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Volumn 281, Issue 1, 1998, Pages 165-181

Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper

Author keywords

Buried salt bridge; H bonds; Leucine zippers; Solution structure; Two dimensional 1H NMR

Indexed keywords

LEUCINE ZIPPER PROTEIN; ONCOPROTEIN; TRANSCRIPTION FACTOR;

EID: 0032493843     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1914     Document Type: Article
Times cited : (96)

References (80)
  • 1
    • 0026665523 scopus 로고
    • Transcriptional activation by the human c-Myc oncoprotein in yeast requires interaction with Max
    • Amati B., Dalton S., Brooks M.W., Littlewood T.D., Evan G.I., Land H. Transcriptional activation by the human c-Myc oncoprotein in yeast requires interaction with Max. Nature. 359:1992;423-426
    • (1992) Nature , vol.359 , pp. 423-426
    • Amati, B.1    Dalton, S.2    Brooks, M.W.3    Littlewood, T.D.4    Evan, G.I.5    Land, H.6
  • 2
    • 0027533679 scopus 로고
    • Oncogenic activity of the c-Myc protein requires dimerization with Max
    • Amati B., Brooks M.W., Levy N., Littlewood T.D., Evan G.I., Land H. Oncogenic activity of the c-Myc protein requires dimerization with Max. Cell. 72:1993;233-245
    • (1993) Cell , vol.72 , pp. 233-245
    • Amati, B.1    Brooks, M.W.2    Levy, N.3    Littlewood, T.D.4    Evan, G.I.5    Land, H.6
  • 3
    • 0003516749 scopus 로고
    • San Francisco: W. H. Freeman and Company
    • Atkins P.W. Physical Chemistry. 1982;W. H. Freeman and Company, San Francisco
    • (1982) Physical Chemistry
    • Atkins, P.W.1
  • 4
    • 0027408096 scopus 로고
    • Mad: A heterodimeric partner for Max that antagonizes Myc transcriptional activity
    • Ayer D.E., Kretzner L., Eisenman R.N. Mad a heterodimeric partner for Max that antagonizes Myc transcriptional activity. Cell. 72:1993;211-222
    • (1993) Cell , vol.72 , pp. 211-222
    • Ayer, D.E.1    Kretzner, L.2    Eisenman, R.N.3
  • 7
    • 0020603359 scopus 로고
    • The human c-myc oncogene: Structural consequences of translocation into the IgH locus in Burkitt lymphoma
    • Battey J., Moulding C., Taub R., Murphy W., Stewart T., Potter H., Lenoir G., Leder P. The human c-myc oncogene structural consequences of translocation into the IgH locus in Burkitt lymphoma. Cell. 34:1983;779-787
    • (1983) Cell , vol.34 , pp. 779-787
    • Battey, J.1    Moulding, C.2    Taub, R.3    Murphy, W.4    Stewart, T.5    Potter, H.6    Lenoir, G.7    Leder, P.8
  • 8
    • 0025763419 scopus 로고
    • Max: A helix-loop-helix zipper protein that forms a sequence-specific DNA binding complex with Myc
    • Blackwood E.M., Eisenman R.N. Max a helix-loop-helix zipper protein that forms a sequence-specific DNA binding complex with Myc. Science. 251:1991;1211-1217
    • (1991) Science , vol.251 , pp. 1211-1217
    • Blackwood, E.M.1    Eisenman, R.N.2
  • 9
    • 0028987269 scopus 로고
    • Coiled-coil regions in the carboxy-terminal domains of dystrophin and related proteins: Potentials for protein-protein interactions
    • Blake D.J., Tinsley J.M., Davies K.E., Knight A.E., Winder S.J., Kendrick-Jones J. Coiled-coil regions in the carboxy-terminal domains of dystrophin and related proteins potentials for protein-protein interactions. Trends Biochem. Sci. 20:1995;133-135
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 133-135
    • Blake, D.J.1    Tinsley, J.M.2    Davies, K.E.3    Knight, A.E.4    Winder, S.J.5    Kendrick-Jones, J.6
  • 11
    • 0000449348 scopus 로고
    • Ribbon models of macromolecules
    • Carson M. Ribbon models of macromolecules. J. Mol. Graph. 5:1987;103-106
