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Volumn , Issue , 2012, Pages 267-298

PKA: Prototyp e for dynamic signaling in time and space

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EID: 84939876894     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/b12676     Document Type: Chapter
Times cited : (5)

References (82)
  • 1
    • 0035413606 scopus 로고    scopus 로고
    • Kinetic and catalytic mechanisms of protein kinases
    • Adams, J. A. (2001). “Kinetic and catalytic mechanisms of protein kinases.” Chem Rev 101(8): 2271-2290.
    • (2001) Chem Rev , vol.101 , Issue.8 , pp. 2271-2290
    • Adams, J.A.1
  • 2
    • 0026698850 scopus 로고
    • Energetic limits of phosphotransfer in the catalytic subunit of cAMPdependent protein kinase as measured by viscosity experiments
    • Adams, J. A. and S. S. Taylor (1992). “Energetic limits of phosphotransfer in the catalytic subunit of cAMPdependent protein kinase as measured by viscosity experiments.” Biochemistry 31(36): 8516-8522.
    • (1992) Biochemistry , vol.31 , Issue.36 , pp. 8516-8522
    • Adams, J.A.1    Taylor, S.S.2
  • 3
    • 52449095361 scopus 로고    scopus 로고
    • The RSK family of kinases: Emerging roles in cellular signalling
    • Anjum, R. and J. Blenis (2008). “The RSK family of kinases: Emerging roles in cellular signalling.” Nat Rev Mol Cell Biol 9(10): 747-758.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , Issue.10 , pp. 747-758
    • Anjum, R.1    Blenis, J.2
  • 4
    • 0034634631 scopus 로고    scopus 로고
    • Isoform-specific differences between the type Iα and IIα cyclic AMP-dependent protein kinase anchoring domains revealed by solution NMR
    • Banky, P., M. G. Newlon, et al. (2000). “Isoform-specific differences between the type Iα and IIα cyclic AMP-dependent protein kinase anchoring domains revealed by solution NMR.” J Biol Chem 275(45): 35146-35152.
    • (2000) J Biol Chem , vol.275 , Issue.45 , pp. 35146-35152
    • Banky, P.1    Newlon, M.G.2
  • 5
    • 79955844083 scopus 로고    scopus 로고
    • Briefly bound to activate: Transient binding of a second catalytic magnesium activates the structure and dynamics of CDK2 kinase for catalysis
    • Bao, Z. Q., D. M. Jacobsen, et al. (2011). “Briefly bound to activate: Transient binding of a second catalytic magnesium activates the structure and dynamics of CDK2 kinase for catalysis.” Structure 19(5): 675-690.
    • (2011) Structure , vol.19 , Issue.5 , pp. 675-690
    • Bao, Z.Q.1    Jacobsen, D.M.2
  • 6
    • 0011627561 scopus 로고
    • Viral src gene products are related to the catalytic chain of mammalian cAMP-dependent protein kinase
    • Barker, W. C. and M. O. Dayhoff (1982). “Viral src gene products are related to the catalytic chain of mammalian cAMP-dependent protein kinase.” Proc Natl Acad Sci U S A 79(9): 2836-2839.
    • (1982) Proc Natl Acad Sci U S A , vol.79 , Issue.9 , pp. 2836-2839
    • Barker, W.C.1    Dayhoff, M.O.2
  • 7
    • 0034625161 scopus 로고    scopus 로고
    • Snapping of the carboxyl terminal tail of the catalytic subunit of PKA onto its core: Characterization of the sites by mutagenesis
    • Batkin, M., Schvartz, I., and S. Shaltiel. (2000). “Snapping of the carboxyl terminal tail of the catalytic subunit of PKA onto its core: Characterization of the sites by mutagenesis.” Biochemistry 39(18), 5366-5373 (2000).
    • (2000) Biochemistry , vol.39 , Issue.18 , pp. 5366-5373
    • Batkin, M.1    Schvartz, I.2    Shaltiel, S.3
  • 9
    • 79551691294 scopus 로고    scopus 로고
    • Realizing the Allosteric Potential of the Tetrameric Protein Kinase A RIα Holoenzyme
    • Boettcher, A. J., J. Wu, et al. (2011). “Realizing the Allosteric Potential of the Tetrameric Protein Kinase A RIα Holoenzyme.” Structure 19(2): 265-276.
    • (2011) Structure , vol.19 , Issue.2 , pp. 265-276
    • Boettcher, A.J.1    Wu, J.2
  • 10
    • 77951591233 scopus 로고    scopus 로고
    • Allosteric communication between cAMP binding sites in the RI subunit of protein kinase A revealed by NMR
    • Byeon, I. J., K. K. Dao, et al. (2010). “Allosteric communication between cAMP binding sites in the RI subunit of protein kinase A revealed by NMR.” J Biol Chem 285(18): 14062-14070.
