메뉴 건너뛰기




Volumn 18, Issue 10, 2011, Pages 966-978

The structural determinations of the leucine zipper coiled-coil domains of the cGMP-dependent protein kinase Iα and its interaction with the myosin binding subunit of the myosin light chains phosphase

Author keywords

CGMP dependent protein kinase; Coiled coil; Myosin binding subunit; NMR; Residual dipolar coupling; Wenxiang diagram

Indexed keywords

CYCLIC GMP DEPENDENT PROTEIN KINASE; CYCLIC GMP DEPENDENT PROTEIN KINASE IALPHA; MYOSIN; MYOSIN LIGHT CHAIN PHOSPHATASE; UNCLASSIFIED DRUG;

EID: 79960617237     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/0929866511107010966     Document Type: Article
Times cited : (82)

References (93)
  • 1
    • 0036479319 scopus 로고    scopus 로고
    • Regulation of cGMP-specific phosphodiesterase (PDE5) phosphorylation in smooth muscle cells
    • DOI 10.1074/jbc.M106562200
    • Rybalkin, S. D.; Rybalkina, I. G.; Feil, R.; Hofmann, F.; Beavo, J. A. Regulation of cGMP-specific phosphodiesterase (PDE5) phosphorylation in smooth muscle cells. J. Biol. Chem., 2002, 277, 3310-3317. (Pubitemid 34953197)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.5 , pp. 3310-3317
    • Rybalkin, S.D.1    Rybalkina, I.G.2    Fei, R.3    Hofmann, F.4    Beavo, J.A.5
  • 2
    • 0033584786 scopus 로고    scopus 로고
    • Regulation of Myosin Phosphatase by a Specific Interaction with cGMP-Dependent Protein Kinase I[alpha]
    • Surks, H. K.; Mochizuki, N.; Kasai, Y.; Georgescu, S. P.; Tang, K. M.; Ito, M.; Lincoln, T. M.; Mendelsohn, M. E. Regulation of Myosin Phosphatase by a Specific Interaction with cGMP-Dependent Protein Kinase I[alpha]. Science, 1999, 286, 1583-1587.
    • (1999) Science , vol.286 , pp. 1583-1587
    • Surks, H.K.1    Mochizuki, N.2    Kasai, Y.3    Georgescu, S.P.4    Tang, K.M.5    Ito, M.6    Lincoln, T.M.7    Mendelsohn, M.E.8
  • 5
    • 0037415730 scopus 로고    scopus 로고
    • PDE5 is converted to an activated state upon cGMP binding to the GAF A domain
    • DOI 10.1093/emboj/cdg051
    • Rybalkin S. D.; Rybalkina, I. G.; Shimizu, A. M., Tang, X. B.; Beavo, J. A. PDE5 is converted to an activated state upon cGMP binding to the GAF A domain. EMBO J., 2003, 22, 469-478. (Pubitemid 36193592)
    • (2003) EMBO Journal , vol.22 , Issue.3 , pp. 469-478
    • Rybalkin, S.D.1    Rybalkina, I.G.2    Shimizu-Albergine, M.3    Tang, X.-B.4    Beavo, J.A.5
  • 6
    • 57749112083 scopus 로고    scopus 로고
    • Probing the Interaction between the Coiled Coil Leucine Zipper of cGMPdependent Protein Kinase and the C Terminus of the Myosin Binding Subunit of the Myosin Light Chain Phosphatase
    • Sharma A.K.; Zhou, G. P.; Kupferman, J.; Surks, H. K.; Christensen, E. N.; Chou, J. J.; Mendelsohn, M. E.; Rigby, A. C. Probing the Interaction between the Coiled Coil Leucine Zipper of cGMPdependent Protein Kinase and the C Terminus of the Myosin Binding Subunit of the Myosin Light Chain Phosphatase. J. Biol. Chem., 2008, 283, 32860-32869.
