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Volumn 44, Issue 37, 2005, Pages 12454-12470

Coupled folding and binding with α-helix-forming molecular recognition elements

Author keywords

[No Author keywords available]

Indexed keywords

ALGORITHMS; BIT ERROR RATE; CONFORMATIONS; DATABASE SYSTEMS; MOLECULAR STRUCTURE; NUCLEIC ACIDS; PROTEINS;

EID: 24944546549     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050736e     Document Type: Article
Times cited : (561)

References (101)
  • 1
    • 0033597729 scopus 로고    scopus 로고
    • The Cap-binding protein eIF4E promotes folding of a functional domain of yeast translation initiation factor eIF4G1
    • Hershey, P. E., McWhirter, S. M., Gross, J. D., Wagner, G., Alber, T., and Sachs, A. B. (1999) The Cap-binding protein eIF4E promotes folding of a functional domain of yeast translation initiation factor eIF4G1, J. Biol. Chem. 274, 21297-21304.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21297-21304
    • Hershey, P.E.1    McWhirter, S.M.2    Gross, J.D.3    Wagner, G.4    Alber, T.5    Sachs, A.B.6
  • 2
    • 0031821410 scopus 로고    scopus 로고
    • The interaction of eIF4E with 4E-BP1 is an induced fit to a completely disordered protein
    • Fletcher, C. M., and Wagner, G. (1998) The interaction of eIF4E with 4E-BP1 is an induced fit to a completely disordered protein, Protein Sci. 7, 1639-1642.
    • (1998) Protein Sci. , vol.7 , pp. 1639-1642
    • Fletcher, C.M.1    Wagner, G.2
  • 3
    • 0032489390 scopus 로고    scopus 로고
    • Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex
    • Pan, G., O'Rourke, K., and Dixit, V. M. (1998) Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex, J. Biol. Chem. 273, 5841-5845.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5841-5845
    • Pan, G.1    O'Rourke, K.2    Dixit, V.M.3
  • 4
    • 0030695837 scopus 로고    scopus 로고
    • Bad is a BH3 domain-containing protein that forms an inactivating dimer with Bcl-XL
    • Kelekar, A., Chang, B. S., Harlan, J. E., Fesik, S. W., and Thompson, C. B. (1997) Bad is a BH3 domain-containing protein that forms an inactivating dimer with Bcl-XL, Mol. Cell. Biol. 17, 7040-7046.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 7040-7046
    • Kelekar, A.1    Chang, B.S.2    Harlan, J.E.3    Fesik, S.W.4    Thompson, C.B.5
  • 7
    • 0034177264 scopus 로고    scopus 로고
    • Antagonists of protein-protein interactions
    • Cochran, A. G. (2000) Antagonists of protein-protein interactions, Chem. Biol. 7, R85-R94.
    • (2000) Chem. Biol. , vol.7
    • Cochran, A.G.1
  • 9
    • 0029913807 scopus 로고    scopus 로고
    • An evolutionary trace method defines binding surfaces common to protein families
    • Lichtarge, O., Bourne, H. R., and Cohen, F. E. (1996) An evolutionary trace method defines binding surfaces common to protein families, J. Mol. Biol. 257, 342-358.
    • (1996) J. Mol. Biol. , vol.257 , pp. 342-358
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 10
    • 0036122073 scopus 로고    scopus 로고
    • Prediction of protein-protein interaction sites in heterocomplexes with neural networks
    • Fariselli, P., Pazos, F., Valencia, A., and Casadio, R. (2002) Prediction of protein-protein interaction sites in heterocomplexes with neural networks, Eur. J. Biochem. 269, 1356-1361.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1356-1361
    • Fariselli, P.1    Pazos, F.2    Valencia, A.3    Casadio, R.4
  • 11
    • 0036601150 scopus 로고    scopus 로고
    • Computational methods for the prediction of protein interactions
    • Valencia, A., and Pazos, F. (2002) Computational methods for the prediction of protein interactions, Curr. Opin. Struct. Biol. 12, 368-373.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 368-373
    • Valencia, A.1    Pazos, F.2
  • 12
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky, V. N., Gillespie, J. R., and Fink, A. L. (2000) Why are "natively unfolded" proteins unstructured under physiologic conditions?, Proteins 41, 415-427.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 13
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright, P. E., and Dyson, H. J. (1999) Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm, J. Mol. Biol. 293, 321-331.
