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Volumn 13, Issue 11, 2015, Pages

Mapping the Free Energy Landscape of PKA Inhibition and Activation: A Double-Conformational Selection Model for the Tandem cAMP-Binding Domains of PKA RIα

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE REGULATORY SUBUNIT IALPHA; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC AMP DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT; HYBRID PROTEIN; PEPTIDE FRAGMENT; PRKACA PROTEIN, MOUSE;

EID: 84949440484     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1002305     Document Type: Article
Times cited : (29)

References (68)
  • 1
    • 79551594605 scopus 로고    scopus 로고
    • Protein kinases: evolution of dynamic regulatory proteins
    • Taylor SS, Kornev AP, Protein kinases: evolution of dynamic regulatory proteins. Trends Biochem Sci. 2011;36: 65–77. doi: 10.1016/j.tibs.2010.09.006 20971646
    • (2011) Trends Biochem Sci , vol.36 , pp. 65-77
    • Taylor, S.S.1    Kornev, A.P.2
  • 3
    • 0036607064 scopus 로고    scopus 로고
    • Crosstalk between cAMP and MAP kinase signaling in the regulation of cell proliferation
    • Stork PJ, Schmitt JM, Crosstalk between cAMP and MAP kinase signaling in the regulation of cell proliferation. Trends Cell Biol. 2002;12: 258–266. 12074885
    • (2002) Trends Cell Biol , vol.12 , pp. 258-266
    • Stork, P.J.1    Schmitt, J.M.2
  • 4
    • 0035413602 scopus 로고    scopus 로고
    • Physiological substrates of cAMP-dependent protein kinase
    • Shabb JB, Physiological substrates of cAMP-dependent protein kinase. Chem Rev. 2001;101: 2381–2411.
    • (2001) Chem Rev , vol.101 , pp. 2381-2411
    • Shabb, J.B.1
  • 5
    • 0029020282 scopus 로고
    • Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification
    • Hanks SK, Hunter T, Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 1995;9: 576–596. 7768349
    • (1995) FASEB J , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 6
    • 84925432611 scopus 로고    scopus 로고
    • Dysfunctional conformational dynamics of protein kinase A induced by a lethal mutant of phospholamban hinder phosphorylation
    • Kim J, Masterson LR, Cembran A, Verardi R, Shi L, Gao J, et al. Dysfunctional conformational dynamics of protein kinase A induced by a lethal mutant of phospholamban hinder phosphorylation. Proc Natl Acad Sci U S A. 2015;112: 3716–21. doi: 10.1073/pnas.1502299112 25775607
    • (2015) Proc Natl Acad Sci U S A , vol.112 , pp. 3716-3721
    • Kim, J.1    Masterson, L.R.2    Cembran, A.3    Verardi, R.4    Shi, L.5    Gao, J.6
  • 7
    • 84914171432 scopus 로고    scopus 로고
    • Synchronous opening and closing motions are essential for cAMP-dependent protein kinase A signaling
    • Srivastava AK, McDonald LR, Cembran A, Kim J, Masterson LR, McClendon CL, et al. Synchronous opening and closing motions are essential for cAMP-dependent protein kinase A signaling. Structure. 2014;22: 1735–43. doi: 10.1016/j.str.2014.09.010 25458836
    • (2014) Structure , vol.22 , pp. 1735-1743
    • Srivastava, A.K.1    McDonald, L.R.2    Cembran, A.3    Kim, J.4    Masterson, L.R.5    McClendon, C.L.6
  • 8
    • 84936762406 scopus 로고    scopus 로고
    • Mapping the Hydrogen Bond Networks in the Catalytic Subunit of Protein Kinase A using H/D Fractionation Factors
    • Li G, Srivastava AK, Kim J, Taylor SS, Veglia G, Mapping the Hydrogen Bond Networks in the Catalytic Subunit of Protein Kinase A using H/D Fractionation Factors. Biochemistry. 2015;54: 4042–9. doi: 10.1021/acs.biochem.5b00387 26030372
    • (2015) Biochemistry , vol.54 , pp. 4042-4049
    • Li, G.1    Srivastava, A.K.2    Kim, J.3    Taylor, S.S.4    Veglia, G.5
  • 9
    • 77956929978 scopus 로고
    • Control by Phosphorylation Part A—General Features, Specific Enzymes (I)
    • Beebe SJ, Corbin JD, Control by Phosphorylation Part A—General Features, Specific Enzymes (I). The Enzymes. 1986;17: 43–111.
