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Volumn 391, Issue 1, 2009, Pages 136-148

Structural Characterization of the Natively Unfolded N-Terminal Domain of Human c-Src Kinase: Insights into the Role of Phosphorylation of the Unique Domain

Author keywords

c Src kinase; natively unfolded domain; NMR; phosphorylation

Indexed keywords

PROTEIN SH4; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG;

EID: 67749121986     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.06.018     Document Type: Article
Times cited : (66)

References (86)
  • 1
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of src
    • Brown M.T., and Cooper J.A. Regulation, substrates and functions of src. Biochim. Biophys. Acta 1287 (1996) 121-149
    • (1996) Biochim. Biophys. Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 2
    • 0035374609 scopus 로고    scopus 로고
    • The hunting of the Src
    • Martin G.S. The hunting of the Src. Nat. Rev. 2 (2001) 467-475
    • (2001) Nat. Rev. , vol.2 , pp. 467-475
    • Martin, G.S.1
  • 3
    • 2942618768 scopus 로고    scopus 로고
    • A renaissance for SRC
    • Yeatman T.J. A renaissance for SRC. Nat. Rev. 4 (2004) 470-480
    • (2004) Nat. Rev. , vol.4 , pp. 470-480
    • Yeatman, T.J.1
  • 4
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • Thomas S.M., and Brugge J.S. Cellular functions regulated by Src family kinases. Annu. Rev. Cell Dev. Biol. 13 (1997) 513-609
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 5
    • 7944236785 scopus 로고    scopus 로고
    • Src family kinases, key regulators of signal transduction
    • Parsons S.J., and Parsons J.T. Src family kinases, key regulators of signal transduction. Oncogene 23 (2004) 7906-7909
    • (2004) Oncogene , vol.23 , pp. 7906-7909
    • Parsons, S.J.1    Parsons, J.T.2
  • 6
    • 34250804789 scopus 로고    scopus 로고
    • Rapid trafficking of c-Src, a non-palmitoylated Src-family kinase, between the plasma membrane and late endosomes/lysosomes
    • Kasahara K., Nakayama Y., Kihara A., Matsuda D., Ikeda K., Kuga T., et al. Rapid trafficking of c-Src, a non-palmitoylated Src-family kinase, between the plasma membrane and late endosomes/lysosomes. Exp. Cell Res. 313 (2007) 2651-2666
    • (2007) Exp. Cell Res. , vol.313 , pp. 2651-2666
    • Kasahara, K.1    Nakayama, Y.2    Kihara, A.3    Matsuda, D.4    Ikeda, K.5    Kuga, T.6
  • 7
    • 0025138727 scopus 로고
    • The src protein contains multiple domains for specific attachment to membranes
    • Kaplan J.M., Varmus H.E., and Bishop J.M. The src protein contains multiple domains for specific attachment to membranes. Mol. Cell. Biol. 10 (1990) 1000-1009
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1000-1009
    • Kaplan, J.M.1    Varmus, H.E.2    Bishop, J.M.3
  • 8
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh M.D. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1451 (1999) 1-16
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 10
    • 0030849446 scopus 로고    scopus 로고
    • The unique domain as the site on Lyn kinase for its constitutive association with the high affinity receptor for IgE
    • Vonakis B.M., Chen H., Haleem-Smith H., and Metzger H. The unique domain as the site on Lyn kinase for its constitutive association with the high affinity receptor for IgE. J. Biol. Chem. 272 (1997) 24072-24080
    • (1997) J. Biol. Chem. , vol.272 , pp. 24072-24080
    • Vonakis, B.M.1    Chen, H.2    Haleem-Smith, H.3    Metzger, H.4
  • 11
    • 0030939784 scopus 로고    scopus 로고
    • Intrinsic signals in the unique domain target p56(lck) to the plasma membrane independently of CD4
    • Bijlmakers M.-J., Isobe-Nakamura M., Ruddock L.J., and Marsh M. Intrinsic signals in the unique domain target p56(lck) to the plasma membrane independently of CD4. J. Cell Biol. 137 (1997) 1029-1040
    • (1997) J. Cell Biol. , vol.137 , pp. 1029-1040
    • Bijlmakers, M.-J.1    Isobe-Nakamura, M.2    Ruddock, L.J.3    Marsh, M.4