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 16
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V. N. (2002) Natively unfolded proteins: a point where biology waits for physics, Protein Sci. 11, 739-756.
    • (2002) Protein Sci. , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 17
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • Uversky, V. N. (2002) What does it mean to be natively unfolded?, Eur. J. Biochem. 269, 2-12.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 18
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson, H. J., and Wright, P. E. (2002) Coupling of folding and binding for unstructured proteins, Curr. Opin. Struct. Biol. 12, 54-60.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 19
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa, P. (2002) Intrinsically unstructured proteins, Trends Biochem. Sci. 27, 527-533.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 527-533
    • Tompa, P.1
  • 20
    • 0035096292 scopus 로고    scopus 로고
    • Recognition between flexible protein molecules: Induced and assisted folding
    • Demchenko, A. P. (2001) Recognition between flexible protein molecules: induced and assisted folding, J. Mol. Recognit. 14, 42-61.
    • (2001) J. Mol. Recognit. , vol.14 , pp. 42-61
    • Demchenko, A.P.1
  • 22
    • 0035131438 scopus 로고    scopus 로고
    • Roles of partly unfolded conformations in macromolecular self-assembly
    • Namba, K. (2001) Roles of partly unfolded conformations in macromolecular self-assembly, Genes Cells 6, 1-12.
    • (2001) Genes Cells , vol.6 , pp. 1-12
    • Namba, K.1
  • 23
    • 0141861067 scopus 로고    scopus 로고
    • Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: Which way to go?
    • Uversky, V. N. (2003) Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: which way to go?, Cell. Mol. Life Sci. 60, 1852-1871.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1852-1871
    • Uversky, V.N.1
  • 24
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H. J., and Wright, P. E. (2005) Intrinsically unstructured proteins and their functions, Nat. Rev. Mol. Cell Biol. 6, 197-208.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 25
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • Weinreb, P. H., Zhen, W., Poon, A. W., Conway, K. A., and Lansbury, P. T., Jr. (1996) NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded, Biochemistry 35, 13709-13715.
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury Jr., P.T.5
  • 26
    • 84889806939 scopus 로고    scopus 로고
    • Natively disordered protein
    • (Buchner, J., and Kiefhaber, T., Eds.), Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
    • Daughdrill, G. W., Pielak, G. J., Uversky, V. N., Cortese, M. S., and Dunker, A. K. (2005) Natively disordered protein, in Protein Folding Handbook (Buchner, J., and Kiefhaber, T., Eds.) pp 275-357, Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
    • (2005) Protein Folding Handbook , pp. 275-357
    • Daughdrill, G.W.1    Pielak, G.J.2    Uversky, V.N.3    Cortese, M.S.4    Dunker, A.K.5
  • 32
    • 0000332920 scopus 로고    scopus 로고
    • Sequence data analysis for long disordered regions prediction in the calcineurin family
    • Romero, P., Obradovic, Z., and Dunker, A. K. (1997) Sequence data analysis for long disordered regions prediction in the calcineurin family, Genome Inf. Ser. No. 8, 110-124.
    • (1997) Genome Inf. Ser. , vol.8 , pp. 110-124
    • Romero, P.1    Obradovic, Z.2    Dunker, A.K.3
  • 33
  • 35
    • 0034808117 scopus 로고    scopus 로고
    • Comparing function and structure between entire proteomes
    • Liu, J., and Rost, B. (2001) Comparing function and structure between entire proteomes, Protein Sci. 10, 1970-1979.
