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Volumn 2, Issue 4, 2006, Pages 238-250

Conformational changes in protein loops and helices induced by post-translational phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; COMPUTATIONAL METHODS; CRYSTAL ATOMIC STRUCTURE; ENZYMES;

EID: 33646266474     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.0020032     Document Type: Article
Times cited : (123)

References (84)
  • 1
    • 0032922002 scopus 로고    scopus 로고
    • PhosphoBase, a database of phosphorylation sites: Release 2.0
    • Kreegipuu A, Blom N, Brunak S (1999) PhosphoBase, a database of phosphorylation sites: release 2.0. Nucleic Acids Res 27: 237-239.
    • (1999) Nucleic Acids Res , vol.27 , pp. 237-239
    • Kreegipuu, A.1    Blom, N.2    Brunak, S.3
  • 2
    • 0035413617 scopus 로고    scopus 로고
    • Chemical inhibitors of protein kinases
    • Bridges AJ (2001) Chemical inhibitors of protein kinases. Chem Rev 101: 2541-2571.
    • (2001) Chem Rev , vol.101 , pp. 2541-2571
    • Bridges, A.J.1
  • 3
    • 0035413607 scopus 로고    scopus 로고
    • Structural basis for control by phosphorylation
    • Johnson LN, Lewis RJ (2001) Structural basis for control by phosphorylation. Chem Rev 101: 2209-2242.
    • (2001) Chem Rev , vol.101 , pp. 2209-2242
    • Johnson, L.N.1    Lewis, R.J.2
  • 4
    • 0028032838 scopus 로고
    • Structural determinants of substrate selection by the human insulin-receptor protein-yyrosine kinase
    • Keane NE, Chavanieu A, Quirk PG, Evans JS, Levine BA, et al. (1994) Structural determinants of substrate selection by the human insulin-receptor protein-yyrosine kinase. Eur J Biochem 226: 525-536.
    • (1994) Eur J Biochem , vol.226 , pp. 525-536
    • Keane, N.E.1    Chavanieu, A.2    Quirk, P.G.3    Evans, J.S.4    Levine, B.A.5
  • 5
    • 0029867420 scopus 로고    scopus 로고
    • Conformational effects of serine phosphorylation in phospholamban peptides
    • Quirk PG, Patchell VB, Colyer J, Drago GA, Gao Y (1996) Conformational effects of serine phosphorylation in phospholamban peptides. Eur J Biochem 236: 85-91.
    • (1996) Eur J Biochem , vol.236 , pp. 85-91
    • Quirk, P.G.1    Patchell, V.B.2    Colyer, J.3    Drago, G.A.4    Gao, Y.5
  • 6
    • 0029096432 scopus 로고
    • Sequential phosphorylation of adjacent serine residues on the N-terminal region of cardiac troponin-I: Structure-activity implications of ordered phosphorylation
    • Quirk PG, Patchell VB, Gao Y, Levine BA, Perry SV (1995) Sequential phosphorylation of adjacent serine residues on the N-terminal region of cardiac troponin-I: Structure-activity implications of ordered phosphorylation. FEBS Lett 370: 175-178.
    • (1995) FEBS Lett , vol.370 , pp. 175-178
    • Quirk, P.G.1    Patchell, V.B.2    Gao, Y.3    Levine, B.A.4    Perry, S.V.5
  • 7
    • 0028067046 scopus 로고
    • Phosphorylation effects on flanking charged residues: Structural implications for signal-transduction in protein-kinases
    • Chavanieu A, Keane NE, Quirk PG, Levine BA, Calas B, et al. (1994) Phosphorylation effects on flanking charged residues: Structural implications for signal-transduction in protein-kinases. Eur J Biochem 224: 115-123.
    • (1994) Eur J Biochem , vol.224 , pp. 115-123
    • Chavanieu, A.1    Keane, N.E.2    Quirk, P.G.3    Levine, B.A.4    Calas, B.5
  • 8
    • 0032906903 scopus 로고    scopus 로고
    • Direct effects of phosphorylation on the preferred backbone conformation of peptides: A nuclear magnetic resonance study
    • Tholey A, Lindemann A, Kinzel V, Reed J (1999) Direct effects of phosphorylation on the preferred backbone conformation of peptides: A nuclear magnetic resonance study. Biophys J 76: 76-87.
    • (1999) Biophys J , vol.76 , pp. 76-87
    • Tholey, A.1    Lindemann, A.2    Kinzel, V.3    Reed, J.4
  • 9
    • 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
    • Tholey A, Pipkorn R, Bossemeyer D, Kinzel V, Reed J (2001) Influence of myristoylation, phosphorylation, and deamidation on the structural behavior of the N-terminus of the catalytic subunit of CAMP-dependent protein kinase. Biochemistry 40: 225-231.
    • (2001) Biochemistry , vol.40 , pp. 225-231
    • Tholey, A.1    Pipkorn, R.2    Bossemeyer, D.3    Kinzel, V.4    Reed, J.5
  • 11
    • 0033609111 scopus 로고    scopus 로고
    • Physical evidence for a phosphorylation-dependent conformational change in the enhancer-binding protein NtrC
    • U S A
    • Hwang I, Thorgeirsson T, Lee J, Kustu S, Shin YK (1999) Physical evidence for a phosphorylation-dependent conformational change in the enhancer-binding protein NtrC. Proc Natl Acad U S A 96: 4880-4885.