  • 12
    • 0035860690 scopus 로고    scopus 로고
    • Palmitoylation of caveolin-1 at a single site (Cys-156) controls its coupling to the c-Src tyrosine kinase: targeting of dually acylated molecules (GPI-linked, transmembrane, or cytoplasmic) to caveolae effectively uncouples c-Src and caveolin-1 (TYR-14)
    • Lee H., Woodman S.E., Engelman J.A., Voloente D., Galbiati F., Kaufman H.L., et al. Palmitoylation of caveolin-1 at a single site (Cys-156) controls its coupling to the c-Src tyrosine kinase: targeting of dually acylated molecules (GPI-linked, transmembrane, or cytoplasmic) to caveolae effectively uncouples c-Src and caveolin-1 (TYR-14). J. Biol. Chem. 276 (2001) 35150-35158
    • (2001) J. Biol. Chem. , vol.276 , pp. 35150-35158
    • Lee, H.1    Woodman, S.E.2    Engelman, J.A.3    Voloente, D.4    Galbiati, F.5    Kaufman, H.L.6
  • 15
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri F., Moarefi I., and Kuriyan J. Crystal structure of the Src family tyrosine kinase Hck. Nature 385 (1997) 602-609
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 16
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu W., Harrison S.C., and Eck M.J. Three-dimensional structure of the tyrosine kinase c-Src. Nature 385 (1997) 595-602
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 17
    • 0033001789 scopus 로고    scopus 로고
    • Crystal structures of c-Src reveal features of its autoinhibitory mechanism
    • Xu W., Doshi A., Lei M., Eck M.J., and Harrison S.C. Crystal structures of c-Src reveal features of its autoinhibitory mechanism. Mol. Cell 3 (1999) 629-638
    • (1999) Mol. Cell , vol.3 , pp. 629-638
    • Xu, W.1    Doshi, A.2    Lei, M.3    Eck, M.J.4    Harrison, S.C.5
  • 18
    • 20444399897 scopus 로고    scopus 로고
    • The crystal structure of a c-Src complex in an active conformation suggests possible steps in c-Src activation
    • Cowan-Jacob S.W., Fendrich G., Manley P.W., Jahnke W., Fabbro D., Liebetanz J., and Meyer T. The crystal structure of a c-Src complex in an active conformation suggests possible steps in c-Src activation. Structure 13 (2005) 861-871
    • (2005) Structure , vol.13 , pp. 861-871
    • Cowan-Jacob, S.W.1    Fendrich, G.2    Manley, P.W.3    Jahnke, W.4    Fabbro, D.5    Liebetanz, J.6    Meyer, T.7
  • 19
    • 38549146411 scopus 로고    scopus 로고
    • Structural characterization of the active and inactive states of Src kinase in solution by small angle X-ray scattering
    • Bernadó P., Pérez Y., Svergun D.I., and Pons M. Structural characterization of the active and inactive states of Src kinase in solution by small angle X-ray scattering. J. Mol. Biol. 376 (2008) 492-505
    • (2008) J. Mol. Biol. , vol.376 , pp. 492-505
    • Bernadó, P.1    Pérez, Y.2    Svergun, D.I.3    Pons, M.4
  • 21
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: a point where biology waits for physics
    • Uversky V.N. Natively unfolded proteins: a point where biology waits for physics. Protein Sci. 11 (2002) 739-756
    • (2002) Protein Sci. , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 22
    • 0030980926 scopus 로고    scopus 로고
    • The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28
    • Daughdrill G.W., Chadsey M.S., Karlinsey J.E., Hughes K.T., and Dahlquist F.W. The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28. Nat. Struct. Biol. 4 (1997) 285-291
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 285-291
    • Daughdrill, G.W.1    Chadsey, M.S.2    Karlinsey, J.E.3    Hughes, K.T.4    Dahlquist, F.W.5
  • 23
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson H.J., and Wright P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. 6 (2005) 197-208
    • (2005) Nat. Rev. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 25
    • 33748280715 scopus 로고    scopus 로고
    • Abundance of intrinsic disorder in protein associated with cardiovascular disease
