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Volumn 6, Issue 6, 2007, Pages 2351-2366

Characterization of molecular recognition features, MoRFs, and their binding partners

Author keywords

Intrinsic disorder; Molecular recognition; MoRF; Protein protein interaction; Signaling

Indexed keywords

BINDING PROTEIN; HETERODIMER; HOMODIMER; MONOMER;

EID: 34250815165     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr0701411     Document Type: Article
Times cited : (412)

References (95)
  • 1
    • 0024046505 scopus 로고
    • An investigation of protein subunit and domain interfaces
    • Argos, P. An investigation of protein subunit and domain interfaces. Protein Eng. 1988, 2, 101-113.
    • (1988) Protein Eng , vol.2 , pp. 101-113
    • Argos, P.1
  • 2
    • 0016708122 scopus 로고
    • Principles of protein-protein recognition
    • Chothia, C.; Janin, J. Principles of protein-protein recognition. Nature 1975, 256, 705-708.
    • (1975) Nature , vol.256 , pp. 705-708
    • Chothia, C.1    Janin, J.2
  • 3
    • 1842405464 scopus 로고    scopus 로고
    • Studies of protein-protein interfaces: A statistical analysis of the hydrophobic effect
    • Tsai, C. J.; Lin, S. L.; Wolfson, H. J.; Nussinov, R. Studies of protein-protein interfaces: a statistical analysis of the hydrophobic effect. Protein Sci. 1997, 6, 53-64.
    • (1997) Protein Sci , vol.6 , pp. 53-64
    • Tsai, C.J.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4
  • 4
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • Janin, J.; Chothia, C. The structure of protein-protein recognition sites. J. Biol. Chem. 1990, 265, 16027-16030.
    • (1990) J. Biol. Chem , vol.265 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 5
    • 0026079134 scopus 로고
    • Distribution and complementarity of hydropathy in multisubunit proteins
    • Korn, A. P.; Burnett, R. M. Distribution and complementarity of hydropathy in multisubunit proteins. Proteins 1991, 9, 37-55.
    • (1991) Proteins , vol.9 , pp. 37-55
    • Korn, A.P.1    Burnett, R.M.2
  • 6
    • 0028575449 scopus 로고
    • Hydrophobic docking: A proposed enhancement to molecular recognition techniques
    • Vakser, I. A.; Aflalo, C. Hydrophobic docking: a proposed enhancement to molecular recognition techniques. Proteins 1994, 20, 320-329.
    • (1994) Proteins , vol.20 , pp. 320-329
    • Vakser, I.A.1    Aflalo, C.2
  • 7
    • 0028332007 scopus 로고
    • A role for surface hydrophobicity in protein-protein recognition
    • Young, L.; Jernigan, R. L.; Covell, D. G. A role for surface hydrophobicity in protein-protein recognition. Protein Sci. 1994, 3, 717-729.
    • (1994) Protein Sci , vol.3 , pp. 717-729
    • Young, L.1    Jernigan, R.L.2    Covell, D.G.3
  • 8
    • 0029109468 scopus 로고
    • Protein-protein interactions: A review of protein dimer structures
    • Jones, S.; Thornton, J. M. Protein-protein interactions: a review of protein dimer structures. Prog. Biophys. Mol. Biol. 1995, 63, 31-65.
    • (1995) Prog. Biophys. Mol. Biol , vol.63 , pp. 31-65
    • Jones, S.1    Thornton, J.M.2
  • 10
    • 0031565725 scopus 로고    scopus 로고
    • Prediction of protein-protein interaction sites using patch analysis
    • Jones, S.; Thornton, J. M. Prediction of protein-protein interaction sites using patch analysis. J. Mol. Biol. 1997, 272, 133-143.
    • (1997) J. Mol. Biol , vol.272 , pp. 133-143
    • Jones, S.1    Thornton, J.M.2
  • 11
    • 0031565729 scopus 로고    scopus 로고
    • Analysis of protein-protein interaction sites using surface patches
    • Jones, S.; Thornton, J. M. Analysis of protein-protein interaction sites using surface patches. J. Mol. Biol. 1997, 272, 121-132.
    • (1997) J. Mol. Biol , vol.272 , pp. 121-132
    • Jones, S.1    Thornton, J.M.2
  • 12
    • 0032522670 scopus 로고    scopus 로고
    • Morphology of protein-protein interfaces
    • Larsen, T. A.; Olson, A. J.; Goodsell, D. S. Morphology of protein-protein interfaces. Structure 1998, 6, 421-427.