    • (1999) Proc Natl Acad , vol.96 , pp. 4880-4885
    • Hwang, I.1    Thorgeirsson, T.2    Lee, J.3    Kustu, S.4    Shin, Y.K.5
  • 12
    • 0032979413 scopus 로고    scopus 로고
    • Phosphorylation stabilizes the N-termini of alpha-helices
    • Smart JL, McCammon JA (1999) Phosphorylation stabilizes the N-termini of alpha-helices. Biopolymers 49: 225-233.
    • (1999) Biopolymers , vol.49 , pp. 225-233
    • Smart, J.L.1    McCammon, J.A.2
  • 13
    • 0035913754 scopus 로고    scopus 로고
    • Atomistic Brownian dynamics simulation of peptide phosphorylation
    • Shen TY, Wong CF, McCammon JA (2001) Atomistic Brownian dynamics simulation of peptide phosphorylation. J Am Chem Soc 123: 9107-9111.
    • (2001) J Am Chem Soc , vol.123 , pp. 9107-9111
    • Shen, T.Y.1    Wong, C.F.2    McCammon, J.A.3
  • 14
    • 13644250683 scopus 로고    scopus 로고
    • Phosphorylation effects on cis/trans isomerization and the backbone conformation of serine-proline motifs: Accelerated molecular dynamics analysis
    • Hamelberg D, Shen T, McCammon JA (2005) Phosphorylation effects on cis/trans isomerization and the backbone conformation of serine-proline motifs: Accelerated molecular dynamics analysis. J Am Chem Soc 127: 1969-1974.
    • (2005) J Am Chem Soc , vol.127 , pp. 1969-1974
    • Hamelberg, D.1    Shen, T.2    McCammon, J.A.3
  • 16
    • 0032574755 scopus 로고    scopus 로고
    • Structural examination of the influence of phosphorylation on the binding of fibrinopeptide A to bovine thrombin
    • Maurer MC, Peng JL, An SS, Trosset JY, Henschen-Edman A, et al. (1998) Structural examination of the influence of phosphorylation on the binding of fibrinopeptide A to bovine thrombin. Biochemistry 37: 5888-5902.
    • (1998) Biochemistry , vol.37 , pp. 5888-5902
    • Maurer, M.C.1    Peng, J.L.2    An, S.S.3    Trosset, J.Y.4    Henschen-Edman, A.5
  • 17
    • 0032424250 scopus 로고    scopus 로고
    • How and why phosphotyrosine-containing peptides bind to the SH2 and PTB domains
    • Zhou Y, Abagyan R (1998) How and why phosphotyrosine-containing peptides bind to the SH2 and PTB domains. Fold Des 3: 513-522.
    • (1998) Fold des , vol.3 , pp. 513-522
    • Zhou, Y.1    Abagyan, R.2
  • 18
    • 0029860548 scopus 로고    scopus 로고
    • Structural characterization of the phosphotyrosine binding region of a high-affinity SH2 domain-phosphopeptide complex by molecular dynamics simulation and chemical shift calculations
    • Feng MH, Philippopoulos M, MacKerell AD, Lim C (1996) Structural characterization of the phosphotyrosine binding region of a high-affinity SH2 domain-phosphopeptide complex by molecular dynamics simulation and chemical shift calculations. J Am Chem Soc 118: 11265-11277.
    • (1996) J Am Chem Soc , vol.118 , pp. 11265-11277
    • Feng, M.H.1    Philippopoulos, M.2    MacKerell, A.D.3    Lim, C.4
  • 19
    • 0037033036 scopus 로고    scopus 로고
    • Phosphorylation-induced conformational changes in a mitogen-activated protein kinase substrate. Implications for tyrosine hydroxylase activation
    • Stultz CM, Levin AD, Edelman ER (2002) Phosphorylation-induced conformational changes in a mitogen-activated protein kinase substrate. Implications for tyrosine hydroxylase activation. J Biol Chem 277: 47653-47661.
    • (2002) J Biol Chem , vol.277 , pp. 47653-47661
    • Stultz, C.M.1    Levin, A.D.2    Edelman, E.R.3
  • 20
    • 0036838326 scopus 로고    scopus 로고
    • Molecular dynamics of the FixJ receiver domain: Movement of the beta 4-alpha 4 loop correlates with the in and out flip of Phe101
    • Roche P, Mouawad L, Perahia D, Samama JP, Kahn D (2002) Molecular dynamics of the FixJ receiver domain: movement of the beta 4-alpha 4 loop correlates with the in and out flip of Phe101. Protein Sci 11: 2622-2630.