    • (2010) J Biol Chem , vol.285 , Issue.18 , pp. 14062-14070
    • Byeon, I.J.1    Dao, K.K.2
  • 11
    • 80052284705 scopus 로고    scopus 로고
    • A mechanism for tunable autoinhibition in the structure of a human Ca2+/calmodulin-dependent kinase II holoenzyme
    • Chao, L. H., M. M. Stratton, et al. (2011). “A mechanism for tunable autoinhibition in the structure of a human Ca2+/calmodulin-dependent kinase II holoenzyme.” Cell 146(5): 732-745.
    • (2011) Cell , vol.146 , Issue.5 , pp. 732-745
    • Chao, L.H.1    Stratton, M.M.2
  • 12
    • 0032544011 scopus 로고    scopus 로고
    • Phosphorylation and activation of cAMP-dependent protein kinase by phosphoinositide-dependent protein kinase
    • Cheng, X., Y. Ma, et al. (1998). “Phosphorylation and activation of cAMP-dependent protein kinase by phosphoinositide-dependent protein kinase.” Proc Natl Acad Sci U S A 95(17): 9849-9854.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , Issue.17 , pp. 9849-9854
    • Cheng, X.1    Ma, Y.2
  • 13
    • 0028943777 scopus 로고
    • Association of protein kinase A and protein phosphatase 2B with a common anchoring protein
    • Coghlan, V. M., B. A. Perrino, et al. (1995). “Association of protein kinase A and protein phosphatase 2B with a common anchoring protein.” Science 267(5194): 108-111.
    • (1995) Science , vol.267 , Issue.5194 , pp. 108-111
    • Coghlan, V.M.1    Perrino, B.A.2
  • 14
    • 0005953097 scopus 로고
    • Protein kinase activity associated with the avian sarcoma virus src gene product
    • Collett, M. S. and R. L. Erikson (1978). “Protein kinase activity associated with the avian sarcoma virus src gene product.” Proc Natl Acad Sci U S A 75(4): 2021-2024.
    • (1978) Proc Natl Acad Sci U S A , vol.75 , Issue.4 , pp. 2021-2024
    • Collett, M.S.1    Erikson, R.L.2
  • 15
    • 25144502820 scopus 로고    scopus 로고
    • Higher-order substrate recognition of eIF2α by the RNA-dependent protein kinase PKR
    • Dar, A. C., T. E. Dever, et al. (2005). “Higher-order substrate recognition of eIF2α by the RNA-dependent protein kinase PKR.” Cell 122(6): 887-900.
    • (2005) Cell , vol.122 , Issue.6 , pp. 887-900
    • Dar, A.C.1    Dever, T.E.2
  • 16
    • 33745685964 scopus 로고    scopus 로고
    • Mapping allostery through equilibrium perturbation NMR spectroscopy
    • Das, R., M. Abu-Abed, et al. (2006). “Mapping allostery through equilibrium perturbation NMR spectroscopy.” J Am Chem Soc 128(26): 8406-8407.
    • (2006) J am Chem Soc , vol.128 , Issue.26 , pp. 8406-8407
    • Das, R.1    Abu-Abed, M.2
  • 17
    • 33846066294 scopus 로고    scopus 로고
    • CAMP activation of PKA defines an ancient signaling mechanism
    • Das, R., V. Esposito, et al. (2007). “cAMP activation of PKA defines an ancient signaling mechanism.” Proc Natl Acad Sci U S A 104(1): 93-98.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.1 , pp. 93-98
    • Das, R.1    Esposito, V.2
  • 18
    • 0033668118 scopus 로고    scopus 로고
    • Type IIβ regulatory subunit of cAMP-dependent protein kinase: Purification strategies to optimize crystallization
    • Diller, T. C., N. H. Xuong, et al. (2000). “Type IIβ regulatory subunit of cAMP-dependent protein kinase: Purification strategies to optimize crystallization.” Protein Expr Purif 20(3): 357-364.
    • (2000) Protein Expr Purif , vol.20 , Issue.3 , pp. 357-364
    • Diller, T.C.1    Xuong, N.H.2
  • 19
    • 0033607226 scopus 로고    scopus 로고
    • Mobilization of the A-kinase N-myristate through an isoform-specific intermolecular switch
    • Gangal, M., T. Clifford, et al. (1999). “Mobilization of the A-kinase N-myristate through an isoform-specific intermolecular switch.” Proc Natl Acad Sci U S A 96(22): 12394-12399.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , Issue.22 , pp. 12394-12399
    • Gangal, M.1    Clifford, T.2
  • 20
    • 0032578423 scopus 로고    scopus 로고
    • Backbone flexibility of five sites on the catalytic subunit of cAMP-dependent protein kinase in the open and closed conformations
    • Gangal, M., S. Cox, et al. (1998). “Backbone flexibility of five sites on the catalytic subunit of cAMP-dependent protein kinase in the open and closed conformations.” Biochemistry 37(39): 13728-13735.
