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Volumn 162, Issue 1, 2015, Pages 198-210

Monoclonal 1- and 3-Phosphohistidine Antibodies: New Tools to Study Histidine Phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

HISTIDINE; IMMUNOGLOBULIN G; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 1 PHOSPHOHISTIDINE; MONOCLONAL ANTIBODY 3 PHOSPHOHISTIDINE; PHOSPHOGLYCERATE MUTASE; PHOSPHOTYROSINE; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG; PEPTIDE;

EID: 84934293234     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2015.05.046     Document Type: Article
Times cited : (160)

References (36)
  • 2
    • 84856279848 scopus 로고    scopus 로고
    • Histone H4 histidine phosphorylation: Kinases, phosphatases, liver regeneration and cancer
    • P.G. Besant, and P.V. Attwood Histone H4 histidine phosphorylation: kinases, phosphatases, liver regeneration and cancer Biochem. Soc. Trans. 40 2012 290 293
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 290-293
    • Besant, P.G.1    Attwood, P.V.2
  • 4
    • 0000183819 scopus 로고
    • Identification of phosphohistidine in digests from a probable intermediate of oxidative phosphorylation
    • P.D. Boyer, M. Deluca, K.E. Ebner, D.E. Hultquist, and J.B. Peter Identification of phosphohistidine in digests from a probable intermediate of oxidative phosphorylation J. Biol. Chem. 237 1962 PC3306 PC3308
    • (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
  • 6
    • 77957284437 scopus 로고    scopus 로고
    • Nucleoside diphosphate kinase Nm23-H1 regulates chromosomal stability by activating the GTPase dynamin during cytokinesis
    • A.R. Conery, S. Sever, and E. Harlow Nucleoside diphosphate kinase Nm23-H1 regulates chromosomal stability by activating the GTPase dynamin during cytokinesis Proc. Natl. Acad. Sci. USA 107 2010 15461 15466
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 15461-15466
    • Conery, A.R.1    Sever, S.2    Harlow, E.3
  • 7
    • 0020806880 scopus 로고
    • Characterization and use of monoclonal antibodies for isolation of phosphotyrosyl proteins from retrovirus-transformed cells and growth factor-stimulated cells
    • A.R. Frackelton Jr., A.H. Ross, and H.N. Eisen Characterization and use of monoclonal antibodies for isolation of phosphotyrosyl proteins from retrovirus-transformed cells and growth factor-stimulated cells Mol. Cell. Biol. 3 1983 1343 1352
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 1343-1352
    • Frackelton, Jr.A.R.1    Ross, A.H.2    Eisen, H.N.3
  • 9
    • 0034705332 scopus 로고    scopus 로고
    • Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase
    • M.E. Fraser, M.N.G. James, W.A. Bridger, and W.T. Wolodko Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase J. Mol. Biol. 299 2000 1325 1339
    • (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
  • 12
    • 84880561371 scopus 로고    scopus 로고
    • Attempting to rewrite history: Challenges with the analysis of histidine-phosphorylated peptides
    • M.B. Gonzalez-Sanchez, F. Lanucara, M. Helm, and C.E. Eyers Attempting to rewrite history: challenges with the analysis of histidine-phosphorylated peptides Biochem. Soc. Trans. 41 2013 1089 1095
    • (2013) Biochem. Soc. Trans. , vol.41 , pp. 1089-1095
    • Gonzalez-Sanchez, M.B.1    Lanucara, F.2    Helm, M.3    Eyers, C.E.4
  • 13
    • 0033766254 scopus 로고    scopus 로고
    • Expression of a catalytically inactive H118Y mutant of nm23-H2 suppresses the metastatic potential of line IV Cl 1 human melanoma cells