    • (2002) Protein Sci , vol.11 , pp. 2622-2630
    • Roche, P.1    Mouawad, L.2    Perahia, D.3    Samama, J.P.4    Kahn, D.5
  • 21
    • 0034026757 scopus 로고    scopus 로고
    • Molecular dynamics simulations of protein-tyrosine phosphatase 1B. II. Substrate-enzyme interactions and dynamics
    • Peters GH, Frimurer TM, Andersen JN, Olsen OH (2000) Molecular dynamics simulations of protein-tyrosine phosphatase 1B. II. Substrate-enzyme interactions and dynamics. Biophys J 78: 2191-2200.
    • (2000) Biophys J , vol.78 , pp. 2191-2200
    • Peters, G.H.1    Frimurer, T.M.2    Andersen, J.N.3    Olsen, O.H.4
  • 22
    • 0029619426 scopus 로고
    • Solution structure of a band 3 peptide inhibitor bound to aldolase: A proposed mechanism for regulating binding by tyrosine phosphorylation
    • Schneider ML, Post CB (1995) Solution structure of a band 3 peptide inhibitor bound to aldolase: A proposed mechanism for regulating binding by tyrosine phosphorylation. Biochemistry 34: 16574-16584.
    • (1995) Biochemistry , vol.34 , pp. 16574-16584
    • Schneider, M.L.1    Post, C.B.2
  • 23
    • 0035224573 scopus 로고    scopus 로고
    • Theoretical models of catalytic domains of protein phosphatases 1 and 2A with Zn2+ and Mn2+ metal dications and putative bioligands in their catalytic centers
    • Wozniak-Celmer E, Oldziej S, Ciarkowski J (2001) Theoretical models of catalytic domains of protein phosphatases 1 and 2A with Zn2+ and Mn2+ metal dications and putative bioligands in their catalytic centers. Acta Biochim Pol 48: 35-52.
    • (2001) Acta Biochim Pol , vol.48 , pp. 35-52
    • Wozniak-Celmer, E.1    Oldziej, S.2    Ciarkowski, J.3
  • 24
    • 0037466314 scopus 로고    scopus 로고
    • Structural features of human initiation factor 4E, studied by X-ray crystal analyses and molecular dynamics simulations
    • Tomoo K, Shen X, Okabe K, Nozoe Y, Fukuhara S, et al. (2003) Structural features of human initiation factor 4E, studied by X-ray crystal analyses and molecular dynamics simulations. J Mol Biol 328: 365-383.
    • (2003) J Mol Biol , vol.328 , pp. 365-383
    • Tomoo, K.1    Shen, X.2    Okabe, K.3    Nozoe, Y.4    Fukuhara, S.5
  • 25
    • 0035815288 scopus 로고    scopus 로고
    • Dynamic coupling between the SH2 and SH3 domains of c-Src and hck underlies their inactivation by C-terminal tyrosine phosphorylation
    • Young MA, Gonfloni S, Superti-Furga G, Roux B, Kuriyan J (2001) Dynamic coupling between the SH2 and SH3 domains of c-Src and hck underlies their inactivation by C-terminal tyrosine phosphorylation. Cell 105: 115-126.
    • (2001) Cell , vol.105 , pp. 115-126
    • Young, M.A.1    Gonfloni, S.2    Superti-Furga, G.3    Roux, B.4    Kuriyan, J.5
  • 26
    • 0037732762 scopus 로고    scopus 로고
    • Solution conformation of the antibody-bound tyrosine phosphorylation site of the nicotinic acetylcholine receptor beta-subunit in its phosphorylated and nonphosphorylated states
    • Phan-Chan-Du A, Hemmerlin C, Krikorian D, Sakarellos-Daitsiotis M, Tsikaris V, et al. (2003) Solution conformation of the antibody-bound tyrosine phosphorylation site of the nicotinic acetylcholine receptor beta-subunit in its phosphorylated and nonphosphorylated states. Biochemistry 42: 7371-7380.
    • (2003) Biochemistry , vol.42 , pp. 7371-7380
    • Phan-Chan-Du, A.1    Hemmerlin, C.2    Krikorian, D.3    Sakarellos-Daitsiotis, M.4    Tsikaris, V.5
  • 27
    • 0037452980 scopus 로고    scopus 로고
    • The structure of the inter-SH2 domain of class IA phosphoinositide 3-kinase determined by site-directed spin labeling EPR and homology modeling
    • U S A
    • Fu Z, Aronoff-Spencer E, Backer JM, Gerfen GJ (2003) The structure of the inter-SH2 domain of class IA phosphoinositide 3-kinase determined by site-directed spin labeling EPR and homology modeling. Proc Natl Acad U S A 100: 3275-3280.
    • (2003) Proc Natl Acad , vol.100 , pp. 3275-3280
    • Fu, Z.1    Aronoff-Spencer, E.2    Backer, J.M.3    Gerfen, G.J.4
  • 28
    • 0043092653 scopus 로고    scopus 로고
    • Proteomic identification of 14-3-3zeta as a mitogen-activated protein kinase-activated protein kinase 2 substrate: Role in dimer formation and ligand binding
    • Powell DW, Rane MJ, Joughin BA, Kalmukova R, Hong JH, et al. (2003) Proteomic identification of 14-3-3zeta as a mitogen-activated protein kinase-activated protein kinase 2 substrate: Role in dimer formation and ligand binding. Mol Cell Biol 23: 5376-5387.