    • (1998) Biochemistry , vol.37 , Issue.39 , pp. 13728-13735
    • Gangal, M.1    Cox, S.2
  • 21
    • 0015042684 scopus 로고
    • Role of the receptor in the mechanism of action of adenosine 3:5’-cyclic monophosphate
    • Gill, G. N. and L. D. Garren (1971). “Role of the receptor in the mechanism of action of adenosine 3’:5’-cyclic monophosphate.” Proc Natl Acad Sci U S A 68(4): 786-790.
    • (1971) Proc Natl Acad Sci U S A , vol.68 , Issue.4 , pp. 786-790
    • Gill, G.N.1    Garren, L.D.2
  • 22
    • 33750480828 scopus 로고    scopus 로고
    • Molecular basis of AKAP specificity for PKA regulatory subunits
    • Gold, M. G., B. Lygren, et al. (2006). “Molecular basis of AKAP specificity for PKA regulatory subunits.” Mol Cell 24(3): 383-395.
    • (2006) Mol Cell , vol.24 , Issue.3 , pp. 383-395
    • Gold, M.G.1    Lygren, B.2
  • 23
    • 64149128633 scopus 로고    scopus 로고
    • The chaperones Hsp90 and Cdc37 mediate the maturation and stabilization of protein kinase C through a conserved PXXP motif in the C-terminal tail
    • Gould, C. M., N. Kannan, et al. (2009). “The chaperones Hsp90 and Cdc37 mediate the maturation and stabilization of protein kinase C through a conserved PXXP motif in the C-terminal tail.” J Biol Chem 284(8): 4921-4935.
    • (2009) J Biol Chem , vol.284 , Issue.8 , pp. 4921-4935
    • Gould, C.M.1    Kannan, N.2
  • 24
    • 0029020282 scopus 로고
    • Protein kinases 6. The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks, S. K. and T. Hunter (1995). “Protein kinases 6. The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification.” FASEB J 9(8): 576-596.
    • (1995) FASEB J , vol.9 , Issue.8 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 25
    • 0021162349 scopus 로고
    • DARPP-32, a dopamine-regulated neuronal phosphoprotein, is a potent inhibitor of protein phosphatase-1
    • Hemmings, H. C., Jr., P. Greengard, et al. (1984). “DARPP-32, a dopamine-regulated neuronal phosphoprotein, is a potent inhibitor of protein phosphatase-1.” Nature 310(5977): 503-505 (1984).
    • (1984) Nature , vol.310 , Issue.5977 , pp. 503-505
    • Hemmings, H.C.1    Greengard, P.2
  • 26
    • 0030891426 scopus 로고    scopus 로고
    • Importance of the A-helix of the catalytic subunit of cAMPdependent protein kinase for stability and for orienting subdomains at the cleft interface
    • Herberg, F. W., B. Zimmermann, et al. (1997). “Importance of the A-helix of the catalytic subunit of cAMPdependent protein kinase for stability and for orienting subdomains at the cleft interface.” Protein Science 6(3): 569-579.
    • (1997) Protein Science , vol.6 , Issue.3 , pp. 569-579
    • Herberg, F.W.1    Zimmermann, B.2
  • 27
    • 0030881687 scopus 로고    scopus 로고
    • D-AKAP2, a novel protein kinase A anchoring protein with a putative RGS domain
    • Huang, L. J., K. Durick, et al. (1997). “D-AKAP2, a novel protein kinase A anchoring protein with a putative RGS domain.” Proc Natl Acad Sci U S A 94(21): 11184-11189.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , Issue.21 , pp. 11184-11189
    • Huang, L.J.1    Durick, K.2
  • 28
    • 0000109995 scopus 로고
    • Transforming gene product of Rous sarcoma virus phosphorylates tyrosine
    • Hunter, T. and B. M. Sefton (1980). “Transforming gene product of Rous sarcoma virus phosphorylates tyrosine.” Proc Natl Acad Sci U S A 77(3): 1311-1315.
    • (1980) Proc Natl Acad Sci U S A , vol.77 , Issue.3 , pp. 1311-1315
    • Hunter, T.1    Sefton, B.M.2
  • 29
    • 0037938847 scopus 로고    scopus 로고
    • Interaction between Src and a C-terminal proline-rich motif of Akt is required for Akt activation
    • Jiang, T. and Y. Qiu (2003). “Interaction between Src and a C-terminal proline-rich motif of Akt is required for Akt activation.” J Biol Chem 278(18): 15789-15793.