    • (1987) J. Mol. Graph. , vol.5 , pp. 103-106
    • Carson, M.1
  • 12
    • 0343457477 scopus 로고
    • The time dependence of coherence transfer in homonuclear isotropic mixing experiments
    • Cavanagh J., Chazin W.J., Rance M. The time dependence of coherence transfer in homonuclear isotropic mixing experiments. J. Magn. Reson. 87:1990;110-131
    • (1990) J. Magn. Reson. , vol.87 , pp. 110-131
    • Cavanagh, J.1    Chazin, W.J.2    Rance, M.3
  • 13
    • 0016169865 scopus 로고
    • Determination of the helix and β form of proteins in aqueous solution by circular dichroism
    • Chen Y.-H., Yang J.T., Chau K.H. Determination of the helix and β form of proteins in aqueous solution by circular dichroism. Biochemistry. 13:1974;3350-3359
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.-H.1    Yang, J.T.2    Chau, K.H.3
  • 14
    • 0025272940 scopus 로고
    • α-Helical coiled-coils and bundles: How to design an α-helical protein
    • Cohen C., Parry D.A.D. α-Helical coiled-coils and bundles how to design an α-helical protein. Proteins: Struct. Funct. Genet. 7:1990;1-15
    • (1990) Proteins: Struct. Funct. Genet. , vol.7 , pp. 1-15
    • Cohen, C.1    Parry, D.A.D.2
  • 15
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled-coil
    • Crick F.H.C. The packing of α-helices simple coiled-coil. Acta Crystallog. 6:1953;689-693
    • (1953) Acta Crystallog. , vol.6 , pp. 689-693
    • Crick, F.H.C.1
  • 16
    • 33845378943 scopus 로고
    • 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy
    • 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy. J. Am. Chem. Soc. 107:1985;2821-2822
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 2821-2822
    • Davis, D.G.1    Bax, A.2
  • 17
    • 0027910469 scopus 로고
    • Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain
    • Ferré-D'Amaré A.R., Prendergast G.C., Ziff E.B., Burley S.K. Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. Nature. 363:1993;38-45
    • (1993) Nature , vol.363 , pp. 38-45
    • Ferré-D'Amaré, A.R.1    Prendergast, G.C.2    Ziff, E.B.3    Burley, S.K.4
  • 18
    • 6444222991 scopus 로고
    • Use of glass electrode to measure acidities in deuterium oxide
    • Glasoe P.F., Long F.A. Use of glass electrode to measure acidities in deuterium oxide. J. Phys. Chem. 64:1960;188-193
    • (1960) J. Phys. Chem , vol.64 , pp. 188-193
    • Glasoe, P.F.1    Long, F.A.2
  • 19
    • 0028894384 scopus 로고
    • Crystal structure of the heterodimeric bzip transcription factor c-Fos-c-Jun bound to DNA
    • Glover J.N.M., Harrison S.C. Crystal structure of the heterodimeric bzip transcription factor c-Fos-c-Jun bound to DNA. Nature. 373:1995;257-261
    • (1995) Nature , vol.373 , pp. 257-261
    • Glover, J.N.M.1    Harrison, S.C.2
  • 21
    • 16944366990 scopus 로고    scopus 로고
    • Buried polar residues and structural specificity in the GCN4 leucine zipper
    • Gonzalez L. Jr, Woolfson D.N., Alber T. Buried polar residues and structural specificity in the GCN4 leucine zipper. Nature Struct. Biol. 3:1996;1011-1018
    • (1996) Nature Struct. Biol. , vol.3 , pp. 1011-1018
    • Gonzalez Jr., L.1    Woolfson, D.N.2    Alber, T.3
  • 22
    • 0026317334 scopus 로고
    • Periodicity of amide proton exchange rates in a coiled-coil leucine zipper peptide
    • Goodman E.M., Kim P.S. Periodicity of amide proton exchange rates in a coiled-coil leucine zipper peptide. Biochemistry. 30:1991;11615-11620
    • (1991) Biochemistry , vol.30 , pp. 11615-11620
    • Goodman, E.M.1    Kim, P.S.2
  • 23
    • 0027756896 scopus 로고
    • A switch between two-, three- and four-stranded coiled-coils in GCN4 leucine zipper mutants