    • (1998) Structure , vol.6 , pp. 421-427
    • Larsen, T.A.1    Olson, A.J.2    Goodsell, D.S.3
  • 13
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte, L.; Chothia, C.; Janin, J. The atomic structure of protein-protein recognition sites. J. Mol. Biol. 1999, 285, 2177-2198.
    • (1999) J. Mol. Biol , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 14
    • 0037093645 scopus 로고    scopus 로고
    • Dissecting protein-protein recognition sites
    • Chakrabarti, P.; Janin, J. Dissecting protein-protein recognition sites. Proteins 2002, 47, 334-343.
    • (2002) Proteins , vol.47 , pp. 334-343
    • Chakrabarti, P.1    Janin, J.2
  • 15
    • 0035342450 scopus 로고    scopus 로고
    • Residue frequencies and pairing preferences at protein-protein interfaces
    • Glaser, F.; Steinberg, D. M.; Vakser, I. A.; Ben-Tal, N. Residue frequencies and pairing preferences at protein-protein interfaces. Proteins 2001, 43, 89-102.
    • (2001) Proteins , vol.43 , pp. 89-102
    • Glaser, F.1    Steinberg, D.M.2    Vakser, I.A.3    Ben-Tal, N.4
  • 16
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • Janin, J.; Miller, S.; Chothia, C. Surface, subunit interfaces and interior of oligomeric proteins. J. Mol. Biol. 1988, 204, 155-164.
    • (1988) J. Mol. Biol , vol.204 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chothia, C.3
  • 17
    • 0035178383 scopus 로고    scopus 로고
    • Protein-protein interfaces: Analysis of amino acid conservation in homodimers
    • Valdar, W. S.; Thornton, J. M. Protein-protein interfaces: analysis of amino acid conservation in homodimers. Proteins 2001, 42, 108-124.
    • (2001) Proteins , vol.42 , pp. 108-124
    • Valdar, W.S.1    Thornton, J.M.2
  • 18
    • 0037422589 scopus 로고    scopus 로고
    • Insufficiently dehydrated hydrogen bonds as determinants of protein interactions
    • Fernandez, A.; Scheraga, H. A. Insufficiently dehydrated hydrogen bonds as determinants of protein interactions. Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 113-118.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 113-118
    • Fernandez, A.1    Scheraga, H.A.2
  • 20
    • 0033757822 scopus 로고    scopus 로고
    • An overview of structural genomics
    • Burley, S. K. An overview of structural genomics. Nat. Struct. Biol. 2000, 7 (Suppl.), 932-934.
    • (2000) Nat. Struct. Biol , vol.7 , Issue.SUPPL. , pp. 932-934
    • Burley, S.K.1
  • 21
    • 15244355250 scopus 로고    scopus 로고
    • The relationship between the flexibility of proteins and their conformational states on forming protein-protein complexes with an application to protein-protein docking
    • Smith, G. R.; Sternberg, M. J.; Bates, P. A. The relationship between the flexibility of proteins and their conformational states on forming protein-protein complexes with an application to protein-protein docking. J. Mol. Biol. 2005, 347, 1077-1101.
    • (2005) J. Mol. Biol , vol.347 , pp. 1077-1101
    • Smith, G.R.1    Sternberg, M.J.2    Bates, P.A.3
  • 22
    • 33646472024 scopus 로고    scopus 로고
    • High-resolution protein-protein docking
    • Gray, J. J. High-resolution protein-protein docking. Curr. Opin. Struct. Biol. 2006, 16, 183-193.
    • (2006) Curr. Opin. Struct. Biol , vol.16 , pp. 183-193
    • Gray, J.J.1
  • 23
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • Uversky, V. N. What does it mean to be natively unfolded? Eur. J. Biochem. 2002, 269, 2-12.
    • (2002) Eur. J. Biochem , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 24
    • 0035906650 scopus 로고    scopus 로고
    • Calculation of ensembles of structures representing the unfolded state of an SH3 domain
    • Choy, W. Y.; Forman-Kay, J. D. Calculation of ensembles of structures representing the unfolded state of an SH3 domain. J. Mol. Biol. 2001, 308, 1011-1032.