    • (1986) The Enzymes , vol.17 , pp. 43-111
    • Beebe, S.J.1    Corbin, J.D.2
  • 10
    • 84908192391 scopus 로고    scopus 로고
    • Using Markov state models to develop a mechanistic understanding of protein kinase A regulatory subunit RIα activation in response to cAMP binding
    • Boras BW, Kornev A, Taylor SS, McCulloch AD, Using Markov state models to develop a mechanistic understanding of protein kinase A regulatory subunit RIα activation in response to cAMP binding. J Biol Chem. 2014;289: 30040–51. doi: 10.1074/jbc.M114.568907 25202018
    • (2014) J Biol Chem , vol.289 , pp. 30040-30051
    • Boras, B.W.1    Kornev, A.2    Taylor, S.S.3    McCulloch, A.D.4
  • 13
    • 34548611290 scopus 로고    scopus 로고
    • PKA-I Holoenzyme Structure Reveals a Mechanism for cAMP-Dependent Activation
    • Kim C, Cheng CY, Saldanha SA, Taylor SS, PKA-I Holoenzyme Structure Reveals a Mechanism for cAMP-Dependent Activation. Cell. 2007;130: 1032–1043. 17889648
    • (2007) Cell , vol.130 , pp. 1032-1043
    • Kim, C.1    Cheng, C.Y.2    Saldanha, S.A.3    Taylor, S.S.4
  • 14
    • 0029143803 scopus 로고
    • Regulatory subunit of protein kinase A: structure of deletion mutant with cAMP binding domains
    • Su Y, Dostmann WR, Herberg FW, Durick K, Xuong NH, Ten Eyck L, et al. Regulatory subunit of protein kinase A: structure of deletion mutant with cAMP binding domains. Science. 1995;269: 807–813. 7638597
    • (1995) Science , vol.269 , pp. 807-813
    • Su, Y.1    Dostmann, W.R.2    Herberg, F.W.3    Durick, K.4    Xuong, N.H.5    Ten Eyck, L.6
  • 15
    • 2542523982 scopus 로고    scopus 로고
    • Crystal structures of RIalpha subunit of cyclic adenosine 5’-monophosphate (cAMP)-dependent protein kinase complexed with (Rp)-adenosine 3',5'-cyclic monophosphothioate and (Sp)-adenosine 3',5'-cyclic monophosphothioate, the phosphothioate analogues of cA
    • Wu J, Jones JM, Nguyen-Huu X, Ten Eyck LF, Taylor SS, Crystal structures of RIalpha subunit of cyclic adenosine 5’-monophosphate (cAMP)-dependent protein kinase complexed with (Rp)-adenosine 3',5'-cyclic monophosphothioate and (Sp)-adenosine 3',5'-cyclic monophosphothioate, the phosphothioate analogues of cA. Biochemistry. 2004;43: 6620–6629. 15157095
    • (2004) Biochemistry , vol.43 , pp. 6620-6629
    • Wu, J.1    Jones, J.M.2    Nguyen-Huu, X.3    Ten Eyck, L.F.4    Taylor, S.S.5
  • 18
    • 0029932259 scopus 로고    scopus 로고
    • Active site mutations define the pathway for the cooperative activation of cAMP-dependent protein kinase
    • Herberg FW, Taylor SS, Dostmann WRG, Active site mutations define the pathway for the cooperative activation of cAMP-dependent protein kinase. Biochemistry. 1996;35: 2934–2942. 8608131
    • (1996) Biochemistry , vol.35 , pp. 2934-2942
    • Herberg, F.W.1    Taylor, S.S.2    Dostmann, W.R.G.3
  • 20
    • 2942527724 scopus 로고    scopus 로고
    • Rl alpha subunit of PKA: A cAMP-free structure reveals a hydrophobic capping mechanism for docking cAMP into site B RID A-3261-2009
    • Wu J, Brown S, Xuong NH, Taylor SS, Rl alpha subunit of PKA: A cAMP-free structure reveals a hydrophobic capping mechanism for docking cAMP into site B RID A-3261-2009. Structure. 2004;12: 1057–1065. 15274925
    • (2004) Structure , vol.12 , pp. 1057-1065
    • Wu, J.1    Brown, S.2    Xuong, N.H.3    Taylor, S.S.4
  • 21
    • 72149087959 scopus 로고    scopus 로고
    • Sensing domain dynamics in protein kinase A-I{alpha} complexes by solution X-ray scattering
