메뉴 건너뛰기




Volumn 1834, Issue 4, 2013, Pages 798-807

Analysis of Molecular Recognition Features (MoRFs) in membrane proteins

Author keywords

Intrinsic disorder; MoRFs; Peripheral membrane proteins; Protein protein interactions; Transmembrane proteins

Indexed keywords

MEMBRANE PROTEIN;

EID: 84874081994     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.01.006     Document Type: Article
Times cited : (21)

References (91)
  • 1
    • 80055012207 scopus 로고    scopus 로고
    • Expanding the proteome: Disordered and alternatively folded proteins
    • H.J. Dyson Expanding the proteome: disordered and alternatively folded proteins Q. Rev. Biophys. 44 2011 467 518
    • (2011) Q. Rev. Biophys. , vol.44 , pp. 467-518
    • Dyson, H.J.1
  • 2
    • 79958741408 scopus 로고    scopus 로고
    • Intrinsically disordered proteins from A to Z
    • V.N. Uversky Intrinsically disordered proteins from A to Z Int. J. Biochem. Cell Biol. 43 2011 1090 1103
    • (2011) Int. J. Biochem. Cell Biol. , vol.43 , pp. 1090-1103
    • Uversky, V.N.1
  • 4
    • 82655175850 scopus 로고    scopus 로고
    • The relationship between proteome size, structural disorder and organism complexity
    • E. Schad, P. Tompa, and H. Hegyi The relationship between proteome size, structural disorder and organism complexity Genome Biol. 12 2011 R120
    • (2011) Genome Biol. , vol.12 , pp. 120
    • Schad, E.1    Tompa, P.2    Hegyi, H.3
  • 5
    • 24944546549 scopus 로고    scopus 로고
    • Coupled folding and binding with alpha-helix-forming molecular recognition elements
    • C.J. Oldfield, Y. Cheng, M.S. Cortese, P. Romero, V.N. Uversky, and A.K. Dunker Coupled folding and binding with alpha-helix-forming molecular recognition elements Biochemistry 44 2005 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
  • 12
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • V.N. Uversky, J.R. Gillespie, and A.L. Fink Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 41 2000 415 427
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 15
    • 84857839467 scopus 로고    scopus 로고
    • Multiparametric analysis of intrinsically disordered proteins: Looking at intrinsic disorder through compound eyes
    • V.N. Uversky, and A.K. Dunker Multiparametric analysis of intrinsically disordered proteins: looking at intrinsic disorder through compound eyes Anal. Chem. 84 2012 2096 2104
    • (2012) Anal. Chem. , vol.84 , pp. 2096-2104
    • Uversky, V.N.1    Dunker, A.K.2
  • 17
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • P. Tompa Intrinsically unstructured proteins Trends Biochem. Sci. 27 2002 527 533
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 527-533
    • Tompa, P.1
  • 18
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets. The roles of intrinsic disorder in protein interaction networks
    • A.K. Dunker, M.S. Cortese, P. Romero, L.M. Iakoucheva, and V.N. Uversky Flexible nets. The roles of intrinsic disorder in protein interaction networks FEBS J. 272 2005 5129 5148
    • (2005) FEBS J. , vol.272 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 19
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling
    • V.N. Uversky, C.J. Oldfield, and A.K. Dunker Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling J. Mol. Recognit. 18 2005 343 384
    • (2005) J. Mol. Recognit. , vol.18 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 20
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • P.E. Wright, and H.J. Dyson Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm J. Mol. Biol. 293 1999 321 331
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 21
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • H.J. Dyson, and P.E. Wright Coupling of folding and binding for unstructured proteins Curr. Opin. Struct. Biol. 12 2002 54 60
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 22