    • (2003) J Biol Chem , vol.278 , Issue.18 , pp. 15789-15793
    • Jiang, T.1    Qiu, Y.2
  • 30
    • 33846590132 scopus 로고    scopus 로고
    • The hallmark of AGC kinase functional divergence is its C-terminal tail, a cis-acting regulatory module
    • Kannan, N., N. Haste, et al. (2007). “The hallmark of AGC kinase functional divergence is its C-terminal tail, a cis-acting regulatory module.” Proc Natl Acad Sci U S A 104(4): 1272-1277.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.4 , pp. 1272-1277
    • Kannan, N.1    Haste, N.2
  • 31
    • 23644452511 scopus 로고    scopus 로고
    • Did protein kinase regulatory mechanisms evolve through elaboration of a simple structural component?
    • Kannan, N. and A. F. Neuwald (2005). “Did protein kinase regulatory mechanisms evolve through elaboration of a simple structural component?” J Mol Biol 351(5): 956-972.
    • (2005) J Mol Biol , vol.351 , Issue.5 , pp. 956-972
    • Kannan, N.1    Neuwald, A.F.2
  • 32
    • 33947226782 scopus 로고    scopus 로고
    • Structural and functional diversity of the microbial kinome
    • Kannan, N., S. S. Taylor, et al. (2007). “Structural and functional diversity of the microbial kinome.” PLoS Biol 5(3): E17.
    • (2007) Plos Biol , vol.5 , Issue.3
    • Kannan, N.1    Taylor, S.S.2
  • 33
    • 40449130769 scopus 로고    scopus 로고
    • Evolution of allostery in the cyclic nucleotide binding module
    • Kannan, N., J. Wu, et al. (2007). “Evolution of allostery in the cyclic nucleotide binding module.” Genome Biol 8(12): R264.
    • (2007) Genome Biol , vol.8 , Issue.12
    • Kannan, N.1    Wu, J.2
  • 34
    • 84861205906 scopus 로고    scopus 로고
    • Cotranslational cis-phosphorylation of the COOH-terminal tail is a key priming step in the maturation of cAMP-dependent protein kinase
    • Keshwani, M. M., C. Klammt, et al. (2012). “Cotranslational cis-phosphorylation of the COOH-terminal tail is a key priming step in the maturation of cAMP-dependent protein kinase.” Proc Natl Acad Sci U S A 109(20): E1221-E1229.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.20 , pp. E1221-E1229
    • Keshwani, M.M.1    Klammt, C.2
  • 35
    • 34548611290 scopus 로고    scopus 로고
    • PKA-I holoenzyme structure reveals a mechanism for cAMP-dependent activation
    • Kim, C., C. Y. Cheng, et al. (2007). “PKA-I holoenzyme structure reveals a mechanism for cAMP-dependent activation.” Cell 130(6): 1032-1043.
    • (2007) Cell , vol.130 , Issue.6 , pp. 1032-1043
    • Kim, C.1    Cheng, C.Y.2
  • 36
    • 13244291292 scopus 로고    scopus 로고
    • Crystal structure of a complex between the catalytic and regulatory (RIα) subunits of PKA
    • Kim, C., N. H. Xuong, et al. (2005). “Crystal structure of a complex between the catalytic and regulatory (RIα) subunits of PKA.” Science 307(5710): 690-696.
    • (2005) Science , vol.307 , Issue.5710 , pp. 690-696
    • Kim, C.1    Xuong, N.H.2
  • 37
    • 33750474414 scopus 로고    scopus 로고
    • A dynamic mechanism for AKAP binding to RII isoforms of cAMPdependent protein kinase
    • Kinderman, F. S., C. Kim, et al. (2006). “A dynamic mechanism for AKAP binding to RII isoforms of cAMPdependent protein kinase.” Mol Cell 24(3): 397-408.
    • (2006) Mol Cell , vol.24 , Issue.3 , pp. 397-408
    • Kinderman, F.S.1    Kim, C.2
  • 38
    • 0000915668 scopus 로고
    • 2.0 Å refined crystal structure of the catalytic subunit of cAMPdependent protein kinase complexed with a peptide inhibitor and detergent
    • Knighton, D. R., S. M. Bell, et al. (1993). “2.0 Å refined crystal structure of the catalytic subunit of cAMPdependent protein kinase complexed with a peptide inhibitor and detergent.” Acta Crystallogr D Biol Crystallogr 49(Pt 3): 357-361.
    • (1993) Acta Crystallogr D Biol Crystallogr , vol.49 , pp. 357-361
    • Knighton, D.R.1    Bell, S.M.2
  • 39
    • 0026342401 scopus 로고
    • Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D. R., J. H. Zheng, et al. (1991a). “Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase.” Science 253(5018): 407-414.
