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Volumn 422, Issue 2, 2012, Pages 215-229

Role of N-Terminal myristylation in the structure and regulation of cAMP-dependent protein kinase

Author keywords

crystal structure; multiple conformations; N myristylation (N myristoylation); protein kinase A; stabilize

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE;

EID: 84864832746     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.05.021     Document Type: Article
Times cited : (42)

References (62)
  • 1
    • 38149061122 scopus 로고    scopus 로고
    • Signaling through cAMP and cAMP-dependent protein kinase: Diverse strategies for drug design
    • Taylor S.S., Kim C., Cheng C.Y., Brown S.H., Wu J., and Kannan N. Signaling through cAMP and cAMP-dependent protein kinase: diverse strategies for drug design Biochim. Biophys. Acta 1784 2008 16 26
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 16-26
    • Taylor, S.S.1    Kim, C.2    Cheng, C.Y.3    Brown, S.H.4    Wu, J.5    Kannan, N.6
  • 3
    • 0037200890 scopus 로고    scopus 로고
    • Clustered distribution of cAMP-dependent protein kinase regulatory isoform RIα during the development of the rat brain
    • DOI 10.1002/cne.10352
    • Mucignat-Caretta C., and Caretta A. Clustered distribution of cAMP-dependent protein kinase regulatory isoform RI alpha during the development of the rat brain J. Comp. Neurol. 451 2002 324 333 (Pubitemid 34971367)
    • (2002) Journal of Comparative Neurology , vol.451 , Issue.4 , pp. 324-333
    • Mucignat-Caretta, C.1    Caretta, A.2
  • 4
    • 0028323256 scopus 로고
    • Structure and function of cyclic nucleotide-dependent protein kinases
    • Francis S.H., and Corbin J.D. Structure and function of cyclic nucleotide-dependent protein kinases Annu. Rev. Physiol. 56 1994 237 272 (Pubitemid 24111861)
    • (1994) Annual Review of Physiology , vol.56 , pp. 237-272
    • Francis, S.H.1    Corbin, J.D.2
  • 6
    • 0035413602 scopus 로고    scopus 로고
    • Physiological substrates of cAMP-dependent protein kinase
    • DOI 10.1021/cr000236l
    • Shabb J.B. Physiological substrates of cAMP-dependent protein kinase Chem. Rev. 101 2001 2381 2411 (Pubitemid 35373025)
    • (2001) Chemical Reviews , vol.101 , Issue.8 , pp. 2381-2411
    • Shabb, J.B.1
  • 8
    • 0026326821 scopus 로고
    • Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton D.R., Zheng J.H., Ten Eyck L.F., Xuong N.H., Taylor S.S., and Sowadski J.M. Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase Science 253 1991 414 420 (Pubitemid 21917166)
    • (1991) Science , vol.253 , Issue.5018 , pp. 414-420
    • Knighton, D.R.1    Zheng, J.2    Ten Eyck, L.F.3    Xuong, N.-H.4    Taylor, S.S.5    Sowadski, J.M.6
  • 9
    • 0037436388 scopus 로고    scopus 로고
    • Dynamic features of cAMP-dependent protein kinase revealed by apoenzyme crystal structure
    • DOI 10.1016/S0022-2836(02)01446-8
    • Akamine P., Madhusudan, Wu J., Xuong N.H., Ten Eyck L.F., and Taylor S.S. Dynamic features of cAMP-dependent protein kinase revealed by apoenzyme crystal structure J. Mol. Biol. 327 2003 159 171 (Pubitemid 36293309)
    • (2003) Journal of Molecular Biology , vol.327 , Issue.1 , pp. 159-171
    • Akamine, P.1    Madhusudan2    Wu, J.3    Xuong, N.-H.4    Ten Eyck, L.F.5    Taylor, S.S.6
  • 10
    • 27644435575 scopus 로고    scopus 로고
    • Crystal structure of the E230Q mutant of cAMP-dependent protein kinase reveals an unexpected apoenzyme conformation and an extended N-terminal A helix
    • DOI 10.1110/ps.051715205