    • C.V. Hamby, R. Abbi, N. Prasad, C. Stauffer, J. Thomson, C.E. Mendola, V. Sidorov, and J.M. Backer Expression of a catalytically inactive H118Y mutant of nm23-H2 suppresses the metastatic potential of line IV Cl 1 human melanoma cells Int. J. Cancer 88 2000 547 553
    • (2000) Int. J. Cancer , vol.88 , pp. 547-553
    • Hamby, C.V.1    Abbi, R.2    Prasad, N.3    Stauffer, C.4    Thomson, J.5    Mendola, C.E.6    Sidorov, V.7    Backer, J.M.8
  • 15
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • W. Huang, B.T. Sherman, and R.A. Lempicki Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources Nat. Protoc. 4 2009 44 57
    • (2009) Nat. Protoc. , vol.4 , pp. 44-57
    • Huang, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 16
    • 0000109995 scopus 로고
    • Transforming gene product of Rous sarcoma virus phosphorylates tyrosine
    • T. Hunter, and B.M. Sefton Transforming gene product of Rous sarcoma virus phosphorylates tyrosine Proc. Natl. Acad. Sci. USA 77 1980 1311 1315
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1311-1315
    • Hunter, T.1    Sefton, B.M.2
  • 17
    • 0021894130 scopus 로고
    • Overexpressed pp60c-src can induce focus formation without complete transformation of NIH 3T3 cells
    • P.J. Johnson, P.M. Coussens, A.V. Danko, and D. Shalloway Overexpressed pp60c-src can induce focus formation without complete transformation of NIH 3T3 cells Mol. Cell. Biol. 5 1985 1073 1083
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 1073-1083
    • Johnson, P.J.1    Coussens, P.M.2    Danko, A.V.3    Shalloway, D.4
  • 18
    • 84856158810 scopus 로고    scopus 로고
    • Chasing phosphohistidine, an elusive sibling in the phosphoamino acid family
    • J.M. Kee, and T.W. Muir Chasing phosphohistidine, an elusive sibling in the phosphoamino acid family ACS Chem. Biol. 7 2012 44 51
    • (2012) ACS Chem. Biol. , vol.7 , pp. 44-51
    • Kee, J.M.1    Muir, T.W.2
  • 20
    • 84879416831 scopus 로고    scopus 로고
    • A pan-specific antibody for direct detection of protein histidine phosphorylation
    • J.M. Kee, R.C. Oslund, D.H. Perlman, and T.W. Muir A pan-specific antibody for direct detection of protein histidine phosphorylation Nat. Chem. Biol. 9 2013 416 421
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 416-421
    • Kee, J.M.1    Oslund, R.C.2    Perlman, D.H.3    Muir, T.W.4
  • 21
    • 84921310093 scopus 로고    scopus 로고
    • A second-generation phosphohistidine analog for production of phosphohistidine antibodies
    • J.M. Kee, R.C. Oslund, A.D. Couvillon, and T.W. Muir A second-generation phosphohistidine analog for production of phosphohistidine antibodies Org. Lett. 17 2015 187 189
    • (2015) Org. Lett. , vol.17 , pp. 187-189
    • Kee, J.M.1    Oslund, R.C.2    Couvillon, A.D.3    Muir, T.W.4
  • 23
    • 0028829688 scopus 로고
    • Protein kinases and phosphatases that act on histidine, lysine, or arginine residues in eukaryotic proteins: A possible regulator of the MAPK cascade
    • H. Matthews Protein kinases and phosphatases that act on histidine, lysine, or arginine residues in eukaryotic proteins: a possible regulator of the MAPK cascade Pharmacol. Ther. 67 1995 232 350
    • (1995) Pharmacol. Ther. , vol.67 , pp. 232-350
    • Matthews, H.1
  • 24
    • 84860711440 scopus 로고    scopus 로고
    • Triazole phosphohistidine analogues compatible with the Fmoc-strategy
