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Volumn 12, Issue 10, 2012, Pages 1527-1546

High-throughput analysis of peptide-binding modules

Author keywords

Cell signaling; Interaction profiling; Peptide array libraries; Post translational modifications; Protein interaction domains; Protein microarrays; Specificity; Technology

Indexed keywords

PDZ PROTEIN; PROTEIN SH3; PROTEIN TYROSINE PHOSPHATASE SHP;

EID: 84862642911     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201100599     Document Type: Review
Times cited : (40)

References (153)
  • 1
    • 70849112486 scopus 로고    scopus 로고
    • Cell signaling in space and time: where proteins come together and when they're apart
    • Scott, J. D., Pawson, T., Cell signaling in space and time: where proteins come together and when they're apart. Science 2009, 326, 1220-1224.
    • (2009) Science , vol.326 , pp. 1220-1224
    • Scott, J.D.1    Pawson, T.2
  • 2
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • Pawson, T., Nash, P., Assembly of cell regulatory systems through protein interaction domains. Science 2003, 300, 445-452.
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 3
    • 0022977712 scopus 로고
    • A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps
    • Sadowski, I., Stone, J. C., Pawson, T., A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps. Mol. Cell. Biol. 1986, 6, 4396-4408.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 4396-4408
    • Sadowski, I.1    Stone, J.C.2    Pawson, T.3
  • 4
    • 0023627442 scopus 로고
    • Catalytic and non-catalytic domains of the Fujinami sarcoma virus P130gag-fps protein-tyrosine kinase distinguished by the expression of v-fps polypeptides in Escherichia coli
    • Sadowski, I., Pawson, T., Catalytic and non-catalytic domains of the Fujinami sarcoma virus P130gag-fps protein-tyrosine kinase distinguished by the expression of v-fps polypeptides in Escherichia coli. Oncogene 1987, 1, 181-191.
    • (1987) Oncogene , vol.1 , pp. 181-191
    • Sadowski, I.1    Pawson, T.2
  • 5
    • 0023864050 scopus 로고
    • A novel viral oncogene with structural similarity to phospholipase C
    • Mayer, B. J., Hamaguchi, M., Hanafusa, H., A novel viral oncogene with structural similarity to phospholipase C. Nature 1988, 332, 272-275.
    • (1988) Nature , vol.332 , pp. 272-275
    • Mayer, B.J.1    Hamaguchi, M.2    Hanafusa, H.3
  • 6
    • 43149094164 scopus 로고    scopus 로고
    • Pfam 10 years on: 10,000 families and still growing
    • Sammut, S. J., Finn, R. D., Bateman, A., Pfam 10 years on: 10, 000 families and still growing. Brief Bioinform 2008, 9, 210-219.
    • (2008) Brief Bioinform , vol.9 , pp. 210-219
    • Sammut, S.J.1    Finn, R.D.2    Bateman, A.3
  • 7
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: identification of signaling domains
    • Schultz, J., Milpetz, F., Bork, P., Ponting, C. P., SMART, a simple modular architecture research tool: identification of signaling domains. Proc. Natl. Acad. Sci. USA. 1998, 95, 5857-5864.
    • (1998) Proc. Natl. Acad. Sci. USA. , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 8
    • 0036087630 scopus 로고    scopus 로고
    • CDD: a database of conserved domain alignments with links to domain three-dimensional structure
    • Marchler-Bauer, A., Panchenko, A. R., Shoemaker, B. A., Thiessen, P. A. et al., CDD: a database of conserved domain alignments with links to domain three-dimensional structure. Nucleic Acids Res. 2002, 30, 281-283.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 281-283
    • Marchler-Bauer, A.1    Panchenko, A.R.2    Shoemaker, B.A.3    Thiessen, P.A.4
  • 9
    • 33746363486 scopus 로고    scopus 로고
    • Domains, motifs, and scaffolds: the role of modular interactions in the evolution and wiring of cell signaling circuits
    • Bhattacharyya, R. P., Remenyi, A., Yeh, B. J., Lim, W. A., Domains, motifs, and scaffolds: the role of modular interactions in the evolution and wiring of cell signaling circuits. Annu. Rev. Biochem. 2006, 75, 655-680.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 655-680
    • Bhattacharyya, R.P.1    Remenyi, A.2    Yeh, B.J.3    Lim, W.A.4
  • 11
    • 0030950608 scopus 로고    scopus 로고
    • Modular peptide recognition domains in eukaryotic signaling
    • Kuriyan, J., Cowburn, D., Modular peptide recognition domains in eukaryotic signaling. Annu. Rev. Biophys. Biomol. Struct. 1997, 26, 259-288.
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 259-288
    • Kuriyan, J.1    Cowburn, D.2
  • 12
    • 0023497801 scopus 로고
    • A conserved domain regulates interactions of the v-fps protein-tyrosine kinase with the host cell
    • DeClue, J. E., Sadowski, I., Martin, G. S., Pawson, T., A conserved domain regulates interactions of the v-fps protein-tyrosine kinase with the host cell. Proc. Natl. Acad. Sci. USA. 1987, 84, 9064-9068.
    • (1987) Proc. Natl. Acad. Sci. USA. , vol.84 , pp. 9064-9068
    • DeClue, J.E.1    Sadowski, I.2    Martin, G.S.3    Pawson, T.4
  • 13
    • 0025681492 scopus 로고
    • Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors
    • Anderson, D., Koch, C. A., Grey, L., Ellis, C. et al., Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors. Science 1990, 250, 979-982.
    • (1990) Science , vol.250 , pp. 979-982
    • Anderson, D.1    Koch, C.A.2    Grey, L.3    Ellis, C.4
  • 14
    • 0025119824 scopus 로고
    • Src homology region 2 domains direct protein-protein interactions in signal transduction
    • Moran, M. F., Koch, C. A., Anderson, D., Ellis, C. et al., Src homology region 2 domains direct protein-protein interactions in signal transduction. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 8622-8626.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 8622-8626
    • Moran, M.F.1    Koch, C.A.2    Anderson, D.3    Ellis, C.4
  • 15
    • 33745185987 scopus 로고    scopus 로고
    • The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling
    • Liu, B. A., Jablonowski, K., Raina, M., Arce, M. et al., The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling. Mol. Cell 2006, 22, 851-868.