    • Cheng CY, Yang J, Taylor SS, Blumenthal DK, Sensing domain dynamics in protein kinase A-I{alpha} complexes by solution X-ray scattering. J Biol Chem. 2009;284: 35916–35925. doi: 10.1074/jbc.M109.059493 19837668
    • (2009) J Biol Chem , vol.284 , pp. 35916-35925
    • Cheng, C.Y.1    Yang, J.2    Taylor, S.S.3    Blumenthal, D.K.4
  • 22
    • 27444444785 scopus 로고    scopus 로고
    • The conformationally dynamic C helix of the RIalpha subunit of protein kinase A mediates isoform-specific domain reorganization upon C subunit binding
    • Vigil D, Blumenthal DK, Taylor SS, Trewhella J, The conformationally dynamic C helix of the RIalpha subunit of protein kinase A mediates isoform-specific domain reorganization upon C subunit binding. J Biol Chem. 2005;280: 35521–35527. 16109722
    • (2005) J Biol Chem , vol.280 , pp. 35521-35527
    • Vigil, D.1    Blumenthal, D.K.2    Taylor, S.S.3    Trewhella, J.4
  • 23
    • 33644788934 scopus 로고    scopus 로고
    • Dynamic binding of PKA regulatory subunit RI alpha
    • Gullingsrud J, Kim C, Taylor SS, McCammon JA, Dynamic binding of PKA regulatory subunit RI alpha. Structure. 2006;14: 141–149. 16407073
    • (2006) Structure , vol.14 , pp. 141-149
    • Gullingsrud, J.1    Kim, C.2    Taylor, S.S.3    McCammon, J.A.4
  • 24
    • 84916887461 scopus 로고    scopus 로고
    • Allostery without a conformational change? Revisiting the paradigm
    • Nussinov R, Tsai C-J, Allostery without a conformational change? Revisiting the paradigm. Curr Opin Struct Biol. 2015;30: 17–24. doi: 10.1016/j.sbi.2014.11.005 25500675
    • (2015) Curr Opin Struct Biol , vol.30 , pp. 17-24
    • Nussinov, R.1    Tsai, C.-J.2
  • 25
    • 84919933634 scopus 로고    scopus 로고
    • Principles of allosteric interactions in cell signaling
    • Nussinov R, Tsai C-J, Liu J, Principles of allosteric interactions in cell signaling. J Am Chem Soc. 2014;136: 17692–701. doi: 10.1021/ja510028c 25474128
    • (2014) J Am Chem Soc , vol.136 , pp. 17692-17701
    • Nussinov, R.1    Tsai, C.-J.2    Liu, J.3
  • 26
    • 84929353747 scopus 로고    scopus 로고
    • Effects of membrane mimetics on cytochrome P450-cytochrome b5 interactions characterized by NMR spectroscopy
    • Zhang M, Huang R, Im S-C, Waskell L, Ramamoorthy A, Effects of membrane mimetics on cytochrome P450-cytochrome b5 interactions characterized by NMR spectroscopy. J Biol Chem. 2015;290: 12705–18. doi: 10.1074/jbc.M114.597096 25795780
    • (2015) J Biol Chem , vol.290 , pp. 12705-12718
    • Zhang, M.1    Huang, R.2    Im, S.-C.3    Waskell, L.4    Ramamoorthy, A.5
  • 27
    • 84929096323 scopus 로고    scopus 로고
    • Kinetic and structural characterization of the interaction between the FMN binding domain of cytochrome P450 reductase and cytochrome c
    • Huang R, Zhang M, Rwere F, Waskell L, Ramamoorthy A, Kinetic and structural characterization of the interaction between the FMN binding domain of cytochrome P450 reductase and cytochrome c. J Biol Chem. 2015;290: 4843–55. doi: 10.1074/jbc.M114.582700 25512382
    • (2015) J Biol Chem , vol.290 , pp. 4843-4855
    • Huang, R.1    Zhang, M.2    Rwere, F.3    Waskell, L.4    Ramamoorthy, A.5
  • 28
    • 84923346691 scopus 로고    scopus 로고
    • Insights into the role of substrates on the interaction between cytochrome b5 and cytochrome P450 2B4 by NMR
    • Zhang M, Le Clair S V, Huang R, Ahuja S, Im S-C, Waskell L, et al. Insights into the role of substrates on the interaction between cytochrome b5 and cytochrome P450 2B4 by NMR. Sci Rep. 2015;5: 8392. doi: 10.1038/srep08392 25687717
    • (2015) Sci Rep , vol.5 , pp. 8392