    • (2001) Protein Sci. , vol.10 , pp. 1970-1979
    • Liu, J.1    Rost, B.2
  • 39
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson, T. (1995) Protein modules and signalling networks, Nature 373, 573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 42
    • 2142757231 scopus 로고    scopus 로고
    • Preformed structural elements feature in partner recognition by intrinsically unstructured proteins
    • Fuxreiter, M., Simon, I., Friedrich, P., and Tompa, P. (2004) Preformed structural elements feature in partner recognition by intrinsically unstructured proteins, J. Mol. Biol. 338, 1015-1026.
    • (2004) J. Mol. Biol. , vol.338 , pp. 1015-1026
    • Fuxreiter, M.1    Simon, I.2    Friedrich, P.3    Tompa, P.4
  • 43
    • 1642512502 scopus 로고    scopus 로고
    • The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner
    • Bourhis, J. M., Johansson, K., Receveur-Brechot, V., Oldfield, C. J., Dunker, K. A., Canard, B., and Longhi, S. (2004) The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner, Virus Res. 99, 157-167.
    • (2004) Virus Res. , vol.99 , pp. 157-167
    • Bourhis, J.M.1    Johansson, K.2    Receveur-Brechot, V.3    Oldfield, C.J.4    Dunker, K.A.5    Canard, B.6    Longhi, S.7
  • 46
    • 0028205447 scopus 로고
    • Enlarged representative set of protein structures
    • Hobohm, U., and Sander, C. (1994) Enlarged representative set of protein structures, Protein Sci. 3, 522-524.
    • (1994) Protein Sci. , vol.3 , pp. 522-524
    • Hobohm, U.1    Sander, C.2
  • 48
    • 0034887203 scopus 로고    scopus 로고
    • Creating the gene ontology resource: Design and implementation
    • The Gene Ontology Consortium (2001) Creating the gene ontology resource: design and implementation, Genome Res. 11, 1425-1433.
    • (2001) Genome Res. , vol.11 , pp. 1425-1433
  • 50
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward, J. J., Sodhi, J. S., McGuffin, L. J., Buxton, B. F., and Jones, D. T. (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life, J. Mol. Biol. 337, 635-645.
    • (2004) J. Mol. Biol. , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 51
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and Sander, C. (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features, Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 52
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein, J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 53
    • 0028361031 scopus 로고
    • Accuracy of protein flexibility predictions
    • Vihinen, M., Torkkila, E., and Riikonen, P. (1994) Accuracy of protein flexibility predictions, Proteins 19, 141-149.
    • (1994) Proteins , vol.19 , pp. 141-149
    • Vihinen, M.1    Torkkila, E.2    Riikonen, P.3
  • 54
    • 84856043672 scopus 로고
    • A mathematical theory of communication
    • Shannon, C. E. (1948) A mathematical theory of communication, Bell Syst. Tech. J. 379-423.
    • (1948) Bell Syst. Tech. J. , pp. 379-423
    • Shannon, C.E.1
  • 55
    • 0019934717 scopus 로고
    • The helical hydrophobic moment: A measure of the amphiphilicity of a helix
    • Eisenberg, D., Weiss, R. M., and Terwilliger, T. C. (1982) The helical hydrophobic moment: a measure of the amphiphilicity of a helix, Nature 299, 371-374.
    • (1982) Nature , vol.299 , pp. 371-374
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 56
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones, D. T. (1999) Protein secondary structure prediction based on position-specific scoring matrices, J. Mol. Biol. 292, 195-202.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 57
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier, J., Osguthorpe, D. J., and Robson, B. (1978) Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins, J. Mol. Biol. 120, 97-120.