    • (2003) Mol Cell Biol , vol.23 , pp. 5376-5387
    • Powell, D.W.1    Rane, M.J.2    Joughin, B.A.3    Kalmukova, R.4    Hong, J.H.5
  • 29
    • 4444336426 scopus 로고    scopus 로고
    • In silico activation of Src tyrosine kinase reveals the molecular basis for intramolecular autophosphorylation
    • Mendieta J, Gago F (2004) In silico activation of Src tyrosine kinase reveals the molecular basis for intramolecular autophosphorylation. J Mol Graph Model 23: 189-198.
    • (2004) J Mol Graph Model , vol.23 , pp. 189-198
    • Mendieta, J.1    Gago, F.2
  • 30
    • 2442667660 scopus 로고    scopus 로고
    • Activation and inhibition of cyclin-dependent kinase-2 by phosphorylation: A molecular dynamics study reveals the functional importance of the glycine-rich loop
    • Bartova I, Otyepka M, Kriz Z, Koca J (2004) Activation and inhibition of cyclin-dependent kinase-2 by phosphorylation: A molecular dynamics study reveals the functional importance of the glycine-rich loop. Protein Sci 13: 1449-1457.
    • (2004) Protein Sci , vol.13 , pp. 1449-1457
    • Bartova, I.1    Otyepka, M.2    Kriz, Z.3    Koca, J.4
  • 31
    • 0029731347 scopus 로고    scopus 로고
    • Phosphorylation events associated with different states of activation of a hepatic cardiolipin protease-activated protein kinase: Structural identity to the protein kinase N-type protein kinases
    • Peng B, Morrice NA, Groenen LC, Wettenhall REH (1996) Phosphorylation events associated with different states of activation of a hepatic cardiolipin protease-activated protein kinase: Structural identity to the protein kinase N-type protein kinases. J Biol Chem 271: 32233-32240.
    • (1996) J Biol Chem , vol.271 , pp. 32233-32240
    • Peng, B.1    Morrice, N.A.2    Groenen, L.C.3    Wettenhall, R.E.H.4
  • 32
    • 0035400394 scopus 로고    scopus 로고
    • Structural basis of oncogenic activation caused by point mutations in the kinase domain of the MET proto-oncogene: Modeling studies
    • Miller M, Ginalski K, Lesyng B, Nakaigawa N, Schmidt L, et al. (2001) Structural basis of oncogenic activation caused by point mutations in the kinase domain of the MET proto-oncogene: Modeling studies. Proteins 44: 32-43.
    • (2001) Proteins , vol.44 , pp. 32-43
    • Miller, M.1    Ginalski, K.2    Lesyng, B.3    Nakaigawa, N.4    Schmidt, L.5
  • 33
    • 2342500001 scopus 로고    scopus 로고
    • Protein modeling combined with spectroscopic techniques: An attractive quick alternative to obtain structural information
    • Kubala M, Obsil T, Obsilova V, Lansky Z, Amler E (2004) Protein modeling combined with spectroscopic techniques: An attractive quick alternative to obtain structural information. Physiol Res 53 (Suppl 1): S187-S197.
    • (2004) Physiol Res , vol.53 , Issue.1 SUPPL.
    • Kubala, M.1    Obsil, T.2    Obsilova, V.3    Lansky, Z.4    Amler, E.5
  • 34
    • 0031575408 scopus 로고    scopus 로고
    • Energetics of nucleophile activation in a protein tyrosine phosphatase
    • Hansson T, Nordlund P, Aqvist J (1997) Energetics of nucleophile activation in a protein tyrosine phosphatase. J Mol Biol 265: 118-127.
    • (1997) J Mol Biol , vol.265 , pp. 118-127
    • Hansson, T.1    Nordlund, P.2    Aqvist, J.3
  • 35
    • 0035235378 scopus 로고    scopus 로고
    • Ser133 phosphate-KIX interactions in the CREB-CBP complex: An ab initio molecular dynamics study
    • Dal Peraro M, Alber F, Carloni P (2001) Ser133 phosphate-KIX interactions in the CREB-CBP complex: An ab initio molecular dynamics study. Eur Biophys J 30: 75-81.
    • (2001) Eur Biophys J , vol.30 , pp. 75-81
    • Dal Peraro, M.1    Alber, F.2    Carloni, P.3
  • 36
    • 0037174865 scopus 로고    scopus 로고
    • Phosphorylation and mutations of Ser(16) in human phenylalanine hydroxylase - Kinetic and structural effects
    • Miranda FF, Teigen K, Thorolfsson M, Svebak RM, Knappskog PM, et al. (2002) Phosphorylation and mutations of Ser(16) in human phenylalanine hydroxylase - Kinetic and structural effects. J Biol Chem 277: 40937-40943.
    • (2002) J Biol Chem , vol.277 , pp. 40937-40943
    • Miranda, F.F.1    Teigen, K.2    Thorolfsson, M.3    Svebak, R.M.4    Knappskog, P.M.5
  • 38
    • 0036310711 scopus 로고    scopus 로고
    • On the role of the crystal environment in determining protein side-chain conformations
    • Jacobson MP, Friesner RA, Xiang ZX, Honig B (2002) On the role of the crystal environment in determining protein side-chain conformations. J Mol Biol 320: 597-608.