    • (2006) Mol. Cell , vol.22 , pp. 851-868
    • Liu, B.A.1    Jablonowski, K.2    Raina, M.3    Arce, M.4
  • 16
    • 83155181907 scopus 로고    scopus 로고
    • The SH2 domain-containing proteins in 21 species establish the provenance and scope of phosphotyrosine signaling in eukaryotes
    • Liu, B. A., Shah, E., Jablonowski, K., Stergachis, A. et al., The SH2 domain-containing proteins in 21 species establish the provenance and scope of phosphotyrosine signaling in eukaryotes. Sci. Signal. 2011, 4, ra83.
    • (2011) Sci. Signal. , vol.4
    • Liu, B.A.1    Shah, E.2    Jablonowski, K.3    Stergachis, A.4
  • 17
    • 46449121011 scopus 로고    scopus 로고
    • Genome wide analysis of pathogenic SH2 domain mutations
    • Lappalainen, I., Thusberg, J., Shen, B., Vihinen, M., Genome wide analysis of pathogenic SH2 domain mutations. Proteins 2008, 72, 779-792.
    • (2008) Proteins , vol.72 , pp. 779-792
    • Lappalainen, I.1    Thusberg, J.2    Shen, B.3    Vihinen, M.4
  • 18
    • 78149463029 scopus 로고    scopus 로고
    • Characterizing tyrosine phosphorylation signaling in lung cancer using SH2 profiling
    • Machida, K., Eschrich, S., Li, J., Bai, Y. et al., Characterizing tyrosine phosphorylation signaling in lung cancer using SH2 profiling. PLoS One 2010, 5, e13470.
    • (2010) PLoS One , vol.5
    • Machida, K.1    Eschrich, S.2    Li, J.3    Bai, Y.4
  • 19
    • 34250641161 scopus 로고    scopus 로고
    • High-throughput phosphotyrosine profiling using SH2 domains
    • Machida, K., Thompson, C. M., Dierck, K., Jablonowski, K. et al., High-throughput phosphotyrosine profiling using SH2 domains. Mol. Cell 2007, 26, 899-915.
    • (2007) Mol. Cell , vol.26 , pp. 899-915
    • Machida, K.1    Thompson, C.M.2    Dierck, K.3    Jablonowski, K.4
  • 20
    • 33847285870 scopus 로고    scopus 로고
    • Oncogenic re-wiring of cellular signaling pathways
    • Pawson, T., Warner, N., Oncogenic re-wiring of cellular signaling pathways. Oncogene 2007, 26, 1268-1275.
    • (2007) Oncogene , vol.26 , pp. 1268-1275
    • Pawson, T.1    Warner, N.2
  • 21
    • 75549086174 scopus 로고    scopus 로고
    • Eukaryotic protein domains as functional units of cellular evolution
    • Jin, J., Xie, X., Chen, C., Park, J. G. et al., Eukaryotic protein domains as functional units of cellular evolution. Sci. Signal. 2009, 2, ra76.
    • (2009) Sci. Signal. , vol.2
    • Jin, J.1    Xie, X.2    Chen, C.3    Park, J.G.4
  • 22
    • 0842346438 scopus 로고    scopus 로고
    • Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems
    • Pawson, T., Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems. Cell 2004, 116, 191-203.
    • (2004) Cell , vol.116 , pp. 191-203
    • Pawson, T.1
  • 23
    • 0034193568 scopus 로고    scopus 로고
    • Protein-protein interactions define specificity in signal transduction
    • Pawson, T., Nash, P., Protein-protein interactions define specificity in signal transduction. Genes Dev. 2000, 14, 1027-1047.
    • (2000) Genes Dev. , vol.14 , pp. 1027-1047
    • Pawson, T.1    Nash, P.2
  • 24
    • 62749097935 scopus 로고    scopus 로고
    • Genomic and structural aspects of protein evolution
    • Chothia, C., Gough, J., Genomic and structural aspects of protein evolution. Biochem. J. 2009, 419, 15-28.
    • (2009) Biochem. J. , vol.419 , pp. 15-28
    • Chothia, C.1    Gough, J.2
  • 25
    • 33646909100 scopus 로고    scopus 로고
    • Protein family expansions and biological complexity
    • Vogel, C., Chothia, C., Protein family expansions and biological complexity. PLoS Comput. Biol. 2006, 2, e48.
    • (2006) PLoS Comput. Biol. , vol.2
    • Vogel, C.1    Chothia, C.2
  • 26
    • 68249125947 scopus 로고    scopus 로고
    • 14-3-3 proteins, FHA domains and BRCT domains in the DNA damage response
    • Mohammad, D. H., Yaffe, M. B., 14-3-3 proteins, FHA domains and BRCT domains in the DNA damage response. DNA Repair (Amst) 2009, 8, 1009-1017.
    • (2009) DNA Repair (Amst) , vol.8 , pp. 1009-1017
    • Mohammad, D.H.1    Yaffe, M.B.2
  • 27
    • 80053132089 scopus 로고    scopus 로고
    • Deciphering arginine methylation: tudor tells the tale
    • Chen, C., Nott, T. J., Jin, J., Pawson, T., Deciphering arginine methylation: tudor tells the tale. Nat. Rev. Mol. Cell. Biol. 2011, 12, 629-642.
    • (2011) Nat. Rev. Mol. Cell. Biol. , vol.12 , pp. 629-642
    • Chen, C.1    Nott, T.J.2    Jin, J.3    Pawson, T.4
  • 29
    • 78649396592 scopus 로고    scopus 로고
    • The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition
    • Gareau, J. R., Lima, C. D., The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nat. Rev. Mol. Cell. Biol. 2010, 11, 861-871.
    • (2010) Nat. Rev. Mol. Cell. Biol. , vol.11 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 30
    • 83055173304 scopus 로고    scopus 로고
    • The first identification of lysine malonylation substrates and its regulatory enzyme
    • 10, M111.012658.
