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Volumn 4, Issue 11, 2007, Pages 957-962

The reverse in-gel kinase assay to profile physiological kinase substrates

Author keywords

[No Author keywords available]

Indexed keywords

CASEIN KINASE II; CASEIN KINASE IIALPHA; CYCLIC AMP DEPENDENT PROTEIN KINASE; PHOSPHOTRANSFERASE; POLYACRYLAMIDE GEL; UNCLASSIFIED DRUG;

EID: 35748949573     PISSN: 15487091     EISSN: 15491676     Source Type: Journal    
DOI: 10.1038/nmeth1106     Document Type: Article
Times cited : (14)

References (27)
  • 1
    • 18744415995 scopus 로고    scopus 로고
    • Kinomics: Methods for deciphering the kinome
    • Johnson, S.A. & Hunter, T. Kinomics: Methods for deciphering the kinome. Nat. Methods 2, 17-25 (2005).
    • (2005) Nat. Methods , vol.2 , pp. 17-25
    • Johnson, S.A.1    Hunter, T.2
  • 3
    • 0034797512 scopus 로고    scopus 로고
    • The role of protein phosphorylation in human health and disease. The Sir Hans Krebs Medal Lecture
    • Cohen, P. The role of protein phosphorylation in human health and disease. The Sir Hans Krebs Medal Lecture. Eur. J. Biochem. 268 5001-5010 (2001).
    • (2001) Eur. J. Biochem , vol.268 , pp. 5001-5010
    • Cohen, P.1
  • 4
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases-the major drug targets of the twenty-first century?
    • Cohen, P. Protein kinases-the major drug targets of the twenty-first century? Nat. Rev. Drug Discov. 1, 309-315 (2002).
    • (2002) Nat. Rev. Drug Discov , vol.1 , pp. 309-315
    • Cohen, P.1
  • 5
    • 2342573665 scopus 로고    scopus 로고
    • Identifying protein kinase substrates: Hunting for the organ-grinder's monkeys
    • Berwick, D.C. & Tavare, J.M. Identifying protein kinase substrates: hunting for the organ-grinder's monkeys. Trends Biochem. Sci. 29, 227-232 (2004).
    • (2004) Trends Biochem. Sci , vol.29 , pp. 227-232
    • Berwick, D.C.1    Tavare, J.M.2
  • 6
    • 0035881737 scopus 로고    scopus 로고
    • A novel method to identify protein kinase substrates: EEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta
    • Knebel, A., Morrice, N. & Cohen, P. A novel method to identify protein kinase substrates: EEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta. EMBO J. 20, 4360-4369 (2001).
    • (2001) EMBO J , vol.20 , pp. 4360-4369
    • Knebel, A.1    Morrice, N.2    Cohen, P.3
  • 7
    • 30044441052 scopus 로고    scopus 로고
    • KESTREL: A powerful method for identifying the physiological substrates of protein kinases
    • Cohen, P. & Knebel, A. KESTREL: A powerful method for identifying the physiological substrates of protein kinases. Biochem. J. 393 1-6 (2006).
    • (2006) Biochem. J , vol.393 , pp. 1-6
    • Cohen, P.1    Knebel, A.2
  • 8
    • 0036008093 scopus 로고    scopus 로고
    • A chemical genetic screen for direct v-Src substrates reveals ordered assembly of a retrograde signaling pathway
    • Shah, K. & Shokat, K.M. A chemical genetic screen for direct v-Src substrates reveals ordered assembly of a retrograde signaling pathway. Chem. Biol. 9, 35-47 (2002).
    • (2002) Chem. Biol , vol.9 , pp. 35-47
    • Shah, K.1    Shokat, K.M.2
  • 9
    • 0022596409 scopus 로고
    • Detection of protein kinase activity in sodium dodecyl sulfate-polyacrylamide gels