    • Cheng Y., LeGall T., Oldfield C.J., Dunker A.K., and Uversky V.N. Abundance of intrinsic disorder in protein associated with cardiovascular disease. Biochemistry 45 (2006) 10448-10460
    • (2006) Biochemistry , vol.45 , pp. 10448-10460
    • Cheng, Y.1    LeGall, T.2    Oldfield, C.J.3    Dunker, A.K.4    Uversky, V.N.5
  • 27
    • 33847783298 scopus 로고    scopus 로고
    • Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins
    • Xie H., Vucetic S., Iakoucheva L.M., Oldfield C.J., Dunker A.K., Obradovic Z., and Uversky V.N. Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins. J. Proteome Res. 6 (2007) 1917-1932
    • (2007) J. Proteome Res. , vol.6 , pp. 1917-1932
    • Xie, H.1    Vucetic, S.2    Iakoucheva, L.M.3    Oldfield, C.J.4    Dunker, A.K.5    Obradovic, Z.6    Uversky, V.N.7
  • 29
    • 0034721860 scopus 로고    scopus 로고
    • Modulation of the catalytic activity of the Src family tyrosine kinase Hck by autophosphorylation at a novel site in the unique domain
    • Williamson N.A., Scholz G., Jaworowski A., Wettenhall R.E., Dunn A.R., Cheng H.C., and Johnson T.M. Modulation of the catalytic activity of the Src family tyrosine kinase Hck by autophosphorylation at a novel site in the unique domain. J. Biol. Chem. 275 (2000) 33353-33364
    • (2000) J. Biol. Chem. , vol.275 , pp. 33353-33364
    • Williamson, N.A.1    Scholz, G.2    Jaworowski, A.3    Wettenhall, R.E.4    Dunn, A.R.5    Cheng, H.C.6    Johnson, T.M.7
  • 30
    • 0028983399 scopus 로고
    • Modification of Ser59 in the unique N-terminal region of tyrosine kinase p56lck regulates specificity of its Src homology 2 domain
    • Joung I., Kim T., Stolz L.A., Payne G., Winkler D.G., Walsh C.T., et al. Modification of Ser59 in the unique N-terminal region of tyrosine kinase p56lck regulates specificity of its Src homology 2 domain. Proc. Natl Acad. Sci. USA 92 (1995) 5778-5782
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5778-5782
    • Joung, I.1    Kim, T.2    Stolz, L.A.3    Payne, G.4    Winkler, D.G.5    Walsh, C.T.6
  • 31
    • 12344333887 scopus 로고    scopus 로고
    • PKA phosphorylation of Src mediates Rap1 activation in NGF and cAMP signaling in PC12 cells
    • Obara Y., Labudda K., Dillon T.J., and Stork P.J.S. PKA phosphorylation of Src mediates Rap1 activation in NGF and cAMP signaling in PC12 cells. J. Cell Sci. 117 (2004) 6085-6094
    • (2004) J. Cell Sci. , vol.117 , pp. 6085-6094
    • Obara, Y.1    Labudda, K.2    Dillon, T.J.3    Stork, P.J.S.4
  • 32
    • 0027337969 scopus 로고
    • Translocation of pp60c-src from the plasma membrane to the cytosol after stimulation by platelet derived growth factor
    • Walker F., deBlaquiere J., and Burgess A.W. Translocation of pp60c-src from the plasma membrane to the cytosol after stimulation by platelet derived growth factor. J. Biol. Chem. 268 (1993) 19552-19558
    • (1993) J. Biol. Chem. , vol.268 , pp. 19552-19558
    • Walker, F.1    deBlaquiere, J.2    Burgess, A.W.3
  • 34
    • 0028171074 scopus 로고
    • Cdc2-mediated modulation of pp60c-src activity
    • Stover D.R., Liebetanz J., and Lydon N.B. Cdc2-mediated modulation of pp60c-src activity. J. Biol. Chem. 269 (1994) 26885-26889
    • (1994) J. Biol. Chem. , vol.269 , pp. 26885-26889
    • Stover, D.R.1    Liebetanz, J.2    Lydon, N.B.3
  • 35
    • 0032754027 scopus 로고    scopus 로고
    • Neuron-specific Cdk5 kinase is responsible for mitosis-independent phosphorylation of c-Src at Ser75 in human Y79 retinoblastoma cells
    • Kato G., and Maeda S. Neuron-specific Cdk5 kinase is responsible for mitosis-independent phosphorylation of c-Src at Ser75 in human Y79 retinoblastoma cells. J. Biochem. 126 (1999) 957-961
    • (1999) J. Biochem. , vol.126 , pp. 957-961
    • Kato, G.1    Maeda, S.2
  • 36
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded proteins and protein folding studied by NMR
    • Dyson H.J., and Wright P.E. Unfolded proteins and protein folding studied by NMR. Chem. Rev. 104 (2004) 3607-3622