    • (1991) Science , vol.253 , Issue.5018 , pp. 407-414
    • Knighton, D.R.1    Zheng, J.H.2
  • 40
    • 0026326821 scopus 로고
    • Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D. R., J. H. Zheng, et al. (1991b). “Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase.” Science 253(5018): 414-420.
    • (1991) Science , vol.253 , Issue.5018 , pp. 414-420
    • Knighton, D.R.1    Zheng, J.H.2
  • 41
    • 33845197964 scopus 로고    scopus 로고
    • Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism
    • Kornev, A. P., N. M. Haste, et al. (2006). “Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism.” Proc Natl Acad Sci U S A 103(47): 17783-17788.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.47 , pp. 17783-17788
    • Kornev, A.P.1    Haste, N.M.2
  • 42
    • 55749102720 scopus 로고    scopus 로고
    • A helix scaffold for the assembly of active protein kinases
    • Kornev, A. P., S. S. Taylor, et al. (2008). “A helix scaffold for the assembly of active protein kinases.” Proc Natl Acad Sci U S A 105(38): 14377-14382.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.38 , pp. 14377-14382
    • Kornev, A.P.1    Taylor, S.S.2
  • 43
    • 49749165001 scopus 로고
    • The phosphorylase b to a converting enzyme of rabbit skeletal muscle
    • Krebs, E. G. and E. H. Fischer (1956). “The phosphorylase b to a converting enzyme of rabbit skeletal muscle.” Biochim Biophys Acta 20(1): 150-157.
    • (1956) Biochim Biophys Acta , vol.20 , Issue.1 , pp. 150-157
    • Krebs, E.G.1    Fischer, E.H.2
  • 44
    • 77954941774 scopus 로고    scopus 로고
    • Calcium transduces plasma membrane receptor signals to produce diacylglycerol at Golgi membranes
    • Kunkel, M. T. and A. C. Newton (2010). “Calcium transduces plasma membrane receptor signals to produce diacylglycerol at Golgi membranes.” J Biol Chem 285(30): 22748-22752.
    • (2010) J Biol Chem , vol.285 , Issue.30 , pp. 22748-22752
    • Kunkel, M.T.1    Newton, A.C.2
  • 45
    • 0018071189 scopus 로고
    • Evidence that the transforming gene of avian sarcoma virus encodes a protein kinase associated with a phosphoprotein
    • Levinson, A. D., H. Oppermann, et al. (1978). “Evidence that the transforming gene of avian sarcoma virus encodes a protein kinase associated with a phosphoprotein.” Cell 15(2): 561-572.
    • (1978) Cell , vol.15 , Issue.2 , pp. 561-572
    • Levinson, A.D.1    Oppermann, H.2
  • 46
    • 0036215864 scopus 로고    scopus 로고
    • Crystal structure of a transition state mimic of the catalytic subunit of cAMP-dependent protein kinase
    • Madhusudan, P. Akamine, et al. (2002). “Crystal structure of a transition state mimic of the catalytic subunit of cAMP-dependent protein kinase.” Nat Struct Biol 9(4): 273-277.
    • (2002) Nat Struct Biol , vol.9 , Issue.4 , pp. 273-277
    • Madhusudan, P.A.1
  • 47
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • Manning, G., D. B. Whyte, et al. (2002). “The protein kinase complement of the human genome.” Science 298(5600): 1912-1934.
    • (2002) Science , vol.298 , Issue.5600 , pp. 1912-1934
    • Manning, G.1    Whyte, D.B.2
  • 48
    • 77958160823 scopus 로고    scopus 로고
    • Dynamics connect substrate recognition to catalysis in protein kinase A
    • Masterson, L. R., C. Cheng, et al. (2010). “Dynamics connect substrate recognition to catalysis in protein kinase A.” Nat Chem Biol 6(11): 821-828.
    • (2010) Nat Chem Biol , vol.6 , Issue.11 , pp. 821-828
    • Masterson, L.R.1    Cheng, C.2
  • 49
    • 79955558165 scopus 로고    scopus 로고
    • Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy
    • Masterson, L. R., L. Shi, et al. (2011). “Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy.” Proc Natl Acad Sci U S A.
    • (2011) Proc Natl Acad Sci U S A
    • Masterson, L.R.1    Shi, L.2
  • 50
    • 0031622703 scopus 로고    scopus 로고
    • Cyclic AMP, PKA, and the physiological regulation of adiposity
    • McKnight, G. S. (1998). “Cyclic AMP, PKA, and the physiological regulation of adiposity.” Recent Prog Horm Res 53: 139-159.
    • (1998) Recent Prog Horm Res , vol.53 , pp. 139-159
    • McKnight, G.S.1
  • 51
    • 77952068200 scopus 로고    scopus 로고
    • Communication between tandem cAMP binding domains in the regulatory subunit of protein kinase A-Iα as revealed by domain-silencing mutations
    • McNicholl, E. T., R. Das, et al. (2010). “Communication between tandem cAMP binding domains in the regulatory subunit of protein kinase A-Iα as revealed by domain-silencing mutations.” J Biol Chem 285(20): 15523-15537.