    • Wu J., Yang J., Kannan N., Madhusudan, Xuong N.H., Ten Eyck L.F., and Taylor S.S. Crystal structure of the E230Q mutant of cAMP-dependent protein kinase reveals an unexpected apoenzyme conformation and an extended N-terminal A helix Protein Sci. 14 2005 2871 2879 (Pubitemid 41577266)
    • (2005) Protein Science , vol.14 , Issue.11 , pp. 2871-2879
    • Wu, J.1    Yang, J.2    Kannan, N.3    Madhusudan4    Xuong, N.-H.5    Ten Eyck, L.F.6    Taylor, S.S.7
  • 11
    • 0001328416 scopus 로고
    • Structure of the mammalian catalytic subunit of cAMP-dependent protein kinase and an inhibitor peptide displays an open conformation
    • Karlsson R., Zheng J., Xuong N., Taylor S.S., and Sowadski J.M. Structure of the mammalian catalytic subunit of cAMP-dependent protein kinase and an inhibitor peptide displays an open conformation Acta Crystallogr., Sect. D: Biol. Crystallogr. 49 1993 381 388
    • (1993) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.49 , pp. 381-388
    • Karlsson, R.1    Zheng, J.2    Xuong, N.3    Taylor, S.S.4    Sowadski, J.M.5
  • 12
    • 0027429591 scopus 로고
    • Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations
    • Zheng J., Knighton D.R., Xuong N.H., Taylor S.S., Sowadski J.M., and Ten Eyck L.F. Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations Protein Sci. 2 1993 1559 1573 (Pubitemid 23294335)
    • (1993) Protein Science , vol.2 , Issue.10 , pp. 1559-1573
    • Zheng, J.1    Knighton, D.R.2    Xuong, N.-H.3    Taylor, S.S.4    Sowadski, J.M.5    Eyck, L.F.T.6
  • 13
    • 0028331080 scopus 로고
    • CAMP-dependent protein kinase: Crystallographic insights into substrate recognition and phosphotransfer
    • Madhusudan, Trafny E.A., Xuong N.H., Adams J.A., Ten Eyck L.F., Taylor S.S., and Sowadski J.M. cAMP-dependent protein kinase: crystallographic insights into substrate recognition and phosphotransfer Protein Sci. 3 1994 176 187 (Pubitemid 24086351)
    • (1994) Protein Science , vol.3 , Issue.2 , pp. 176-187
    • Madhusudan1    Trafny, E.A.2    Xuong, N.-H.3    Adams, J.A.4    Ten Eyck, L.F.5    Taylor, S.S.6    Sowadski, J.M.7
  • 15
    • 0742324523 scopus 로고    scopus 로고
    • Crystal Structure of a cAMP-dependent Protein Kinase Mutant at 1.26 Å: New Insights into the Catalytic Mechanism
    • DOI 10.1016/j.jmb.2003.11.044
    • Yang J., Ten Eyck L.F., Xuong N.H., and Taylor S.S. Crystal structure of a cAMP-dependent protein kinase mutant at 1.26 Å: new insights into the catalytic mechanism J. Mol. Biol. 336 2004 473 487 (Pubitemid 38147641)
    • (2004) Journal of Molecular Biology , vol.336 , Issue.2 , pp. 473-487
    • Yang, J.1    Ten Eyck, L.F.2    Xuong, N.-H.3    Taylor, S.S.4
  • 16
    • 84856232223 scopus 로고    scopus 로고
    • A conserved Glu-Arg salt bridge connects coevolved motifs that define the eukaryotic protein kinase fold
    • Yang J., Wu J., Steichen J.M., Kornev A.P., Deal M.S., and Li S. A conserved Glu-Arg salt bridge connects coevolved motifs that define the eukaryotic protein kinase fold J. Mol. Biol. 415 2012 666 679
    • (2012) J. Mol. Biol. , vol.415 , pp. 666-679
    • Yang, J.1    Wu, J.2    Steichen, J.M.3    Kornev, A.P.4    Deal, M.S.5    Li, S.6
  • 18
    • 0035830403 scopus 로고    scopus 로고
    • Influence of myristoylation, phosphorylation, and deamidation on the structural behavior of the N-terminus of the catalytic subunit of CAMP-dependent protein kinase
    • DOI 10.1021/bi0021277
    • Tholey A., Pipkorn R., Bossemeyer D., Kinzel V., and Reed J. Influence of myristylation, phosphorylation, and deamidation on the structural behavior of the N-terminus of the catalytic subunit of cAMP-dependent protein kinase Biochemistry 40 2001 225 231 (Pubitemid 32052695)