    • Zhang, M.1    Le Clair, S.V.2    Huang, R.3    Ahuja, S.4    Im, S.-C.5    Waskell, L.6
  • 30
    • 84894039820 scopus 로고    scopus 로고
    • Integrated RAS signaling defined by parallel NMR detection of effectors and regulators
    • Smith MJ, Ikura M, Integrated RAS signaling defined by parallel NMR detection of effectors and regulators. Nat Chem Biol. 2014;10: 223–30. doi: 10.1038/nchembio.1435 24441586
    • (2014) Nat Chem Biol , vol.10 , pp. 223-230
    • Smith, M.J.1    Ikura, M.2
  • 31
    • 84952628203 scopus 로고    scopus 로고
    • Structural insights into endoplasmic reticulum stored calcium regulation by inositol 1,4,5-trisphosphate and ryanodine receptors
    • Seo M-D, Enomoto M, Ishiyama N, Stathopulos PB, Ikura M, Structural insights into endoplasmic reticulum stored calcium regulation by inositol 1,4,5-trisphosphate and ryanodine receptors. Biochim Biophys Acta. doi: 10.1016/j.bbamcr.2014.11.023
    • Biochim Biophys Acta
    • Seo, M.-D.1    Enomoto, M.2    Ishiyama, N.3    Stathopulos, P.B.4    Ikura, M.5
  • 32
    • 77952068200 scopus 로고    scopus 로고
    • Communication between tandem cAMP binding domains in the regulatory subunit of protein kinase A-Ialpha as revealed by domain-silencing mutations
    • McNicholl ET, Das R, SilDas S, Taylor SS, Melacini G, Communication between tandem cAMP binding domains in the regulatory subunit of protein kinase A-Ialpha as revealed by domain-silencing mutations. J Biol Chem. 2010;285: 15523–15537. doi: 10.1074/jbc.M110.105783 20202931
    • (2010) J Biol Chem , vol.285 , pp. 15523-15537
    • McNicholl, E.T.1    Das, R.2    SilDas, S.3    Taylor, S.S.4    Melacini, G.5
  • 33
    • 77951591233 scopus 로고    scopus 로고
    • Allosteric communication between cAMP binding sites in the RI subunit of protein kinase A revealed by NMR
    • Byeon IJ, Dao KK, Jung J, Keen J, Leiros I, Doskeland SO, et al. Allosteric communication between cAMP binding sites in the RI subunit of protein kinase A revealed by NMR. J Biol Chem. 2010;285: 14062–14070. doi: 10.1074/jbc.M110.106666 20197278
    • (2010) J Biol Chem , vol.285 , pp. 14062-14070
    • Byeon, I.J.1    Dao, K.K.2    Jung, J.3    Keen, J.4    Leiros, I.5    Doskeland, S.O.6
  • 34
    • 84902138801 scopus 로고    scopus 로고
    • Isomerase-catalyzed binding of interleukin-1 receptor-associated kinase 1 to the EVH1 domain of vasodilator-stimulated phosphoprotein
    • Greenwood AI, Kwon J, Nicholson LK, Isomerase-catalyzed binding of interleukin-1 receptor-associated kinase 1 to the EVH1 domain of vasodilator-stimulated phosphoprotein. Biochemistry. 2014;53: 3593–607. doi: 10.1021/bi500031e 24857403
    • (2014) Biochemistry , vol.53 , pp. 3593-3607
    • Greenwood, A.I.1    Kwon, J.2    Nicholson, L.K.3
  • 35
    • 78650447046 scopus 로고    scopus 로고
    • Structural biology: The twist in Crk signaling revealed
    • Nicholson LK, De S, Structural biology: The twist in Crk signaling revealed. Nat Chem Biol. 2011;7: 5–6. doi: 10.1038/nchembio.504 21164511
    • (2011) Nat Chem Biol , vol.7 , pp. 5-6
    • Nicholson, L.K.1    De, S.2
  • 37
    • 84856748688 scopus 로고    scopus 로고
    • The Projection Analysis of NMR Chemical Shifts Reveals Extended EPAC Autoinhibition Determinants
    • Selvaratnam R, Vanschouwen B, Fogolari F, Mazhab-Jafari MT, Das R, Melacini G, The Projection Analysis of NMR Chemical Shifts Reveals Extended EPAC Autoinhibition Determinants. Biophys J. 2012;102: 630–639. doi: 10.1016/j.bpj.2011.12.030 22325287
    • (2012) Biophys J , vol.102 , pp. 630-639
    • Selvaratnam, R.1    Vanschouwen, B.2    Fogolari, F.3    Mazhab-Jafari, M.T.4    Das, R.5    Melacini, G.6