    • (2010) J Biol Chem , vol.285 , Issue.20 , pp. 15523-15537
    • McNicholl, E.T.1    Das, R.2
  • 53
    • 2342595896 scopus 로고    scopus 로고
    • The CREB family: Key regulators of hepatic metabolism
    • Montminy, M., S. H. Koo, et al. (2004). “The CREB family: Key regulators of hepatic metabolism.” Ann Endocrinol (Paris) 65(1): 73-75.
    • (2004) Ann Endocrinol (Paris) , vol.65 , Issue.1 , pp. 73-75
    • Montminy, M.1    Koo, S.H.2
  • 54
    • 0035794551 scopus 로고    scopus 로고
    • A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes
    • Newlon, M. G., M. Roy, et al. (2001). “A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes.” EMBO J 20(7): 1651-1662.
    • (2001) EMBO J , vol.20 , Issue.7 , pp. 1651-1662
    • Newlon, M.G.1    Roy, M.2
  • 55
    • 0032972739 scopus 로고    scopus 로고
    • The molecular basis for protein kinase A anchoring revealed by solution NMR
    • Newlon, M. G., M. Roy, et al. (1999). “The molecular basis for protein kinase A anchoring revealed by solution NMR.” Nat Struct Biol 6(3): 222-227.
    • (1999) Nat Struct Biol , vol.6 , Issue.3 , pp. 222-227
    • Newlon, M.G.1    Roy, M.2
  • 56
    • 78650510151 scopus 로고    scopus 로고
    • Signaling diversity of PKA achieved via a Ca2+-cAMP-PKA oscillatory circuit
    • Ni, Q., A. Ganesan, et al. (2011). “Signaling diversity of PKA achieved via a Ca2+-cAMP-PKA oscillatory circuit.” Nat Chem Biol 7(1): 34-40.
    • (2011) Nat Chem Biol , vol.7 , Issue.1 , pp. 34-40
    • Ni, Q.1    Ganesan, A.2
  • 57
    • 33645018289 scopus 로고    scopus 로고
    • Protein kinase resource: An integrated environment for phosphorylation research
    • Niedner, R. H., O. V. Buzko, et al. (2006). “Protein kinase resource: An integrated environment for phosphorylation research.” Proteins 63(1): 78-86.
    • (2006) Proteins , vol.63 , Issue.1 , pp. 78-86
    • Niedner, R.H.1    Buzko, O.V.2
  • 58
    • 0017810076 scopus 로고
    • The regulation of glycogen metabolism. Purification and characterisation of protein phosphatase inhibitor-1 from rabbit skeletal muscle
    • Nimmo, G. A. and P. Cohen. (1978). “The regulation of glycogen metabolism. Purification and characterisation of protein phosphatase inhibitor-1 from rabbit skeletal muscle.” Eur J Biochem 87(2): 341-351.
    • (1978) Eur J Biochem , vol.87 , Issue.2 , pp. 341-351
    • Nimmo, G.A.1    Cohen, P.2
  • 59
    • 33745821637 scopus 로고    scopus 로고
    • Phosphoinositide-dependent kinase 1 targets protein kinase A in a pathway that regulates interleukin 4
    • Nirula, A., M. Ho, et al. (2006). “Phosphoinositide-dependent kinase 1 targets protein kinase A in a pathway that regulates interleukin 4.” J Exp Med 203(7): 1733-1744.
    • (2006) J Exp Med , vol.203 , Issue.7 , pp. 1733-1744
    • Nirula, A.1    Ho, M.2
  • 60
    • 78649712949 scopus 로고    scopus 로고
    • MTORC2 can associate with ribosomes to promote cotranslational phosphorylation and stability of nascent Akt polypeptide
    • Oh, W.J., C. C. Wu, et al. (2010). “mTORC2 can associate with ribosomes to promote cotranslational phosphorylation and stability of nascent Akt polypeptide.” EMBO J 29(23): 3939-3951.
    • (2010) EMBO J , vol.29 , Issue.23 , pp. 3939-3951
    • Oh, W.J.1    Wu, C.C.2
  • 61
    • 0019198929 scopus 로고
    • Nucleotide sequence analysis of the transforming region and large terminal redundancies of Moloney murine sarcoma virus
    • Reddy, E. P., M. J. Smith, et al. (1980). “Nucleotide sequence analysis of the transforming region and large terminal redundancies of Moloney murine sarcoma virus.” Proc Natl Acad Sci U S A 77(9): 5234-5238.