    • (2001) Biochemistry , vol.40 , Issue.1 , pp. 225-231
    • Tholey, A.1    Pipkorn, R.2    Bossemeyer, D.3    Kinzel, V.4    Reed, J.5
  • 19
    • 0035955697 scopus 로고    scopus 로고
    • The biology and enzymology of protein N-myristylation
    • Farazi T.A., Waksman G., and Gordon J.I. The biology and enzymology of protein N-myristylation J. Biol. Chem. 276 2001 39501 39504
    • (2001) J. Biol. Chem. , vol.276 , pp. 39501-39504
    • Farazi, T.A.1    Waksman, G.2    Gordon, J.I.3
  • 20
    • 0039493929 scopus 로고    scopus 로고
    • Targeting of a G alpha subunit (Gi1 alpha) and c-Src tyrosine kinase to caveolae membranes: Clarifying the role of N-myristylation
    • Song K.S., Sargiacomo M., Galbiati F., Parenti M., and Lisanti M.P. Targeting of a G alpha subunit (Gi1 alpha) and c-Src tyrosine kinase to caveolae membranes: clarifying the role of N-myristylation Cell. Mol. Biol. (Noisy-le-grand) 43 1997 293 303
    • (1997) Cell. Mol. Biol. (Noisy-le-grand) , vol.43 , pp. 293-303
    • Song, K.S.1    Sargiacomo, M.2    Galbiati, F.3    Parenti, M.4    Lisanti, M.P.5
  • 21
    • 36349029236 scopus 로고    scopus 로고
    • Myristoylation is required for human immunodeficiency virus type 1 Gag-Gag multimerization in mammalian cells
    • DOI 10.1128/JVI.01280-07
    • Li H., Dou J., Ding L., and Spearman P. Myristylation is required for human immunodeficiency virus type 1 Gag-Gag multimerization in mammalian cells J. Virol. 81 2007 12899 12910 (Pubitemid 350156927)
    • (2007) Journal of Virology , vol.81 , Issue.23 , pp. 12899-12910
    • Li, H.1    Dou, J.2    Ding, L.3    Spearman, P.4
  • 24
    • 77956621729 scopus 로고    scopus 로고
    • Myristylation and membrane binding regulate c-Src stability and kinase activity
    • Patwardhan P., and Resh M.D. Myristylation and membrane binding regulate c-Src stability and kinase activity Mol. Cell. Biol. 30 2010 4094 4107
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 4094-4107
    • Patwardhan, P.1    Resh, M.D.2
  • 25
    • 0028922345 scopus 로고
    • Amino-terminal myristoylation induces cooperative calcium binding to recoverin
    • Ames J.B., Porumb T., Tanaka T., Ikura M., and Stryer L. Amino-terminal myristoylation induces cooperative calcium binding to recoverin J. Biol. Chem. 270 1995 4526 4533
    • (1995) J. Biol. Chem. , vol.270 , pp. 4526-4533
    • Ames, J.B.1    Porumb, T.2    Tanaka, T.3    Ikura, M.4    Stryer, L.5
  • 26
    • 0029135419 scopus 로고
    • Sequestration of the membrane-targeting myristyl group of recoverin in the calcium-free state
    • Tanaka T., Ames J.B., Harvey T.S., Stryer L., and Ikura M. Sequestration of the membrane-targeting myristyl group of recoverin in the calcium-free state Nature 376 1995 444 447
    • (1995) Nature , vol.376 , pp. 444-447
    • Tanaka, T.1    Ames, J.B.2    Harvey, T.S.3    Stryer, L.4    Ikura, M.5
  • 28
    • 0027475668 scopus 로고
    • N-myristylation of the catalytic subunit of cAMP-dependent protein kinase conveys structural stability
    • Yonemoto W., McGlone M.L., and Taylor S.S. N-myristylation of the catalytic subunit of cAMP-dependent protein kinase conveys structural stability J. Biol. Chem. 268 1993 2348 2352 (Pubitemid 23057850)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.4 , pp. 2348-2352
    • Yonemoto, W.1    McGlone, M.L.2    Taylor, S.S.3
  • 31
    • 24944532072 scopus 로고    scopus 로고