  • 38
    • 50349092827 scopus 로고    scopus 로고
    • Entropy-driven cAMP-dependent allosteric control of inhibitory interactions in exchange proteins directly activated by cAMP
    • Das R, Mazhab-Jafari MT, Chowdhury S, SilDas S, Selvaratnam R, Melacini G, Entropy-driven cAMP-dependent allosteric control of inhibitory interactions in exchange proteins directly activated by cAMP. J Biol Chem. 2008;283: 19691–703. doi: 10.1074/jbc.M802164200 18411261
    • (2008) J Biol Chem , vol.283 , pp. 19691-19703
    • Das, R.1    Mazhab-Jafari, M.T.2    Chowdhury, S.3    SilDas, S.4    Selvaratnam, R.5    Melacini, G.6
  • 39
    • 84905836722 scopus 로고    scopus 로고
    • A mechanism for the auto-inhibition of hyperpolarization-activated cyclic nucleotide-gated (HCN) channel opening and its relief by cAMP
    • Akimoto M, Zhang Z, Boulton S, Selvaratnam R, VanSchouwen B, Gloyd M, et al. A mechanism for the auto-inhibition of hyperpolarization-activated cyclic nucleotide-gated (HCN) channel opening and its relief by cAMP. J Biol Chem. 2014;289: 22205–22220. doi: 10.1074/jbc.M114.572164 24878962
    • (2014) J Biol Chem , vol.289 , pp. 22205-22220
    • Akimoto, M.1    Zhang, Z.2    Boulton, S.3    Selvaratnam, R.4    VanSchouwen, B.5    Gloyd, M.6
  • 40
    • 0242331659 scopus 로고    scopus 로고
    • The energetic cost of domain reorientation in maltose-binding protein as studied by NMR and fluorescence spectroscopy
    • Millet O, Hudson RP, Kay LE, The energetic cost of domain reorientation in maltose-binding protein as studied by NMR and fluorescence spectroscopy. Proc Natl Acad Sci U S A. 2003;100: 12700–5. 14530390
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 12700-12705
    • Millet, O.1    Hudson, R.P.2    Kay, L.E.3
  • 41
    • 0037192127 scopus 로고    scopus 로고
    • Characterization of the ATP-binding domain of the sarco(endo)plasmic reticulum Ca(2+)-ATPase: probing nucleotide binding by multidimensional NMR
    • Abu-Abed M, Mal TK, Kainosho M, MacLennan DH, Ikura M, Characterization of the ATP-binding domain of the sarco(endo)plasmic reticulum Ca(2+)-ATPase: probing nucleotide binding by multidimensional NMR. Biochemistry. 2002;41: 1156–64. 11802714
    • (2002) Biochemistry , vol.41 , pp. 1156-1164
    • Abu-Abed, M.1    Mal, T.K.2    Kainosho, M.3    MacLennan, D.H.4    Ikura, M.5
  • 42
    • 84870604188 scopus 로고    scopus 로고
    • pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR
    • Lorieau JL, Louis JM, Schwieters CD, Bax A, pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR. Proc Natl Acad Sci U S A. 2012;109: 19994–9. doi: 10.1073/pnas.1213801109 23169643
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 19994-19999
    • Lorieau, J.L.1    Louis, J.M.2    Schwieters, C.D.3    Bax, A.4
  • 43
    • 77952725646 scopus 로고    scopus 로고
    • Dissecting the cAMP-inducible allosteric switch in protein kinase A RIalpha
    • Sjoberg TJ, Kornev AP, Taylor SS, Dissecting the cAMP-inducible allosteric switch in protein kinase A RIalpha. Protein Sci. 2010;19: 1213–1221. doi: 10.1002/pro.400 20512974
    • (2010) Protein Sci , vol.19 , pp. 1213-1221
    • Sjoberg, T.J.1    Kornev, A.P.2    Taylor, S.S.3
  • 44
    • 84936103060 scopus 로고    scopus 로고
    • Allostery through the computational microscope: cAMP activation of a canonical signalling domain
    • Malmstrom RD, Kornev AP, Taylor SS, Amaro RE, Allostery through the computational microscope: cAMP activation of a canonical signalling domain. Nat Commun.; 2015;6: 7588.