    • Harbury P.B., Zhang T., Kim P.S., Alber T. A switch between two-, three- and four-stranded coiled-coils in GCN4 leucine zipper mutants. Science. 252:1993;1401-1408
    • (1993) Science , vol.252 , pp. 1401-1408
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 24
    • 0029686266 scopus 로고    scopus 로고
    • Proteins of the Myc network: Essential regulators of cell growth and differentiation
    • Henriksson M., Lüscher B. Proteins of the Myc network essential regulators of cell growth and differentiation. Advan. Cancer Res. 68:1996;109-182
    • (1996) Advan. Cancer Res. , vol.68 , pp. 109-182
    • Henriksson, M.1    Lüscher, B.2
  • 25
    • 0000779539 scopus 로고
    • Unzipping the secrets of coiled-coils
    • Hodges R.S. Unzipping the secrets of coiled-coils. Curr. Biol. 2:1992;122-124
    • (1992) Curr. Biol. , vol.2 , pp. 122-124
    • Hodges, R.S.1
  • 26
    • 0030345054 scopus 로고    scopus 로고
    • De novo design of α-helical proteins: Basic research to medical applications
    • Hodges R.S. De novo design of α-helical proteins basic research to medical applications. Biochem. Cell Biol. 74:1996;133-154
    • (1996) Biochem. Cell Biol. , vol.74 , pp. 133-154
    • Hodges, R.S.1
  • 28
    • 0003151250 scopus 로고
    • The basic-region leucine-zipper family of DNA binding proteins
    • Hu J.C., Sauer R.T. The basic-region leucine-zipper family of DNA binding proteins. Nucl. Acids Mol. Biol. 6:1992;82-101
    • (1992) Nucl. Acids Mol. Biol. , vol.6 , pp. 82-101
    • Hu, J.C.1    Sauer, R.T.2
  • 29
    • 0028889811 scopus 로고
    • Mad3 and Mad4: Novel Max-interacting transcriptonal repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation
    • Hurlin P.J., Quéva C., Koskinen P.J., Steingrímsson E., Ayer D.E., Copeland N.G., Jenkins N.A., Eisenmann R.N. Mad3 and Mad4 novel Max-interacting transcriptonal repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation. EMBO J. 14:1995;5646-5659
    • (1995) EMBO J. , vol.14 , pp. 5646-5659
    • Hurlin, P.J.1    Quéva, C.2    Koskinen, P.J.3    Steingrímsson, E.4    Ayer, D.E.5    Copeland, N.G.6    Jenkins, N.A.7    Eisenmann, R.N.8
  • 30
    • 0031027008 scopus 로고    scopus 로고
    • Mnt, a novel Max-interacting protein is coexpressed with Myc in proliferating cells and mediates repression at Myc binding sites
    • Hurlin P.J., Quéva C., Eisenmann R.N. Mnt, a novel Max-interacting protein is coexpressed with Myc in proliferating cells and mediates repression at Myc binding sites. Genes Dev. 11:1997;44-58
    • (1997) Genes Dev. , vol.11 , pp. 44-58
    • Hurlin, P.J.1    Quéva, C.2    Eisenmann, R.N.3
  • 31
    • 0028678794 scopus 로고
    • Transcription factor I: B-zip proteins
    • Hurst H. Transcription factor I b-zip proteins. Protein Profile. 1:1994;123-152
    • (1994) Protein Profile , vol.1 , pp. 123-152
    • Hurst, H.1
  • 32
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener J., Meier B.H., Bachmann P., Ernst R.R. Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71:1979;4546-4553
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 33
    • 0027311980 scopus 로고
    • The solution structure of the leucine zipper motif of the jun oncoprotein homodimer
    • Junius F.K., Weiss A.S., King G.F. The solution structure of the leucine zipper motif of the jun oncoprotein homodimer. Eur. J. Biochem. 214:1993;415-424
    • (1993) Eur. J. Biochem , vol.214 , pp. 415-424
    • Junius, F.K.1    Weiss, A.S.2    King, G.F.3
  • 34
    • 0029068108 scopus 로고
    • Nuclear magnetic resonance characterization of the jun leucine zipper domain: Unusual properties of coiled-coil interfacial polar residues