    • (2002) J Mol Biol , vol.320 , pp. 597-608
    • Jacobson, M.P.1    Friesner, R.A.2    Xiang, Z.X.3    Honig, B.4
  • 40
    • 1842532008 scopus 로고    scopus 로고
    • A hierarchical approach to all-atom protein loop prediction
    • Jacobson MP, Pincus DL, Rapp CS, Day TJ, Honig B, et al. (2004) A hierarchical approach to all-atom protein loop prediction. Proteins 55: 351-367.
    • (2004) Proteins , vol.55 , pp. 351-367
    • Jacobson, M.P.1    Pincus, D.L.2    Rapp, C.S.3    Day, T.J.4    Honig, B.5
  • 41
    • 1442277682 scopus 로고    scopus 로고
    • Computational modeling of the catalytic reaction in triose phosphate isomerase
    • Guallar V, Jacobson MP, McDermott A, Friesner RA (2004) Computational modeling of the catalytic reaction in triose phosphate isomerase. J Mol Biol 337: 227-239.
    • (2004) J Mol Biol , vol.337 , pp. 227-239
    • Guallar, V.1    Jacobson, M.P.2    McDermott, A.3    Friesner, R.A.4
  • 42
    • 1842584571 scopus 로고    scopus 로고
    • High-resolution prediction of protein helix positions and orientations
    • Li X, Jacobson MP, Friesner RA (2004) High-resolution prediction of protein helix positions and orientations. Proteins 55: 368-382.
    • (2004) Proteins , vol.55 , pp. 368-382
    • Li, X.1    Jacobson, M.P.2    Friesner, R.A.3
  • 43
    • 0035413616 scopus 로고    scopus 로고
    • Cyclin-dependent kinases
    • Harper JW, Adams PD (2001) Cyclin-dependent kinases. Chem Rev 101: 2511-2526.
    • (2001) Chem Rev , vol.101 , pp. 2511-2526
    • Harper, J.W.1    Adams, P.D.2
  • 44
    • 0029767016 scopus 로고    scopus 로고
    • Structural basis of cyclin-dependent kinase activation by phosphorylation
    • Russo AA, Jeffrey PD, Pavletich NP (1996) Structural basis of cyclin-dependent kinase activation by phosphorylation. Nat Struct Biol 3: 696-700.
    • (1996) Nat Struct Biol , vol.3 , pp. 696-700
    • Russo, A.A.1    Jeffrey, P.D.2    Pavletich, N.P.3
  • 45
    • 0033605643 scopus 로고    scopus 로고
    • Effects of phosphorylation of threonine 160 on cyclin-dependent kinase 2 structure and activity
    • Brown NR, Noble MEM, Lawrie AM, Morris MC, Tunnah P, et al. (1999) Effects of phosphorylation of threonine 160 on cyclin-dependent kinase 2 structure and activity. J Biol Chem 274: 8746-8756.
    • (1999) J Biol Chem , vol.274 , pp. 8746-8756
    • Brown, N.R.1    Noble, M.E.M.2    Lawrie, A.M.3    Morris, M.C.4    Tunnah, P.5
  • 46
    • 0035265679 scopus 로고    scopus 로고
    • Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2
    • Song HW, Hanlon N, Brown NR, Noble MEM, Johnson LN, et al. (2001) Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2. Mol Cell 7: 615-626.
    • (2001) Mol Cell , vol.7 , pp. 615-626
    • Song, H.W.1    Hanlon, N.2    Brown, N.R.3    Noble, M.E.M.4    Johnson, L.N.5
  • 47
    • 0027532449 scopus 로고
    • Phosphorylation independent activation of human cyclin-dependent kinase 2 by cyclin A in vitro
    • Connell-Crowley L, Solomon MJ, Wei N, Harper JW (1993) Phosphorylation independent activation of human cyclin-dependent kinase 2 by cyclin A in vitro. Mol Biol Cell 4: 79-92.
    • (1993) Mol Biol Cell , vol.4 , pp. 79-92
    • Connell-Crowley, L.1    Solomon, M.J.2    Wei, N.3    Harper, J.W.4
  • 48
    • 0029029617 scopus 로고
    • Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
    • Jeffrey PD, Russo AA, Polyak K, Gibbs E, Hurwitz J, et al. (1995) Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature 376: 313-320.
    • (1995) Nature , vol.376 , pp. 313-320
    • Jeffrey, P.D.1    Russo, A.A.2    Polyak, K.3    Gibbs, E.4    Hurwitz, J.5
  • 49
    • 0037089017 scopus 로고    scopus 로고
    • The SGB/NP hydration free energy model based on the Surface Generalized Born solvent reaction field and novel nonpolar hydration free energy estimators
    • Gallicchio E, Zhang LY, Levy RM (2002) The SGB/NP hydration free energy model based on the Surface Generalized Born solvent reaction field and novel nonpolar hydration free energy estimators. J Comput Chem 23: 517-529.