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • H.J. Dyson, and P.E. Wright Intrinsically unstructured proteins and their functions Nat. Rev. Mol. Cell Biol. 6 2005 197 208
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 23
    • 0034867975 scopus 로고    scopus 로고
    • The protein trinity - Linking function and disorder
    • A.K. Dunker, and Z. Obradovic The protein trinity - linking function and disorder Nat. Biotechnol. 19 2001 805 806
    • (2001) Nat. Biotechnol. , vol.19 , pp. 805-806
    • Dunker, A.K.1    Obradovic, Z.2
  • 24
    • 0036402827 scopus 로고    scopus 로고
    • Identification and functions of usefully disordered proteins
    • A.K. Dunker, C.J. Brown, and Z. Obradovic Identification and functions of usefully disordered proteins Adv. Protein Chem. 62 2002 25 49
    • (2002) Adv. Protein Chem. , vol.62 , pp. 25-49
    • Dunker, A.K.1    Brown, C.J.2    Obradovic, Z.3
  • 29
    • 77954267294 scopus 로고    scopus 로고
    • SLiMFinder: A web server to find novel, significantly over-represented, short protein motifs
    • N.E. Davey, N.J. Haslam, D.C. Shields, and R.J. Edwards SLiMFinder: a web server to find novel, significantly over-represented, short protein motifs Nucleic Acids Res. 38 2010 W534 W539
    • (2010) Nucleic Acids Res. , vol.38
    • Davey, N.E.1    Haslam, N.J.2    Shields, D.C.3    Edwards, R.J.4
  • 30
    • 84870600202 scopus 로고    scopus 로고
    • SLiMPrints: Conservation-based discovery of functional motif fingerprints in intrinsically disordered protein regions
    • N.E. Davey, J.L. Cowan, D.C. Shields, T.J. Gibson, M.J. Coldwell, and R.J. Edwards SLiMPrints: conservation-based discovery of functional motif fingerprints in intrinsically disordered protein regions Nucleic Acids Res. 40 2012 10628 10641
    • (2012) Nucleic Acids Res. , vol.40 , pp. 10628-10641
    • Davey, N.E.1    Cowan, J.L.2    Shields, D.C.3    Gibson, T.J.4    Coldwell, M.J.5    Edwards, R.J.6
  • 31
    • 49749117432 scopus 로고    scopus 로고
    • Contextual specificity in peptide-mediated protein interactions
    • A. Stein, and P. Aloy Contextual specificity in peptide-mediated protein interactions PLoS One 3 2008 e2524
    • (2008) PLoS One , vol.3 , pp. 2524
    • Stein, A.1    Aloy, P.2
  • 34
    • 84867055643 scopus 로고    scopus 로고
    • Disordered binding regions and linear motifs - Bridging the gap between two models of molecular recognition
    • B. Meszaros, Z. Dosztanyi, and I. Simon Disordered binding regions and linear motifs - bridging the gap between two models of molecular recognition PLoS One 7 2012 e46829
    • (2012) PLoS One , vol.7 , pp. 46829
    • Meszaros, B.1    Dosztanyi, Z.2    Simon, I.3
  • 37
    • 36749037699 scopus 로고    scopus 로고
    • Mining alpha-helix-forming molecular recognition features with cross species sequence alignments
    • Y. Cheng, C.J. Oldfield, J. Meng, P. Romero, V.N. Uversky, and A.K. Dunker Mining alpha-helix-forming molecular recognition features with cross species sequence alignments Biochemistry 46 2007 13468 13477
    • (2007) Biochemistry , vol.46 , pp. 13468-13477
    • Cheng, Y.1    Oldfield, C.J.2    Meng, J.3    Romero, P.4    Uversky, V.N.5    Dunker, A.K.6
  • 38
    • 70349996473 scopus 로고    scopus 로고
    • ANCHOR: Web server for predicting protein binding regions in disordered proteins
    • Z. Dosztanyi, B. Meszaros, and I. Simon ANCHOR: web server for predicting protein binding regions in disordered proteins Bioinformatics (Oxford, England) 25 2009 2745 2746
    • (2009) Bioinformatics (Oxford, England) , vol.25 , pp. 2745-2746
    • Dosztanyi, Z.1    Meszaros, B.2    Simon, I.3
  • 39
    • 84863518014 scopus 로고    scopus 로고
    • MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins
    • F.M. Disfani, W.L. Hsu, M.J. Mizianty, C.J. Oldfield, B. Xue, A.K. Dunker, V.N. Uversky, and L. Kurgan MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins Bioinformatics (Oxford, England) 28 2012 75 83