    • Junius F.K., Mackay J.P., Bubb W.A., Jensen S.A., Weiss A.S., King G.F. Nuclear magnetic resonance characterization of the jun leucine zipper domain unusual properties of coiled-coil interfacial polar residues. Biochemistry. 34:1995;6164-6174
    • (1995) Biochemistry , vol.34 , pp. 6164-6174
    • Junius, F.K.1    MacKay, J.P.2    Bubb, W.A.3    Jensen, S.A.4    Weiss, A.S.5    King, G.F.6
  • 35
    • 15844402153 scopus 로고    scopus 로고
    • High resolution NMR structure of the leucine zipper domain of the c-Jun homodimer
    • Junius F.K., O'Donoghue S.I., Nilges M., Weiss A.S., King G.F. High resolution NMR structure of the leucine zipper domain of the c-Jun homodimer. J. Biol. Chem. 271:1996;13663-13667
    • (1996) J. Biol. Chem. , vol.271 , pp. 13663-13667
    • Junius, F.K.1    O'Donoghue, S.I.2    Nilges, M.3    Weiss, A.S.4    King, G.F.5
  • 36
    • 0029146297 scopus 로고
    • A calorimetric characterization of the salt dependence of the stability of the GCN4 leucine zipper
    • Kenar K.T., García-Moreno B., Freire E. A calorimetric characterization of the salt dependence of the stability of the GCN4 leucine zipper. Protein Sci. 4:1995;1934-1938
    • (1995) Protein Sci. , vol.4 , pp. 1934-1938
    • Kenar, K.T.1    García-Moreno, B.2    Freire, E.3
  • 37
    • 0027375522 scopus 로고
    • Protein internal flexibility and global stability: Effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor
    • Kim K.-S., Woodward C. Protein internal flexibility and global stability effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor. Biochemstry. 32:1993;9609-9613
    • (1993) Biochemstry , vol.32 , pp. 9609-9613
    • Kim, K.-S.1    Woodward, C.2
  • 38
    • 0030203153 scopus 로고    scopus 로고
    • NMR spectroscopy and X-ray crystallography provide complementary information on the structure and dynamics of leucine zippers
    • King G.F. NMR spectroscopy and X-ray crystallography provide complementary information on the structure and dynamics of leucine zippers. Biophys. J. 71:1996;1152-1154
    • (1996) Biophys. J. , vol.71 , pp. 1152-1154
    • King, G.F.1
  • 39
    • 0028959280 scopus 로고
    • Protein destabilization by electrostatic repulsions in the two-stranded α-helical coiled-coil/leucine zipper
    • Kohn W.D., Kay C.M., Hodges R.S. Protein destabilization by electrostatic repulsions in the two-stranded α-helical coiled-coil/leucine zipper. Protein Sci. 4:1995;237-250
    • (1995) Protein Sci. , vol.4 , pp. 237-250
    • Kohn, W.D.1    Kay, C.M.2    Hodges, R.S.3
  • 40
    • 0026737875 scopus 로고
    • The Myc and Max proteins possess distinct transcriptional activities
    • Kretzner L., Blackwood E.M., Eisenman R.E. The Myc and Max proteins possess distinct transcriptional activities. Nature. 359:1992;426-429
    • (1992) Nature , vol.359 , pp. 426-429
    • Kretzner, L.1    Blackwood, E.M.2    Eisenman, R.E.3
  • 41
    • 0026029051 scopus 로고
    • Amide chemical shifts in many helices and proteins are periodic
    • Kuntz I.D., Kosen P.A., Craig E.C. Amide chemical shifts in many helices and proteins are periodic. J. Am. Chem. Soc. 113:1991;1406-1408
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 1406-1408
    • Kuntz, I.D.1    Kosen, P.A.2    Craig, E.C.3
  • 43
    • 0029563395 scopus 로고
    • Preferential heterodimeric parallel coiled-coil formation by synthetic Max and c-Myc leucine zippers: A description of putative electrostatic interactions responsible for the specificity of heterodimerization