    • (2001) J. Mol. Biol , vol.308 , pp. 1011-1032
    • Choy, W.Y.1    Forman-Kay, J.D.2
  • 25
    • 0034867975 scopus 로고    scopus 로고
    • The protein trinity-linking function and disorder
    • Dunker, A. K.; Obradovic, Z. The protein trinity-linking function and disorder. Nat. Biotechnol. 2001, 19, 805-806.
    • (2001) Nat. Biotechnol , vol.19 , pp. 805-806
    • Dunker, A.K.1    Obradovic, Z.2
  • 26
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson, H. J.; Wright, P. E. Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol. 2002, 12, 54-60.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 27
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling
    • Uversky, V. N.; Oldfield, C. J.; Dunker, A. K. Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling. J. Mol. Recognit. 2005, 18, 343-384.
    • (2005) J. Mol. Recognit , vol.18 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 28
    • 33744459472 scopus 로고    scopus 로고
    • Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis
    • Strong, M.; Sawaya, M. R.; Wang, S.; Phillips, M.; Cascio, D.; Eisenberg, D. Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 8060-8065.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 8060-8065
    • Strong, M.1    Sawaya, M.R.2    Wang, S.3    Phillips, M.4    Cascio, D.5    Eisenberg, D.6
  • 30
    • 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.; Jones, D. T. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J. Mol. Biol. 2004, 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
  • 32
    • 24944546549 scopus 로고    scopus 로고
    • Coupled folding and binding with alpha-helix-forming molecular recognition elements
    • Oldfield, C. J.; Cheng, Y.; Cortese, M. S.; Romero, P.; Uversky, V. N.; Dunker, A. K. Coupled folding and binding with alpha-helix-forming molecular recognition elements. Biochemistry 2005, 44, 12454-12470.
    • (2005) Biochemistry , vol.44 , pp. 12454-12470
    • Oldfield, C.J.1    Cheng, Y.2    Cortese, M.S.3    Romero, P.4    Uversky, V.N.5    Dunker, A.K.6
  • 34
    • 0027311259 scopus 로고
    • Close encounters: Why unstructured, polymeric domains can increase rates of specific macromolecular association
    • Pontius, B. W. Close encounters: why unstructured, polymeric domains can increase rates of specific macromolecular association. Trends Biochem. Sci. 1993, 18, 181-186.
    • (1993) Trends Biochem. Sci , vol.18 , pp. 181-186
    • Pontius, B.W.1
  • 35
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: The fly-casting mechanism
    • Shoemaker, B. A.; Portman, J. J.; Wolynes, P. G. Speeding molecular recognition by using the folding funnel: the fly-casting mechanism. Proc. Natl. Acad. Sci. U.S.A. 2000, 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
  • 36
    • 0036909262 scopus 로고    scopus 로고
    • Endocytosis and vesicle trafficking
    • Evans, P. R.; Owen, D. J. Endocytosis and vesicle trafficking. Curr. Opin. Struct. Biol. 2002, 12, 814-821.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 814-821
    • Evans, P.R.1    Owen, D.J.2
  • 38
    • 0029865623 scopus 로고    scopus 로고
    • Context-dependent secondary structure formation of a designed protein sequence
    • Minor, D. L., Jr.; Kim, P. S. Context-dependent secondary structure formation of a designed protein sequence. Nature 1996, 380, 730-734.
    • (1996) Nature , vol.380 , pp. 730-734
    • Minor Jr., D.L.1    Kim, P.S.2
  • 39
    • 0034563423 scopus 로고    scopus 로고
    • Predictions of protein segments with the same aminoacid sequence and different secondary structure: A benchmark for predictive methods
    • Jacoboni, I.; Martelli, P. L.; Fariselli, P.; Compiani, M.; Casadio, R. Predictions of protein segments with the same aminoacid sequence and different secondary structure: a benchmark for predictive methods. Proteins 2000, 41, 535-544.
    • (2000) Proteins , vol.41 , pp. 535-544
    • Jacoboni, I.1    Martelli, P.L.2    Fariselli, P.3    Compiani, M.4    Casadio, R.5
  • 40
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W.; Sander, C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983, 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 41
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly, M. L. Solvent-accessible surfaces of proteins and nucleic acids. Science 1983, 221, 709-713.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 42
    • 0023645203 scopus 로고
    • Interior and surface of monomeric proteins
    • Miller, S.; Janin, J.; Lesk, A. M.; Chothia, C. Interior and surface of monomeric proteins. J. Mol. Biol. 1987, 196, 641-656.
