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Volumn 19, Issue 11, 2005, Pages 1389-1395

The folding energy landscape and phosphorylation: Modeling the conformational switch of the NFAT regulatory domain

Author keywords

Conformational switch; Contact map PCA; Effective charge; Multi phosphorylation; Transcription factor

Indexed keywords

TRANSCRIPTION FACTOR NFAT;

EID: 24644442164     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.04-3590hyp     Document Type: Article
Times cited : (45)

References (27)
  • 1
    • 0035478709 scopus 로고    scopus 로고
    • Analysis of phosphorylated proteins and peptides by mass spectrometry
    • McLachlin, D. T., and Chait, B. T. (2001) Analysis of phosphorylated proteins and peptides by mass spectrometry. Curr. Opin. Chem. Biol. 5, 591-602
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 591-602
    • McLachlin, D.T.1    Chait, B.T.2
  • 2
    • 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., and 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
  • 3
    • 0035970301 scopus 로고    scopus 로고
    • Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasmic tail detected by NMR
    • Ramelot, T. A., and Nicholson, L. K. (2001) Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasmic tail detected by NMR. J. Mol. Biol. 307, 871-884
    • (2001) J. Mol. Biol. , vol.307 , pp. 871-884
    • Ramelot, T.A.1    Nicholson, L.K.2
  • 4
    • 0042591409 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the well packed ephrinb cytoplasmic beta-hairpin for reverse signaling - Structural consequences and binding properties
    • Song, J. (2003) Tyrosine phosphorylation of the well packed ephrinb cytoplasmic beta-hairpin for reverse signaling - structural consequences and binding properties. J. Biol. Chem. 278, 24714-24720
    • (2003) J. Biol. Chem. , vol.278 , pp. 24714-24720
    • Song, J.1
  • 5
    • 0035937549 scopus 로고    scopus 로고
    • Flipping a switch
    • Buck, M., and Rosen, M. K. (2001) Flipping a switch. Science 291, 2329-2330
    • (2001) Science , vol.291 , pp. 2329-2330
    • Buck, M.1    Rosen, M.K.2
  • 6
    • 0035937443 scopus 로고    scopus 로고
    • Two-state allosteric behavior in a single-domain signaling protein
    • Volkman, B. F., Lipson, D., Wemmer, D. E., and Kern, D. (2001) Two-state allosteric behavior in a single-domain signaling protein. Science 291, 2429-2433
    • (2001) Science , vol.291 , pp. 2429-2433
    • Volkman, B.F.1    Lipson, D.2    Wemmer, D.E.3    Kern, D.4
  • 7
    • 0032922002 scopus 로고    scopus 로고
    • Phosphobase, a database of phosphorylation sites: Release 2.0
    • Kreegipuu, A., Blom, N., and 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
  • 8
    • 0036901003 scopus 로고    scopus 로고
    • Multisite phosphorylation provides sophisticated regulation of transcription factors
    • Holmberg, C., Tran, S., Eriksson, J., and Sistonen, L. (2002) Multisite phosphorylation provides sophisticated regulation of transcription factors. Trends Biochem. Sci. 27, 619-627
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 619-627
    • Holmberg, C.1    Tran, S.2    Eriksson, J.3    Sistonen, L.4
  • 10
    • 0141483523 scopus 로고    scopus 로고
    • Transcriptional regulation by calcium, calcineurin, and NFAT
    • Hogan, P. G., Chen, L., Nardone, J., and Rao, A. (2003) Transcriptional regulation by calcium, calcineurin, and NFAT. Genes Dev. 17, 2205-2232
    • (2003) Genes Dev. , vol.17 , pp. 2205-2232
    • Hogan, P.G.1    Chen, L.2    Nardone, J.3    Rao, A.4
  • 11
    • 0036234543 scopus 로고    scopus 로고
    • NFAT signaling: Choreographing the social lives of cells
    • Crabtree, G. R., and Olson, E. N. (2002) NFAT signaling: choreographing the social lives of cells. Cell 109, S67-S79
    • (2002) Cell , vol.109
    • Crabtree, G.R.1    Olson, E.N.2
  • 12
    • 0034691195 scopus 로고    scopus 로고
    • A second calcineurin binding site on the NFAT regulatory domain
    • Park, S., Uesugi, M., and Verdine, G. (2000) A second calcineurin binding site on the NFAT regulatory domain. Proc. Natl. Acad. Sci. USA 97, 7130-7135
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7130-7135
    • Park, S.1    Uesugi, M.2    Verdine, G.3
  • 13
    • 0035913754 scopus 로고    scopus 로고
    • Atomistic Brownian dynamics simulation of peptide phosphorylation
    • Shen, T., Wong, C., and McCammon, J. (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.1    Wong, C.2    McCammon, J.3
  • 14
    • 0035327183 scopus 로고    scopus 로고
    • Evaluating protein structure-prediction schemes using energy landscape theory
    • Eastwood, M., Hardin, C., Luthey-Schulten, Z., and Wolynes, P. G. (2001) Evaluating protein structure-prediction schemes using energy landscape theory. IBM J. Res. Dev. 45, 475-497