    • (2002) J Comput Chem , vol.23 , pp. 517-529
    • Gallicchio, E.1    Zhang, L.Y.2    Levy, R.M.3
  • 50
    • 0001246294 scopus 로고    scopus 로고
    • Generalized Born model based on a surface integral formulation
    • Ghosh A, Rapp CS, Friesner RA (1998) Generalized Born model based on a surface integral formulation. J Phys Chem B 102: 10983-10990.
    • (1998) J Phys Chem B , vol.102 , pp. 10983-10990
    • Ghosh, A.1    Rapp, C.S.2    Friesner, R.A.3
  • 51
    • 2942568007 scopus 로고    scopus 로고
    • Key role of Ser562/661 in Snf1-dependent regulation of Cat8p in Saccharomyces cerevisiae and Kluyveromyces lactis
    • Charbon G, Breunig KD, Wattiez R, Vandenhaute J, Noel-Georis I (2004) Key role of Ser562/661 in Snf1-dependent regulation of Cat8p in Saccharomyces cerevisiae and Kluyveromyces lactis. Mol Cell Biol 24: 4083-4091.
    • (2004) Mol Cell Biol , vol.24 , pp. 4083-4091
    • Charbon, G.1    Breunig, K.D.2    Wattiez, R.3    Vandenhaute, J.4    Noel-Georis, I.5
  • 52
    • 3142618052 scopus 로고    scopus 로고
    • Regulation of ubiquitin protein ligase activity in c-Cbl by phosphorylation-induced conformational change and constitutive activation by tyrosine to glutamate point mutations
    • Kassenbrock CK, Anderson SM (2004) Regulation of ubiquitin protein ligase activity in c-Cbl by phosphorylation-induced conformational change and constitutive activation by tyrosine to glutamate point mutations. J Biol Chem 279: 28017-28027.
    • (2004) J Biol Chem , vol.279 , pp. 28017-28027
    • Kassenbrock, C.K.1    Anderson, S.M.2
  • 53
    • 0028567874 scopus 로고
    • Constitutive activation of Mek1 by mutation of serine phosphorylation sites
    • U S A
    • Huang W, Erikson RL (1994) Constitutive activation of Mek1 by mutation of serine phosphorylation sites. Proc Natl Acad Sci U S A 91: 8960-8963.
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 8960-8963
    • Huang, W.1    Erikson, R.L.2
  • 54
    • 0027162310 scopus 로고
    • Glutamate at the site of phosphorylation of nitrogen-regulatory protein NTRC mimics aspartyl-phosphate and activates the protein
    • Klose KE, Weiss DS, Kustu S (1993) Glutamate at the site of phosphorylation of nitrogen-regulatory protein NTRC mimics aspartyl-phosphate and activates the protein. J Mol Biol 232: 67-78.
    • (1993) J Mol Biol , vol.232 , pp. 67-78
    • Klose, K.E.1    Weiss, D.S.2    Kustu, S.3
  • 55
    • 0034054493 scopus 로고    scopus 로고
    • Enhanced electron flux and reduced calmodulin dissociation may explain "calcium-independent" eNOS activation by phosphorylation
    • McCabe TJ, Fulton D, Roman LJ, Sessa WC (2000) Enhanced electron flux and reduced calmodulin dissociation may explain "calcium-independent" eNOS activation by phosphorylation. J Biol Chem 275: 6123-6128.
    • (2000) J Biol Chem , vol.275 , pp. 6123-6128
    • McCabe, T.J.1    Fulton, D.2    Roman, L.J.3    Sessa, W.C.4
  • 56
    • 0036787760 scopus 로고    scopus 로고
    • Combining conformational flexibility and continuum electrostatics for calculating pK(a)s in proteins
    • Georgescu RE, Alexov EG, Gunner MR (2002) Combining conformational flexibility and continuum electrostatics for calculating pK(a)s in proteins. Biophys J 83: 1731-1748.
    • (2002) Biophys J , vol.83 , pp. 1731-1748
    • Georgescu, R.E.1    Alexov, E.G.2    Gunner, M.R.3
  • 57
    • 0033573063 scopus 로고    scopus 로고
    • Conformational changes induced by phosphorylation of the FixJ receiver domain
    • Birck C, Mourey L, Gouet P, Fabry B, Schumacher J, et al. (1999) Conformational changes induced by phosphorylation of the FixJ receiver domain. Structure Fold Des 7: 1505-1515.
    • (1999) Structure Fold Des , vol.7 , pp. 1505-1515
    • Birck, C.1    Mourey, L.2    Gouet, P.3    Fabry, B.4    Schumacher, J.5
  • 59
    • 0024290703 scopus 로고
    • Structural changes in glycogen phosphorylase induced by phosphorylation
    • Sprang SR, Acharya KR, Goldsmith EJ, Stuart DI, Varvill K, et al. (1988) Structural changes in glycogen phosphorylase induced by phosphorylation. Nature 336: 215-221.
    • (1988) Nature , vol.336 , pp. 215-221
    • Sprang, S.R.1    Acharya, K.R.2    Goldsmith, E.J.3    Stuart, D.I.4    Varvill, K.5
  • 60
    • 0030766163 scopus 로고    scopus 로고
    • Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog
    • Hubbard SR (1997) Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J 16: 5572-5581.