    • (1980) Proc Natl Acad Sci U S A , vol.77 , Issue.9 , pp. 5234-5238
    • Reddy, E.P.1    Smith, M.J.2
  • 62
    • 78149460164 scopus 로고    scopus 로고
    • Structure of yeast regulatory subunit: A glimpse into the evolution of PKA signaling
    • Rinaldi, J., J. Wu, et al. (2010). “Structure of yeast regulatory subunit: A glimpse into the evolution of PKA signaling.” Structure 18(11): 1471-1482.
    • (2010) Structure , vol.18 , Issue.11 , pp. 1471-1482
    • Rinaldi, J.1    Wu, J.2
  • 64
    • 67650082449 scopus 로고    scopus 로고
    • A chimeric mechanism for polyvalent trans-phosphorylation of PKA by PDK1
    • Romano, R. A., N. Kannan, et al. (2009). “A chimeric mechanism for polyvalent trans-phosphorylation of PKA by PDK1.” Protein Sci 18(7): 1486-1497.
    • (2009) Protein Sci , vol.18 , Issue.7 , pp. 1486-1497
    • Romano, R.A.1    Kannan, N.2
  • 65
    • 75849127506 scopus 로고    scopus 로고
    • Structure of D-AKAP2:PKA RI complex: Insights into AKAP specificity and selectivity
    • Sarma, G. N., F. S. Kinderman, et al. (2010). “Structure of D-AKAP2:PKA RI complex: Insights into AKAP specificity and selectivity.” Structure 18(2): 155-166.
    • (2010) Structure , vol.18 , Issue.2 , pp. 155-166
    • Sarma, G.N.1    Kinderman, F.S.2
  • 66
    • 12244266093 scopus 로고    scopus 로고
    • A-kinase-interacting protein localizes protein kinase A in the nucleus
    • Sastri, M., D. M. Barraclough, et al. (2005). “A-kinase-interacting protein localizes protein kinase A in the nucleus.” Proc Natl Acad Sci U S A 102(2): 349-354.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.2 , pp. 349-354
    • Sastri, M.1    Barraclough, D.M.2
  • 67
    • 77957937199 scopus 로고    scopus 로고
    • Atomic-level characterization of the structural dynamics of proteins
    • Shaw, D. E., P. Maragakis, et al. (2010). “Atomic-level characterization of the structural dynamics of proteins.” Science 330(6002): 341-346.
    • (2010) Science , vol.330 , Issue.6002 , pp. 341-346
    • Shaw, D.E.1    Maragakis, P.2
  • 68
    • 2442591728 scopus 로고    scopus 로고
    • Comparative analysis of the receptor-like kinase family in Arabidopsis and rice
    • Shiu, S. H., W. M. Karlowski, et al. (2004). “Comparative analysis of the receptor-like kinase family in Arabidopsis and rice.” Plant Cell 16(5): 1220-1234.
    • (2004) Plant Cell , vol.16 , Issue.5 , pp. 1220-1234
    • Shiu, S.H.1    Karlowski, W.M.2
  • 69
    • 2642618791 scopus 로고
    • Complete amino acid sequence of the catalytic subunit of bovine cardiac muscle cyclic AMP-dependent protein kinase
    • Shoji, S., D. C. Parmelee, et al. (1981). “Complete amino acid sequence of the catalytic subunit of bovine cardiac muscle cyclic AMP-dependent protein kinase.” Proc Natl Acad Sci U S A 78(2): 848-851.
    • (1981) Proc Natl Acad Sci U S A , vol.78 , Issue.2 , pp. 848-851
    • Shoji, S.1    Parmelee, D.C.2
  • 70
    • 0029143803 scopus 로고
    • Regulatory subunit of protein kinase A: Structure of deletion mutant with cAMP binding domains
    • Su, Y., W. R. Dostmann, et al. (1995). “Regulatory subunit of protein kinase A: Structure of deletion mutant with cAMP binding domains.” Science 269(5225): 807-813.
    • (1995) Science , vol.269 , Issue.5225 , pp. 807-813
    • Su, Y.1    Dostmann, W.R.2
  • 71
    • 79551594605 scopus 로고    scopus 로고
    • Protein kinases: Evolution of dynamic regulatory proteins
    • Taylor, S. S. and A. P. Kornev (2011). “Protein kinases: Evolution of dynamic regulatory proteins.” Trends Biochem Sci 36(2): 65-77.