    • (2008) J. Biol. Chem. , vol.283 , pp. 32860-32869
    • Sharma, A.K.1    Zhou, G.P.2    Kupferman, J.3    Surks, H.K.4    Christensen, E.N.5    Chou, J.J.6    Mendelsohn, M.E.7    Rigby, A.C.8
  • 7
    • 0031034680 scopus 로고    scopus 로고
    • Interactions of the subunits of smooth muscle myosin phosphatase
    • Hartshorne, D. J.; Interactions of the Subunits of Smooth Muscle Myosin Phosphatase. J. Biol. Chem., 1997, 272, 3683.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3683
    • Hartshorne, D.J.1
  • 8
    • 0032969182 scopus 로고    scopus 로고
    • Interactions of protein phosphatase type 1, with a focus on myosin phosphatase
    • Hartshorne, D. J.; Hirano, K. Review Interactions of protein phosphatase type 1, with a focus on myosin phosphatase. Mol. Cell. Biochem., 1999, 190, 79-84. (Pubitemid 29094991)
    • (1999) Molecular and Cellular Biochemistry , vol.190 , Issue.1-2 , pp. 79-84
    • Hartshorne, D.J.1    Hirano, K.2
  • 9
    • 0038447042 scopus 로고    scopus 로고
    • Dimerization of cGMP-dependent protein kinase 1α and the myosin-binding subunit of myosin phosphatase: Role of leucine zipper domains
    • DOI 10.1016/S0898-6568(03)00057-3
    • Surks, H. K.; Mendelsohn, M. E. Dimerization of cGMP-dependent protein kinase 1 [alpha] and the myosin-binding subunit of myosin phosphatase: Role of leucine zipper domains. Cellular Signalling., 2003, 15, 937-944. (Pubitemid 36859805)
    • (2003) Cellular Signalling , vol.15 , Issue.10 , pp. 937-944
    • Surks, H.K.1    Mendelsohn, M.E.2
  • 10
    • 36349014835 scopus 로고    scopus 로고
    • cGMP-dependent protein kinase I and smooth muscle relaxation: A tale of two isoforms
    • DOI 10.1161/CIRCRESAHA.107.165779, PII 0000301220071126000004
    • Surks, H. cGMP-Dependent Protein Kinase I and Smooth Muscle Relaxation- A Tale of Two Isoforms. Circ. Res., 2007, 101, 1078-1080. (Pubitemid 350146432)
    • (2007) Circulation Research , vol.101 , Issue.11 , pp. 1078-1080
    • Surks, H.K.1
  • 11
    • 24344487878 scopus 로고    scopus 로고
    • Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: Application to cGMP-dependent protein kinase Iα
    • DOI 10.1110/ps.051528905
    • Schnell, J. R.; Zhou, G. P.; Zweckstetter, M.; Rigby, A. C.; Chou, J. J. Rapid and Accurate Structure Determination of Coiled-coil Domains Using NMR Dipolar ouplings: Application to cGMPdependent Protein Kinase Ia. Protein Science, 2005, 14(9), 2421-2428. (Pubitemid 41252810)
    • (2005) Protein Science , vol.14 , Issue.9 , pp. 2421-2428
    • Schnell, J.R.1    Zhou, G.-P.2    Zweckstetter, M.3    Rigby, A.C.4    Chou, J.J.5
  • 12
    • 0030939096 scopus 로고    scopus 로고
    • Disposition of amphiphilic helices in heteropolar environments
    • DOI 10.1002/(SICI)1097-0134(199705)28:1<99::AID-PROT10>3.0.CO;2-C
    • Chou, K. C.; Zhang, C. T.; Maggiora, G. M. Disposition of Amphiphilic Helices in Heteropolar Environments. Proteins: Structure, Function, and Genetics, 1997, 28, 99-108. (Pubitemid 27194023)
    • (1997) Proteins: Structure, Function and Genetics , vol.28 , Issue.1 , pp. 99-108
    • Chou, K.-C.1    Zhang, C.-T.2    Maggiora, G.M.3
  • 13
    • 0029051959 scopus 로고
    • A novel approach to predicting protein structural classes in a (20-1)-D amino acid composition space
    • Chou, K. C. A novel approach to predicting protein structural classes in a (20-1)-D amino acid composition space. Proteins: Structure, Function & Genetics, 1995, 21, 319-344.
    • (1995) Proteins: Structure, Function & Genetics , vol.21 , pp. 319-344
    • Chou, K.C.1
  • 14
    • 0029157083 scopus 로고
    • Review: Prediction of protein structural classes
    • Chou, K. C.; Zhang, C. T. Review: Prediction of protein structural classes. Crit. Rev. Biochem. Mol. Biol., 1995, 30, 275-349.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 275-349
    • Chou, K.C.1    Zhang, C.T.2
  • 15
    • 0035874091 scopus 로고    scopus 로고
    • Prediction of protein cellular attributes using pseudo amino acid composition
    • (Erratum: Ibid., 2001, 43
    • Chou, K. C. Prediction of protein cellular attributes using pseudo amino acid composition. Proteins: Structure, Function, and Genetics (Erratum: Ibid., 2001, Vol.44, 60), 2001, 43, 246-255.
    • (2001) Proteins: Structure, Function, and Genetics , vol.44 , Issue.60 , pp. 246-255
    • Chou, K.C.1
  • 16
    • 79951518208 scopus 로고    scopus 로고
    • Some remarks on protein attribute prediction and pseudo amino acid composition (50th Anniversary Year Review)
    • Chou, K. C. Some remarks on protein attribute prediction and pseudo amino acid composition (50th Anniversary Year Review). J. Theor. Biol., 2011, 273, 236-247
    • (2011) J. Theor. Biol. , vol.273 , pp. 236-247
    • Chou, K.C.1
  • 17
    • 0021764092 scopus 로고
    • An extension of Chou's graphical rules for deriving enzyme kinetic equations to system involving parallel reaction pathways
    • Zhou, G. P.; Deng, M. H. An extension of Chou's graphical rules for deriving enzyme kinetic equations to system involving parallel reaction pathways. Biochem. J., 1984, 222, 169-176.