    • (1987) J. Mol. Biol , vol.196 , pp. 641-656
    • Miller, S.1    Janin, J.2    Lesk, A.M.3    Chothia, C.4
  • 46
    • 0028931857 scopus 로고
    • Multiple significance tests: The Bonferroni method
    • Bland, J. M.; Altman, D. G. Multiple significance tests: the Bonferroni method. BMJ [Br. Med. J.] 1995, 310, 170.
    • (1995) BMJ [Br. Med. J.] , vol.310 , pp. 170
    • Bland, J.M.1    Altman, D.G.2
  • 47
    • 0018784438 scopus 로고
    • Surface and inside volumes in globular proteins
    • Janin, J. Surface and inside volumes in globular proteins. Nature 1979, 277, 491-492.
    • (1979) Nature , vol.277 , pp. 491-492
    • Janin, J.1
  • 48
    • 0028361031 scopus 로고
    • Accuracy of protein flexibility predictions
    • Vihinen, M.; Torkkila, E.; Riikonen, P. Accuracy of protein flexibility predictions. Proteins 1994, 19, 141-149.
    • (1994) Proteins , vol.19 , pp. 141-149
    • Vihinen, M.1    Torkkila, E.2    Riikonen, P.3
  • 49
    • 0000484499 scopus 로고
    • Hydrophobic parameters pi of amino acid side chains from the partitioning of N-acetyl-amino acid amides
    • Fauchere, J.-L.; Pliska, V. Hydrophobic parameters pi of amino acid side chains from the partitioning of N-acetyl-amino acid amides. Eur. J. Med. Chem. 1983, 18, 369-375.
    • (1983) Eur. J. Med. Chem , vol.18 , pp. 369-375
    • Fauchere, J.-L.1    Pliska, V.2
  • 50
    • 0031269184 scopus 로고    scopus 로고
    • On the optimality of the simple Bayesian classifier under zero-one loss
    • Domingos, P.; Pazzani, M. On the optimality of the simple Bayesian classifier under zero-one loss. Mach. Learning 1997, 29, 103-137.
    • (1997) Mach. Learning , vol.29 , pp. 103-137
    • Domingos, P.1    Pazzani, M.2
  • 51
    • 30344485673 scopus 로고    scopus 로고
    • Exploiting heterogeneous sequence properties improves prediction of protein disorder
    • Obradovic, Z.; Peng, K.; Vucetic, S.; Radivojac, P.; Dunker, A. K. Exploiting heterogeneous sequence properties improves prediction of protein disorder. Proteins 2005, 61 (Suppl. 7), 176-182.
    • (2005) Proteins , vol.61 , Issue.SUPPL. 7 , pp. 176-182
    • Obradovic, Z.1    Peng, K.2    Vucetic, S.3    Radivojac, P.4    Dunker, A.K.5
  • 52
    • 0029665852 scopus 로고    scopus 로고
    • Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex
    • Russo, A. A.; Jeffrey, P. D.; Patten, A. K.; Massague, J.; Pavletich, N. P. Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex. Nature 1996, 382, 325-331.
    • (1996) Nature , vol.382 , pp. 325-331
    • Russo, A.A.1    Jeffrey, P.D.2    Patten, A.K.3    Massague, J.4    Pavletich, N.P.5
  • 53
    • 0030592544 scopus 로고    scopus 로고
    • Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA
    • Gulbis, J. M.; Kelman, Z.; Hurwitz, J.; O'Donnell, M.; Kuriyan, J. Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA. Cell 1996, 87, 297-306.
    • (1996) Cell , vol.87 , pp. 297-306
    • Gulbis, J.M.1    Kelman, Z.2    Hurwitz, J.3    O'Donnell, M.4    Kuriyan, J.5
  • 54
    • 0029662315 scopus 로고    scopus 로고
    • Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: Conformational disorder mediates binding diversity
    • Kriwacki, R. W.; Hengst, L.; Tennant, L.; Reed, S. I.; Wright, P. E. Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 11504-11509.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 11504-11509
    • Kriwacki, R.W.1    Hengst, L.2    Tennant, L.3    Reed, S.I.4    Wright, P.E.5
  • 56
    • 3242802943 scopus 로고    scopus 로고
    • Callaghan, A. J.; Aurikko, J. P.; Hag, L. L.; Gunter, Grossmann, J.; Chandran, V.; Kuhnel, K.; Poljak, L.; Carpousis, A. J.; Robinson, C. V.; Symmons, M. F.; Luisi, B. F. Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. J. Mol. Biol. 2004, 340, 965-979.