    • (2012) Bioinformatics (Oxford, England) , vol.28 , pp. 75-83
    • Disfani, F.M.1    Hsu, W.L.2    Mizianty, M.J.3    Oldfield, C.J.4    Xue, B.5    Dunker, A.K.6    Uversky, V.N.7    Kurgan, L.8
  • 41
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • A. Krogh, B. Larsson, G. von Heijne, and E.L. Sonnhammer Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes J. Mol. Biol. 305 2001 567 580
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 43
    • 72949087534 scopus 로고    scopus 로고
    • Analysis of structured and intrinsically disordered regions of transmembrane proteins
    • B. Xue, L. Li, S.O. Meroueh, V.N. Uversky, and A.K. Dunker Analysis of structured and intrinsically disordered regions of transmembrane proteins Mol. Biosyst. 5 2009 1688 1702
    • (2009) Mol. Biosyst. , vol.5 , pp. 1688-1702
    • Xue, B.1    Li, L.2    Meroueh, S.O.3    Uversky, V.N.4    Dunker, A.K.5
  • 44
    • 34047113297 scopus 로고    scopus 로고
    • Intrinsically disordered regions of human plasma membrane proteins preferentially occur in the cytoplasmic segment
    • Y. Minezaki, K. Homma, and K. Nishikawa Intrinsically disordered regions of human plasma membrane proteins preferentially occur in the cytoplasmic segment J. Mol. Biol. 368 2007 902 913
    • (2007) J. Mol. Biol. , vol.368 , pp. 902-913
    • Minezaki, Y.1    Homma, K.2    Nishikawa, K.3
  • 45
    • 84866050024 scopus 로고    scopus 로고
    • Protein disorder and short conserved motifs in disordered regions are enriched near the cytoplasmic side of single-pass transmembrane proteins
    • I. Stavropoulos, N. Khaldi, N.E. Davey, K. O'Brien, F. Martin, and D.C. Shields Protein disorder and short conserved motifs in disordered regions are enriched near the cytoplasmic side of single-pass transmembrane proteins PLoS One 7 2012 e44389
    • (2012) PLoS One , vol.7 , pp. 44389
    • Stavropoulos, I.1    Khaldi, N.2    Davey, N.E.3    O'Brien, K.4    Martin, F.5    Shields, D.C.6
  • 46
    • 0031889752 scopus 로고    scopus 로고
    • Domain assignment for protein structures using a consensus approach: Characterization and analysis
    • S. Jones, M. Stewart, A. Michie, M.B. Swindells, C. Orengo, and J.M. Thornton Domain assignment for protein structures using a consensus approach: characterization and analysis Protein Sci. 7 1998 233 242
    • (1998) Protein Sci. , vol.7 , pp. 233-242
    • Jones, S.1    Stewart, M.2    Michie, A.3    Swindells, M.B.4    Orengo, C.5    Thornton, J.M.6
  • 47
    • 84874724662 scopus 로고    scopus 로고
    • Update on activities at the Universal Protein Resource (UniProt) in 2013
    • Update on activities at the Universal Protein Resource (UniProt) in 2013 Nucleic Acids Res. 41 2013 D43 D47
    • (2013) Nucleic Acids Res. , vol.41
  • 48
    • 0043122933 scopus 로고    scopus 로고
    • UniqueProt: Creating representative protein sequence sets
    • S. Mika, and B. Rost UniqueProt: creating representative protein sequence sets Nucleic Acids Res. 31 2003 3789 3791
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3789-3791
    • Mika, S.1    Rost, B.2
  • 49
    • 4143107222 scopus 로고    scopus 로고
    • Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers
    • K. Gunasekaran, C.J. Tsai, and R. Nussinov Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers J. Mol. Biol. 341 2004 1327 1341
    • (2004) J. Mol. Biol. , vol.341 , pp. 1327-1341
    • Gunasekaran, K.1    Tsai, C.J.2    Nussinov, R.3
  • 50
    • 84870431038 scopus 로고    scopus 로고
    • CD-HIT: Accelerated for clustering the next-generation sequencing data
    • L. Fu, B. Niu, Z. Zhu, S. Wu, and W. Li CD-HIT: accelerated for clustering the next-generation sequencing data Bioinformatics (Oxford, England) 28 2012 3150 3152
    • (2012) Bioinformatics (Oxford, England) , vol.28 , pp. 3150-3152
    • Fu, L.1    Niu, B.2    Zhu, Z.3    Wu, S.4    Li, W.5