    • (1984) Biochem. J. , vol.222 , pp. 169-176
    • Zhou, G.P.1    Deng, M.H.2
  • 18
    • 0024971003 scopus 로고
    • Graphic rules in steady and non-steady enzyme kinetics
    • Chou, K. C. Graphic rules in steady and non-steady enzyme kinetics. J. Biol. Chem., 1989, 264, 12074-12079.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12074-12079
    • Chou, K.C.1
  • 19
    • 42149097173 scopus 로고    scopus 로고
    • Kinetic plasticity and the determination of product ratios for kinetic schemes leading to multiple products without rate laws - New methods based on directed graphs
    • DOI 10.1139/V08-020
    • Andraos, J. Kinetic plasticity and the determination of product ratios for kinetic schemes leading to multiple products without rate laws: New methods based on directed graphs. Can. J. Chem., 2008, 86, 342-357. (Pubitemid 351536311)
    • (2008) Canadian Journal of Chemistry , vol.86 , Issue.4 , pp. 342-357
    • Andraos, J.1
  • 20
    • 77952868004 scopus 로고    scopus 로고
    • Graphic rule for drug metabolism systems
    • Chou, K. C. Graphic rule for drug metabolism systems. Curr. Drug Metab., 2010, 11, 369-378.
    • (2010) Curr. Drug Metab. , vol.11 , pp. 369-378
    • Chou, K.C.1
  • 21
    • 0024005728 scopus 로고
    • Review: Low-frequency collective motion in biomacromolecules and its biological functions
    • Chou, K. C. Review: Low-frequency collective motion in biomacromolecules and its biological functions. Biophysical Chemistry, 1988, 30, 3-48.
    • (1988) Biophysical Chemistry , vol.30 , pp. 3-48
    • Chou, K.C.1
  • 22
    • 20244385679 scopus 로고
    • Biological functions of soliton and extra electron motion in DNA structure
    • Zhou, G. P. Biological functions of soliton and extra electron motion in DNA structure. Phys. Scr., 1989, 40, 698-701.
    • (1989) Phys. Scr. , vol.40 , pp. 698-701
    • Zhou, G.P.1
  • 23
    • 0028182102 scopus 로고
    • Solitary wave dynamics as a mechanism for explaining the internal motion during microtubule growth
    • Chou, K. C.; Zhang, C. T.; Maggiora, G. M. Solitary wave dynamics as a mechanism for explaining the internal motion during microtubule growth. Biopolymers, 1994, 34, 143-153.
    • (1994) Biopolymers , vol.34 , pp. 143-153
    • Chou, K.C.1    Zhang, C.T.2    Maggiora, G.M.3
  • 24
    • 0020102584 scopus 로고
    • Role of the protein outside active site on the diffusion-controlled reaction of enzyme
    • Chou, K. C.; Zhou, G. P. Role of the protein outside active site on the diffusion-controlled reaction of enzyme. J. Am. Chem. Soc., 1982, 104, 1409-1413.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 1409-1413
    • Chou, K.C.1    Zhou, G.P.2
  • 25
    • 77649339280 scopus 로고    scopus 로고
    • Review: Recent advances in developing web-servers for predicting protein attributes
    • (openly accessible at
    • Chou, K. C.; Shen, H. B. Review: Recent advances in developing web-servers for predicting protein attributes. Natural Science, 2009, 2, 63-92 (openly accessible at http://www.scirp.org/journal/NS/).
    • (2009) Natural Science , vol.2 , pp. 63-92
    • Chou, K.C.1    Shen, H.B.2
  • 26
    • 0017709445 scopus 로고
    • β-Turns in proteins
    • Chou, P. Y.; Fasman, G. D. β-Turns in Proteins, J. Mol. Biol, 1977, 115, 135-175.
    • (1977) J. Mol. Biol , vol.115 , pp. 135-175
    • Chou, P.Y.1    Fasman, G.D.2
  • 28
    • 0031027211 scopus 로고    scopus 로고
    • β-Helical protein assembly motifs
    • Kohn, W. D.; Mant, C. T.; Hodges, R. S. β-Helical Protein Assembly Motifs. J. Biol. Chem. 1997, 272, 2583-2586.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2583-2586
    • Kohn, W.D.1    Mant, C.T.2    Hodges, R.S.3
  • 29
    • 33747184794 scopus 로고    scopus 로고
    • Prediction of transmembrane helix orientation in polytopic membrane proteins
    • Adamian, L.; Liang, J. Prediction of transmembrane helix orientation in polytopic membrane proteins. BMC Structural Biology, 2006, 6, 13
    • (2006) BMC Structural Biology , vol.6 , pp. 13
    • Adamian, L.1    Liang, J.2
  • 31
    • 0037195776 scopus 로고    scopus 로고
    • Using functional domain composition and support vector machines for prediction of protein subcellular location
    • Chou, K.C.; Cai, Y.D. Using functional domain composition and support vector machines for prediction of protein subcellular location. J. Biol. Chem, 2002, 277, 45765-45769.
    • (2002) J. Biol. Chem , vol.277 , pp. 45765-45769
    • Chou, K.C.1    Cai, Y.D.2
  • 32
    • 12744279642 scopus 로고    scopus 로고
    • Using amphiphilic pseudo amino acid composition to predict enzyme subfamily classes
    • Chou, K. C. Using amphiphilic pseudo amino acid composition to predict enzyme subfamily classes. Bioinformatics, 2005, 21, 10-19.
    • (2005) Bioinformatics , vol.21 , pp. 10-19
    • Chou, K.C.1
  • 33
    • 0025678671 scopus 로고
    • Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins
    • Chambers, P.; Pringle, C. R.; Easton, A. J. Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins. J. Gen. Virol., 1990, 71, 3075-3080.
