterns
    • Himmel, S., Wolff, S., Becker, S., Lee, D., and Griesinger, C. (2010) Detection and identification of protein-phosphorylation sites in histidines through HNP correlation patterns Angew. Chem., Int. Ed. 49, 8971-8974
    • (2010) Angew. Chem., Int. Ed. , vol.49 , pp. 8971-8974
    • Himmel, S.1    Wolff, S.2    Becker, S.3    Lee, D.4    Griesinger, C.5
  • 68
    • 27844600289 scopus 로고    scopus 로고
    • Phosphoproteomics by mass spectrometry and classical protein chemistry approaches
    • DOI 10.1002/mas.20042
    • Salih, E. (2005) Phosphoproteomics by mass spectrometry and classical protein chemistry approaches Mass Spectrom. Rev. 24, 828-846 (Pubitemid 41641700)
    • (2005) Mass Spectrometry Reviews , vol.24 , Issue.6 , pp. 828-846
    • Salih, E.1
  • 69
    • 34250827346 scopus 로고    scopus 로고
    • Identification of Histidine Phosphorylations in Proteins Using Mass Spectrometry and Affinity-Based Techniques
    • DOI 10.1016/S0076-6879(07)23027-7, PII S0076687907230277, Two Component Signaling Systems, Part B
    • Ross, A. R. S. (2007) Identification of histidine phosphorylations in proteins using mass spectrometry and affinity-based techniques Methods Enzymol. 423, 549-572 (Pubitemid 46991115)
    • (2007) Methods in Enzymology , vol.423 , pp. 549-572
    • Ross, A.R.S.1
  • 70
    • 34548392335 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation on a proteome-scale
    • DOI 10.1002/pmic.200700145
    • Collins, M. O., Yu, L., and Choudhary, J. S. (2007) Analysis of protein phosphorylation on a proteome-scale Proteomics 7, 2751-2768 (Pubitemid 47359919)
    • (2007) Proteomics , vol.7 , Issue.16 , pp. 2751-2768
    • Collins, M.O.1    Yu, L.2    Choudhary, J.S.3
  • 71
    • 0037398648 scopus 로고    scopus 로고
    • Selective extraction and characterization of a histidine-phosphorylated peptide using immobilized copper(II) ion affinity chromatography and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • DOI 10.1021/ac026340f
    • Napper, S., Kindrachuk, J., Olson, D., Ambrose, S., Dereniwsky, C., and Ross, A. R. S. (2003) Selective extraction and characterization of a histidine-phosphorylated peptide using immobilized copper(II) ion affinity chromatography and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry Anal. Chem. 75, 1741-1747 (Pubitemid 36512617)
    • (2003) Analytical Chemistry , vol.75 , Issue.7 , pp. 1741-1747
    • Napper, S.1    Kindrachuk, J.2    Olson, D.J.H.3    Ambrose, S.J.4    Dereniwsky, C.5    Ross, A.R.S.6
  • 72
    • 35348988588 scopus 로고    scopus 로고
    • Analysis of histidine phosphorylation using tandem MS and ion-electron reactions
    • DOI 10.1021/ac0707838
    • Kleinnijenhuis, A. J., Kjeldsen, F., Kallipolitis, B., Haselmann, K. F., and Jensen, O. N. (2007) Analysis of histidine phosphorylation using tandem MS and ion-electron reactions Anal. Chem. 79, 7450-7456 (Pubitemid 47606113)
    • (2007) Analytical Chemistry , vol.79 , Issue.19 , pp. 7450-7456
    • Kleinnijenhuis, A.J.1    Kjeldsen, F.2    Kallipolitis, B.3    Haselmann, K.F.4    Jensen, O.N.5
  • 74
    • 34147111725 scopus 로고    scopus 로고
    • Mass spectrometric analysis of protein histidine phosphorylation
    • DOI 10.1007/s00726-007-0493-4, Special Issue: Focus on Excitatory Amino Acids in Epilepsy
    • Zu, X.-L., Besant, P. G., Imhof, A., and Attwood, P. V. (2007) Mass spectrometric analysis of protein histidine phosphorylation Amino Acids 32, 347-357 (Pubitemid 46559589)
    • (2007) Amino Acids , vol.32 , Issue.3 , pp. 347-357
    • Zu, X.-L.1    Besant, P.G.2    Imhof, A.3    Attwood, P.V.4