    • Peng, C., Lu, Z., Xie, Z., Cheng, Z. et al., The first identification of lysine malonylation substrates and its regulatory enzyme. Mol. Cell. Proteomics 2011, 10, M111.012658.
    • (2011) Mol. Cell. Proteomics
    • Peng, C.1    Lu, Z.2    Xie, Z.3    Cheng, Z.4
  • 31
    • 80052942443 scopus 로고    scopus 로고
    • Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification
    • Tan, M., Luo, H., Lee, S., Jin, F. et al., Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification. Cell 2011, 146, 1016-1028.
    • (2011) Cell , vol.146 , pp. 1016-1028
    • Tan, M.1    Luo, H.2    Lee, S.3    Jin, F.4
  • 32
    • 78650516004 scopus 로고    scopus 로고
    • Identification of lysine succinylation as a new post-translational modification
    • Zhang, Z., Tan, M., Xie, Z., Dai, L. et al., Identification of lysine succinylation as a new post-translational modification. Nat. Chem. Biol. 2011, 7, 58-63.
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 58-63
    • Zhang, Z.1    Tan, M.2    Xie, Z.3    Dai, L.4
  • 33
    • 0042622240 scopus 로고    scopus 로고
    • GlobPlot: exploring protein sequences for globularity and disorder
    • 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.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4
  • 34
    • 0013033597 scopus 로고    scopus 로고
    • The structure and function of proline recognition domains
    • Zarrinpar, A., Bhattacharyya, R. P., Lim, W. A., The structure and function of proline recognition domains. Sci STKE 2003, 2003, RE8.
    • (2003) Sci STKE , vol.2003
    • Zarrinpar, A.1    Bhattacharyya, R.P.2    Lim, W.A.3
  • 35
    • 0037031154 scopus 로고    scopus 로고
    • A high-affinity Arg-X-X-Lys SH3 binding motif confers specificity for the interaction between Gads and SLP-76 in T cell signaling
    • Berry, D. M., Nash, P., Liu, S. K., Pawson, T. et al., A high-affinity Arg-X-X-Lys SH3 binding motif confers specificity for the interaction between Gads and SLP-76 in T cell signaling. Curr. Biol. 2002, 12, 1336-1341.
    • (2002) Curr. Biol. , vol.12 , pp. 1336-1341
    • Berry, D.M.1    Nash, P.2    Liu, S.K.3    Pawson, T.4
  • 36
    • 33846212272 scopus 로고    scopus 로고
    • Ubiquitin binds to and regulates a subset of SH3 domains
    • Stamenova, S. D., French, M. E., He, Y., Francis, S. A. et al., Ubiquitin binds to and regulates a subset of SH3 domains. Mol. Cell. 2007, 25, 273-284.
    • (2007) Mol. Cell. , vol.25 , pp. 273-284
    • Stamenova, S.D.1    French, M.E.2    He, Y.3    Francis, S.A.4
  • 37
    • 0034740693 scopus 로고    scopus 로고
    • Mechanism and role of PDZ domains in signaling complex assembly
    • Harris, B. Z., Lim, W. A., Mechanism and role of PDZ domains in signaling complex assembly. J. Cell. Sci. 2001, 114, 3219-3231.
    • (2001) J. Cell. Sci. , vol.114 , pp. 3219-3231
    • Harris, B.Z.1    Lim, W.A.2
  • 38
    • 0036289460 scopus 로고    scopus 로고
    • PIP(2)-PDZ domain binding controls the association of syntenin with the plasma membrane
    • Zimmermann, P., Meerschaert, K., Reekmans, G., Leenaerts, I. et al., PIP(2)-PDZ domain binding controls the association of syntenin with the plasma membrane. Mol. Cell. 2002, 9, 1215-1225.
    • (2002) Mol. Cell. , vol.9 , pp. 1215-1225
    • Zimmermann, P.1    Meerschaert, K.2    Reekmans, G.3    Leenaerts, I.4
  • 39
    • 36749070993 scopus 로고    scopus 로고
    • PDZ domains of Par-3 as potential phosphoinositide signaling integrators
    • Wu, H., Feng, W., Chen, J., Chan, L. N. et al., PDZ domains of Par-3 as potential phosphoinositide signaling integrators. Mol. Cell. 2007, 28, 886-898.
    • (2007) Mol. Cell. , vol.28 , pp. 886-898
    • Wu, H.1    Feng, W.2    Chen, J.3    Chan, L.N.4
  • 41
    • 24044465136 scopus 로고    scopus 로고
    • Novel Src homology 3 domain-binding motifs identified from proteomic screen of a Pro-rich region
    • Jia, C. Y., Nie, J., Wu, C., Li, C. et al., Novel Src homology 3 domain-binding motifs identified from proteomic screen of a Pro-rich region. Mol. Cell. Proteomics 2005, 4, 1155-1166.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1155-1166
    • Jia, C.Y.1    Nie, J.2    Wu, C.3    Li, C.4
  • 42
    • 0029959928 scopus 로고    scopus 로고
    • Distinct ligand preferences of Src homology 3 domains from Src, Yes, Abl, Cortactin, p53bp2, PLCgamma, Crk, and Grb2
    • Sparks, A. B., Rider, J. E., Hoffman, N. G., Fowlkes, D. M. et al., Distinct ligand preferences of Src homology 3 domains from Src, Yes, Abl, Cortactin, p53bp2, PLCgamma, Crk, and Grb2. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 1540-1544.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 1540-1544
    • Sparks, A.B.1    Rider, J.E.2    Hoffman, N.G.3    Fowlkes, D.M.4
  • 43
    • 78149333493 scopus 로고    scopus 로고
    • SH2 domains recognize contextual peptide sequence information to determine selectivity
    • Liu, B. A., Jablonowski, K., Shah, E. E., Engelmann, B. W., et al., SH2 domains recognize contextual peptide sequence information to determine selectivity. Mol. Cell. Proteomics 2010, 9, 2391-2404.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 2391-2404
    • Liu, B.A.1    Jablonowski, K.2    Shah, E.E.3    Engelmann, B.W.4
  • 44
    • 0027403027 scopus 로고
    • SH2 domains recognize specific phosphopeptide sequences
    • Songyang, Z., Shoelson, S. E., Chaudhuri, M., Gish, G. et al., SH2 domains recognize specific phosphopeptide sequences. Cell 1993, 72, 767-778.