    • (1990) J. Gen. Virol. , vol.71 , pp. 3075-3080
    • Chambers, P.1    Pringle, C.R.2    Easton, A.J.3
  • 34
    • 63449109018 scopus 로고    scopus 로고
    • The coiled-coil neck domain of human pulmonary surfactant protein d drives trimerization and stabilization of thioredoxin, a heterologous non-collagenous protein
    • Li, P.; Zhou, J. Y.; Zhou, Y. Y.; Qian, C. D.; Li, O.; Min, H.; and Wu, X. C. The Coiled-Coil Neck Domain of Human Pulmonary Surfactant Protein D Drives Trimerization and Stabilization of Thioredoxin, a Heterologous Non-Collagenous Protein. Protein Pept. Lett., 2009, 16, 306-311.
    • (2009) Protein Pept. Lett. , vol.16 , pp. 306-311
    • Li, P.1    Zhou, J.Y.2    Zhou, Y.Y.3    Qian, C.D.4    Li, O.5    Min, H.6    Wu, X.C.7
  • 35
    • 0037252853 scopus 로고    scopus 로고
    • pH-induced conformational change in an helical coiled-coil is controlled by his residues in the hydrophobic core
    • DOI 10.2174/0929866033408354
    • Wada K.; Mizuno T.; Oku J-i., Tanaka T. ph-Induced Conformational Change in An A- Helical Coiled-Coil is Controlled by His Residues in the Hydrophobic Core. Protein Pept. Lett., 2003, 10, 27-33. (Pubitemid 36144767)
    • (2003) Protein and Peptide Letters , vol.10 , Issue.1 , pp. 27-33
    • Wada, K.1    Mizuno, T.2    Oku, J.-I.3    Tanaka, T.4
  • 36
    • 17444424974 scopus 로고    scopus 로고
    • The structure of alpha-helical coiled coils
    • Lupas, A. N.; Gruber M., The structure of alpha-helical coiled coils. Adv Protein Chem., 2005, 70, 37-7078.
    • (2005) Adv Protein Chem. , vol.70 , pp. 37-7078
    • Lupas, A.N.1    Gruber, M.2
  • 37
    • 0000920828 scopus 로고
    • The packing of a-helices: Simple coiled-coils
    • Crick, F.H.C. The packing of a-helices: Simple coiled-coils. Acta Crystallogr., 1953, 6, 689-697.
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 38
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Min Lu, M.; Blacklow, S. C.; Kim, P. S. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nature Structural Biology, 1995, 2, 1075-1082.
    • (1995) Nature Structural Biology , vol.2 , pp. 1075-1082
    • Min Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 39
    • 79960604768 scopus 로고    scopus 로고
    • The Disposition of the Leucine Zipper Coiled-Coil (LZCC) Protein Residues in Wenxiang Diagram Provides a New Insights into the Protein-Protein Interaction Mechanism
    • in press)
    • Zhou, G. P. The Disposition of the Leucine Zipper Coiled-Coil (LZCC) Protein Residues in Wenxiang Diagram Provides a New Insights into the Protein-Protein Interaction Mechanism. J. Theor. Biol., 2011 (in press).
    • (2011) J. Theor. Biol.
    • Zhou, G.P.1
  • 40
    • 34548666396 scopus 로고    scopus 로고
    • Folding of the C-terminal fragment V111-D143 of staphylococcal nuclease in aqueous solution
    • DOI 10.2174/092986607781483769
    • Geng, Y.; Wang, M.; Xie, T.; Feng, Y.; Wang, F. Folding of the CTerminal Fragment V111-D143 of Staphylococcal Nuclease in Aqueous Solution. Protein Pept. Lett., 2007, 14, 747-755. (Pubitemid 47416395)
    • (2007) Protein and Peptide Letters , vol.14 , Issue.8 , pp. 747-755
    • Geng, Y.1    Wang, M.2    Xie, T.3    Feng, Y.4    Wang, J.5
  • 41
    • 79951669244 scopus 로고    scopus 로고
    • Helix Conformation of a Small Peptide Melittin in a Methanol-Water Mixed Solvent Studied by NMR
    • Miura, Y. Helix Conformation of a Small Peptide Melittin in a Methanol-Water Mixed Solvent Studied by NMR. Protein Pept. Lett., 2011, 18, 318-326,
    • (2011) Protein Pept. Lett. , vol.18 , pp. 318-326
    • Miura, Y.1
  • 42
    • 44949291986 scopus 로고
    • Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins
    • Kay, L.E.; Ikura, M.; Tschudin, R.; Bax, A. Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins. J. Magn. Reson., 1990, 89, 496-514.
    • (1990) J. Magn. Reson. , vol.89 , pp. 496-514
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 44
    • 0026158667 scopus 로고
    • An efficient 3D NMR technique for correlating the proton and 15N backbone amide resonances with the alphacarbon of the preceding residue in uniformly 15N/13C enriched proteins
    • Bax, A.; Ikura, M. An efficient 3D NMR technique for correlating the proton and 15N backbone amide resonances with the alphacarbon of the preceding residue in uniformly 15N/13C enriched proteins. J. Biomol. NMR, 1991, 1(1), 99-104.