    • (2004) Chem. Rev. , vol.104 , pp. 3607-3622
    • Dyson, H.J.1    Wright, P.E.2
  • 37
    • 41449109638 scopus 로고    scopus 로고
    • Conformational distributions of unfolded polypeptides from novel NMR techniques
    • Meier S., Blackledge M., and Grzesiek S. Conformational distributions of unfolded polypeptides from novel NMR techniques. J. Chem. Phys. 128 (2008) 052204
    • (2008) J. Chem. Phys. , vol.128 , pp. 052204
    • Meier, S.1    Blackledge, M.2    Grzesiek, S.3
  • 38
    • 33645452144 scopus 로고    scopus 로고
    • Protonless NMR experiments for sequence-specific assignment of backbone nuclei in unfolded proteins
    • Bermel W., Bertini I., Felli I.C., Lee Y.M., Luchinat C., and Pierattelli R. Protonless NMR experiments for sequence-specific assignment of backbone nuclei in unfolded proteins. J. Am. Chem. Soc. 128 (2006) 3918-3919
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 3918-3919
    • Bermel, W.1    Bertini, I.2    Felli, I.C.3    Lee, Y.M.4    Luchinat, C.5    Pierattelli, R.6
  • 40
    • 33745042221 scopus 로고    scopus 로고
    • Alanine check points in HNN and HN(C)N spectra
    • Chatterjee A., Kumar A., and Hosur R.V. Alanine check points in HNN and HN(C)N spectra. J. Magn. Reson. 181 (2006) 21-28
    • (2006) J. Magn. Reson. , vol.181 , pp. 21-28
    • Chatterjee, A.1    Kumar, A.2    Hosur, R.V.3
  • 43
    • 3242789489 scopus 로고    scopus 로고
    • Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings
    • Mohana-Borges R., Goto N.K., Kroon G.J.A., Dyson H.J., and Wright P.E. Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings. J. Mol. Biol. 340 (2004) 1131-1142
    • (2004) J. Mol. Biol. , vol.340 , pp. 1131-1142
    • Mohana-Borges, R.1    Goto, N.K.2    Kroon, G.J.A.3    Dyson, H.J.4    Wright, P.E.5
  • 44
    • 24944542708 scopus 로고    scopus 로고
    • Statistical coil model of the unfolded state: resolving the reconciliation problem
    • Jha A.K., Colubri A., Freed K.F., and Sosnick T.R. Statistical coil model of the unfolded state: resolving the reconciliation problem. Proc. Natl Acad. Sci. USA 102 (2005) 13099-13104
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 13099-13104
    • Jha, A.K.1    Colubri, A.2    Freed, K.F.3    Sosnick, T.R.4
  • 45
  • 46
    • 29844433240 scopus 로고    scopus 로고
    • Defining long-range order and local disorder in native α-synuclein using residual dipolar couplings
    • Bernadó P., Bertoncini C.W., Griesinger C., Zweckstetter M., and Blackledge M. Defining long-range order and local disorder in native α-synuclein using residual dipolar couplings. J. Am. Chem. Soc. 127 (2005) 17968-17969
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 17968-17969
    • Bernadó, P.1    Bertoncini, C.W.2    Griesinger, C.3    Zweckstetter, M.4    Blackledge, M.5
  • 47
    • 34247499863 scopus 로고    scopus 로고
    • Highly populated turn conformations in natively unfolded Tau protein identified from residual dipolar couplings and molecular simulations
    • Mukrasch M.D., Markwick P., Biernat J., von Bergen M., Bernadó P., Griesinger C., et al. Highly populated turn conformations in natively unfolded Tau protein identified from residual dipolar couplings and molecular simulations. J. Am. Chem. Soc. 129 (2007) 5235-5243
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5235-5243
    • Mukrasch, M.D.1    Markwick, P.2    Biernat, J.3    von Bergen, M.4    Bernadó, P.5    Griesinger, C.6
  • 48
    • 45749102885 scopus 로고    scopus 로고
    • Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: application to the molecular recognition element of Sendai virus nucleoprotein
    • Jensen M.R., Houben K., Lescop E., Blanchard L., Ruigrok R.W.H., and Blackledge M. Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: application to the molecular recognition element of Sendai virus nucleoprotein. J. Am. Chem. Soc. 130 (2008) 8055-8061
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 8055-8061