    • Callaghan, A. J.; Aurikko, J. P.; Hag, L. L.; Gunter, Grossmann, J.; Chandran, V.; Kuhnel, K.; Poljak, L.; Carpousis, A. J.; Robinson, C. V.; Symmons, M. F.; Luisi, B. F. Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. J. Mol. Biol. 2004, 340, 965-979.
  • 57
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture, and transport mechanism
    • Rout, M. P.; Aitchison, J. D.; Suprapto, A.; Hjertaas, K.; Zhao, Y.; Chait, B. T. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J. Cell Biol. 2000, 148, 635-651.
    • (2000) J. Cell Biol , vol.148 , pp. 635-651
    • Rout, M.P.1    Aitchison, J.D.2    Suprapto, A.3    Hjertaas, K.4    Zhao, Y.5    Chait, B.T.6
  • 58
    • 0028834428 scopus 로고
    • Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors, and nucleoporins
    • Rexach, M.; Blobel, G. Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins. Cell 1995, 83, 683-692.
    • (1995) Cell , vol.83 , pp. 683-692
    • Rexach, M.1    Blobel, G.2
  • 59
    • 0035802121 scopus 로고    scopus 로고
    • The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p at the nuclear pore complex
    • Denning, D.; Mykytka, B.; Allen, N. P.; Huang, L.; Al, B.; Rexach, M. The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p at the nuclear pore complex. J. Cell Biol. 2001, 154, 937-950.
    • (2001) J. Cell Biol , vol.154 , pp. 937-950
    • Denning, D.1    Mykytka, B.2    Allen, N.P.3    Huang, L.4    Al, B.5    Rexach, M.6
  • 60
    • 0037031842 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein
    • Denning, D. P.; Uversky, V.; Patel, S. S.; Fink, A. L.; Rexach, M. The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein. J. Biol. Chem. 2002, 277, 33447-33455.
    • (2002) J. Biol. Chem , vol.277 , pp. 33447-33455
    • Denning, D.P.1    Uversky, V.2    Patel, S.S.3    Fink, A.L.4    Rexach, M.5
  • 61
    • 0021162488 scopus 로고
    • Overexpression and sequence of the Escherichia coli cheY gene and biochemical activities of the CheY protein
    • Matsumura, P.; Rydel, J. J.; Linzmeier, R.; Vacante, D. Overexpression and sequence of the Escherichia coli cheY gene and biochemical activities of the CheY protein. J. Bacteriol. 1984, 160, 36-41.
    • (1984) J. Bacteriol , vol.160 , pp. 36-41
    • Matsumura, P.1    Rydel, J.J.2    Linzmeier, R.3    Vacante, D.4
  • 62
    • 0027243652 scopus 로고
    • Signal transduction schemes of bacteria
    • Parkinson, J. S. Signal transduction schemes of bacteria. Cell 1993, 73 857-871.
    • (1993) Cell , vol.73 , pp. 857-871
    • Parkinson, J.S.1
  • 63
    • 0030595328 scopus 로고    scopus 로고
    • Signal transduction via the multi-step phosphorelay: Not necessarily a road less traveled
    • Appleby, J. L.; Parkinson, J. S.; Bourret, R. B. Signal transduction via the multi-step phosphorelay: not necessarily a road less traveled. Cell 1996, 86, 845-848.
    • (1996) Cell , vol.86 , pp. 845-848
    • Appleby, J.L.1    Parkinson, J.S.2    Bourret, R.B.3
  • 64
    • 0033603635 scopus 로고    scopus 로고
    • Identification of the binding interfaces on CheY for two of its targets, the phosphatase CheZ and the flagellar switch protein fliM
    • McEvoy, M. M.; Bren, A.; Eisenbach, M.; Dahlquist, F. W. Identification of the binding interfaces on CheY for two of its targets, the phosphatase CheZ and the flagellar switch protein fliM. J. Mol. Biol. 1999, 289, 1423-1433.
    • (1999) J. Mol. Biol , vol.289 , pp. 1423-1433
    • McEvoy, M.M.1    Bren, A.2    Eisenbach, M.3    Dahlquist, F.W.4
  • 66
    • 0034256090 scopus 로고    scopus 로고
    • Calmodulin: A prototypical calcium sensor
    • Chin, D.; Means, A. R. Calmodulin: a prototypical calcium sensor. Trends Cell Biol. 2000, 10, 322-328.