    • (1991) J. Biomol. NMR , vol.1 , Issue.1 , pp. 99-104
    • Bax, A.1    Ikura, M.2
  • 45
    • 35148819200 scopus 로고    scopus 로고
    • Interactions between the Leucine-zipper Motif of cGMP-Dependent Protein Kinase and the C-terminal Region of the Targeting Subunit of Myosin Light Chain Phosphatase
    • DOI 10.1016/j.jmb.2007.08.049, PII S0022283607011205
    • Lee, E.; Hayes, D. B.; Langsetmo, K.; Sundberg, E. J.; Tao, T. C. Interactions between the Leucine-zipper Motif of cGMPDependent Protein Kinase and the C-terminal Region of the Targeting Subunit of Myosin Light Chain Phosphatase. J. Mol. Biol., 2007, 373, 1198-1212 (Pubitemid 47539483)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.5 , pp. 1198-1212
    • Lee, E.1    Hayes, D.B.2    Langsetmo, K.3    Sundberg, E.J.4    Tao, T.C.5
  • 46
    • 0025681549 scopus 로고
    • Protein structure determination in solution by NMR spectroscopy
    • Wüthrich, K. Protein structure determination in solution by NMR spectroscopy. J. Biol. Chem., 1990, 265(36), 22059-22062. (Pubitemid 120014262)
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.36 , pp. 22059-22062
    • Wuthrich, K.1
  • 47
    • 0024449503 scopus 로고
    • 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
    • Kay, L. E.; Torchia, D. A.; Bax, A. Backbone Dynamics of Proteins As Studied by 15N Inverse Detected Heteronuclear NMR Spectroscopy: Application to Staphylococcal Nuclease? Biochemistry, 1989, 28, 8972-8979. (Pubitemid 19283459)
    • (1989) Biochemistry , vol.28 , Issue.23 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 48
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L. E.; Keifer, P.; Saarinen, T. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc., 1992, 114, 10663-10665.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 49
    • 0028578764 scopus 로고
    • A Suite of Triple Resonance NMR Experiments for the Backbone Assignment of 15N, 13C, 2H Labeled Proteins with High Sensitivity
    • Yamazaki, T.; Lee, W.; Arrowsmith, C. H.; Muhandiram, D. R.; Kay, L. E. A Suite of Triple Resonance NMR Experiments for the Backbone Assignment of 15N, 13C, 2H Labeled Proteins with High Sensitivity. J. Am. Chem. Soc., 1994, 116, 11655-11666.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 11655-11666
    • Yamazaki, T.1    Lee, W.2    Arrowsmith, C.H.3    Muhandiram, D.R.4    Kay, L.E.5
  • 50
    • 43949161325 scopus 로고
    • Simultanous acquisition of 15 N/ 13 C-edited NOE spectra of proteins dissolved in H2O
    • ser. B
    • Pascal, S. M.; Muhandiram, D. R.; Yamazaki, T.; Formankay, J. D.; Kay, L. E. Simultanous acquisition of 15 N/ 13 C-edited NOE spectra of proteins dissolved in H2O. J. Magn. Reson., 1994, ser. B, 103, 197-201.
    • (1994) J. Magn. Reson. , vol.103 , pp. 197-201
    • Pascal, S.M.1    Muhandiram, D.R.2    Yamazaki, T.3    Formankay, J.D.4    Kay, L.E.5
  • 52
    • 0032528033 scopus 로고    scopus 로고
    • Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase
    • DOI 10.1021/ja9812610
    • Cornilescu, G.; Marquardt, J.L.; Ottiger, M.; Bax, A. Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase. J. Am. Chem.Soc., 1998, 120, 6836-6837. (Pubitemid 28347351)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.27 , pp. 6836-6837
    • Cornilescu, G.1    Marquardt, J.L.2    Ottiger, M.3    Bax, A.4
  • 53
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Shen, Y.; Delaglio, F.; Cornilescu, G.; Bax, A. TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J. Biomol. NMR, 2009, 44, 213-223.
    • (2009) J. Biomol. NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 54
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • DOI 10.1023/A:1008392405740
    • Cornilescu, G.; Delaglio, F.; Bax, Ad. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR, 1999, 13, 289-302. (Pubitemid 29143535)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.3 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 55
    • 77950683267 scopus 로고    scopus 로고
    • A flexible bipartite coiled coil structure is required for the interaction of hexim1 with the p-tefb subunit cyclin T1
    • Schönichen, A.; Bigalke, J. M.; Urbanke, C.; Grzesiek, S.; Dames, S. A.; Geyer, M. A Flexible Bipartite Coiled Coil Structure Is Required for the Interaction of Hexim1 with the P-TEFb Subunit Cyclin T1. Biochemistry, 2010, 49, 3083-3091.