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 62
    • 0029166687 scopus 로고
    • The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins
    • Mader, S., Lee, H., Pause, A., and Sonenberg, N. (1995) The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins, Mol. Cell. Biol. 15, 4990-4997.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4990-4997
    • Mader, S.1    Lee, H.2    Pause, A.3    Sonenberg, N.4
  • 64
    • 0030669223 scopus 로고    scopus 로고
    • A single chain Fv fragment of P-glycoprotein-specific monoclonal antibody C219. Design, expression, and crystal structure at 2.4 Å resolution
    • Hoedemaeker, F. J., Signorelli, T., Johns, K., Kuntz, D. A., and Rose, D. R. (1997) A single chain Fv fragment of P-glycoprotein-specific monoclonal antibody C219. Design, expression, and crystal structure at 2.4 Å resolution, J. Biol. Chem. 272, 29784-29789.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29784-29789
    • Hoedemaeker, F.J.1    Signorelli, T.2    Johns, K.3    Kuntz, D.A.4    Rose, D.R.5
  • 67
    • 0032146987 scopus 로고    scopus 로고
    • Bcl-2-family proteins: The role of the BH3 domain in apoptosis
    • Kelekar, A., and Thompson, C. B. (1998) Bcl-2-family proteins: the role of the BH3 domain in apoptosis, Trends Cell Biol. 8, 324-330.
    • (1998) Trends Cell Biol. , vol.8 , pp. 324-330
    • Kelekar, A.1    Thompson, C.B.2
  • 69
    • 0027299935 scopus 로고
    • The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: A kinetic analysis of the inhibition of gelatinase A
    • Willenbrock, F., Crabbe, T., Slocombe, P. M., Sutton, C. W., Docherty, A. J., Cockett, M. I., O'Shea, M., Brocklehurst, K., Phillips, I. R., and Murphy, G. (1993) The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: a kinetic analysis of the inhibition of gelatinase A, Biochemistry 32, 4330-4337.
    • (1993) Biochemistry , vol.32 , pp. 4330-4337
    • Willenbrock, F.1    Crabbe, T.2    Slocombe, P.M.3    Sutton, C.W.4    Docherty, A.J.5    Cockett, M.I.6    O'Shea, M.7    Brocklehurst, K.8    Phillips, I.R.9    Murphy, G.10
  • 70
    • 0030575937 scopus 로고    scopus 로고
    • Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain
    • Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., and Pavletich, N. P. (1996) Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain, Science 274, 948-953.
    • (1996) Science , vol.274 , pp. 948-953
    • Kussie, P.H.1    Gorina, S.2    Marechal, V.3    Elenbaas, B.4    Moreau, J.5    Levine, A.J.6    Pavletich, N.P.7
  • 71
    • 0032496388 scopus 로고    scopus 로고
    • The N terminus of the flagellar switch protein, FliM, is the binding domain for the chemotactic response regulator, CheY
    • Bren, A., and Eisenbach, M. (1998) The N terminus of the flagellar switch protein, FliM, is the binding domain for the chemotactic response regulator, CheY, J. Mol. Biol. 278, 507-514.
    • (1998) J. Mol. Biol. , vol.278 , pp. 507-514
    • Bren, A.1    Eisenbach, M.2
  • 72
    • 0034600952 scopus 로고    scopus 로고
    • The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography
    • Mosyak, L., Zhang, Y., Glasfeld, E., Haney, S., Stahl, M., Seehra, J., and Somers, W. S. (2000) The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography, EMBO J. 19, 3179-3191.