    • Lavigne P., Kondelewski L.H., Houston M.E. Jr, Sönnichsen F.D., Lix B., Sykes B.D., Hodges R.S., Kay C.M. Preferential heterodimeric parallel coiled-coil formation by synthetic Max and c-Myc leucine zippers a description of putative electrostatic interactions responsible for the specificity of heterodimerization. J. Mol. Biol. 254:1995;505-520
    • (1995) J. Mol. Biol. , vol.254 , pp. 505-520
    • Lavigne, P.1    Kondelewski, L.H.2    Houston Jr., M.E.3    Sönnichsen, F.D.4    Lix, B.5    Sykes, B.D.6    Hodges, R.S.7    Kay, C.M.8
  • 44
    • 0029926150 scopus 로고    scopus 로고
    • Interhelical salt bridges, coiled-coil stability and specificity of dimerization
    • Lavigne P., Sönnichsen F.D., Kay C.M., Hodges R.S. Interhelical salt bridges, coiled-coil stability and specificity of dimerization. Science. 271:1996;1136-1138
    • (1996) Science , vol.271 , pp. 1136-1138
    • Lavigne, P.1    Sönnichsen, F.D.2    Kay, C.M.3    Hodges, R.S.4
  • 46
    • 0028679626 scopus 로고
    • Transcription factors 2: Helix-loop-helix
    • Littlewood T.D., Evan G.I. Transcription factors 2 helix-loop-helix. Protein Profile. 1:1994;639-741
    • (1994) Protein Profile , vol.1 , pp. 639-741
    • Littlewood, T.D.1    Evan, G.I.2
  • 47
    • 0029008590 scopus 로고
    • A buried polar interaction imparts structural uniqueness in a design heterodimeric coiled-coil
    • Lumb K.J., Kim P.S. A buried polar interaction imparts structural uniqueness in a design heterodimeric coiled-coil. Biochemistry. 34:1995;8642-8648
    • (1995) Biochemistry , vol.34 , pp. 8642-8648
    • Lumb, K.J.1    Kim, P.S.2
  • 48
    • 0029030233 scopus 로고
    • Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper
    • Lumb K.J., Kim P.S. Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper. Science. 268:1995;436-439
    • (1995) Science , vol.268 , pp. 436-439
    • Lumb, K.J.1    Kim, P.S.2
  • 49
    • 0029926150 scopus 로고    scopus 로고
    • Interhelical salt bridges, coiled-coil stability and specificity of dimerization
    • Lumb K.J., Kim P.S. Interhelical salt bridges, coiled-coil stability and specificity of dimerization. Science. 271:1996;1136-1138
    • (1996) Science , vol.271 , pp. 1136-1138
    • Lumb, K.J.1    Kim, P.S.2
  • 52
    • 0016774265 scopus 로고
    • Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure
    • McLachlan A.D., Stewart M. Tropomyosin coiled-coil interactions evidence for an unstaggered structure. J. Mol. Biol. 98:1975;293-304
    • (1975) J. Mol. Biol. , vol.98 , pp. 293-304
    • McLachlan, A.D.1    Stewart, M.2
  • 53
    • 0028168627 scopus 로고
    • The dimerization stability of the HLH-LZ transcription protein is modulated by the leucine zippers: A CD and NMR study of TFEB and c-Myc
    • Muhle-Goll C., Gibson T., Schuck P., Nalis D., Nilges M., Pastore A. The dimerization stability of the HLH-LZ transcription protein is modulated by the leucine zippers a CD and NMR study of TFEB and c-Myc. Biochemistry. 33:1994;11296-11306
    • (1994) Biochemistry , vol.33 , pp. 11296-11306
    • Muhle-Goll, C.1    Gibson, T.2    Schuck, P.3    Nalis, D.4    Nilges, M.5    Pastore, A.6
  • 54
    • 0028839440 scopus 로고
    • The leucine zippers of the HLH-LZ proteins Max and c-Myc preferentially form heterodimers
    • Muhle-Goll C., Nilges M., Pastore A. The leucine zippers of the HLH-LZ proteins Max and c-Myc preferentially form heterodimers. Biochemistry. 34:1995;13554-13564
    • (1995) Biochemistry , vol.34 , pp. 13554-13564
    • Muhle-Goll, C.1    Nilges, M.2    Pastore, A.3
  • 55
    • 0024285896 scopus 로고
    • Determination of the three-dimensional structure of proteins from interproton distances data by hybrid distance geometry-dynamical simulated annealing calculations