    • (2010) Biochemistry , vol.49 , pp. 3083-3091
    • Schönichen, A.1    Bigalke, J.M.2    Urbanke, C.3    Grzesiek, S.4    Dames, S.A.5    Geyer, M.6
  • 57
    • 0024412074 scopus 로고
    • Streptococcal M protein: Molecular design and biological behavior
    • Fischetti, V. A. Streptococcal M Protein: Molecular Design and Biological Behavior, American Society for Microbiology: Clinical Microbiology Reviews, 1989, 2(3), 285-314. (Pubitemid 19181596)
    • (1989) Clinical Microbiology Reviews , vol.2 , Issue.3 , pp. 285-314
    • Fischetti, V.A.1
  • 58
    • 0034837622 scopus 로고    scopus 로고
    • Hybrid hydrogels cross-linked by genetically engineered coiled-coil block proteins
    • DOI 10.1021/bm0155322
    • Wang, C.; Kopeciek, J.; Stewart, R. J. Hybrid Hydrogels Cross- Linked by Genetically Engineered Coiled-Coil Block Proteins. Biomacromolecules, 2001, 1, 912-920. (Pubitemid 32895516)
    • (2001) Biomacromolecules , vol.2 , Issue.3 , pp. 912-920
    • Wang, C.1    Kopecek, J.2    Stewart, R.J.3
  • 59
    • 0028028334 scopus 로고
    • Characterization of the KLP68D kinesin-like protein in Drosophila: Possible roles in axonal transport
    • DOI 10.1083/jcb.127.4.1041
    • Pesavento, P. A.; Stewart, R. J.; Goldstein, L. S. Characterization of the KLP68D kinesin-like protein in Drosophila: Possible roles in axonal transpor. JCB, 1994, 127(4), 1041-1048. (Pubitemid 24355991)
    • (1994) Journal of Cell Biology , vol.127 , Issue.4 , pp. 1041-1048
    • Pesavento, P.A.1    Stewart, R.J.2    Goldstein, L.S.B.3
  • 61
    • 0037215324 scopus 로고    scopus 로고
    • Weak alignment offers new NMR opportunities to study protein structure and dynamics
    • DOI 10.1110/ps.0233303
    • Bax, A. Weak alignment offers new NMR opportunities to study protein structure and dynamics. Protein Sci., 2003, 12, 1-16. (Pubitemid 36020129)
    • (2003) Protein Science , vol.12 , Issue.1 , pp. 1-16
    • Bax, A.1
  • 62
    • 33745698459 scopus 로고    scopus 로고
    • Enhancement of boundstate residual dipolar couplings: Conformational analysis of lactose bound to Galectin-3
    • Zhuang, T.; Leffler, H.; Prestegard, J. H. Enhancement of boundstate residual dipolar couplings: Conformational analysis of lactose bound to Galectin-3. Protein Science, 2006, 15, 1780-1790.
    • (2006) Protein Science , vol.15 , pp. 1780-1790
    • Zhuang, T.1    Leffler, H.2    Prestegard, J.H.3
  • 63
    • 0034620764 scopus 로고    scopus 로고
    • Protein structure determination using molecular fragment replacement and NMR dipolar couplings
    • DOI 10.1021/ja993603n
    • Delaglio, F.; Kontaxis, G.; Bax, A. Protein structure determination using molecular fragment replacement and NMR dipolar couplings. J. Am. Chem. Soc., 2000, 122, 2142-2143. (Pubitemid 30143929)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.9 , pp. 2142-2143
    • Delaglio, F.1    Kontaxis, G.2    Bax, A.3
  • 64
    • 0034653908 scopus 로고    scopus 로고
    • The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges
    • DOI 10.1016/S0969-2126(00)00100-3
    • Burkhard, P.; Kammerer, R. A.; Steinmetz, M. O.; Bourenkov, G. P.; Aebi, U. The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges. Structure, 2000, 8, 223-230. (Pubitemid 30148689)
    • (2000) Structure , vol.8 , Issue.3 , pp. 223-230
    • Burkhard, P.1    Kammerer, R.A.2    Steinmetz, M.O.3    Bourenkov, G.P.4    Aebi, U.5
  • 65
    • 0029050883 scopus 로고
    • Nuclear magnetic dipole interactions in field-oriented proteins-Information for structure determination in solution
    • Tolman, J.; Flanagan, J.; Kennedy, M.; Prestegard, J. Nuclear magnetic dipole interactions in field-oriented proteins-Information for structure determination in solution. Proc. Natl. Acad. Sci., 1995, 92, 9279-9283.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 9279-9283
    • Tolman, J.1    Flanagan, J.2    Kennedy, M.3    Prestegard, J.4
  • 66
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • DOI 10.1126/science.278.5340.1111
    • Tjandra, N.; Bax, A. Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science, 1997, 278, 1111-1114. (Pubitemid 27517889)
    • (1997) Science , vol.278 , Issue.5340 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 67
    • 0034685436 scopus 로고    scopus 로고
    • Prediction of sterically induced alignment in a dilute liquid crystalline phase: Aid to protein structure determination by NMR [11]
    • DOI 10.1021/ja0000908
    • 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., 2000, 122, 3791-3792. (Pubitemid 30233459)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.15 , pp. 3791-3792
    • Zweckstetter, M.1    Bax, A.2
  • 68
    • 2942653357 scopus 로고    scopus 로고
    • Prediction of charge-induced molecular alignment of biomolecules dissolved in dilute liquid-crystalline phases
    • DOI 10.1529/biophysj.103.035790