    • Biological significance of isoaspartate and its repair system
    • DOI 10.1248/bpb.28.1590
    • Shimizu T., Matsuoka Y., and Shirasawa T. Biological significance of isoaspartate and its repair system Biol. Pharm. Bull. 28 2005 1590 1596 (Pubitemid 41324114)
    • (2005) Biological and Pharmaceutical Bulletin , vol.28 , Issue.9 , pp. 1590-1596
    • Shimizu, T.1    Matsuoka, Y.2    Shirasawa, T.3
  • 32
    • 0242592107 scopus 로고    scopus 로고
    • Structural Elements Required for Deamidation of RhoA by Cytotoxic Necrotizing Factor 1
    • DOI 10.1021/bi035123l
    • Buetow L., and Ghosh P. Structural elements required for deamidation of RhoA by cytotoxic necrotizing factor 1 Biochemistry 42 2003 12784 12791 (Pubitemid 37385809)
    • (2003) Biochemistry , vol.42 , Issue.44 , pp. 12784-12791
    • Buetow, L.1    Ghosh, P.2
  • 33
    • 77956296853 scopus 로고    scopus 로고
    • Glutamine deamidation and dysfunction of ubiquitin/NEDD8 induced by a bacterial effector family
    • Cui J., Yao Q., Li S., Ding X., Lu Q., and Mao H. Glutamine deamidation and dysfunction of ubiquitin/NEDD8 induced by a bacterial effector family Science 329 2010 1215 1218
    • (2010) Science , vol.329 , pp. 1215-1218
    • Cui, J.1    Yao, Q.2    Li, S.3    Ding, X.4    Lu, Q.5    Mao, H.6
  • 34
    • 0031935718 scopus 로고    scopus 로고
    • A conserved deamidation site at Asn 2 in the catalytic subunit of mammalian cAMP-dependent protein kinase detected by capillary LC-MS and tandem mass spectrometry
    • Jedrzejewski P.T., Girod A., Tholey A., Konig N., Thullner S., Kinzel V., and Bossemeyer D. A conserved deamidation site at Asn 2 in the catalytic subunit of mammalian cAMP-dependent protein kinase detected by capillary LC-MS and tandem mass spectrometry Protein Sci. 7 1998 457 469 (Pubitemid 28092868)
    • (1998) Protein Science , vol.7 , Issue.2 , pp. 457-469
    • Jedrzejewski, P.T.1    Girod, A.2    Tholey, A.3    Konig, N.4    Thullner, S.5    Kinzel, V.6    Bossemeyer, D.7
  • 35
    • 0034695932 scopus 로고    scopus 로고
    • Intracellular distribution of mammalian protein kinase A catalytic subunit altered by conserved Asn2 deamidation
    • Pepperkok R., Hotz-Wagenblatt A., Konig N., Girod A., Bossemeyer D., and Kinzel V. Intracellular distribution of mammalian protein kinase A catalytic subunit altered by conserved Asn2 deamidation J. Cell Biol. 148 2000 715 726
    • (2000) J. Cell Biol. , vol.148 , pp. 715-726
    • Pepperkok, R.1    Hotz-Wagenblatt, A.2    Konig, N.3    Girod, A.4    Bossemeyer, D.5    Kinzel, V.6
  • 36
    • 0027199055 scopus 로고
    • Identification of phosphorylation sites in the recombinant catalytic subunit of cAMP-dependent protein kinase
    • Yonemoto W., Garrod S.M., Bell S.M., and Taylor S.S. Identification of phosphorylation sites in the recombinant catalytic subunit of cAMP-dependent protein kinase J. Biol. Chem. 268 1993 18626 18632 (Pubitemid 23273801)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.25 , pp. 18626-18632
    • Yonemoto, W.1    Garrod, S.M.2    Bell, S.M.3    Taylor, S.S.4
  • 37
    • 0026461124 scopus 로고
    • Autophosphorylation of the catalytic subunit of cAMP-dependent protein kinase
    • Toner-Webb J., van Patten S.M., Walsh D.A., and Taylor S.S. Autophosphorylation of the catalytic subunit of cAMP-dependent protein kinase J. Biol. Chem. 267 1992 25174 25180
    • (1992) J. Biol. Chem. , vol.267 , pp. 25174-25180
    • Toner-Webb, J.1    Van Patten, S.M.2    Walsh, D.A.3    Taylor, S.S.4
  • 38
    • 79955558165 scopus 로고    scopus 로고
    • Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy
    • Masterson L.R., Shi L., Metcalfe E., Gao J., Taylor S.S., and Veglia G. Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy Proc. Natl Acad. Sci. USA 108 2011 6969 6974
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 6969-6974
    • Masterson, L.R.1    Shi, L.2    Metcalfe, E.3    Gao, J.4    Taylor, S.S.5    Veglia, G.6
  • 39
    • 0028898390 scopus 로고
    • Phosphorylation modulates catalytic function and regulation in the cAMP-dependent protein kinase
    • Adams J.A., McGlone M.L., Gibson R., and Taylor S.S. Phosphorylation modulates catalytic function and regulation in the cAMP-dependent protein kinase Biochemistry 34 1995 2447 2454
    • (1995) Biochemistry , vol.34 , pp. 2447-2454
    • Adams, J.A.1    McGlone, M.L.2    Gibson, R.3    Taylor, S.S.4
  • 41
    • 65249108791 scopus 로고    scopus 로고
    • Contribution of non-catalytic core residues to activity and regulation in protein kinase A
    • Yang J., Kennedy E.J., Wu J., Deal M.S., Pennypacker J., Ghosh G., and Taylor S.S. Contribution of non-catalytic core residues to activity and regulation in protein kinase A J. Biol. Chem. 284 2009 6241 6248
    • (2009) J. Biol. Chem. , vol.284 , pp. 6241-6248
    • Yang, J.1    Kennedy, E.J.2    Wu, J.3    Deal, M.S.4    Pennypacker, J.5    Ghosh, G.6    Taylor, S.S.7
  • 43
    • 2942720799 scopus 로고    scopus 로고
    • The typically disordered N-terminus of PKA can fold as a helix and project the myristoylation site into solution
    • DOI 10.1021/bi0362525
    • Breitenlechner C., Engh R.A., Huber R., Kinzel V., Bossemeyer D., and Gassel M. The typically disordered N-terminus of PKA can fold as a helix and project the myristoylation site into solution Biochemistry 43 2004 7743 7749 (Pubitemid 38787682)
    • (2004) Biochemistry , vol.43 , Issue.24 , pp. 7743-7749
    • Breitenlechner, C.1    Engh, R.A.2    Huber, R.3    Kinzel, V.4    Bossemeyer, D.5    Gassel, M.6
  • 46
    • 35748956109 scopus 로고    scopus 로고
    • Stabilizing Function for Myristoyl Group Revealed by the Crystal Structure of a Neuronal Calcium Sensor, Guanylate Cyclase-Activating Protein 1
    • DOI 10.1016/j.str.2007.09.013, PII S0969212607003395
    • Stephen R., Bereta G., Golczak M., Palczewski K., and Sousa M.C. Stabilizing function for myristyl group revealed by the crystal structure of a neuronal calcium sensor, guanylatecyclase-activating protein 1 Structure 15 2007 1392 1402 (Pubitemid 350051925)
    • (2007) Structure , vol.15 , Issue.11 , pp. 1392-1402
    • Stephen, R.1    Bereta, G.2    Golczak, M.3    Palczewski, K.4    Sousa, M.C.5
  • 48
    • 70350365399 scopus 로고    scopus 로고
    • N-myristylated c-Abl tyrosine kinase localizes to the endoplasmic reticulum upon binding to an allosteric inhibitor
    • Choi Y., Seeliger M.A., Panjarian S.B., Kim H., Deng X., and Sim T. N-myristylated c-Abl tyrosine kinase localizes to the endoplasmic reticulum upon binding to an allosteric inhibitor J. Biol. Chem. 284 2009 29005 29014
    • (2009) J. Biol. Chem. , vol.284 , pp. 29005-29014
    • Choi, Y.1    Seeliger, M.A.2    Panjarian, S.B.3    Kim, H.4    Deng, X.5    Sim, T.6
  • 49
    • 79951816826 scopus 로고    scopus 로고
    • Discovery and characterization of a cell-permeable, small-molecule c-Abl kinase activator that binds to the myristyl binding site
    • Yang J., Campobasso N., Biju M.P., Fisher K., Pan X.Q., and Cottom J. Discovery and characterization of a cell-permeable, small-molecule c-Abl kinase activator that binds to the myristyl binding site Chem. Biol. 18 2011 177 186