    • (1993) Cell , vol.72 , pp. 767-778
    • Songyang, Z.1    Shoelson, S.E.2    Chaudhuri, M.3    Gish, G.4
  • 45
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin, A. J., Tanner, J. W., Allen, P. M., Shaw, A. S., Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 1996, 84, 889-897.
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 46
    • 0040017910 scopus 로고    scopus 로고
    • Function of WW domains as phosphoserine- or phosphothreonine-binding modules
    • Lu, P. J., Zhou, X. Z., Shen, M., Lu, K. P., Function of WW domains as phosphoserine- or phosphothreonine-binding modules. Science 1999, 283, 1325-1328.
    • (1999) Science , vol.283 , pp. 1325-1328
    • Lu, P.J.1    Zhou, X.Z.2    Shen, M.3    Lu, K.P.4
  • 47
    • 0033197541 scopus 로고    scopus 로고
    • The FHA domain is a modular phosphopeptide recognition motif
    • Durocher, D., Henckel, J., Fersht, A. R., Jackson, S. P., The FHA domain is a modular phosphopeptide recognition motif. Mol. Cell 1999, 4, 387-394.
    • (1999) Mol. Cell , vol.4 , pp. 387-394
    • Durocher, D.1    Henckel, J.2    Fersht, A.R.3    Jackson, S.P.4
  • 48
    • 0029067403 scopus 로고
    • PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine
    • Kavanaugh, W. M., Turck, C. W., Williams, L. T., PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine. Science 1995, 268, 1177-1179.
    • (1995) Science , vol.268 , pp. 1177-1179
    • Kavanaugh, W.M.1    Turck, C.W.2    Williams, L.T.3
  • 49
    • 8544232133 scopus 로고    scopus 로고
    • Regulation of the NMDA receptor complex and trafficking by activity-dependent phosphorylation of the NR2B subunit PDZ ligand
    • Chung, H. J., Huang, Y. H., Lau, L. F., Huganir, R. L., Regulation of the NMDA receptor complex and trafficking by activity-dependent phosphorylation of the NR2B subunit PDZ ligand. J. Neurosci. 2004, 24, 10248-10259.
    • (2004) J. Neurosci. , vol.24 , pp. 10248-10259
    • Chung, H.J.1    Huang, Y.H.2    Lau, L.F.3    Huganir, R.L.4
  • 50
    • 0242666140 scopus 로고    scopus 로고
    • CaMKII-dependent phosphorylation regulates SAP97/NR2A interaction
    • Gardoni, F., Mauceri, D., Fiorentini, C., Bellone, C. et al., CaMKII-dependent phosphorylation regulates SAP97/NR2A interaction. J. Biol. Chem. 2003, 278, 44745-44752.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44745-44752
    • Gardoni, F.1    Mauceri, D.2    Fiorentini, C.3    Bellone, C.4
  • 51
    • 80052180666 scopus 로고    scopus 로고
    • Inhibition of PI3K binding to activators by serine phosphorylation of PI3K regulatory subunit p85{alpha} Src homology-2 domains
    • Lee, J. Y., Chiu, Y. H., Asara, J., Cantley, L. C., Inhibition of PI3K binding to activators by serine phosphorylation of PI3K regulatory subunit p85{alpha} Src homology-2 domains. Proc. Natl. Acad. Sci. USA. 2011, 108, 14157-14162.
    • (2011) Proc. Natl. Acad. Sci. USA. , vol.108 , pp. 14157-14162
    • Lee, J.Y.1    Chiu, Y.H.2    Asara, J.3    Cantley, L.C.4
  • 52
    • 0035969559 scopus 로고    scopus 로고
    • Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication
    • Nash, P., Tang, X., Orlicky, S., Chen, Q. et al., Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication. Nature 2001, 414, 514-521.
    • (2001) Nature , vol.414 , pp. 514-521
    • Nash, P.1    Tang, X.2    Orlicky, S.3    Chen, Q.4
  • 53
    • 34249885757 scopus 로고    scopus 로고
    • Engineering synthetic signaling proteins with ultrasensitive input/output control
    • Dueber, J. E., Mirsky, E. A., Lim, W. A., Engineering synthetic signaling proteins with ultrasensitive input/output control. Nat. Biotechnol. 2007, 25, 660-662.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 660-662
    • Dueber, J.E.1    Mirsky, E.A.2    Lim, W.A.3
  • 54
    • 77951631601 scopus 로고    scopus 로고
    • Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase
    • Mittag, T., Marsh, J., Grishaev, A., Orlicky, S. et al., Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase. Structure 2010, 18, 494-506.
    • (2010) Structure , vol.18 , pp. 494-506
    • Mittag, T.1    Marsh, J.2    Grishaev, A.3    Orlicky, S.4
  • 55
    • 75849126506 scopus 로고    scopus 로고
    • The structural basis of peptide-protein binding strategies
    • London, N., Movshovitz-Attias, D., Schueler-Furman, O., The structural basis of peptide-protein binding strategies. Structure 2010, 18, 188-199.
    • (2010) Structure , vol.18 , pp. 188-199
    • London, N.1    Movshovitz-Attias, D.2    Schueler-Furman, O.3
  • 56
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan, A. A., Thorn, K. S., Anatomy of hot spots in protein interfaces. J. Mol. Biol. 1998, 280, 1-9.
    • (1998) J. Mol. Biol. , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 57
    • 0024745871 scopus 로고
    • The price of lost freedom: entropy of bimolecular complex formation
    • Finkelstein, A. V., Janin, J., The price of lost freedom: entropy of bimolecular complex formation. Protein Eng. 1989, 3, 1-3.