    • Nilges M., Clore G.M., Gronenborn A.M. Determination of the three-dimensional structure of proteins from interproton distances data by hybrid distance geometry-dynamical simulated annealing calculations. FEBS Letters. 229:1988;317-324
    • (1988) FEBS Letters , vol.229 , pp. 317-324
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 56
    • 0025272236 scopus 로고
    • Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy
    • Oas T.G., McIntosh L.P., O'Shea E.K., Dahlquist F.W., Kim P.S. Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy. Biochemistry. 29:1990;2891-2894
    • (1990) Biochemistry , vol.29 , pp. 2891-2894
    • Oas, T.G.1    McIntosh, L.P.2    O'Shea, E.K.3    Dahlquist, F.W.4    Kim, P.S.5
  • 57
    • 0024384644 scopus 로고
    • Preferential heterodimer formation by isolated leucine zippers from Fos and Jun
    • O'Shea E.K., Ruthkowski R., Stafford W.F., Kim P.S. Preferential heterodimer formation by isolated leucine zippers from Fos and Jun. Science. 241:1989;646-648
    • (1989) Science , vol.241 , pp. 646-648
    • O'Shea, E.K.1    Ruthkowski, R.2    Stafford, W.F.3    Kim, P.S.4
  • 58
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled-coil
    • O'Shea E.K., Klemm J.D., Kim P.S., Alber T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled-coil. Science. 254:1991;539-544
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 59
    • 0026571898 scopus 로고
    • Mechanism of specificity in the Fos-Jun oncoprotein heterodimer
    • O'Shea E.K., Ruthkowski R., Kim P.S. Mechanism of specificity in the Fos-Jun oncoprotein heterodimer. Cell. 66:1992;699-708
    • (1992) Cell , vol.66 , pp. 699-708
    • O'Shea, E.K.1    Ruthkowski, R.2    Kim, P.S.3
  • 60
    • 0000236570 scopus 로고
    • Peptide 'Velcro' design of a heterodimeric coiled-coil
    • O'Shea E.K., Lumb K.J., Kim P.S. Peptide 'Velcro' design of a heterodimeric coiled-coil. Curr. Biol. 3:1993;658-667
    • (1993) Curr. Biol. , vol.3 , pp. 658-667
    • O'Shea, E.K.1    Lumb, K.J.2    Kim, P.S.3
  • 61
    • 0021105573 scopus 로고
    • Protein conformation and proton nuclear-magnetic-resonance chemical shift
    • Pardi A., Wagner G., Wüthrich K. Protein conformation and proton nuclear-magnetic-resonance chemical shift. Eur. J. Biochem. 137:1983;445-454
    • (1983) Eur. J. Biochem. , vol.137 , pp. 445-454
    • Pardi, A.1    Wagner, G.2    Wüthrich, K.3
  • 62
    • 0025829169 scopus 로고
    • Association of Myn, the murine homolog of Max, with c-Myc stimulates methylation sensitive DNA binding and Ras cotransformation
    • Prendergast G.C., Lawe D., Ziff E.B. Association of Myn, the murine homolog of Max, with c-Myc stimulates methylation sensitive DNA binding and Ras cotransformation. Cell. 65:1991;395-407
    • (1991) Cell , vol.65 , pp. 395-407
    • Prendergast, G.C.1    Lawe, D.2    Ziff, E.B.3
  • 63
    • 0018588511 scopus 로고
    • Stability of proteins, small globular proteins
    • Privalov P. Stability of proteins, small globular proteins. Advan. Protein Chem. 33:1979;167-241
    • (1979) Advan. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.1
  • 65
    • 0021755764 scopus 로고
    • Solvent accessible surface area and excluded volume in proteins
    • Richmond T.J. Solvent accessible surface area and excluded volume in proteins. J. Mol. Biol. 82:1984;63-89
    • (1984) J. Mol. Biol. , vol.82 , pp. 63-89
    • Richmond, T.J.1
  • 66
    • 0030844740 scopus 로고    scopus 로고
    • A designed buried salt bridge in a heterodimeric coiled-coil