    • (2000) EMBO J. , vol.19 , pp. 3179-3191
    • Mosyak, L.1    Zhang, Y.2    Glasfeld, E.3    Haney, S.4    Stahl, M.5    Seehra, J.6    Somers, W.S.7
  • 73
    • 0031924788 scopus 로고    scopus 로고
    • Interaction between subunits of heterodimeric splicing factor U2AF is essential in vivo
    • Rudner, D. Z., Kanaar, R., Breger, K. S., and Rio, D. C. (1998) Interaction between subunits of heterodimeric splicing factor U2AF is essential in vivo, Mol. Cell. Biol. 18, 1765-1773.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1765-1773
    • Rudner, D.Z.1    Kanaar, R.2    Breger, K.S.3    Rio, D.C.4
  • 75
    • 0034657187 scopus 로고    scopus 로고
    • Structural basis of the Axin-adenomatous polyposis coli interaction
    • Spink, K. E., Polakis, P., and Weis, W. I. (2000) Structural basis of the Axin-adenomatous polyposis coli interaction, EMBO J. 19, 2270-2279.
    • (2000) EMBO J. , vol.19 , pp. 2270-2279
    • Spink, K.E.1    Polakis, P.2    Weis, W.I.3
  • 76
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • Heery, D. M., Kalkhoven, E., Hoare, S., and Parker, M. G. (1997) A signature motif in transcriptional co-activators mediates binding to nuclear receptors, Nature 387, 733-736.
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 77
    • 0030871048 scopus 로고    scopus 로고
    • Loss of beta-catenin regulation by the APC tumor suppressor protein correlates with loss of structure due to common somatic mutations of the gene
    • Rubinfeld, B., Albert, I., Porfiri, E., Munemitsu, S., and Polakis, P. (1997) Loss of beta-catenin regulation by the APC tumor suppressor protein correlates with loss of structure due to common somatic mutations of the gene, Cancer Res. 57, 4624-4630.
    • (1997) Cancer Res. , vol.57 , pp. 4624-4630
    • Rubinfeld, B.1    Albert, I.2    Porfiri, E.3    Munemitsu, S.4    Polakis, P.5
  • 78
    • 0035890060 scopus 로고    scopus 로고
    • Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex
    • Eklof, S. K., Fridman, S. G., and Weis, W. I. (2001) Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex, EMBO J. 20, 6203-6212.
    • (2001) EMBO J. , vol.20 , pp. 6203-6212
    • Eklof, S.K.1    Fridman, S.G.2    Weis, W.I.3
  • 79
    • 0032931517 scopus 로고    scopus 로고
    • The p53 pathway
    • Prives, C., and Hall, P. A. (1999) The p53 pathway, J. Pathol 187, 112-126.
    • (1999) J. Pathol , vol.187 , pp. 112-126
    • Prives, C.1    Hall, P.A.2
  • 80
    • 0033945124 scopus 로고    scopus 로고
    • Structure of the negative regulatory domain of p53 bound to S100B(betabeta)
    • Rustandi, R. R., Baldisseri, D. M., and Weber, D. J. (2000) Structure of the negative regulatory domain of p53 bound to S100B(betabeta), Nat. Struct. Biol. 7, 570-574.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 570-574
    • Rustandi, R.R.1    Baldisseri, D.M.2    Weber, D.J.3
  • 82
    • 0033607003 scopus 로고    scopus 로고
    • Placement of protein and RNA structures into a 5 Å-resolution map of the 50S ribosomal subunit
    • Ban, N., Nissen, P., Hansen, J., Capel, M., Moore, P. B., and Steitz, T. A. (1999) Placement of protein and RNA structures into a 5 Å-resolution map of the 50S ribosomal subunit, Nature 400, 841-847.
    • (1999) Nature , vol.400 , pp. 841-847
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Capel, M.4    Moore, P.B.5    Steitz, T.A.6
  • 83
    • 0002086583 scopus 로고
    • Nucleotide binding proteins
    • (Balaban, M., Ed.), Elsevier/North-Holland Biomedical Press, New York
    • Schulz, G. E. (1979) Nucleotide binding proteins, in Molecular Mechanism of Biological Recognition (Balaban, M., Ed.) pp 79-94, Elsevier/North-Holland Biomedical Press, New York.