    • (1989) Protein Eng. , vol.3 , pp. 1-3
    • Finkelstein, A.V.1    Janin, J.2
  • 58
    • 77955567116 scopus 로고    scopus 로고
    • Constraining Binding Hot Spots: NMR and MD Simulations Provide a Structural Explanation for Enthalp-Entropy Compensation in SH2-Ligand Binding
    • 11070.
    • Ward, J. M., Gorenstein, N. M., Tian, J., Martin, S. F. et al. Constraining Binding Hot Spots: NMR and MD Simulations Provide a Structural Explanation for Enthalp-Entropy Compensation in SH2-Ligand Binding. J. Am. Chem. Soc. 2010, 132, 11058-11070.
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 11058
    • Ward, J.M.1    Gorenstein, N.M.2    Tian, J.3    Martin, S.F.4
  • 59
    • 0033527682 scopus 로고    scopus 로고
    • Investigation of phosphotyrosine recognition by the SH2 domain of the Src kinase
    • Bradshaw, J. M., Mitaxov, V., Waksman, G., Investigation of phosphotyrosine recognition by the SH2 domain of the Src kinase. J. Mol. Biol. 1999, 293, 971-985.
    • (1999) J. Mol. Biol. , vol.293 , pp. 971-985
    • Bradshaw, J.M.1    Mitaxov, V.2    Waksman, G.3
  • 60
    • 61449194210 scopus 로고    scopus 로고
    • Binding specificity of SH2 domains: insight from free energy simulations
    • Gan, W., Roux, B., Binding specificity of SH2 domains: insight from free energy simulations. Proteins 2009, 74, 996-1007.
    • (2009) Proteins , vol.74 , pp. 996-1007
    • Gan, W.1    Roux, B.2
  • 61
    • 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
  • 62
    • 0028346469 scopus 로고
    • SH2 domain specificity and activity modified by a single residue
    • Marengere, L. E., Songyang, Z., Gish, G. D., Schaller, M. D. et al., SH2 domain specificity and activity modified by a single residue. Nature 1994, 369, 502-505.
    • (1994) Nature , vol.369 , pp. 502-505
    • Marengere, L.E.1    Songyang, Z.2    Gish, G.D.3    Schaller, M.D.4
  • 63
    • 79957604998 scopus 로고    scopus 로고
    • A conserved residue in the yeast Bem1p SH3 domain maintains the high level of binding specificity required for function
    • Gorelik, M., Stanger, K., Davidson, A. R., A conserved residue in the yeast Bem1p SH3 domain maintains the high level of binding specificity required for function. J. Biol. Chem. 2011, 286, 19470-19477.
    • (2011) J. Biol. Chem. , vol.286 , pp. 19470-19477
    • Gorelik, M.1    Stanger, K.2    Davidson, A.R.3
  • 64
    • 79959706804 scopus 로고    scopus 로고
    • Spatial exclusivity combined with positive and negative selection of phosphorylation motifs is the basis for context-dependent mitotic signaling
    • Alexander, J., Lim, D., Joughin, B. A., Hegemann, B. et al., Spatial exclusivity combined with positive and negative selection of phosphorylation motifs is the basis for context-dependent mitotic signaling. Sci. signal., 4, ra42.
    • Sci. signal. , vol.4
    • Alexander, J.1    Lim, D.2    Joughin, B.A.3    Hegemann, B.4
  • 65
    • 79952399087 scopus 로고    scopus 로고
    • Beyond natural antibodies: the power of in vitro display technologies
    • Bradbury, A. R., Sidhu, S., Dubel, S., McCafferty, J., Beyond natural antibodies: the power of in vitro display technologies. Nat. Biotechnol., 29, 245-254.
    • Nat. Biotechnol. , vol.29 , pp. 245-254
    • Bradbury, A.R.1    Sidhu, S.2    Dubel, S.3    McCafferty, J.4
  • 66
    • 0031820966 scopus 로고    scopus 로고
    • Specific RNA binding proteins constructed from zinc fingers
    • Friesen, W. J., Darby, M. K., Specific RNA binding proteins constructed from zinc fingers. Nat. Struct. Boil. 1998, 5, 543-546.
    • (1998) Nat. Struct. Boil. , vol.5 , pp. 543-546
    • Friesen, W.J.1    Darby, M.K.2
  • 67
    • 42649123723 scopus 로고    scopus 로고
    • Defining the specificity space of the human SRC homology 2 domain
    • Huang, H., Li, L., Wu, C., Schibli, D. et al., Defining the specificity space of the human SRC homology 2 domain. Mol. Cell. Proteomics 2008, 7, 768-784.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 768-784
    • Huang, H.1    Li, L.2    Wu, C.3    Schibli, D.4
  • 68
    • 34547127612 scopus 로고    scopus 로고
    • PDZ domain binding selectivity is optimized across the mouse proteome
    • Stiffler, M. A., Chen, J. R., Grantcharova, V. P., Lei, Y. et al., PDZ domain binding selectivity is optimized across the mouse proteome. Science 2007, 317, 364-369.
    • (2007) Science , vol.317 , pp. 364-369
    • Stiffler, M.A.1    Chen, J.R.2    Grantcharova, V.P.3    Lei, Y.4
  • 69
    • 77953853695 scopus 로고    scopus 로고
    • Loops govern SH2 domain specificity by controlling access to binding pockets
    • Kaneko, T., Huang, H., Zhao, B., Li, L. et al., Loops govern SH2 domain specificity by controlling access to binding pockets. Sci. Signal., 3, ra34.
    • Sci. Signal. , vol.3
    • Kaneko, T.1    Huang, H.2    Zhao, B.3    Li, L.4
  • 70
    • 49749117432 scopus 로고    scopus 로고
    • Contextual specificity in peptide-mediated protein interactions
    • Stein, A., Aloy, P., Contextual specificity in peptide-mediated protein interactions. PLoS One 2008, 3, e2524.
    • (2008) PLoS One , vol.3
    • Stein, A.1    Aloy, P.2
  • 71
    • 68049110634 scopus 로고    scopus 로고
    • The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site
    • Bae, J. H., Lew, E. D., Yuzawa, S., Tome, F. et al., The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site. Cell 2009, 138, 514-524.