    • (2000) Trends Cell Biol , vol.10 , pp. 322-328
    • Chin, D.1    Means, A.R.2
  • 67
    • 33645292569 scopus 로고    scopus 로고
    • Calmodulin signaling: Analysis and prediction of a disorder-dependent molecular recognition
    • Radivojac, P.; Vucetic, S.; O'Connor, T. R.; Uversky, V. N.; Obradovic, Z.; Dunker, A. K. Calmodulin signaling: analysis and prediction of a disorder-dependent molecular recognition. Proteins 2006, 63, 398-410.
    • (2006) Proteins , vol.63 , pp. 398-410
    • Radivojac, P.1    Vucetic, S.2    O'Connor, T.R.3    Uversky, V.N.4    Obradovic, Z.5    Dunker, A.K.6
  • 68
    • 0037453258 scopus 로고    scopus 로고
    • Structural basis for simultaneous binding of two carboxy-terminal peptides of plant glutamate decarboxylase to calmodulin
    • Yap, K. L.; Yuan, T.; Mai, T. K.; Vogel, H. J.; Ikura, M. Structural basis for simultaneous binding of two carboxy-terminal peptides of plant glutamate decarboxylase to calmodulin. J. Mol. Biol. 2003, 328, 193-204.
    • (2003) J. Mol. Biol , vol.328 , pp. 193-204
    • Yap, K.L.1    Yuan, T.2    Mai, T.K.3    Vogel, H.J.4    Ikura, M.5
  • 69
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • Zhang, M.; Tanaka, T.; Ikura, M. Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nat. Struct. Biol. 1995, 2, 758-767.
    • (1995) Nat. Struct. Biol , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 70
    • 0031054051 scopus 로고    scopus 로고
    • Enzymes and reactions at the eukaryotic DNA replication fork
    • Bambara, R. A.; Murante, R. S.; Henricksen, L. A. Enzymes and reactions at the eukaryotic DNA replication fork. J. Biol. Chem. 1997, 272, 4647-4650.
    • (1997) J. Biol. Chem , vol.272 , pp. 4647-4650
    • Bambara, R.A.1    Murante, R.S.2    Henricksen, L.A.3
  • 71
    • 0035807967 scopus 로고    scopus 로고
    • Okazaki fragment processing: Modulation of the strand displacement activity of DNA polymerase delta by the concerted action of replication protein A, proliferating cell nuclear antigen, and flap endonuclease-1
    • Maga, G.; Villani, G.; Tillement, V.; Stucki, M.; Locatelli, G. A.; Frouin, I.; Spadari, S.; Hubscher, U. Okazaki fragment processing: modulation of the strand displacement activity of DNA polymerase delta by the concerted action of replication protein A, proliferating cell nuclear antigen, and flap endonuclease-1. Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 14298-14303.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 14298-14303
    • Maga, G.1    Villani, G.2    Tillement, V.3    Stucki, M.4    Locatelli, G.A.5    Frouin, I.6    Spadari, S.7    Hubscher, U.8
  • 72
    • 0035225868 scopus 로고    scopus 로고
    • Molecular mechanism of PCNA-dependent base excision repair
    • Matsumoto, Y. Molecular mechanism of PCNA-dependent base excision repair. Prog. Nucleic Acid Res. Mol. Biol. 2001, 68, 129-138.
    • (2001) Prog. Nucleic Acid Res. Mol. Biol , vol.68 , pp. 129-138
    • Matsumoto, Y.1
  • 73
    • 0742321956 scopus 로고    scopus 로고
    • Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair
    • Chapados, B. R.; Hosfield, D. J.; Han, S.; Qiu, J.; Yelent, B.; Shen, B.; Tainer, J. A. Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair. Cell 2004, 116, 39-50.
    • (2004) Cell , vol.116 , pp. 39-50
    • Chapados, B.R.1    Hosfield, D.J.2    Han, S.3    Qiu, J.4    Yelent, B.5    Shen, B.6    Tainer, J.A.7
  • 74
    • 0042220409 scopus 로고    scopus 로고
    • The structure of a Bcl-xL/Bim fragment complex: Implications for Bim function
    • Liu, X.; Dai, S.; Zhu, Y.; Marrack, P.; Kappler, J. W. The structure of a Bcl-xL/Bim fragment complex: implications for Bim function. Immunity 2003, 19, 341-352.