    • Jensen, M.R.1    Houben, K.2    Lescop, E.3    Blanchard, L.4    Ruigrok, R.W.H.5    Blackledge, M.6
  • 49
    • 0031585990 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of Staphyloccocal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels
    • Gillespie J.R., and Shortle D. Characterization of long-range structure in the denatured state of Staphyloccocal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels. J. Mol. Biol. 268 (1997) 158-169
    • (1997) J. Mol. Biol. , vol.268 , pp. 158-169
    • Gillespie, J.R.1    Shortle, D.2
  • 50
    • 0031585992 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of Staphyloccocal nuclease. II. Paramagnetic relaxation enhancement by nitroxide spin labels
    • Gillespie J.R., and Shortle D. Characterization of long-range structure in the denatured state of Staphyloccocal nuclease. II. Paramagnetic relaxation enhancement by nitroxide spin labels. J. Mol. Biol. 268 (1997) 170-184
    • (1997) J. Mol. Biol. , vol.268 , pp. 170-184
    • Gillespie, J.R.1    Shortle, D.2
  • 53
    • 44049097465 scopus 로고    scopus 로고
    • Modeling transient collapsed states of an unfolded protein to provide insights into early folding events
    • Felitsky D.J., Lietzow M.A., Dyson H.J., and Wright P.E. Modeling transient collapsed states of an unfolded protein to provide insights into early folding events. Proc. Natl Acad. Sci. USA 105 (2008) 6278-6283
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 6278-6283
    • Felitsky, D.J.1    Lietzow, M.A.2    Dyson, H.J.3    Wright, P.E.4
  • 54
    • 0141654999 scopus 로고    scopus 로고
    • A zinc clasp structure tethers Lck to T cell coreceptors CD4 and CD8
    • Kim P.V., Sun Z.-Y.J., Blacklow S.C., Wagner G., and Eck M.J. A zinc clasp structure tethers Lck to T cell coreceptors CD4 and CD8. Science 301 (2003) 1725-1728
    • (2003) Science , vol.301 , pp. 1725-1728
    • Kim, P.V.1    Sun, Z.-Y.J.2    Blacklow, S.C.3    Wagner, G.4    Eck, M.J.5
  • 55
    • 3042580029 scopus 로고    scopus 로고
    • Structure determination of human Lck unique and SH3 domains by nuclear magnetic resonance spectroscopy
    • Briese L., and Willbold D. Structure determination of human Lck unique and SH3 domains by nuclear magnetic resonance spectroscopy. BMC Struct. Biol. 3 (2003) 1-17
    • (2003) BMC Struct. Biol. , vol.3 , pp. 1-17
    • Briese, L.1    Willbold, D.2
  • 56
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart D.S., Sykes B.D., and Richards F.M. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222 (1991) 311-333
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 57
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigation of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigation of nearest-neighbor effects. J. Biomol. NMR 5 (1994) 67-81
    • (1994) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 58
    • 33947362842 scopus 로고    scopus 로고
    • Amino acid bulkiness defines the local conformations and dynamics of natively unfolded α-synuclein and tau
    • Cho M.-K., Kim H.-Y., Bernadó P., Fernández C.O., Blackledge M., and Zweckstetter M. Amino acid bulkiness defines the local conformations and dynamics of natively unfolded α-synuclein and tau. J. Am. Chem. Soc. 129 (2007) 3032-3033
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 3032-3033
    • Cho, M.-K.1    Kim, H.-Y.2    Bernadó, P.3    Fernández, C.O.4    Blackledge, M.5    Zweckstetter, M.6
  • 59
    • 34547766676 scopus 로고    scopus 로고
    • Mapping the conformational landscape of urea-denatured ubiquitin using residual dipolar couplings
    • Meier S., Grzesiek S., and Blackledge M. Mapping the conformational landscape of urea-denatured ubiquitin using residual dipolar couplings. J. Am. Chem. Soc. 129 (2007) 9799-9807
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 9799-9807
    • Meier, S.1    Grzesiek, S.2    Blackledge, M.3
  • 60
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiological conditions?