    • (2009) Cell , vol.138 , pp. 514-524
    • Bae, J.H.1    Lew, E.D.2    Yuzawa, S.3    Tome, F.4
  • 72
    • 0028789982 scopus 로고
    • Differential inhibition of signaling pathways by dominant-negative SH2/SH3 adapter proteins
    • Tanaka, M., Gupta, R., Mayer, B. J., Differential inhibition of signaling pathways by dominant-negative SH2/SH3 adapter proteins. Mol. Cell. Biol. 1995, 15, 6829-6837.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6829-6837
    • Tanaka, M.1    Gupta, R.2    Mayer, B.J.3
  • 73
    • 40849100220 scopus 로고    scopus 로고
    • Using engineered scaffold interactions to reshape MAP kinase pathway signaling dynamics
    • Bashor, C. J., Helman, N. C., Yan, S., Lim, W. A., Using engineered scaffold interactions to reshape MAP kinase pathway signaling dynamics. Science (New York, N.Y) 2008, 319, 1539-1543.
    • (2008) Science (New York, N.Y) , vol.319 , pp. 1539-1543
    • Bashor, C.J.1    Helman, N.C.2    Yan, S.3    Lim, W.A.4
  • 74
    • 33847718707 scopus 로고    scopus 로고
    • Dynamic control of signaling by modular adaptor proteins
    • Pawson, T., Dynamic control of signaling by modular adaptor proteins. Curr. Opin. Cell. Biol. 2007, 19, 112-116.
    • (2007) Curr. Opin. Cell. Biol. , vol.19 , pp. 112-116
    • Pawson, T.1
  • 75
    • 0034842129 scopus 로고    scopus 로고
    • Enteropathogenic E. coli Tir binds Nck to initiate actin pedestal formation in host cells
    • Gruenheid, S., DeVinney, R., Bladt, F., Goosney, D. et al., Enteropathogenic E. coli Tir binds Nck to initiate actin pedestal formation in host cells. Nat. Cell. Biol. 2001, 3, 856-859.
    • (2001) Nat. Cell. Biol. , vol.3 , pp. 856-859
    • Gruenheid, S.1    DeVinney, R.2    Bladt, F.3    Goosney, D.4
  • 76
    • 0141483011 scopus 로고    scopus 로고
    • Redirecting tyrosine kinase signaling to an apoptotic caspase pathway through chimeric adaptor proteins
    • Del
    • Howard, P. L., Chia, M. C., Del Rizzo, S., Liu, F. F., et al., Redirecting tyrosine kinase signaling to an apoptotic caspase pathway through chimeric adaptor proteins. Proc. Natl. Acad. Sci. USA. 2003, 100, 11267-11272.
    • (2003) Proc. Natl. Acad. Sci. USA. , vol.100 , pp. 11267-11272
    • Howard, P.L.1    Chia, M.C.2    Rizzo, S.3    Liu, F.F.4
  • 77
    • 43249100633 scopus 로고    scopus 로고
    • Membrane-dependent signal integration by the Ras activator Son of sevenless
    • Gureasko, J., Galush, W. J., Boykevisch, S., Sondermann, H. et al., Membrane-dependent signal integration by the Ras activator Son of sevenless. Nat. Struct. Mol. Biolo. 2008, 15, 452-461.
    • (2008) Nat. Struct. Mol. Biolo. , vol.15 , pp. 452-461
    • Gureasko, J.1    Galush, W.J.2    Boykevisch, S.3    Sondermann, H.4
  • 78
    • 0141838136 scopus 로고    scopus 로고
    • Mathematical modeling suggests cooperative interactions between a disordered polyvalent ligand and a single receptor site
    • Klein, P., Pawson, T., Tyers, M., Mathematical modeling suggests cooperative interactions between a disordered polyvalent ligand and a single receptor site. Curr. Biol. 2003, 13, 1669-1678.
    • (2003) Curr. Biol. , vol.13 , pp. 1669-1678
    • Klein, P.1    Pawson, T.2    Tyers, M.3
  • 79
    • 34547462095 scopus 로고    scopus 로고
    • Polyelectrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity
    • Borg, M., Mittag, T., Pawson, T., Tyers, M. et al., Polyelectrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity. Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 9650-9655.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 9650-9655
    • Borg, M.1    Mittag, T.2    Pawson, T.3    Tyers, M.4
  • 80
    • 0038608273 scopus 로고    scopus 로고
    • Four-dimensional organization of protein kinase signaling cascades: the roles of diffusion, endocytosis and molecular motors
    • Kholodenko, B. N., Four-dimensional organization of protein kinase signaling cascades: the roles of diffusion, endocytosis and molecular motors. J. Exp. Biol. 2003, 206, 2073-2082.
    • (2003) J. Exp. Biol. , vol.206 , pp. 2073-2082
    • Kholodenko, B.N.1
  • 81
    • 33644524741 scopus 로고    scopus 로고
    • Cell-signalling dynamics in time and space
    • Kholodenko, B. N., Cell-signalling dynamics in time and space. Nat. Rev. 2006, 7, 165-176.
    • (2006) Nat. Rev. , vol.7 , pp. 165-176
    • Kholodenko, B.N.1
  • 82
    • 0034194467 scopus 로고    scopus 로고
    • Why cytoplasmic signalling proteins should be recruited to cell membranes
    • Kholodenko, B. N., Hoek, J. B., Westerhoff, H. V., Why cytoplasmic signalling proteins should be recruited to cell membranes. Trend Cell Biol. 2000, 10, 173-178.
    • (2000) Trend Cell Biol. , vol.10 , pp. 173-178
    • Kholodenko, B.N.1    Hoek, J.B.2    Westerhoff, H.V.3
  • 83
    • 77953293697 scopus 로고    scopus 로고
    • Molecular mechanisms in signal transduction at the membrane
    • 2010
    • Groves, J. T., Kuriyan, J., Molecular mechanisms in signal transduction at the membrane. Nat. Struct. Mol. Biol. 2010, 17, 659-665.