    • Geahlen, R.L., Anostario, M. Jr., Low, P.S. & Harrison, M.L. Detection of protein kinase activity in sodium dodecyl sulfate-polyacrylamide gels. Anal. Biochem. 153, 151-158 (1986).
    • (1986) Anal. Biochem , vol.153 , pp. 151-158
    • Geahlen, R.L.1    Anostario Jr., M.2    Low, P.S.3    Harrison, M.L.4
  • 10
    • 0037044198 scopus 로고    scopus 로고
    • In-gel kinase assay as a method to identify kinase substrates
    • Wooten, M.W. In-gel kinase assay as a method to identify kinase substrates. Sci. STKE 2002, PL15 (2002).
    • (2002) Sci. STKE , vol.2002
    • Wooten, M.W.1
  • 11
    • 0001010573 scopus 로고
    • The enzymatic phosphorylation of proteins
    • Burnett, G. & Kennedy, E.P. The enzymatic phosphorylation of proteins. J. Biol. Chem. 211, 969-980 (1954).
    • (1954) J. Biol. Chem , vol.211 , pp. 969-980
    • Burnett, G.1    Kennedy, E.P.2
  • 12
    • 0018847558 scopus 로고
    • The LNCaP cell line-a new model for studies on human prostatic carcinoma
    • Horoszewicz, J.S. et al. The LNCaP cell line-a new model for studies on human prostatic carcinoma. Prog. Clin. Biol. Res. 37 115-132 (1980).
    • (1980) Prog. Clin. Biol. Res , vol.37 , pp. 115-132
    • Horoszewicz, J.S.1
  • 13
    • 0035413602 scopus 로고    scopus 로고
    • Physiological substrates of cAMP-dependent protein kinase
    • Shabb, J.B. Physiological substrates of cAMP-dependent protein kinase. Chem. Rev. 101, 2381-2411 (2001).
    • (2001) Chem. Rev , vol.101 , pp. 2381-2411
    • Shabb, J.B.1
  • 14
    • 0037269847 scopus 로고    scopus 로고
    • Protein kinase CK2: Structure, regulation and role in cellular decisions of life and death
    • Litchfield, D.W. Protein kinase CK2: Structure, regulation and role in cellular decisions of life and death. Biochem. J. 369, 1-15 (2003).
    • (2003) Biochem. J , vol.369 , pp. 1-15
    • Litchfield, D.W.1
  • 15
    • 0024970557 scopus 로고
    • Discovery of a protein phosphatase activity encoded in the genome of bacteriophage lambda. Probable identity with open reading frame 221
    • Cohen, P.T. & Cohen, P. Discovery of a protein phosphatase activity encoded in the genome of bacteriophage lambda. Probable identity with open reading frame 221. Biochem. J. 260, 931-934 (1989).
    • (1989) Biochem. J , vol.260 , pp. 931-934
    • Cohen, P.T.1    Cohen, P.2
  • 16
    • 0035805108 scopus 로고    scopus 로고
    • Samo, S. et al. Selectivity of 4,5,6,7-tetrabromobenzotriazole, an ATP site-directed inhibitor of protein kinase CK2 ('casein kinase-2'). FEBS Lett. 496, 44-48 (2001).
    • Samo, S. et al. Selectivity of 4,5,6,7-tetrabromobenzotriazole, an ATP site-directed inhibitor of protein kinase CK2 ('casein kinase-2'). FEBS Lett. 496, 44-48 (2001).
  • 17
    • 0032408268 scopus 로고    scopus 로고
    • Protein kinase CK2 activities in human prostatic and seminal-vesicle secretions and seminal plasma
    • Wilson, M.J. et al. Protein kinase CK2 activities in human prostatic and seminal-vesicle secretions and seminal plasma. J. Androl. 19, 754-760 (1998).
    • (1998) J. Androl , vol.19 , pp. 754-760
    • Wilson, M.J.1
  • 18
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • Meggio, F. & Pinna, L.A. One-thousand-and-one substrates of protein kinase CK2? FASEB J. 17, 349-368 (2003).