  • 75
    • 0142244231 scopus 로고    scopus 로고
    • Phosphorylation State-Specific Antibodies: Applications in Investigative and Diagnostic Pathology
    • Mandell, J. W. (2003) Phosphorylation state-specific antibodies applications in investigative and diagnostic pathology Am. J. Pathol. 163, 1687-1698 (Pubitemid 37309997)
    • (2003) American Journal of Pathology , vol.163 , Issue.5 , pp. 1687-1698
    • Mandell, J.W.1
  • 76
    • 0019790941 scopus 로고
    • Phosphotyrosine-containing proteins isolated by affinity chromatography with antibodies to a synthetic hapten
    • Ross, A. H., Baltimore, D., and Eisen, H. N. (1981) Phosphotyrosine- containing proteins isolated by affinity chromatography with antibodies to a synthetic hapten Nature 294, 654-656 (Pubitemid 12213964)
    • (1981) Nature , vol.294 , Issue.5842 , pp. 654-656
    • Ross, A.H.1    Baltimore, D.2    Eisen, H.N.3
  • 77
    • 0020806880 scopus 로고
    • Characterization and use of monoclonal antibodies for isolation of phosphotyrosyl proteins from retrovirus-transformed cells and growth factor-stimulated cells
    • Frackelton, A. R., Ross, A. H., and Eisen, H. N. (1983) Characterization and use of monoclonal antibodies for isolation of phosphotyrosyl proteins from retrovirus-transformed cells and growth factor-stimulated cells Mol. Cell. Biol. 3, 1343-1352
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 1343-1352
    • Frackelton, A.R.1    Ross, A.H.2    Eisen, H.N.3
  • 78
  • 81
    • 0034670497 scopus 로고    scopus 로고
    • Thiophosphorylation of histidine
    • Pirrung, M. C., James, K. D., and Rana, V. S. (2000) Thiophosphorylation of histidine J. Org. Chem. 65, 8448-8453
    • (2000) J. Org. Chem. , vol.65 , pp. 8448-8453
    • Pirrung, M.C.1    James, K.D.2    Rana, V.S.3
  • 84
    • 67650725201 scopus 로고    scopus 로고
    • Protein phosphorylation by semisynthesis: From paper to practice
    • Szewczuk, L. M., Tarrant, M. K., and Cole, P. A. (2009) Protein phosphorylation by semisynthesis: From paper to practice Methods Enzymol. 462, 1-24
    • (2009) Methods Enzymol. , vol.462 , pp. 1-24
    • Szewczuk, L.M.1    Tarrant, M.K.2    Cole, P.A.3
  • 85
    • 84856132981 scopus 로고    scopus 로고
    • Preparation and incorporation into small peptides and combinatorial libraries of phosphohistidine analogs for study of prokaryotic two-component signal transduction systems
    • In, (Fields, G. B. Tam, and J. P. and Barany, G. Eds.) pp, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • Pirrung, M. C., Drabik, S. J., Gothelf, K. V., James, K. D., and Pel, T. (2000) Preparation and incorporation into small peptides and combinatorial libraries of phosphohistidine analogs for study of prokaryotic two-component signal transduction systems. In Peptides for the New Millennium: Proceedings of the 16th American Peptide Symposium, (Fields, G. B., Tam, and J. P., and Barany, G., Eds.) pp 86-88, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (2000) Peptides for the New Millennium: Proceedings of the 16th American Peptide Symposium , pp. 86-88
    • Pirrung, M.C.1    Drabik, S.J.2    Gothelf, K.V.3    James, K.D.4    Pel, T.5
  • 86
    • 78651305248 scopus 로고    scopus 로고
    • Fmoc-chemistry of a stable phosphohistidine analogue
    • McAllister, T. E., Nix, M. G., and Webb, M. E. (2011) Fmoc-chemistry of a stable phosphohistidine analogue Chem. Commun. 47, 1297-1299
    • (2011) Chem. Commun. , vol.47 , pp. 1297-1299
    • McAllister, T.E.1    Nix, M.G.2    Webb, M.E.3


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