    • Nat. Struct. Mol. Biol. , vol.17 , pp. 659-665
    • Groves, J.T.1    Kuriyan, J.2
  • 84
    • 78649613554 scopus 로고    scopus 로고
    • Rate enhancement of an interfacial biochemical reaction through localization of substrate and enzyme by an adaptor domain
    • 2010
    • Li, J., Nayak, S., Mrksich, M., Rate enhancement of an interfacial biochemical reaction through localization of substrate and enzyme by an adaptor domain. J. Phys. Chem. 2010, 114, 15113-15118.
    • J. Phys. Chem. , vol.114 , pp. 15113-15118
    • Li, J.1    Nayak, S.2    Mrksich, M.3
  • 85
    • 36849068465 scopus 로고    scopus 로고
    • Evolvable signaling networks of receptor tyrosine kinases: relevance of robustness to malignancy and to cancer therapy
    • Amit, I., Wides, R., Yarden, Y., Evolvable signaling networks of receptor tyrosine kinases: relevance of robustness to malignancy and to cancer therapy. Mol. Syst. Biol. 2007, 3, 151.
    • (2007) Mol. Syst. Biol. , vol.3 , pp. 151
    • Amit, I.1    Wides, R.2    Yarden, Y.3
  • 86
    • 0038483826 scopus 로고    scopus 로고
    • Emergence of scaling in random networks
    • Barabasi, A. L., Albert, R., Emergence of scaling in random networks. Science (New York, N.Y 1999, 286, 509-512.
    • (1999) Science (New York, N.Y , vol.286 , pp. 509-512
    • Barabasi, A.L.1    Albert, R.2
  • 88
    • 0036017388 scopus 로고    scopus 로고
    • Evolutionary rate heterogeneity in proteins with long disordered regions
    • Brown, C. J., Takayama, S., Campen, A. M., Vise, P. et al., Evolutionary rate heterogeneity in proteins with long disordered regions. J. Mol. Evol. 2002, 55, 104-110.
    • (2002) J. Mol. Evol. , vol.55 , pp. 104-110
    • Brown, C.J.1    Takayama, S.2    Campen, A.M.3    Vise, P.4
  • 89
    • 20444414545 scopus 로고    scopus 로고
    • Linear motifs: evolutionary interaction switches
    • Neduva, V., Russell, R. B., Linear motifs: evolutionary interaction switches. FEBS Lett. 2005, 579, 3342-3345.
    • (2005) FEBS Lett. , vol.579 , pp. 3342-3345
    • Neduva, V.1    Russell, R.B.2
  • 90
    • 33748074139 scopus 로고    scopus 로고
    • Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes
    • Haynes, C., Oldfield, C. J., Ji, F., Klitgord, N. et al., Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes. PLoS Comput. Biol. 2006, 2, e100.
    • (2006) PLoS Comput. Biol. , vol.2
    • Haynes, C.1    Oldfield, C.J.2    Ji, F.3    Klitgord, N.4
  • 91
    • 33847783298 scopus 로고    scopus 로고
    • Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins
    • Xie, H., Vucetic, S., Iakoucheva, L. M., Oldfield, C. J. et al., Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins. J. Proteome Res. 2007, 6, 1917-1932.
    • (2007) J. Proteome Res. , vol.6 , pp. 1917-1932
    • Xie, H.1    Vucetic, S.2    Iakoucheva, L.M.3    Oldfield, C.J.4
  • 92
    • 49449101097 scopus 로고    scopus 로고
    • High-order combination effects and biological robustness
    • 10.1038/msb.2008.51.
    • Lehar, J., Krueger, A., Zimmermann, G., Borisy, A., High-order combination effects and biological robustness. Mol. Syst. Biol. 2008, 4, 10.1038/msb.2008.51.
    • (2008) Mol. Syst. Biol , vol.4
    • Lehar, J.1    Krueger, A.2    Zimmermann, G.3    Borisy, A.4
  • 93
    • 0021101099 scopus 로고
    • A new general approach for the simultaneous chemical synthesis of large numbers of oligonucleotides: segmental solid supports
    • Frank, R., Heikens, W., Heisterberg-Moutsis, G., Blocker, H., A new general approach for the simultaneous chemical synthesis of large numbers of oligonucleotides: segmental solid supports. Nucleic Acids Res. 1983, 11, 4365-4377.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 4365-4377
    • Frank, R.1    Heikens, W.2    Heisterberg-Moutsis, G.3    Blocker, H.4
  • 94
    • 0000951677 scopus 로고
    • Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid
    • Geysen, H. M., Meloen, R. H., Barteling, S. J., Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid. Proc. Natl. Acad. Sci. USA. 1984, 81, 3998-4002.
    • (1984) Proc. Natl. Acad. Sci. USA. , vol.81 , pp. 3998-4002
    • Geysen, H.M.1    Meloen, R.H.2    Barteling, S.J.3
  • 95
    • 0036721834 scopus 로고    scopus 로고
    • The SPOT-synthesis technique. Synthetic peptide arrays on membrane supports-principles and applications
    • Frank, R., The SPOT-synthesis technique. Synthetic peptide arrays on membrane supports-principles and applications. J. Immunol. Methods 2002, 267, 13-26.
    • (2002) J. Immunol. Methods , vol.267 , pp. 13-26
    • Frank, R.1
  • 96
    • 1942509578 scopus 로고    scopus 로고
    • An improved method for the synthesis of cellulose membrane-bound peptides with free C termini is useful for PDZ domain binding studies
    • Boisguerin, P., Leben, R., Ay, B., Radziwill, G. et al., An improved method for the synthesis of cellulose membrane-bound peptides with free C termini is useful for PDZ domain binding studies. Chem. Biol. 2004, 11, 449-459.