    • (2003) Immunity , vol.19 , pp. 341-352
    • Liu, X.1    Dai, S.2    Zhu, Y.3    Marrack, P.4    Kappler, J.W.5
  • 75
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Arbiters of cell survival
    • Adams, J. M.; Cory, S. The Bcl-2 protein family: arbiters of cell survival. Science 1998, 281, 1322-1326.
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 77
    • 0025823572 scopus 로고
    • On the role of methionine residues in the sequence-independent recognition of nonpolar protein surfaces
    • Gellman, S. H. On the role of methionine residues in the sequence-independent recognition of nonpolar protein surfaces. Biochemistry 1991, 30, 6633-6636.
    • (1991) Biochemistry , vol.30 , pp. 6633-6636
    • Gellman, S.H.1
  • 78
    • 4143107222 scopus 로고    scopus 로고
    • Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers
    • Gunasekaran, K.; Tsai, C. J.; Nussinov, R. Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers. J. Mol. Biol. 2004, 341, 1327-1341.
    • (2004) J. Mol. Biol , vol.341 , pp. 1327-1341
    • Gunasekaran, K.1    Tsai, C.J.2    Nussinov, R.3
  • 80
    • 0042622240 scopus 로고    scopus 로고
    • Linding, R.; Russell, R. B.; Neduva, V.; Gibson, T. J. GlobPlot: Exploring protein sequences for globularity and disorder. Nucleic Acids Res. 2003, 31, 3701-3708.
    • Linding, R.; Russell, R. B.; Neduva, V.; Gibson, T. J. GlobPlot: Exploring protein sequences for globularity and disorder. Nucleic Acids Res. 2003, 31, 3701-3708.
  • 81
    • 0034669882 scopus 로고    scopus 로고
    • Uversky, V. N.; Gillespie, J. R.; Fink, A. L. Why are natively unfolded proteins unstructured under physiologic conditions? Proteins 2000, 41, 415-427.
    • Uversky, V. N.; Gillespie, J. R.; Fink, A. L. Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 2000, 41, 415-427.
  • 82
    • 10844235653 scopus 로고    scopus 로고
    • Optimal docking area: A new method for predicting protein-protein interaction sites
    • Fernandez-Recio, J.; Totrov, M.; Skorodumov, C.; Abagyan, R. Optimal docking area: a new method for predicting protein-protein interaction sites. Proteins 2005, 58, 134-143.
    • (2005) Proteins , vol.58 , pp. 134-143
    • Fernandez-Recio, J.1    Totrov, M.2    Skorodumov, C.3    Abagyan, R.4
  • 84
    • 0033618555 scopus 로고    scopus 로고
    • Detecting protein function and protein-protein interactions from genome sequences
    • Marcotte, E. M.; Pellegrini, M.; Ng, H. L.; Rice, D. W.; Yeates, T. O.; Eisenberg, D. Detecting protein function and protein-protein interactions from genome sequences. Science 1999, 285, 751-753.
    • (1999) Science , vol.285 , pp. 751-753
    • Marcotte, E.M.1    Pellegrini, M.2    Ng, H.L.3    Rice, D.W.4    Yeates, T.O.5    Eisenberg, D.6
  • 85
    • 0032169271 scopus 로고    scopus 로고
    • Conservation of gene order: A fingerprint of proteins that physically interact
    • Dandekar, T.; Snel, B.; Huynen, M.; Bork, P. Conservation of gene order: a fingerprint of proteins that physically interact. Trends Biochem. Sci. 1998, 23, 324-328.
    • (1998) Trends Biochem. Sci , vol.23 , pp. 324-328
    • Dandekar, T.1    Snel, B.2    Huynen, M.3    Bork, P.4
  • 86
    • 3242892063 scopus 로고    scopus 로고
    • ADVICE: Automated Detection and Validation of Interaction by Co-Evolution
    • Tan, S. H.; Zhang, Z.; Ng, S. K. ADVICE: Automated Detection and Validation of Interaction by Co-Evolution. Nucleic Acids Res. 2004, 32, W69-72.
    • (2004) Nucleic Acids Res , vol.32
    • Tan, S.H.1    Zhang, Z.2    Ng, S.K.3
  • 88
    • 0034725628 scopus 로고    scopus 로고
    • Interaction of inhibitor-2 with the catalytic subunit of type I protein phosphatase
    • Yang, J.; Hurley, T. D.; DePaoli-Roach, A. A. Interaction of inhibitor-2 with the catalytic subunit of type I protein phosphatase. J. Biol. Chem. 2000, 275, 22635-22644.