  • 51
    • 84874677954 scopus 로고    scopus 로고
    • PDBTM: Protein data bank of transmembrane proteins after 8 years
    • D. Kozma, I. Simon, and G.E. Tusnady PDBTM: protein data bank of transmembrane proteins after 8 years Nucleic Acids Res. 41 2013 D524 D529
    • (2013) Nucleic Acids Res. , vol.41
    • Kozma, D.1    Simon, I.2    Tusnady, G.E.3
  • 52
    • 34447539760 scopus 로고    scopus 로고
    • Composition profiler: A tool for discovery and visualization of amino acid composition differences
    • V. Vacic, V.N. Uversky, A.K. Dunker, and S. Lonardi Composition profiler: a tool for discovery and visualization of amino acid composition differences BMC Bioinforma. 8 2007 211
    • (2007) BMC Bioinforma. , vol.8 , pp. 211
    • Vacic, V.1    Uversky, V.N.2    Dunker, A.K.3    Lonardi, S.4
  • 54
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • W. Kabsch, and C. Sander Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22 1983 2577 2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 56
    • 17444397116 scopus 로고    scopus 로고
    • Porter: A new, accurate server for protein secondary structure prediction
    • G. Pollastri, and A. McLysaght Porter: a new, accurate server for protein secondary structure prediction Bioinformatics (Oxford, England) 21 2005 1719 1720
    • (2005) Bioinformatics (Oxford, England) , vol.21 , pp. 1719-1720
    • Pollastri, G.1    McLysaght, A.2
  • 58
    • 12344269924 scopus 로고    scopus 로고
    • GO::TermFinder - Open source software for accessing Gene Ontology information and finding significantly enriched Gene Ontology terms associated with a list of genes
    • E.I. Boyle, S. Weng, J. Gollub, H. Jin, D. Botstein, J.M. Cherry, and G. Sherlock GO::TermFinder - open source software for accessing Gene Ontology information and finding significantly enriched Gene Ontology terms associated with a list of genes Bioinformatics (Oxford, England) 20 2004 3710 3715
    • (2004) Bioinformatics (Oxford, England) , vol.20 , pp. 3710-3715
    • Boyle, E.I.1    Weng, S.2    Gollub, J.3    Jin, H.4    Botstein, D.5    Cherry, J.M.6    Sherlock, G.7
  • 60
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • J. Kyte, and R.F. Doolittle A simple method for displaying the hydropathic character of a protein J. Mol. Biol. 157 1982 105 132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 61
    • 67049119327 scopus 로고    scopus 로고
    • Prediction of protein binding regions in disordered proteins
    • B. Meszaros, I. Simon, and Z. Dosztanyi Prediction of protein binding regions in disordered proteins PLoS Comput. Biol. 5 2009 e1000376
    • (2009) PLoS Comput. Biol. , vol.5 , pp. 1000376
    • Meszaros, B.1    Simon, I.2    Dosztanyi, Z.3
  • 62
    • 0000651660 scopus 로고
    • The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology
    • G. Heijne The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology EMBO J. 5 1986 3021 3027
    • (1986) EMBO J. , vol.5 , pp. 3021-3027
    • Heijne, G.1
  • 63
    • 34249683488 scopus 로고    scopus 로고
    • Membrane protein structure: Prediction versus reality
    • A. Elofsson, and G. von Heijne Membrane protein structure: prediction versus reality Annu. Rev. Biochem. 76 2007 125 140
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 125-140
    • Elofsson, A.1    Von Heijne, G.2
  • 65
    • 0000332920 scopus 로고    scopus 로고
    • Sequence data analysis for long disordered regions prediction in the calcineurin family
    • Obradovic Romero, and K. Dunker Sequence data analysis for long disordered regions prediction in the calcineurin family Genome Inform. Ser. Workshop Genome Inform. 8 1997 110 124
    • (1997) Genome Inform. Ser. Workshop Genome Inform. , vol.8 , pp. 110-124
    • Romero, O.1    Dunker, K.2
  • 67
    • 33847768609 scopus 로고    scopus 로고
    • Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions
    • H. Xie, S. Vucetic, L.M. Iakoucheva, C.J. Oldfield, A.K. Dunker, V.N. Uversky, and Z. Obradovic Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions J. Proteome Res. 6 2007 1882 1898
    • (2007) J. Proteome Res. , vol.6 , pp. 1882-1898
    • Xie, H.1    Vucetic, S.2    Iakoucheva, L.M.3    Oldfield, C.J.4    Dunker, A.K.5    Uversky, V.N.6    Obradovic, Z.7
  • 68
    • 49849097024 scopus 로고    scopus 로고
    • Prevalence of intrinsic disorder in the intracellular region of human single-pass type i proteins: The case of the notch ligand Delta-4
    • A. De Biasio, C. Guarnaccia, M. Popovic, V.N. Uversky, A. Pintar, and S. Pongor Prevalence of intrinsic disorder in the intracellular region of human single-pass type I proteins: the case of the notch ligand Delta-4 J. Proteome Res. 7 2008 2496 2506
    • (2008) J. Proteome Res. , vol.7 , pp. 2496-2506
    • De Biasio, A.1    Guarnaccia, C.2    Popovic, M.3    Uversky, V.N.4    Pintar, A.5    Pongor, S.6
  • 69
    • 70350038016 scopus 로고    scopus 로고
    • Mapping the human membrane proteome: A majority of the human membrane proteins can be classified according to function and evolutionary origin
    • M.S. Almen, K.J. Nordstrom, R. Fredriksson, and H.B. Schioth Mapping the human membrane proteome: a majority of the human membrane proteins can be classified according to function and evolutionary origin BMC Biol. 7 2009 50
    • (2009) BMC Biol. , vol.7 , pp. 50
    • Almen, M.S.1    Nordstrom, K.J.2    Fredriksson, R.3    Schioth, H.B.4
  • 70
    • 77953584951 scopus 로고    scopus 로고
    • Single-spanning transmembrane domains in cell growth and cell-cell interactions: More than meets the eye?
    • P. Hubert, P. Sawma, J.P. Duneau, J. Khao, J. Henin, D. Bagnard, and J. Sturgis Single-spanning transmembrane domains in cell growth and cell-cell interactions: more than meets the eye? Cell Adhes. Migr. 4 2010 313 324
    • (2010) Cell Adhes. Migr. , vol.4 , pp. 313-324
    • Hubert, P.1    Sawma, P.2    Duneau, J.P.3    Khao, J.4    Henin, J.5    Bagnard, D.6    Sturgis, J.7
  • 71
    • 34249282661 scopus 로고    scopus 로고
    • Functional anthology of intrinsic disorder. 2. Cellular components, domains, technical terms, developmental processes, and coding sequence diversities correlated with long disordered regions
    • S. Vucetic, H. Xie, L.M. Iakoucheva, C.J. Oldfield, A.K. Dunker, Z. Obradovic, and V.N. Uversky Functional anthology of intrinsic disorder. 2. Cellular components, domains, technical terms, developmental processes, and coding sequence diversities correlated with long disordered regions J. Proteome Res. 6 2007 1899 1916
    • (2007) J. Proteome Res. , vol.6 , pp. 1899-1916
    • Vucetic, S.1    Xie, H.2    Iakoucheva, L.M.3    Oldfield, C.J.4    Dunker, A.K.5    Obradovic, Z.6    Uversky, V.N.7
  • 72
    • 57149116929 scopus 로고    scopus 로고
    • Tight regulation of unstructured proteins: From transcript synthesis to protein degradation
    • J. Gsponer, M.E. Futschik, S.A. Teichmann, and M.M. Babu Tight regulation of unstructured proteins: from transcript synthesis to protein degradation Science (New York, N.Y.) 322 2008 1365 1368
    • (2008) Science (New York, N.Y.) , vol.322 , pp. 1365-1368
    • Gsponer, J.1    Futschik, M.E.2    Teichmann, S.A.3    Babu, M.M.4
  • 73
    • 33645214608 scopus 로고    scopus 로고
    • Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks
    • A. Patil, and H. Nakamura Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks FEBS Lett. 580 2006 2041 2045
    • (2006) FEBS Lett. , vol.580 , pp. 2041-2045
    • Patil, A.1    Nakamura, H.2
  • 74
    • 77955121836 scopus 로고    scopus 로고
    • Domain distribution and intrinsic disorder in hubs in the human protein-protein interaction network
    • A. Patil, K. Kinoshita, and H. Nakamura Domain distribution and intrinsic disorder in hubs in the human protein-protein interaction network Protein Sci. 19 2010 1461 1468