    • (2015) Nat Commun , vol.6 , pp. 7588
    • Malmstrom, R.D.1    Kornev, A.P.2    Taylor, S.S.3    Amaro, R.E.4
  • 45
    • 0034642224 scopus 로고    scopus 로고
    • Consequences of cAMP-binding site mutations on the structural stability of the type I regulatory subunit of cAMP-dependent protein kinase
    • Canaves JM, Leon DA, Taylor SS, Consequences of cAMP-binding site mutations on the structural stability of the type I regulatory subunit of cAMP-dependent protein kinase. Biochemistry. 2000;39: 15022–15031. 11106480
    • (2000) Biochemistry , vol.39 , pp. 15022-15031
    • Canaves, J.M.1    Leon, D.A.2    Taylor, S.S.3
  • 46
    • 0025851505 scopus 로고
    • Unfolding of the regulatory subunit of cAMP-dependent protein kinase I
    • León D a Dostmann WR, Taylor SS, Unfolding of the regulatory subunit of cAMP-dependent protein kinase I. Biochemistry. 1991;30: 3035–3040. 1848784
    • (1991) Biochemistry , vol.30 , pp. 3035-3040
    • León D a, D.W.R.1    Taylor, S.S.2
  • 47
    • 0034673984 scopus 로고    scopus 로고
    • Probing the multidomain structure of the type I regulatory subunit of cAMP-dependent protein kinase using mutational analysis: role and environment of endogenous tryptophans
    • Leon DA, Canaves JM, Taylor SS, Probing the multidomain structure of the type I regulatory subunit of cAMP-dependent protein kinase using mutational analysis: role and environment of endogenous tryptophans. Biochemistry 2000;39: 5662–5671.
    • (2000) Biochemistry , vol.39 , pp. 5662-5671
    • Leon, D.A.1    Canaves, J.M.2    Taylor, S.S.3
  • 48
    • 84896970480 scopus 로고    scopus 로고
    • Tapping the translation potential of cAMP signalling: molecular basis for selectivity in cAMP agonism and antagonism as revealed by NMR
    • Boulton S, Akimoto M, Vanschouwen B, Moleschi K, Selvaratnam R, Giri R, et al. Tapping the translation potential of cAMP signalling: molecular basis for selectivity in cAMP agonism and antagonism as revealed by NMR. Biochem. Soc. Trans. 2014;42: 302–307.
    • (2014) Biochem. Soc. Trans , vol.42 , pp. 302-307
    • Boulton, S.1    Akimoto, M.2    Vanschouwen, B.3    Moleschi, K.4    Selvaratnam, R.5    Giri, R.6
  • 50
    • 84937509615 scopus 로고    scopus 로고
    • Role of Dynamics in the Auto-Inhibition and Activation of the Hyperpolarization-Activated Cyclic-Nucleotide-Modulated (HCN) Ion Channels
    • VanSchouwen B, Akimoto M, Sayadi M, Fogolari F, Melacini G, Role of Dynamics in the Auto-Inhibition and Activation of the Hyperpolarization-Activated Cyclic-Nucleotide-Modulated (HCN) Ion Channels. J Biol Chem. 2015 Jul 17;290(29):17642–54 doi: 10.1074/jbc.M115.651877 25944904
    • (2015) J Biol Chem , vol.290 , Issue.29 , pp. 17642-17654
    • VanSchouwen, B.1    Akimoto, M.2    Sayadi, M.3    Fogolari, F.4    Melacini, G.5
  • 51
    • 84909607968 scopus 로고    scopus 로고
    • Signaling at crossroads: the dialogue between PDEs and PKA is spoken in multiple languages
    • Moleschi K, Melacini G, Signaling at crossroads: the dialogue between PDEs and PKA is spoken in multiple languages. Biophys J. 2014;107: 1259–60. doi: 10.1016/j.bpj.2014.07.051 25229132
    • (2014) Biophys J , vol.107 , pp. 1259-1260
    • Moleschi, K.1    Melacini, G.2
  • 52
    • 84909580096 scopus 로고    scopus 로고
    • Active site coupling in PDE:PKA complexes promotes resetting of mammalian cAMP signaling