    • (2000) J. Biol. Chem , vol.275 , pp. 22635-22644
    • Yang, J.1    Hurley, T.D.2    DePaoli-Roach, A.A.3
  • 89
    • 0028143054 scopus 로고
    • Domains of phosphatase inhibitor-2 involved in the control of the ATP-MG-dependent protein phosphatase
    • Park, I. K.; DePaoli-Roach, A. A. Domains of phosphatase inhibitor-2 involved in the control of the ATP-MG-dependent protein phosphatase. J. Biol Chem. 1994, 269, 28919-28928.
    • (1994) J. Biol Chem , vol.269 , pp. 28919-28928
    • Park, I.K.1    DePaoli-Roach, A.A.2
  • 90
    • 0031821410 scopus 로고    scopus 로고
    • The interaction of eIF4E with 4E-BP1 is an induced fit to a completely disorderd protein
    • Fletcher, C. M.; Wagner, G. The interaction of eIF4E with 4E-BP1 is an induced fit to a completely disorderd protein. Protein Sci. 1998, 7, 1639-1642.
    • (1998) Protein Sci , vol.7 , pp. 1639-1642
    • Fletcher, C.M.1    Wagner, G.2
  • 91
    • 0033152072 scopus 로고    scopus 로고
    • Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G
    • Marcotrigiano, J.; Gingras, A-C.; Sonenberg, N.; Burley, S. K. Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G. Mol. Cell 1999, 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
  • 92
    • 14844361449 scopus 로고    scopus 로고
    • Primary contact sites in intrinsically unstructured proteins: The case of calpastatin and microtubule-associated protein 2
    • Csizmok, V; Bokor, M.; Banki, P.; Klement, E.; Medzihradszky, K. F.; Friedrich, P.; Tompa, K.; Tompa, P. Primary contact sites in intrinsically unstructured proteins: the case of calpastatin and microtubule-associated protein 2. Biochemistry 2005, 44, 2955-2964.
    • (2005) Biochemistry , vol.44 , pp. 2955-2964
    • Csizmok, V.1    Bokor, M.2    Banki, P.3    Klement, E.4    Medzihradszky, K.F.5    Friedrich, P.6    Tompa, K.7    Tompa, P.8
  • 94
    • 0042622252 scopus 로고    scopus 로고
    • Puntervoll, P.; Linding, R.; Gemund, C.; Chabanis-Davidson, S.; Mattingsdal, M.; Cameron, S.; Martin, D. M.; Ausiello, G.; Brannetti, B.; Costantini, A.; Ferre, F.; Maselli, V.; Via, A.; Cesareni, G.; Diella, F.; Superti-Furga, G.; Wyrwicz, L.; Ramu, C.; McGuigan, C.; Gudavalli, R.; Letunic, I.; Bork, P.; Rychlewski, L.; Kuster, B.; Helmer-Citterich, M.; Hunter, W. N., Aasland, R.; Gibson, T. J. ELM server: a new resource for investigating short functional sites in modular eukaryotic proteins. Nucleic Acids Res. 2003, 31, 3625-3630.
    • Puntervoll, P.; Linding, R.; Gemund, C.; Chabanis-Davidson, S.; Mattingsdal, M.; Cameron, S.; Martin, D. M.; Ausiello, G.; Brannetti, B.; Costantini, A.; Ferre, F.; Maselli, V.; Via, A.; Cesareni, G.; Diella, F.; Superti-Furga, G.; Wyrwicz, L.; Ramu, C.; McGuigan, C.; Gudavalli, R.; Letunic, I.; Bork, P.; Rychlewski, L.; Kuster, B.; Helmer-Citterich, M.; Hunter, W. N., Aasland, R.; Gibson, T. J. ELM server: a new resource for investigating short functional sites in modular eukaryotic proteins. Nucleic Acids Res. 2003, 31, 3625-3630.
  • 95
    • 34249695447 scopus 로고    scopus 로고
    • Local structural disorder imparts plasticity on linear motifs
    • Fuxreiter, M.; Tompa, P.; Simon, I. Local structural disorder imparts plasticity on linear motifs. Bioinformatics 2007, 23, 950-956.
    • (2007) Bioinformatics , vol.23 , pp. 950-956
    • Fuxreiter, M.1    Tompa, P.2    Simon, I.3


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