    • (1997) EMBO J , vol.16 , pp. 5572-5581
    • Hubbard, S.R.1
  • 61
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • Hubbard SR, Wei L, Ellis L, Hendrickson WA (1994) Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 372: 746-754.
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 63
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides
    • Kaminski GA, Friesner RA, Tirado-Rives J, Jorgensen WL (2001) Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides. J Phys Chem B 105: 6474-6487.
    • (2001) J Phys Chem B , vol.105 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 64
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • Jorgensen WL, Maxwell DS, Tirado-Rives J (1996) Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. J Am Chem Soc 118: 11225-11236.
    • (1996) J Am Chem Soc , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 65
    • 15744387842 scopus 로고    scopus 로고
    • Competition between intramolecular hydrogen bonds and solvation in phosphorylated peptides: Simulations with explicit and implicit solvent
    • Wong SE, Bernacki K, Jacobson M (2005) Competition between intramolecular hydrogen bonds and solvation in phosphorylated peptides: Simulations with explicit and implicit solvent. J Phys Chem B 109: 5249-5258.
    • (2005) J Phys Chem B , vol.109 , pp. 5249-5258
    • Wong, S.E.1    Bernacki, K.2    Jacobson, M.3
  • 66
    • 0347095360 scopus 로고    scopus 로고
    • Portland (Oregon): Schrodinger, L.L.C.
    • Schrodinger LLC (2002) Jaguar 5.0 [computer program]. Portland (Oregon): Schrodinger, L.L.C.
    • (2002) Jaguar 5.0 [Computer Program]
  • 67
    • 0030180875 scopus 로고    scopus 로고
    • New model for calculation of solvation free energies: Correction of self-consistent reaction field continuum dielectric theory for short-range hydrogen-bonding effects
    • Marten B, Kim K, Cortis C, Friesner RA, Murphy RB, et al. (1996) New model for calculation of solvation free energies: Correction of self-consistent reaction field continuum dielectric theory for short-range hydrogen-bonding effects. J Phys Chem 100: 11775-11788.
    • (1996) J Phys Chem , vol.100 , pp. 11775-11788
    • Marten, B.1    Kim, K.2    Cortis, C.3    Friesner, R.A.4    Murphy, R.B.5
  • 68
    • 0000304948 scopus 로고
    • Accurate first principles calculation of molecular charge distributions and solvation energies from ab initio quantum mechanics and continuum dielectric theory
    • Tannor DJ, Marten B, Murphy R, Friesner RA, Sitkoff D, et al. (1994) Accurate first principles calculation of molecular charge distributions and solvation energies from ab initio quantum mechanics and continuum dielectric theory. J Am Chem Soc 116: 11875-11882.
    • (1994) J Am Chem Soc , vol.116 , pp. 11875-11882
    • Tannor, D.J.1    Marten, B.2    Murphy, R.3    Friesner, R.A.4    Sitkoff, D.5
  • 69
    • 0027955787 scopus 로고
    • Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins
    • Abagyan R, Totrov M (1994) Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins. J Mol Biol 235: 983-1002.
    • (1994) J Mol Biol , vol.235 , pp. 983-1002
    • Abagyan, R.1    Totrov, M.2
  • 70
    • 0023173201 scopus 로고
    • Prediction of the folding of short polypeptide segments by uniform conformational sampling
    • Bruccoleri RE, Karplus M (1987) Prediction of the folding of short polypeptide segments by uniform conformational sampling. Biopolymers 26: 137-168.
    • (1987) Biopolymers , vol.26 , pp. 137-168
    • Bruccoleri, R.E.1    Karplus, M.2
  • 71
    • 0037375742 scopus 로고    scopus 로고
    • Ab initio construction of polypeptide fragments: Efficient generation of accurate, representative ensembles
    • DePristo MA, de Bakker PIW, Lovell SC, Blundell TL (2003) Ab initio construction of polypeptide fragments: Efficient generation of accurate, representative ensembles. Proteins 51: 41-55.
    • (2003) Proteins , vol.51 , pp. 41-55
    • DePristo, M.A.1    De Bakker, P.I.W.2    Lovell, S.C.3    Blundell, T.L.4
  • 73
    • 0034601916 scopus 로고    scopus 로고
    • The 1.9 A resolution structure of phospho-serine 46 HPr from Enterococcus faecalis
    • Audette GF, Engelmann R, Hengstenberg W, Deutscher J, Hayakawa K, et al. (2000) The 1.9 A resolution structure of phospho-serine 46 HPr from Enterococcus faecalis. J Mol Biol 303: 545-553.
    • (2000) J Mol Biol , vol.303 , pp. 545-553
    • Audette, G.F.1    Engelmann, R.2    Hengstenberg, W.3    Deutscher, J.4    Hayakawa, K.5
  • 74
    • 0028056155 scopus 로고
    • The 1.6 A structure of histidine-containing phosphotransfer protein HPr from Streptococcus faecalis
    • Jia Z, Vandonselaar M, Hengstenberg W, Quail JW, Delbaere LT (1994) The 1.6 A structure of histidine-containing phosphotransfer protein HPr from Streptococcus faecalis. J Mol Biol 236: 1341-1355.