    • Krishnamurthy S, Moorthy BS, Xin Xiang L, Xin Shan L, Bharatham K, Tulsian NK, et al. Active site coupling in PDE:PKA complexes promotes resetting of mammalian cAMP signaling. Biophys J. 2014;107: 1426–40. doi: 10.1016/j.bpj.2014.07.050 25229150
    • (2014) Biophys J , vol.107 , pp. 1426-1440
    • Krishnamurthy, S.1    Moorthy, B.S.2    Xin Xiang, L.3    Xin Shan, L.4    Bharatham, K.5    Tulsian, N.K.6
  • 53
    • 84941810399 scopus 로고    scopus 로고
    • Parallel Allostery by cAMP and PDE Coordinates Activation and Termination Phases in cAMP Signaling
    • Krishnamurthy S, Tulsian NK, Chandramohan A, Anand GS, Parallel Allostery by cAMP and PDE Coordinates Activation and Termination Phases in cAMP Signaling. Biophys J. 2015 Sep 15;109(6):1251–63. doi: 10.1016/j.bpj.2015.06.067 26276689
    • (2015) Biophys J , vol.109 , Issue.6 , pp. 1251-1263
    • Krishnamurthy, S.1    Tulsian, N.K.2    Chandramohan, A.3    Anand, G.S.4
  • 54
    • 0034254510 scopus 로고    scopus 로고
    • 8-Substituted cAMP analogues reveal marked differences in adaptability, hydrogen bonding, and charge accommodation between homologous binding sites (AI/AII and BI/BII) in cAMP kinase I and II
    • Schwede F, Christensen A, Liauw S, Hippe T, Kopperud R, Jastorff B, et al. 8-Substituted cAMP analogues reveal marked differences in adaptability, hydrogen bonding, and charge accommodation between homologous binding sites (AI/AII and BI/BII) in cAMP kinase I and II. Biochemistry. 2000;39: 8803–8812. 10913291
    • (2000) Biochemistry , vol.39 , pp. 8803-8812
    • Schwede, F.1    Christensen, A.2    Liauw, S.3    Hippe, T.4    Kopperud, R.5    Jastorff, B.6
  • 55
    • 0035170874 scopus 로고    scopus 로고
    • Solution structure of ThiS and implications for the evolutionary roots of ubiquitin
    • Wang C, Xi J, Begley TP, Nicholson LK, Solution structure of ThiS and implications for the evolutionary roots of ubiquitin. Nat Struct Biol. 2001;8: 47–51. 11135670
    • (2001) Nat Struct Biol , vol.8 , pp. 47-51
    • Wang, C.1    Xi, J.2    Begley, T.P.3    Nicholson, L.K.4
  • 57
    • 79958182720 scopus 로고    scopus 로고
    • Recurrent PRKAR1A mutation in acrodysostosis with hormone resistance
    • Linglart A, Menguy C, Couvineau A, Auzan C, Gunes Y, Cancel M, et al. Recurrent PRKAR1A mutation in acrodysostosis with hormone resistance. N Engl J Med. 2011;364: 2218–26. doi: 10.1056/NEJMoa1012717 21651393
    • (2011) N Engl J Med , vol.364 , pp. 2218-2226
    • Linglart, A.1    Menguy, C.2    Couvineau, A.3    Auzan, C.4    Gunes, Y.5    Cancel, M.6
  • 58
    • 84866170771 scopus 로고    scopus 로고
    • PRKAR1A mutation affecting cAMP-mediated G protein-coupled receptor signaling in a patient with acrodysostosis and hormone resistance
    • Nagasaki K, Iida T, Sato H, Ogawa Y, Kikuchi T, Saitoh A, et al. PRKAR1A mutation affecting cAMP-mediated G protein-coupled receptor signaling in a patient with acrodysostosis and hormone resistance. J Clin Endocrinol Metab. 2012;97: E1808–13. doi: 10.1210/jc.2012-1369 22723333
    • (2012) J Clin Endocrinol Metab , vol.97 , pp. 13-1808
    • Nagasaki, K.1    Iida, T.2    Sato, H.3    Ogawa, Y.4    Kikuchi, T.5    Saitoh, A.6
  • 59
    • 84937541703 scopus 로고    scopus 로고
    • Protein kinase A alterations in adrenocortical tumors
    • Espiard S, Ragazzon B, Bertherat J, Protein kinase A alterations in adrenocortical tumors. Horm Metab Res. 2014;46: 869–75. doi: 10.1055/s-0034-1385908 25105543
    • (2014) Horm Metab Res , vol.46 , pp. 869-875
    • Espiard, S.1    Ragazzon, B.2    Bertherat, J.3
  • 60