    • (2003) FASEB J , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 19
    • 3142677813 scopus 로고    scopus 로고
    • Regulation of cytosolic prostaglandin E synthase by phosphorylation
    • Kobayashi, T. et al. Regulation of cytosolic prostaglandin E synthase by phosphorylation. Biochem. J. 381, 59-69 (2004).
    • (2004) Biochem. J , vol.381 , pp. 59-69
    • Kobayashi, T.1
  • 20
    • 33748374486 scopus 로고    scopus 로고
    • Biochemical characterization of suramin as a selective inhibitor for the PKA-mediated phosphorylation of HBV core protein in vitro
    • Okabe, M., Enomoto, M., Maeda, H., Kuroki, K. & Ohtsuki, K. Biochemical characterization of suramin as a selective inhibitor for the PKA-mediated phosphorylation of HBV core protein in vitro. Biol. Pharm. Bull. 29, 1810-1814 (2006).
    • (2006) Biol. Pharm. Bull , vol.29 , pp. 1810-1814
    • Okabe, M.1    Enomoto, M.2    Maeda, H.3    Kuroki, K.4    Ohtsuki, K.5
  • 21
    • 0033199392 scopus 로고    scopus 로고
    • cAMP induces co-translational modification of proteins in IPC-81 cells
    • Hovland, R., Doskeland, A.P., Eikhom, T.S., Robaye, B. & Doskeland, S.O. cAMP induces co-translational modification of proteins in IPC-81 cells. Biochem. J. 342, 369-377 (1999).
    • (1999) Biochem. J , vol.342 , pp. 369-377
    • Hovland, R.1    Doskeland, A.P.2    Eikhom, T.S.3    Robaye, B.4    Doskeland, S.O.5
  • 22
    • 0033768106 scopus 로고    scopus 로고
    • Analysis of yeast protein kinases using protein chips
    • Zhu, H. et al. Analysis of yeast protein kinases using protein chips. Nat. Genet. 26, 283-289 (2000).
    • (2000) Nat. Genet , vol.26 , pp. 283-289
    • Zhu, H.1
  • 24
    • 33745899048 scopus 로고    scopus 로고
    • Alternative splicing: New insights from global analyses
    • Blencowe, B.J. Alternative splicing: New insights from global analyses. Cell 126, 37-47 (2006).
    • (2006) Cell , vol.126 , pp. 37-47
    • Blencowe, B.J.1
  • 25
    • 26444456180 scopus 로고    scopus 로고
    • Application of mass spectrometry in proteomics
    • Guerrera, I.C. & Kleiner, O. Application of mass spectrometry in proteomics. Biosci. Rep. 25, 71-93 (2005).
    • (2005) Biosci. Rep , vol.25 , pp. 71-93
    • Guerrera, I.C.1    Kleiner, O.2
  • 26
    • 23944477376 scopus 로고    scopus 로고
    • Searching for biomarkers of Aurora-A kinase activity: Identification of in vitro substrates through a modified KESTREL approach
    • Troiani, S. et al. Searching for biomarkers of Aurora-A kinase activity: Identification of in vitro substrates through a modified KESTREL approach. J. Proteome Res. 4, 1296-1303 (2005).
    • (2005) J. Proteome Res , vol.4 , pp. 1296-1303
    • Troiani, S.1
  • 27
    • 0029049102 scopus 로고
    • An activity gel assay detects a single, catalytically active histone acetyltransferase subunit in Tetrahymena macronuclei
    • Brownell, J.E. & Allis, C.D. An activity gel assay detects a single, catalytically active histone acetyltransferase subunit in Tetrahymena macronuclei. Proc. Natl. Acad. Sci. USA 92, 6364-6368 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6364-6368
    • Brownell, J.E.1    Allis, C.D.2


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