    • (2010) Protein Sci. , vol.19 , pp. 1461-1468
    • Patil, A.1    Kinoshita, K.2    Nakamura, H.3
  • 75
    • 40949117264 scopus 로고    scopus 로고
    • Flexible nets: Disorder and induced fit in the associations of p53 and 14-3-3 with their partners
    • C.J. Oldfield, J. Meng, J.Y. Yang, M.Q. Yang, V.N. Uversky, and A.K. Dunker Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners BMC Genomics 9 Suppl. 1 2008 S1
    • (2008) BMC Genomics , vol.9 , Issue.SUPPL. 1 , pp. 1
    • Oldfield, C.J.1    Meng, J.2    Yang, J.Y.3    Yang, M.Q.4    Uversky, V.N.5    Dunker, A.K.6
  • 76
  • 77
    • 33750999318 scopus 로고    scopus 로고
    • Disorder and sequence repeats in hub proteins and their implications for network evolution
    • Z. Dosztanyi, J. Chen, A.K. Dunker, I. Simon, and P. Tompa Disorder and sequence repeats in hub proteins and their implications for network evolution J. Proteome Res. 5 2006 2985 2995
    • (2006) J. Proteome Res. , vol.5 , pp. 2985-2995
    • Dosztanyi, Z.1    Chen, J.2    Dunker, A.K.3    Simon, I.4    Tompa, P.5
  • 80
    • 33847081239 scopus 로고    scopus 로고
    • Role of intrinsic disorder in transient interactions of hub proteins
    • G.P. Singh, M. Ganapathi, and D. Dash Role of intrinsic disorder in transient interactions of hub proteins Proteins 66 2007 761 765
    • (2007) Proteins , vol.66 , pp. 761-765
    • Singh, G.P.1    Ganapathi, M.2    Dash, D.3
  • 81
    • 33745686603 scopus 로고    scopus 로고
    • What properties characterize the hub proteins of the protein-protein interaction network of Saccharomyces cerevisiae?
    • D. Ekman, S. Light, A.K. Bjorklund, and A. Elofsson What properties characterize the hub proteins of the protein-protein interaction network of Saccharomyces cerevisiae? Genome Biol. 7 2006 R45
    • (2006) Genome Biol. , vol.7 , pp. 45
    • Ekman, D.1    Light, S.2    Bjorklund, A.K.3    Elofsson, A.4
  • 82
    • 70149097069 scopus 로고    scopus 로고
    • Interaction between intrinsically disordered proteins frequently occurs in a human protein-protein interaction network
    • K. Shimizu, and H. Toh Interaction between intrinsically disordered proteins frequently occurs in a human protein-protein interaction network J. Mol. Biol. 392 2009 1253 1265
    • (2009) J. Mol. Biol. , vol.392 , pp. 1253-1265
    • Shimizu, K.1    Toh, H.2
  • 83
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • Z. Dosztanyi, V. Csizmok, P. Tompa, and I. Simon IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content Bioinformatics (Oxford, England) 21 2005 3433 3434
    • (2005) Bioinformatics (Oxford, England) , vol.21 , pp. 3433-3434
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 84
    • 0043029286 scopus 로고    scopus 로고
    • SNARE selectivity of the COPII coat
    • E. Mossessova, L.C. Bickford, and J. Goldberg SNARE selectivity of the COPII coat Cell 114 2003 483 495
    • (2003) Cell , vol.114 , pp. 483-495
    • Mossessova, E.1    Bickford, L.C.2    Goldberg, J.3
  • 85
    • 0037112932 scopus 로고    scopus 로고
    • Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p
    • A. Bracher, and W. Weissenhorn Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p EMBO J. 21 2002 6114 6124
    • (2002) EMBO J. , vol.21 , pp. 6114-6124
    • Bracher, A.1    Weissenhorn, W.2
  • 90
    • 3843118843 scopus 로고    scopus 로고
    • The trihelical bundle subdomain of the GGA proteins interacts with multiple partners through overlapping but distinct sites
    • R. Mattera, R. Puertollano, W.J. Smith, and J.S. Bonifacino The trihelical bundle subdomain of the GGA proteins interacts with multiple partners through overlapping but distinct sites J. Biol. Chem. 279 2004 31409 31418
    • (2004) J. Biol. Chem. , vol.279 , pp. 31409-31418
    • Mattera, R.1    Puertollano, R.2    Smith, W.J.3    Bonifacino, J.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.