    • Zweckstetter, M., Hummer, G., and Bax, A. Prediction of chargeinduced molecular alignment of biomolecules dissolved in dilute liquid crystalline phases. Biophys. J., 2004, 86, 3444-3460. (Pubitemid 38780229)
    • (2004) Biophysical Journal , vol.86 , Issue.6 , pp. 3444-3460
    • Zweckstetter, M.1    Hummer, G.2    Bax, A.3
  • 70
    • 34250334756 scopus 로고    scopus 로고
    • Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from influenza A virus
    • DOI 10.1529/biophysj.106.090183
    • Hu, J.; Asbury, T., Achuthan, S.; Li, C.; Bertram, R.; Quine, J. R.; Fu, R.; Cross, T. A. Backbone Structure of the Amantadine- Blocked Trans-Membrane Domain M2 Proton Channel from Influenza A Virus. Biophys. J., 2007, 92, 4335-4343. (Pubitemid 46915327)
    • (2007) Biophysical Journal , vol.92 , Issue.12 , pp. 4335-4343
    • Hu, J.1    Asbury, T.2    Achuthan, S.3    Li, C.4    Bertram, R.5    Quine, J.R.6    Fu, R.7    Cross, T.A.8
  • 71
    • 4344713234 scopus 로고    scopus 로고
    • The basolateral targeting signal of CD147 (EMMPRIN) consists of a single leucine and is not recognized by retinal pigment epithelium
    • DOI 10.1091/mbc.E04-01-0058
    • Deora, A.A.; Gravotta, D.; Kreitzer, G.; Hu, J.; Bok, D.; Rodriguez- Boulan, E. The Basolateral Targeting Signal of CD147 (EMMPRIN) Consists of a Single Leucine and Is Not Recognized by Retinal Pigment Epithelium. Molecular Biology of the Cell, 2004, 15, 4148-4165. (Pubitemid 39122019)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.9 , pp. 4148-4165
    • Deora, A.A.1    Gravotta, D.2    Kreitzer, G.3    Hu, J.4    Bok, D.5    Rodriguez-Boulan, E.6
  • 74
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network
    • Andrade, M. A.; Chacón, P.; Merelo, J. J.; Morán, F. Evaluation of secondary structure of protein from UV circular dichroism spectra using unsupervised learning neural network. Protein Eng., 1993, 6, 383-390. (Pubitemid 23197398)
    • (1993) Protein Engineering , vol.6 , Issue.4 , pp. 383-390
    • Andrade, M.A.1    Chacon, P.2    Merelo, J.J.3    Moran, F.4
  • 76
  • 77
    • 0141844580 scopus 로고    scopus 로고
    • Structure of the ubiquitin-associated domain of p62 (SQSTM1) and implications for mutations that cause Paget's disease of bone
    • DOI 10.1074/jbc.M307416200
    • Ciani, B.; Layfield, R.; Cavey, J. R.; Sheppard, P. W.; Searle, M. S. Structure of the Ubiquitin-associated Domain of p62 (SQSTM1) and Implications for Mutations That Cause Paget's Disease of Bone. J. Biol. Chem., 2003, 278, 37409-37412. (Pubitemid 37175260)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 37409-37412
    • Ciani, B.1    Layfield, R.2    Cavey, J.R.3    Sheppard, P.W.4    Searle, M.S.5
  • 78
    • 0028204451 scopus 로고
    • Solution structure and dynamics of Ras p21 GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy
    • Kraulis, P. J.; Domaille, P. J.; Campbell-Burk, S. L.; van Aken, T.; Laue, E. D. Solution Structure and Dynamics of Ras p21.cntdot.GDP Determined by Heteronuclear Three- and Four- Dimensional NMR Spectroscopy. Biochemistry, 1994, 33, 3515-3531 (Pubitemid 24115999)
    • (1994) Biochemistry , vol.33 , Issue.12 , pp. 3515-3531
    • Kraulis, P.J.1    Domaille, P.J.2    Campbell-Burk, S.L.3    Van Aken, T.4    Laue, E.D.5
  • 79
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • DOI 10.1016/0263-7855(96)00009-4
    • Koradi, R.; Billeter, M.; Wüthrich, K. MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graph., 1996, 14, 51-55 (Pubitemid 26152976)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 80
    • 0031595590 scopus 로고    scopus 로고
    • 15N multidimensional NMR to study the structure and dynamics of proteins
    • DOI 10.1146/annurev.biophys.27.1.357
    • Gardner, K. H.; Kay, L. E. The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins. Annu. Rev. Biophys. Biomol. Struct., 1998, 27, 357-406. (Pubitemid 28286019)
    • (1998) Annual Review of Biophysics and Biomolecular Structure , vol.27 , pp. 357-406
    • Gardner, K.H.1    Kay, L.E.2
  • 81
    • 33644539839 scopus 로고    scopus 로고
    • NMR distinction of single and multiple-mode binding of small-molecule protein ligands
    • Reibarkh, M.; Malia, T. J.; Wagner, G. NMR Distinction of Single and Multiple-Mode Binding of Small-Molecule Protein Ligands. J. Am. Chem. Soc., 2006, 128(7), 2160-2161.
    • (2006) J. Am. Chem. Soc. , vol.128 , Issue.7 , pp. 2160-2161
    • Reibarkh, M.1    Malia, T.J.2    Wagner, G.3
  • 82
    • 67650069432 scopus 로고    scopus 로고
    • Evidence for domain motion in proteins affecting global diffusion properties: A nuclear magnetic resonance study
    • Yury E. Shapiro, Y. E.; Meirovitch, E. Evidence for Domain Motion in Proteins Affecting Global Diffusion Properties: A Nuclear Magnetic Resonance Study. J. Phys. Chem. B, 2009, 113(19), 7003-7011.