    • (1994) J Mol Biol , vol.236 , pp. 1341-1355
    • Jia, Z.1    Vandonselaar, M.2    Hengstenberg, W.3    Quail, J.W.4    Delbaere, L.T.5
  • 75
    • 0034939369 scopus 로고    scopus 로고
    • Structure of the Bacillus cell fate determinant SpoIIAA in phosphorylated and unphosphorylated forms
    • Seavers PR, Lewis RJ, Brannigan JA, Verschueren KH, Murshudov GN, et al. (2001) Structure of the Bacillus cell fate determinant SpoIIAA in phosphorylated and unphosphorylated forms. Structure 9: 605-614.
    • (2001) Structure , vol.9 , pp. 605-614
    • Seavers, P.R.1    Lewis, R.J.2    Brannigan, J.A.3    Verschueren, K.H.4    Murshudov, G.N.5
  • 76
    • 0035902464 scopus 로고    scopus 로고
    • BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: Structure of a BeF(3)(-) complex with phosphoserine phosphatase
    • U S A
    • Cho H, Wang W, Kim R, Yokota H, Damo S, et al. (2001) BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: Structure of a BeF(3)(-) complex with phosphoserine phosphatase. Proc Natl Acad Sci U S A 98: 8525-8530.
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 8525-8530
    • Cho, H.1    Wang, W.2    Kim, R.3    Yokota, H.4    Damo, S.5
  • 77
    • 0036301579 scopus 로고    scopus 로고
    • Structural characterization of the reaction pathway in phosphoserine phosphatase: Crystallographic "snapshots" of intermediate states
    • Wang W, Cho HS, Kim R, Jancarik J, Yokota H, et al. (2002) Structural characterization of the reaction pathway in phosphoserine phosphatase: Crystallographic "snapshots" of intermediate states. J Mol Biol 319: 421-431.
    • (2002) J Mol Biol , vol.319 , pp. 421-431
    • Wang, W.1    Cho, H.S.2    Kim, R.3    Jancarik, J.4    Yokota, H.5
  • 78
    • 0030866897 scopus 로고    scopus 로고
    • Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
    • Canagarajah BJ, Khokhlatchev A, Cobb MH, Goldsmith EJ (1997) Activation mechanism of the MAP kinase ERK2 by dual phosphorylation. Cell 90: 859-869.
    • (1997) Cell , vol.90 , pp. 859-869
    • Canagarajah, B.J.1    Khokhlatchev, A.2    Cobb, M.H.3    Goldsmith, E.J.4
  • 79
    • 0028157664 scopus 로고
    • Atomic structure of the MAP kinase ERK2 at 2.3 A resolution
    • Zhang F, Strand A, Robbins D, Cobb MH, Goldsmith EJ (1994) Atomic structure of the MAP kinase ERK2 at 2.3 A resolution. Nature 367: 704-711.
    • (1994) Nature , vol.367 , pp. 704-711
    • Zhang, F.1    Strand, A.2    Robbins, D.3    Cobb, M.H.4    Goldsmith, E.J.5
  • 81
    • 0036174748 scopus 로고    scopus 로고
    • Crystal structure of PMM/PGM: An enzyme in the biosynthetic pathway of P. aeruginosa virulence factors
    • Regni C, Tipton PA, Beamer LJ (2002) Crystal structure of PMM/PGM: An enzyme in the biosynthetic pathway of P. aeruginosa virulence factors. Structure 10: 269-279.
    • (2002) Structure , vol.10 , pp. 269-279
    • Regni, C.1    Tipton, P.A.2    Beamer, L.J.3
  • 82
    • 0033567706 scopus 로고    scopus 로고
    • The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation
    • Bellon S, Fitzgibbon MJ, Fox T, Hsiao HM, Wilson KP (1999) The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation. Structure Fold Des 7: 1057-1065.
    • (1999) Structure Fold Des , vol.7 , pp. 1057-1065
    • Bellon, S.1    Fitzgibbon, M.J.2    Fox, T.3    Hsiao, H.M.4    Wilson, K.P.5
  • 83
    • 0037008092 scopus 로고    scopus 로고
    • Caught in the act: The structure of phosphorylated beta-phosphoglucomutase from Lactococcus lactis
    • Lahiri SD, Zhang G, Dunaway-Mariano D, Allen KN (2002) Caught in the act: The structure of phosphorylated beta-phosphoglucomutase from Lactococcus lactis. Biochemistry 41: 8351-8359.
    • (2002) Biochemistry , vol.41 , pp. 8351-8359
    • Lahiri, S.D.1    Zhang, G.2    Dunaway-Mariano, D.3    Allen, K.N.4
  • 84
    • 16144364951 scopus 로고    scopus 로고
    • Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation
    • Yamaguchi H, Hendrickson WA (1996) Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation. Nature 384: 484-489.
    • (1996) Nature , vol.384 , pp. 484-489
    • Yamaguchi, H.1    Hendrickson, W.A.2


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