    • (1979) Molecular Mechanism of Biological Recognition , pp. 79-94
    • Schulz, G.E.1
  • 85
    • 0033152072 scopus 로고    scopus 로고
    • Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of elF4G
    • Marcotrigiano, J., Gingras, A. C., Sonenberg, N., and Burley, S. K. (1999) Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of elF4G, Mol. Cell 3, 707-716.
    • (1999) Mol. Cell , vol.3 , pp. 707-716
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 87
    • 0001178028 scopus 로고    scopus 로고
    • Paramyxoviridae: The viruses and their replication
    • (Fields, B. N., Knipe, D. M., and Howley, P. M., Eds.) 4th ed., Lippincott Williams & Wilkins, Philadelphia
    • Lamb, R. A., and Kolakofsky, D. (2001) Paramyxoviridae: the viruses and their replication, in Fields Virology (Fields, B. N., Knipe, D. M., and Howley, P. M., Eds.) 4th ed., pp 1305-1340, Lippincott Williams & Wilkins, Philadelphia.
    • (2001) Fields Virology , pp. 1305-1340
    • Lamb, R.A.1    Kolakofsky, D.2
  • 88
    • 0023866378 scopus 로고
    • Antibodies against Sendai virus L protein: Distribution of the protein in nucleocapsids revealed by immunoelectron microscopy
    • Portner, A., Murti, K. G., Morgan, E. M., and Kingsbury, D. W. (1988) Antibodies against Sendai virus L protein: distribution of the protein in nucleocapsids revealed by immunoelectron microscopy, Virology 163, 236-239.
    • (1988) Virology , vol.163 , pp. 236-239
    • Portner, A.1    Murti, K.G.2    Morgan, E.M.3    Kingsbury, D.W.4
  • 89
    • 0029926011 scopus 로고    scopus 로고
    • Domains of the measles virus N protein required for binding to P protein and self-assembly
    • Bankamp, B., Horikami, S. M., Thompson, P. D., Huber, M., Billeter, M., and Moyer, S. A. (1996) Domains of the measles virus N protein required for binding to P protein and self-assembly, Virology 216, 272-277.
    • (1996) Virology , vol.216 , pp. 272-277
    • Bankamp, B.1    Horikami, S.M.2    Thompson, P.D.3    Huber, M.4    Billeter, M.5    Moyer, S.A.6
  • 90
    • 0027994818 scopus 로고
    • The carboxy-terminal domain of Sendai virus nucleocapsid protein is involved in complex formation between phosphoprotein and nucleocapsid-like particles
    • Buchholz, C. J., Retzler, C., Homann, H. E., and Neubert, W. J. (1994) The carboxy-terminal domain of Sendai virus nucleocapsid protein is involved in complex formation between phosphoprotein and nucleocapsid-like particles, Virology 204, 770-776.
    • (1994) Virology , vol.204 , pp. 770-776
    • Buchholz, C.J.1    Retzler, C.2    Homann, H.E.3    Neubert, W.J.4
  • 91
    • 0027159962 scopus 로고
    • The hypervariable C-terminal tail of the Sendai paramyxovirus nucleocapsid protein is required for template function but not for RNA encapsidation
    • Curran, J., Homann, H., Buchholz, C., Rochat, S., Neubert, W., and Kolakofsky, D. (1993) The hypervariable C-terminal tail of the Sendai paramyxovirus nucleocapsid protein is required for template function but not for RNA encapsidation, J. Virol. 67, 4358-4364.
    • (1993) J. Virol. , vol.67 , pp. 4358-4364
    • Curran, J.1    Homann, H.2    Buchholz, C.3    Rochat, S.4    Neubert, W.5    Kolakofsky, D.6
  • 92
    • 0028803809 scopus 로고
    • Measles virus phosphoprotein (P) requires the NH2- And COOH-terminal domains for interactions with the nucleoprotein (N) but only the COOH terminus for interactions with itself
    • Harty, R. N., and Palese, P. (1995) Measles virus phosphoprotein (P) requires the NH2- and COOH-terminal domains for interactions with the nucleoprotein (N) but only the COOH terminus for interactions with itself, J. Gen. Virol. 76 (Part 11), 2863-2867.