    • (2011) Chem. Biol. , vol.18 , pp. 177-186
    • Yang, J.1    Campobasso, N.2    Biju, M.P.3    Fisher, K.4    Pan, X.Q.5    Cottom, J.6
  • 51
    • 84860369376 scopus 로고    scopus 로고
    • Structural basis for the regulation of protein kinase A by activation loop phosphorylation
    • Steichen J.M., Kuchinskas M., Keshwani M.M., Yang J., Adams J.A., and Taylor S.S. Structural basis for the regulation of protein kinase A by activation loop phosphorylation J. Biol. Chem. 287 2012 14672 14680
    • (2012) J. Biol. Chem. , vol.287 , pp. 14672-14680
    • Steichen, J.M.1    Kuchinskas, M.2    Keshwani, M.M.3    Yang, J.4    Adams, J.A.5    Taylor, S.S.6
  • 52
    • 0027504169 scopus 로고
    • Divalent metal ions influence catalysis and active-site accessibility in the cAMP-dependent protein kinase
    • Adams J.A., and Taylor S.S. Divalent metal ions influence catalysis and active-site accessibility in the cAMP-dependent protein kinase Protein Sci. 2 1993 2177 2186 (Pubitemid 23354720)
    • (1993) Protein Science , vol.2 , Issue.12 , pp. 2177-2186
    • Adams, J.A.1    Taylor, S.S.2
  • 53
    • 84861483734 scopus 로고    scopus 로고
    • Structure and function of the human sperm-specific isoform of protein kinase A (PKA) catalytic subunit Calpha2
    • Hereng T.H., Backe P.H., Kahmann J., Scheich C., Bjoras M., Skalhegg B.S., and Rosendal K.R. Structure and function of the human sperm-specific isoform of protein kinase A (PKA) catalytic subunit Calpha2 J. Struct. Biol. 178 2012 300 310
    • (2012) J. Struct. Biol. , vol.178 , pp. 300-310
    • Hereng, T.H.1    Backe, P.H.2    Kahmann, J.3    Scheich, C.4    Bjoras, M.5    Skalhegg, B.S.6    Rosendal, K.R.7
  • 54
    • 0027527937 scopus 로고
    • Expression of the catalytic subunit of cAMP-dependent protein kinase in Escherichia coli: Multiple isozymes reflect different phosphorylation states
    • Herberg F.W., Bell S.M., and Taylor S.S. Expression of the catalytic subunit of cAMP-dependent protein kinase in Escherichia coli: multiple isozymes reflect different phosphorylation states Protein Eng. 6 1993 771 777 (Pubitemid 23293207)
    • (1993) Protein Engineering , vol.6 , Issue.7 , pp. 771-777
    • Herberg, F.W.1    Bell, S.M.2    Taylor, S.S.3
  • 56
    • 0031568921 scopus 로고    scopus 로고
    • Recombinant strategies for rapid purification of catalytic subunits of cAMP-dependent protein kinase
    • DOI 10.1006/abio.1996.9952
    • Hemmer W., McGlone M., and Taylor S.S. Recombinant strategies for rapid purification of catalytic subunits of cAMP-dependent protein kinase Anal. Biochem. 245 1997 115 122 (Pubitemid 27082238)
    • (1997) Analytical Biochemistry , vol.245 , Issue.2 , pp. 115-122
    • Hemmer, W.1    McGlone, M.2    Taylor, S.S.3
  • 59
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, No. 4
    • Collaborative Computational Project, No. 4 The CCP4 suite: programs for protein crystallography Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 61
    • 0020478357 scopus 로고
    • Adenosine cyclic 3′,5′-monophosphate dependent protein kinase: Kinetic mechanism for the bovine skeletal muscle catalytic subunit
    • Cook P.F., Neville M.E. Jr, Vrana K.E., Hartl F.T., and Roskoski R. Jr Adenosine cyclic 3′,5′-monophosphate dependent protein kinase: kinetic mechanism for the bovine skeletal muscle catalytic subunit Biochemistry 21 1982 5794 5799
    • (1982) Biochemistry , vol.21 , pp. 5794-5799
    • Cook, P.F.1    Neville, Jr.M.E.2    Vrana, K.E.3    Hartl, F.T.4    Roskoski, Jr.R.5


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