    • T.E. McAllister, and M.E. Webb Triazole phosphohistidine analogues compatible with the Fmoc-strategy Org. Biomol. Chem. 10 2012 4043 4049
    • (2012) Org. Biomol. Chem. , vol.10 , pp. 4043-4049
    • McAllister, T.E.1    Webb, M.E.2
  • 25
    • 78651305248 scopus 로고    scopus 로고
    • Fmoc-chemistry of a stable phosphohistidine analogue
    • T.E. McAllister, M.G. Nix, and M.E. Webb Fmoc-chemistry of a stable phosphohistidine analogue Chem. Commun. (Camb.) 47 2011 1297 1299
    • (2011) Chem. Commun. (Camb.) , vol.47 , pp. 1297-1299
    • McAllister, T.E.1    Nix, M.G.2    Webb, M.E.3
  • 26
    • 0028091859 scopus 로고
    • Refined X-ray structure of Dictyostelium discoideum nucleoside diphosphate kinase at 1.8 A resolution
    • S. Moréra, G. LeBras, I. Lascu, M.L. Lacornbe, M. Véron, and J. Janin Refined X-ray structure of Dictyostelium discoideum nucleoside diphosphate kinase at 1.8 A resolution J. Mol. Biol. 243 1994 873 890
    • (1994) J. Mol. Biol. , vol.243 , pp. 873-890
    • Moréra, S.1    Lebras, G.2    Lascu, I.3    Lacornbe, M.L.4    Véron, M.5    Janin, J.6
  • 27
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • J.V. Olsen, B. Blagoev, F. Gnad, B. Macek, C. Kumar, P. Mortensen, and M. Mann Global, in vivo, and site-specific phosphorylation dynamics in signaling networks Cell 127 2006 635 648
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 28
    • 0024295995 scopus 로고
    • Phosphohistidine is found in basic nuclear proteins of Physarum polycephalum
    • K.H. Pesis, Y. Wei, M. Lewis, and H.R. Matthews Phosphohistidine is found in basic nuclear proteins of Physarum polycephalum FEBS Lett. 239 1988 151 154
    • (1988) FEBS Lett. , vol.239 , pp. 151-154
    • Pesis, K.H.1    Wei, Y.2    Lewis, M.3    Matthews, H.R.4
  • 31
  • 32
    • 84874983252 scopus 로고    scopus 로고
    • RGS19 inhibits Ras signaling through Nm23H1/2-mediated phosphorylation of the kinase suppressor of Ras
    • P.H. Tso, Y. Wang, L.Y. Yung, Y. Tong, M.M. Lee, and Y.H. Wong RGS19 inhibits Ras signaling through Nm23H1/2-mediated phosphorylation of the kinase suppressor of Ras Cell. Signal. 25 2013 1064 1074
    • (2013) Cell. Signal. , vol.25 , pp. 1064-1074
    • Tso, P.H.1    Wang, Y.2    Yung, L.Y.3    Tong, Y.4    Lee, M.M.5    Wong, Y.H.6
  • 34
    • 0029101744 scopus 로고
    • Phosphorylation of ATP-citrate lyase by nucleoside diphosphate kinase
    • P.D. Wagner, and N.D. Vu Phosphorylation of ATP-citrate lyase by nucleoside diphosphate kinase J. Biol. Chem. 270 1995 21758 21764
    • (1995) J. Biol. Chem. , vol.270 , pp. 21758-21764
    • Wagner, P.D.1    Vu, N.D.2
  • 35
    • 79952202394 scopus 로고    scopus 로고
    • Reversible histidine phosphorylation in mammalian cells: A teeter-totter formed by nucleoside diphosphate kinase and protein histidine phosphatase 1
    • T. Wieland, H.-J. Hippe, K. Ludwig, X.-B. Zhou, M. Korth, and S. Klumpp Reversible histidine phosphorylation in mammalian cells: a teeter-totter formed by nucleoside diphosphate kinase and protein histidine phosphatase 1 Methods Enzymol. 471 2010 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
  • 36
    • 58849167699 scopus 로고    scopus 로고
    • The isolation and characterization of murine macrophages
    • Unit 14.1
    • X. Zhang, R. Goncalves, and D.M. Mosser The isolation and characterization of murine macrophages Curr. Protoc. Immunol. Chapter 14 2008 Unit 14.1
    • (2008) Curr. Protoc. Immunol. , vol.14
    • Zhang, X.1    Goncalves, R.2    Mosser, D.M.3


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