    • (1995) J. Gen. Virol. , vol.76 , Issue.PART 11 , pp. 2863-2867
    • Harty, R.N.1    Palese, P.2
  • 93
    • 0032807746 scopus 로고    scopus 로고
    • Mapping of domains on the human parainfluenza virus type 2 nucleocapsid protein (NP) required for NP-phosphoprotein or NP-NP interaction
    • Nishio, M., Tsurudome, M., Ito, M., Kawano, M., Kusagawa, S., Komada, H., and Ito, Y. (1999) Mapping of domains on the human parainfluenza virus type 2 nucleocapsid protein (NP) required for NP-phosphoprotein or NP-NP interaction, J. Gen. Virol. 80 (Part 8), 2017-2022.
    • (1999) J. Gen. Virol. , vol.80 , Issue.PART 8 , pp. 2017-2022
    • Nishio, M.1    Tsurudome, M.2    Ito, M.3    Kawano, M.4    Kusagawa, S.5    Komada, H.6    Ito, Y.7
  • 94
    • 0037705413 scopus 로고    scopus 로고
    • The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein
    • Longhi, S., Receveur-Brechot, V., Karlin, D., Johansson, K., Darbon, H., Bhella, D., Yeo, R., Finet, S., and Canard, B. (2003) The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein, J. Biol. Chem. 278, 18638-18648.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18638-18648
    • Longhi, S.1    Receveur-Brechot, V.2    Karlin, D.3    Johansson, K.4    Darbon, H.5    Bhella, D.6    Yeo, R.7    Finet, S.8    Canard, B.9
  • 96
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • Cho, Y., Gorina, S., Jeffrey, P. D., and Pavletich, N. P. (1994) Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations, Science 265, 346-355.
    • (1994) Science , vol.265 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 97
    • 0028952841 scopus 로고
    • Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms
    • Jeffrey, P. D., Gorina, S., and Pavletich, N. P. (1995) Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms, Science 267, 1498-1502.
    • (1995) Science , vol.267 , pp. 1498-1502
    • Jeffrey, P.D.1    Gorina, S.2    Pavletich, N.P.3
  • 98
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: The fly-casting mechanism
    • Shoemaker, B. A., Portman, J. J., and Wolynes, P. G. (2000) Speeding molecular recognition by using the folding funnel: the fly-casting mechanism, Proc. Natl. Acad. Sci. U.S.A. 97, 8868-8873.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8868-8873
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.G.3
  • 99
    • 0027311259 scopus 로고
    • Close encounters: Why unstructured, polymeric domains can increase rates of specific macromolecular association
    • Pontius, B. W. (1993) Close encounters: why unstructured, polymeric domains can increase rates of specific macromolecular association, Trends Biochem. Sci. 18, 181-186.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 181-186
    • Pontius, B.W.1
  • 100
    • 0037067343 scopus 로고    scopus 로고
    • Staudinger ligation of alpha-azido acids retains stereochemistry
    • Soellner, M. B., Nilsson, B. L., and Raines, R. T. (2002) Staudinger ligation of alpha-azido acids retains stereochemistry, J. Org. Chem. 67, 4993-4996.
    • (2002) J. Org. Chem. , vol.67 , pp. 4993-4996
    • Soellner, M.B.1    Nilsson, B.L.2    Raines, R.T.3
  • 101
    • 0033918391 scopus 로고    scopus 로고
    • Mass spectrometry: A tool for the identification of proteins separated by gels
    • Lahm, H. W., and Langen, H. (2000) Mass spectrometry: a tool for the identification of proteins separated by gels, Electrophoresis 21, 2105-2114.
    • (2000) Electrophoresis , vol.21 , pp. 2105-2114
    • Lahm, H.W.1    Langen, H.2


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