    • (2011) Trends Biochem Sci , vol.36 , Issue.2 , pp. 65-77
    • Taylor, S.S.1    Kornev, A.P.2
  • 72
    • 48249116424 scopus 로고    scopus 로고
    • Congenital disease SNPs target lineage specific structural elements in protein kinases
    • Torkamani, A., N. Kannan, et al. (2008). “Congenital disease SNPs target lineage specific structural elements in protein kinases.” Proc Natl Acad Sci U S A 105(26): 9011-9016.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.26 , pp. 9011-9016
    • Torkamani, A.1    Kannan, N.2
  • 73
    • 1842575826 scopus 로고    scopus 로고
    • Conformational differences among solution structures of the type Iα, IIα and IIβ protein kinase A regulatory subunit homodimers: Role of the linker regions
    • Vigil, D., D. K. Blumenthal, et al. (2004). “Conformational differences among solution structures of the type Iα, IIα and IIβ protein kinase A regulatory subunit homodimers: Role of the linker regions.” J Mol Biol 337(5): 1183-1194.
    • (2004) J Mol Biol , vol.337 , Issue.5 , pp. 1183-1194
    • Vigil, D.1    Blumenthal, D.K.2
  • 74
    • 33644932999 scopus 로고    scopus 로고
    • Solution scattering reveals large differences in the global structures of type II protein kinase A isoforms
    • Vigil, D., D. K. Blumenthal, et al. (2006). “Solution scattering reveals large differences in the global structures of type II protein kinase A isoforms.” J Mol Biol 357(3): 880-889.
    • (2006) J Mol Biol , vol.357 , Issue.3 , pp. 880-889
    • Vigil, D.1    Blumenthal, D.K.2
  • 75
    • 0037780971 scopus 로고    scopus 로고
    • A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C
    • Violin, J. D., J. Zhang, et al. (2003). “A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C.” J Cell Biol 161(5): 899-909.
    • (2003) J Cell Biol , vol.161 , Issue.5 , pp. 899-909
    • Violin, J.D.1    Zhang, J.2
  • 76
    • 0014409394 scopus 로고
    • An adenosine 3,5’-monophosphate-dependant protein kinase from rabbit skeletal muscle
    • Walsh, D. A., J. P. Perkins, et al. (1968). “An adenosine 3’,5’-monophosphate-dependant protein kinase from rabbit skeletal muscle.” J Biol Chem 243(13): 3763-3765.
    • (1968) J Biol Chem , vol.243 , Issue.13 , pp. 3763-3765
    • Walsh, D.A.1    Perkins, J.P.2
  • 77
    • 33845278824 scopus 로고
    • Rates and mechanisms of hydrolysis of esters of phosphorus-acid
    • Westheimer, F. H. and S. Huang (1988). “Rates and mechanisms of hydrolysis of esters of phosphorus-acid.” J Am Chem Soc 110(1): 181-185.
    • (1988) J am Chem Soc , vol.110 , Issue.1 , pp. 181-185
    • Westheimer, F.H.1    Huang, S.2
  • 78
    • 35348885465 scopus 로고    scopus 로고
    • PKA type IIα holoenzyme reveals a combinatorial strategy for isoform diversity
    • Wu, J., S. H. Brown, et al. (2007). “PKA type IIα holoenzyme reveals a combinatorial strategy for isoform diversity.” Science 318(5848): 274-279.
    • (2007) Science , vol.318 , Issue.5848 , pp. 274-279
    • Wu, J.1    Brown, S.H.2
  • 79
    • 0033001789 scopus 로고    scopus 로고
    • Crystal structures of c-Src reveal features of its autoinhibitory mechanism
    • Xu, W., A. Doshi, et al. (1999). “Crystal structures of c-Src reveal features of its autoinhibitory mechanism.” Mol Cell 3(5): 629-638.
    • (1999) Mol Cell , vol.3 , Issue.5 , pp. 629-638
    • Xu, W.1    Doshi, A.2
  • 80
    • 12344334691 scopus 로고    scopus 로고
    • Allosteric network of cAMP-dependent protein kinase revealed by mutation of Tyr204 in the P+1 loop
    • Yang, J., S. M. Garrod, et al. (2005). “Allosteric network of cAMP-dependent protein kinase revealed by mutation of Tyr204 in the P+1 loop.” J Mol Biol 346(1): 191-201.
    • (2005) J Mol Biol , vol.346 , Issue.1 , pp. 191-201
    • Yang, J.1    Garrod, S.M.2
  • 81
    • 65249108791 scopus 로고    scopus 로고
    • Contribution of non-catalytic core residues to activity and regulation in protein kinase A
    • Yang, J., E. J. Kennedy, et al. (2009). “Contribution of non-catalytic core residues to activity and regulation in protein kinase A.” J Biol Chem 284(10): 6241-6248.
    • (2009) J Biol Chem , vol.284 , Issue.10 , pp. 6241-6248
    • Yang, J.1    Kennedy, E.J.2
  • 82
    • 75749146563 scopus 로고    scopus 로고
    • Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors
    • Zhang, J., F. J. Adrian, et al. (2010). “Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors.” Nature 463(7280): 501-506.
    • (2010) Nature , vol.463 , Issue.7280 , pp. 501-506
    • Zhang, J.1    Adrian, F.J.2


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