    • Uversky V.N., Gillespie J.R., and Fink A.L. Why are "natively unfolded" proteins unstructured under physiological conditions?. Proteins: Struct., Funct., Genet. 41 (2000) 415-427
    • (2000) Proteins: Struct., Funct., Genet. , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 61
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: web server for the prediction of intrinsically unstructured regions of proteins base don estimated energy content
    • Dosztanyi Z., Csizmok V., Tompa P., and Simon I. IUPred: web server for the prediction of intrinsically unstructured regions of proteins base don estimated energy content. Bioinformatics 21 (2005) 3433-3434
    • (2005) Bioinformatics , vol.21 , pp. 3433-3434
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 62
    • 24744453057 scopus 로고    scopus 로고
    • Striped sheets and protein contact prediction
    • MacCallum R.M. Striped sheets and protein contact prediction. Bioinformatics 20 (2004) i224-i231
    • (2004) Bioinformatics , vol.20
    • MacCallum, R.M.1
  • 65
    • 0023755783 scopus 로고
    • Platelet-derived growth factor induces multisite phosphorylation of pp60-cSrc and increases its protein-tyrosine kinase activity
    • Gould K.L., and Hunter T. Platelet-derived growth factor induces multisite phosphorylation of pp60-cSrc and increases its protein-tyrosine kinase activity. Mol. Cell. Biol. 8 (1988) 3345-3356
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3345-3356
    • Gould, K.L.1    Hunter, T.2
  • 67
    • 0033579464 scopus 로고    scopus 로고
    • Sequence- and structure-based prediction of eukaryotic protein phosphorylation sites
    • Blom N., Gammeltoft S., and Brunak S. Sequence- and structure-based prediction of eukaryotic protein phosphorylation sites. J. Mol. Biol. 294 (1999) 1351-1362
    • (1999) J. Mol. Biol. , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 72
    • 21744436606 scopus 로고    scopus 로고
    • Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region
    • Pufall M.A., Lee G.M., Nelson M.L., Kang H.S., Velyvis A., Kay L.E., et al. Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region. Science 309 (2005) 142-145
    • (2005) Science , vol.309 , pp. 142-145
    • Pufall, M.A.1    Lee, G.M.2    Nelson, M.L.3    Kang, H.S.4    Velyvis, A.5    Kay, L.E.6
  • 73
    • 0032530369 scopus 로고    scopus 로고
    • Engagement of T cell receptor triggers its recruitment to low-density detergent-insoluble membrana domains
    • Montixi C., Langlet C., Bernard A.-M., Thimonier J., Dubois C., Wurbel M.-A., et al. Engagement of T cell receptor triggers its recruitment to low-density detergent-insoluble membrana domains. EMBO J. 17 (1998) 5334-5348
    • (1998) EMBO J. , vol.17 , pp. 5334-5348
    • Montixi, C.1    Langlet, C.2    Bernard, A.-M.3    Thimonier, J.4    Dubois, C.5    Wurbel, M.-A.6
  • 74
    • 0032882619 scopus 로고    scopus 로고
    • Translocation of tyrosine-phosphorylated TCRζ chain to glycolipid-enriched membrane domains upon T cell activation
    • Kosugi A., Saitoh S.-I., Noda S., Yasuda K., Hayashi F., Ogata M., and Hamaoka T. Translocation of tyrosine-phosphorylated TCRζ chain to glycolipid-enriched membrane domains upon T cell activation. Int. Immunol. 11 (1999) 1395-1401
    • (1999) Int. Immunol. , vol.11 , pp. 1395-1401
    • Kosugi, A.1    Saitoh, S.-I.2    Noda, S.3    Yasuda, K.4    Hayashi, F.5    Ogata, M.6    Hamaoka, T.7
  • 75
    • 33846671062 scopus 로고    scopus 로고
    • Tunning bulk electrostatics to regulate protein function
    • Serber Z., and Ferrell Jr. J.E. Tunning bulk electrostatics to regulate protein function. Cell 128 (2007) 441-444
    • (2007) Cell , vol.128 , pp. 441-444
    • Serber, Z.1    Ferrell Jr., J.E.2
  • 76
    • 33846686408 scopus 로고    scopus 로고