    • (2001) IBM J. Res. Dev. , vol.45 , pp. 475-497
    • Eastwood, M.1    Hardin, C.2    Luthey-Schulten, Z.3    Wolynes, P.G.4
  • 15
    • 0001683768 scopus 로고
    • Toward protein tertiary structure recognition by means of associative memory hamiltonians
    • Friedrichs, M., and Wolynes, P. (1989) Toward protein tertiary structure recognition by means of associative memory hamiltonians. Science 246, 371-373
    • (1989) Science , vol.246 , pp. 371-373
    • Friedrichs, M.1    Wolynes, P.2
  • 16
    • 0026124585 scopus 로고
    • Electrostatics and diffusion of molecules in solution: Simulations with the University of Houston Brownian Dynamics program
    • Davis, M. E., Madura, J. D., Luty, B. A., and McCammon, J. A. (1991) Electrostatics and diffusion of molecules in solution: simulations with the University of Houston Brownian Dynamics program. Comput. Phys. Commun. 62, 187-197
    • (1991) Comput. Phys. Commun. , vol.62 , pp. 187-197
    • Davis, M.E.1    Madura, J.D.2    Luty, B.A.3    McCammon, J.A.4
  • 18
    • 4043171970 scopus 로고    scopus 로고
    • The GB/SA continuum model for solvation. A fast analytical method for the calculation of approximate Born radii
    • Qiu, D., Shenkin, P. S., Hollinger, F. P., and Clark Still, W. (1997) The GB/SA continuum model for solvation. A fast analytical method for the calculation of approximate Born radii. J. Phys. Chem. A 101, 3005-3014
    • (1997) J. Phys. Chem. A , vol.101 , pp. 3005-3014
    • Qiu, D.1    Shenkin, P.S.2    Hollinger, F.P.3    Clark Still, W.4
  • 19
    • 3042524904 scopus 로고
    • A well-behaved electrostatic potential based method using charge restraints for deriving atom in charges: The resp model
    • Bayly, C. I., Cieplak, P., Cornell, W. D., and Kollman, P. A. (1993) A well-behaved electrostatic potential based method using charge restraints for deriving atom in charges: the resp model. J. Phys. Chem. 97, 10269-10280
    • (1993) J. Phys. Chem. , vol.97 , pp. 10269-10280
    • Bayly, C.I.1    Cieplak, P.2    Cornell, W.D.3    Kollman, P.A.4
  • 20
    • 0029895539 scopus 로고    scopus 로고
    • Self-consistently optimized statistical mechanical energy functions for sequence structure alignment
    • Koretke, K. K., Luthey-Schulten, Z., and Wolynes, P. (1996) Self-consistently optimized statistical mechanical energy functions for sequence structure alignment. Protein Sci. 5, 1043-1059
    • (1996) Protein Sci. , vol.5 , pp. 1043-1059
    • Koretke, K.K.1    Luthey-Schulten, Z.2    Wolynes, P.3
  • 21
    • 0032554636 scopus 로고    scopus 로고
    • Role of phosphorylation in determining the backbone dynamics of the serine/threonine-proline motif and pin1 substrate recognition
    • Schutkowski, M., Bernhardt, A., Zhou, X. Z., Shen, M., Reimer, U., Rahfeld, J.-U., Lu, K P., and Fischer, G. (1998) Role of phosphorylation in determining the backbone dynamics of the serine/threonine-proline motif and pin1 substrate recognition. Biochemistry 37, 5566-5575
    • (1998) Biochemistry , vol.37 , pp. 5566-5575
    • Schutkowski, M.1    Bernhardt, A.2    Zhou, X.Z.3    Shen, M.4    Reimer, U.5    Rahfeld, J.-U.6    Lu, K.P.7    Fischer, G.8
  • 22
    • 0027474991 scopus 로고
    • Left-handed polyproline II helices commonly occur in globular proteins
    • Adzhubei, A. A., and Sternberg, M. J. E. (1993) Left-handed polyproline II helices commonly occur in globular proteins. J. Mol. Biol. 229, 472-493
    • (1993) J. Mol. Biol. , vol.229 , pp. 472-493
    • Adzhubei, A.A.1    Sternberg, M.J.E.2
  • 25
    • 0034687712 scopus 로고    scopus 로고
    • Associative memory hamiltonians for structure prediction without homology: Alpha-helical proteins
    • Hardin, C., Eastwood, M. P., Luthey-Schulten, Z., and Wolynes, P. G. (2000) Associative memory hamiltonians for structure prediction without homology: Alpha-helical proteins. Proc. Natl. Acad. Sci. USA 97, 14235-14240
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14235-14240
    • Hardin, C.1    Eastwood, M.P.2    Luthey-Schulten, Z.3    Wolynes, P.G.4
  • 27
    • 0026633117 scopus 로고
    • Natural polypeptides in left-handed helical conformation a circular dichroism study of the linker histones' C-terminal fragments and small beta-endorphin
    • Makarov, A. A., Lobachov, V. M., Adzhubei, I. A., and Esipova, N. G. (1992) Natural polypeptides in left-handed helical conformation a circular dichroism study of the linker histones' C-terminal fragments and small beta-endorphin. FEBS Lett. 306, 63-65
    • (1992) FEBS Lett. , vol.306 , pp. 63-65
    • Makarov, A.A.1    Lobachov, V.M.2    Adzhubei, I.A.3    Esipova, N.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.