    • (2009) J. Phys. Chem. B , vol.113 , Issue.19 , pp. 7003-7011
    • Yury, E.1    Shapiro, Y.E.2    Meirovitch, E.3
  • 83
    • 0014062165 scopus 로고
    • Use of helical wheels to represent the structures of proteins and to identify segments with helical potential
    • Schiffer, M.; Edmundson, A.B. Use of helical wheels to represent the structures of proteins and to identify segments with helical potential. Biophys. J., 1967, 7, 121-135.
    • (1967) Biophys. J. , vol.7 , pp. 121-135
    • Schiffer, M.1    Edmundson, A.B.2
  • 84
    • 0024534241 scopus 로고
    • Evidence that the leucine zipper is a coiled coil
    • O'Shea, E. K.; Rutkowski, R..; Kim, P. S. Evidence that the leucine zipper is a coiled coil. Science, 1989, 243, 538-542. (Pubitemid 19048755)
    • (1989) Science , vol.243 , Issue.4890 , pp. 538-542
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 85
    • 54249165105 scopus 로고    scopus 로고
    • Toward prediction of binding affinities between the MHC protein and its peptide ligands using quantitative structure-activity relationship approach
    • Tian, F.; Lv, F.; Zhou, P.; Yang, Q.; Jalbout, A. F. Toward prediction of binding affinities between the MHC protein and its peptide ligands using quantitative structure-activity relationship approach. Protein Pept. Lett., 2008, 15, 1033-1043.
    • (2008) Protein Pept. Lett. , vol.15 , pp. 1033-1043
    • Tian, F.1    Lv, F.2    Zhou, P.3    Yang, Q.4    Jalbout, A.F.5
  • 86
    • 77955971760 scopus 로고    scopus 로고
    • Development of tools and database for analysis of metal binding sites in protein
    • Kuntal, B. K.; Aparoy, P.; Reddanna, P. Development of tools and database for analysis of metal binding sites in protein. Protein Pept. Lett., 2010, 17, 765-773.
    • (2010) Protein Pept. Lett. , vol.17 , pp. 765-773
    • Kuntal, B.K.1    Aparoy, P.2    Reddanna, P.3
  • 87
    • 40449101540 scopus 로고    scopus 로고
    • Empirical parameters for estimating proteinprotein binding free energies: Number of short- and long-distance atom-atom contacts
    • Li, Y. C.; Zeng, Z. H. Empirical parameters for estimating proteinprotein binding free energies: Number of short- and long-distance atom-atom contacts. Protein Pept. Lett., (mistake), 2008, 15, 223-231.
    • (2008) Protein Pept. Lett., (mistake) , vol.15 , pp. 223-231
    • Li, Y.C.1    Zeng, Z.H.2
  • 89
    • 25844506708 scopus 로고    scopus 로고
    • Weak alignment NMR: A hawk-eyed view of biomolecular structure
    • DOI 10.1016/j.sbi.2005.08.006, PII S0959440X05001545, Carbohydrates and Glycoconjugates/Biophysical Methods
    • Bax, A.; Grishaev, A. Weak alignment NMR: A hawk-eyed view of biomolecular structure. Curr. Opin. Struct. Biol., 2005, 15, 563-570. (Pubitemid 41393488)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.5 , pp. 563-570
    • Bax, A.1    Grishaev, A.2
  • 91
    • 68849090776 scopus 로고    scopus 로고
    • Identification of ligand-binding pockets in proteins using residue preference methods
    • Qiu, Z.; Wang, X. Identification of ligand-binding pockets in proteins using residue preference methods. Protein Pept. Lett., 2009, 16, 984-990.
    • (2009) Protein Pept. Lett. , vol.16 , pp. 984-990
    • Qiu, Z.1    Wang, X.2
  • 92
    • 79952176461 scopus 로고    scopus 로고
    • A glucuronic acid binding leguminous lectin with mitogenic activity toward mouse splenocytes
    • Chan, Y. S.; Wong, J. H.; Ng, T. B. A glucuronic acid binding leguminous lectin with mitogenic activity toward mouse splenocytes. Protein Pept. Lett., 2011, 18, 194-202.
    • (2011) Protein Pept. Lett. , vol.18 , pp. 194-202
    • Chan, Y.S.1    Wong, J.H.2    Ng, T.B.3
  • 93
    • 63449088575 scopus 로고    scopus 로고
    • Interaction models of a series of oxadiazole-substituted alphaisopropoxy phenylpropanoic acids against PPARalpha and PPARgamma: Molecular modeling and comparative molecular similarity indices analysis studies
    • Cheng, F.; Shen, J.; Xu, X.; Luo, X.; Chen, K.; Shen, X.; Jiang, H. Interaction models of a series of oxadiazole-substituted alphaisopropoxy phenylpropanoic acids against PPARalpha and PPARgamma: Molecular modeling and comparative molecular similarity indices analysis studies. Protein Pept. Lett., 2009, 16, 150-162.
    • (2009) Protein Pept. Lett. , vol.16 , pp. 150-162
    • Cheng, F.1    Shen, J.2    Xu, X.3    Luo, X.4    Chen, K.5    Shen, X.6    Jiang, H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.