    • 84941703228 scopus 로고    scopus 로고
    • Measurement of State-Specific Association Constants in Allosteric Sensors through Molecular Stapling and NMR
    • Moleschi KJ, Akimoto M, Melacini G, Measurement of State-Specific Association Constants in Allosteric Sensors through Molecular Stapling and NMR. J Am Chem Soc. 2015; 137 (33): 10777–10785. doi: 10.1021/jacs.5b06557
    • (2015) J Am Chem Soc , vol.137 , Issue.33 , pp. 10777-10785
    • Moleschi, K.J.1    Akimoto, M.2    Melacini, G.3
  • 61
    • 0029400480 scopus 로고
    • Nmrpipe—a Multidimensional Spectral Processing System Based on Unix Pipes
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A, Nmrpipe—a Multidimensional Spectral Processing System Based on Unix Pipes. J Biomol NMR. 1995;6: 277–293. 8520220
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 62
    • 84949461307 scopus 로고    scopus 로고
    • T. D. Goddard and D. G. Kneller University of California SF. SPARKY. https://www.cgl.ucsf.edu/home/sparky/
  • 63
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • Sattler M, Schleucher J, Griesinger C, Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog Nucl Magn Reson Spectrosc. 1999;34: 93–158.
    • (1999) Prog Nucl Magn Reson Spectrosc , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 64
    • 0032506009 scopus 로고    scopus 로고
    • TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins
    • Salzmann M, Pervushin K, Wider G, Senn H, Wuthrich K, TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins. Proc Natl Acad Sci U S A. 1998;95: 13585–13590. 9811843
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 13585-13590
    • Salzmann, M.1    Pervushin, K.2    Wider, G.3    Senn, H.4    Wuthrich, K.5
  • 65
    • 24344440618 scopus 로고    scopus 로고
    • Probabilistic identification of spin systems and their assignments including coil-helix inference as output (PISTACHIO)
    • Eghbalnia HR, Bahrami A, Wang LY, Assadi A, Markley JL, Probabilistic identification of spin systems and their assignments including coil-helix inference as output (PISTACHIO). J Biomol NMR. 2005;32: 219–233. 16132822
    • (2005) J Biomol NMR , vol.32 , pp. 219-233
    • Eghbalnia, H.R.1    Bahrami, A.2    Wang, L.Y.3    Assadi, A.4    Markley, J.L.5
  • 66
    • 33846954752 scopus 로고    scopus 로고
    • A model for agonism and antagonism in an ancient and ubiquitous cAMP-binding domain
    • Das R, Melacini G, A model for agonism and antagonism in an ancient and ubiquitous cAMP-binding domain. J Biol Chem. 2007;282: 581–593. 17074757
    • (2007) J Biol Chem , vol.282 , pp. 581-593
    • Das, R.1    Melacini, G.2
  • 67
    • 0035996729 scopus 로고    scopus 로고
    • Interpretation of 15N NMR relaxation data of globular proteins using hydrodynamic calculations with HYDRONMR
    • Bernadó P, De la Torre JG, Pons M, Interpretation of 15N NMR relaxation data of globular proteins using hydrodynamic calculations with HYDRONMR. J Biomol NMR. 2002;23: 139–150. 12153039
    • (2002) J Biomol NMR , vol.23 , pp. 139-150
    • Bernadó, P.1    De la Torre, J.G.2    Pons, M.3
  • 68
    • 0035951175 scopus 로고    scopus 로고
    • Building hydrodynamic bead-shell models for rigid bioparticles of arbitrary shape
    • Garcia de la Torre J, Building hydrodynamic bead-shell models for rigid bioparticles of arbitrary shape. Biophys Chem. 2001;94: 265–274. 11804736
    • (2001) Biophys Chem , vol.94 , pp. 265-274
    • Garcia de la Torre, J.1


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