    • Schneider J.P., Lear J.D., DeGrado W.F. A designed buried salt bridge in a heterodimeric coiled-coil. J. Am. Chem. Soc. 119:1997;5742-5743
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 5742-5743
    • Schneider, J.P.1    Lear, J.D.2    Degrado, W.F.3
  • 67
    • 0024298839 scopus 로고
    • Stability mutants of staphylococcal nuclease: Large compensating enthalpy-entropy changes for the reversible denaturation reaction
    • Shortle D., Meeker A.K., Freire E. Stability mutants of staphylococcal nuclease large compensating enthalpy-entropy changes for the reversible denaturation reaction. Biochemistry. 27:1988;4761-4768
    • (1988) Biochemistry , vol.27 , pp. 4761-4768
    • Shortle, D.1    Meeker, A.K.2    Freire, E.3
  • 68
    • 2642628181 scopus 로고
    • A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quandrants
    • States D.J., Haberkorn R.A., Ruben D.J. A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quandrants. J. Magn. Res. 48:1982;292-296
    • (1982) J. Magn. Res , vol.48 , pp. 292-296
    • States, D.J.1    Haberkorn, R.A.2    Ruben, D.J.3
  • 70
    • 0001647480 scopus 로고
    • Tropomyosin: A model protein for studying coiled-coils and α-helix stabilization
    • Talbot J.A., Hodges R.S. Tropomyosin a model protein for studying coiled-coils and α-helix stabilization. Acc. Chem. Res. 15:1982;224-230
    • (1982) Acc. Chem. Res. , vol.15 , pp. 224-230
    • Talbot, J.A.1    Hodges, R.S.2
  • 72
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart D.S., Sykes B.D., Richards F.M. The chemical shift index a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry. 31:1992;1647-1651
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 74
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J. Biomol. NMR. 5:1995;67-81
    • (1995) 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
  • 76
    • 0021095743 scopus 로고
    • Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance
    • Wüthrich K., Billeter M., Braun W. Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance. J. Mol. Biol. 169:1983;949-961
    • (1983) J. Mol. Biol. , vol.169 , pp. 949-961
    • Wüthrich, K.1    Billeter, M.2    Braun, W.3
  • 77
    • 0027231258 scopus 로고
    • On the pH dependence of protein stability
    • Yang A.-S., Honig B. On the pH dependence of protein stability. J. Mol. Biol. 231:1993;459-474
    • (1993) J. Mol. Biol. , vol.231 , pp. 459-474
    • Yang, A.-S.1    Honig, B.2
  • 78
    • 0027511606 scopus 로고
    • Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites
    • Zervos A.S., Gyuris J., Brent R. Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites. Cell. 72:1993;223-232
    • (1993) Cell , vol.72 , pp. 223-232
    • Zervos, A.S.1    Gyuris, J.2    Brent, R.3
  • 79
    • 0028364239 scopus 로고
    • The role of interhelical ionic interactions in controlling protein folding and stability: De novo designed synthetic two-stranded α-helical coiled-coils
    • Zhou N.E., Kay C.M., Hodges R.S. The role of interhelical ionic interactions in controlling protein folding and stability de novo designed synthetic two-stranded α-helical coiled-coils. J. Mol. Biol. 237:1994;500-512
    • (1994) J. Mol. Biol. , vol.237 , pp. 500-512
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3
  • 80
    • 0027949381 scopus 로고
    • The net energetic contribution of interhelical electrostatic attractions to coiled-coil stability
    • Zhou N.E., Kay C.M., Hodges R.S. The net energetic contribution of interhelical electrostatic attractions to coiled-coil stability. Protein Eng. 7:1994;1365-1372
    • (1994) Protein Eng. , vol.7 , pp. 1365-1372
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.