    • A mechanism for cell-cycle regulation of MAP kinase in a yeast differentiation pathway
    • Strickfaden S.C., Winters M.J., Ben-Ari G., Lamson R.E., Tyers M., and Pryciak P.M. A mechanism for cell-cycle regulation of MAP kinase in a yeast differentiation pathway. Cell 128 (2007) 519-531
    • (2007) Cell , vol.128 , pp. 519-531
    • Strickfaden, S.C.1    Winters, M.J.2    Ben-Ari, G.3    Lamson, R.E.4    Tyers, M.5    Pryciak, P.M.6
  • 77
    • 28844471980 scopus 로고    scopus 로고
    • 13C direct detection experiments, including extension to the third dimension, to perform the complete assignment of proteins
    • 13C direct detection experiments, including extension to the third dimension, to perform the complete assignment of proteins. J. Magn. Reson. 178 (2006) 56-64
    • (2006) J. Magn. Reson. , vol.178 , pp. 56-64
    • Bermel, W.1    Bertini, I.2    Felli, I.C.3    Kümmerle, R.4    Pierattelli, R.5
  • 78
    • 0004040543 scopus 로고    scopus 로고
    • University of California, San Francisco, CA
    • Goddard T.D., and Kneller D.G. SPARKY 3 (2003), University of California, San Francisco, CA
    • (2003) SPARKY 3
    • Goddard, T.D.1    Kneller, D.G.2
  • 81
    • 0032042263 scopus 로고    scopus 로고
    • Measurement of J and dipolar couplings from simplified two-dimensional spectra
    • Ottiger M., Delaglio F., and Bax A. Measurement of J and dipolar couplings from simplified two-dimensional spectra. J. Magn. Reson. 131 (1998) 373-378
    • (1998) J. Magn. Reson. , vol.131 , pp. 373-378
    • Ottiger, M.1    Delaglio, F.2    Bax, A.3
  • 82
    • 0037551646 scopus 로고    scopus 로고
    • Alignment of biological nacromolecules in novel nonionic liquid crystalline media for NMR experiments
    • Rückert M., and Otting G. Alignment of biological nacromolecules in novel nonionic liquid crystalline media for NMR experiments. J. Am. Chem. Soc. 122 (2000) 7793-7797
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 7793-7797
    • Rückert, M.1    Otting, G.2
  • 83
    • 0034685436 scopus 로고    scopus 로고
    • Prediction of sterically induced alignment in a dilute liquid crystalline phase: aid to protein structure determination by NMR
    • Zweckstetter M., and Bax A. Prediction of sterically induced alignment in a dilute liquid crystalline phase: aid to protein structure determination by NMR. J. Am. Chem. Soc. 122 (2000) 3791-3792
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 3791-3792
    • Zweckstetter, M.1    Bax, A.2
  • 84
    • 0036438881 scopus 로고    scopus 로고
    • Transient structure formation in unfolded acyl-coenzyme A-binding protein observed by site-directed spin labelling
    • Teilum K., Kragelund B.B., and Poulsen F.M. Transient structure formation in unfolded acyl-coenzyme A-binding protein observed by site-directed spin labelling. J. Mol. Biol. 324 (2002) 349-357
    • (2002) J. Mol. Biol. , vol.324 , pp. 349-357
    • Teilum, K.1    Kragelund, B.B.2    Poulsen, F.M.3
  • 85
    • 0024853292 scopus 로고
    • Spin labeling of proteins
    • Kosen P.A. Spin labeling of proteins. Methods Enzymol. 177 (1989) 86-121
    • (1989) Methods Enzymol. , vol.177 , pp. 86-121
    • Kosen, P.A.1
  • 86
    • 0034625121 scopus 로고    scopus 로고
    • Utilization of site-directed spin labeling and high resolution heteronuclear nuclear magnetic resonance for global Fol. Determination of large proteins with limited nuclear Overhauser effect data
    • Battiste J.L., and Wagner G. Utilization of site-directed spin labeling and high resolution heteronuclear nuclear magnetic resonance for global Fol. Determination of large proteins with limited nuclear Overhauser effect data. Biochemistry 39 (2000) 5355-5365
    • (2000) Biochemistry , vol.39 , pp. 5355-5365
    • Battiste, J.L.1    Wagner, G.2


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