    • (2004) Chem. Biol. , vol.11 , pp. 449-459
    • Boisguerin, P.1    Leben, R.2    Ay, B.3    Radziwill, G.4
  • 97
    • 1542305566 scopus 로고    scopus 로고
    • An oriented peptide array library (OPAL) strategy to study protein-protein interactions
    • Rodriguez, M., Li, S. S., Harper, J. W., Songyang, Z., An oriented peptide array library (OPAL) strategy to study protein-protein interactions. J. Biol. Chem. 2004, 279, 8802-8807.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8802-8807
    • Rodriguez, M.1    Li, S.S.2    Harper, J.W.3    Songyang, Z.4
  • 98
    • 21244463400 scopus 로고    scopus 로고
    • SPOT synthesis: reliability of array-based measurement of peptide binding affinity
    • Weiser, A. A., Or-Guil, M., Tapia, V., Leichsenring, A. et al., SPOT synthesis: reliability of array-based measurement of peptide binding affinity. Anal. Biochem. 2005, 342, 300-311.
    • (2005) Anal. Biochem. , vol.342 , pp. 300-311
    • Weiser, A.A.1    Or-Guil, M.2    Tapia, V.3    Leichsenring, A.4
  • 99
    • 70349156763 scopus 로고    scopus 로고
    • Dissecting protein function and signaling using protein microarrays
    • Wolf-Yadlin, A., Sevecka, M., MacBeath, G., Dissecting protein function and signaling using protein microarrays. Curr. Opin. Chem. Biol. 2009, 13, 398-405.
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 398-405
    • Wolf-Yadlin, A.1    Sevecka, M.2    MacBeath, G.3
  • 100
    • 0036898579 scopus 로고    scopus 로고
    • Protein microarrays and proteomics
    • MacBeath, G., Protein microarrays and proteomics. Nat. Genet. 2002, 32(Suppl), 526-532.
    • (2002) Nat. Genet. , vol.32 , Issue.SUPPL. , pp. 526-532
    • MacBeath, G.1
  • 101
    • 80054741181 scopus 로고    scopus 로고
    • Contact printing of protein microarrays
    • Austin, J., Holway, A. H., Contact printing of protein microarrays. Methods Mol. Biol. 2011, 785, 379-394.
    • (2011) Methods Mol. Biol. , vol.785 , pp. 379-394
    • Austin, J.1    Holway, A.H.2
  • 102
    • 33645502395 scopus 로고    scopus 로고
    • Tudor, MBT and chromo domains gauge the degree of lysine methylation
    • Kim, J., Daniel, J., Espejo, A., Lake, A. et al., Tudor, MBT and chromo domains gauge the degree of lysine methylation. EMBO Rep. 2006, 7, 397-403.
    • (2006) EMBO Rep. , vol.7 , pp. 397-403
    • Kim, J.1    Daniel, J.2    Espejo, A.3    Lake, A.4
  • 103
    • 0036846034 scopus 로고    scopus 로고
    • A protein-domain microarray identifies novel protein-protein interactions
    • Espejo, A., Cote, J., Bednarek, A., Richard, S. et al., A protein-domain microarray identifies novel protein-protein interactions. Biochem. J. 2002, 367, 697-702.
    • (2002) Biochem. J. , vol.367 , pp. 697-702
    • Espejo, A.1    Cote, J.2    Bednarek, A.3    Richard, S.4
  • 105
    • 0037415014 scopus 로고    scopus 로고
    • Exploring protein-protein interactions with phage display
    • Sidhu, S. S., Fairbrother, W. J., Deshayes, K., Exploring protein-protein interactions with phage display. Chembiochem 2003, 4, 14-25.
    • (2003) Chembiochem , vol.4 , pp. 14-25
    • Sidhu, S.S.1    Fairbrother, W.J.2    Deshayes, K.3
  • 107
    • 77949772254 scopus 로고    scopus 로고
    • Rapid evolution of functional complexity in a domain family
    • Ernst, A., Sazinsky, S. L., Hui, S., Currell, B. et al., Rapid evolution of functional complexity in a domain family. Sci. Signal. 2009, 2, ra50.
    • (2009) Sci. Signal. , vol.2
    • Ernst, A.1    Sazinsky, S.L.2    Hui, S.3    Currell, B.4
  • 108
    • 77956338533 scopus 로고    scopus 로고
    • High-resolution mapping of protein sequence-function relationships
    • Fowler, D. M., Araya, C. L., Fleishman, S. J., Kellogg, E. H. et al., High-resolution mapping of protein sequence-function relationships. Nat. Methods 2010, 7, 741-746.
    • (2010) Nat. Methods , vol.7 , pp. 741-746
    • Fowler, D.M.1    Araya, C.L.2    Fleishman, S.J.3    Kellogg, E.H.4
  • 109
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann, M., Jensen, O. N., Proteomic analysis of post-translational modifications. Nat. Biotechnol. 2003, 21, 255-261.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 111
    • 77958489760 scopus 로고    scopus 로고
    • Generating and navigating proteome maps using mass spectrometry
    • Ahrens, C. H., Brunner, E., Qeli, E., Basler, K. et al., Generating and navigating proteome maps using mass spectrometry. Nat. Rev. Mol. Cell. Biol. 2010, 11, 789-801.
    • (2010) Nat. Rev. Mol. Cell. Biol. , vol.11 , pp. 789-801
    • Ahrens, C.H.1    Brunner, E.2    Qeli, E.3    Basler, K.4
  • 112
    • 23344436258 scopus 로고    scopus 로고
    • WW domains provide a platform for the assembly of multiprotein networks
    • Ingham, R. J., Colwill, K., Howard, C., Dettwiler, S. et al., WW domains provide a platform for the assembly of multiprotein networks. Mol. Cell. Biol. 2005, 25, 7092-7106.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 7092-7106
    • Ingham, R.J.1    Colwill, K.2    Howard, C.3    Dettwiler, S.4
  • 113
    • 34247605084 scopus 로고    scopus 로고
    • Proteomic screen defines the Polo-box domain interactome and identifies Rock2 as a Plk1 substrate
    • Lowery, D. M., Clauser, K. R., Hjerrild, M., Lim, D. et al., Proteomic screen defines the Polo-box domain interactome and identifies Rock2 as a Plk1 substrate. EMBO J. 2007, 26, 2262-2273.
    • (2007) EMBO J. , vol.26 , pp. 2262-2273
    • Lowery, D.M.1    Clauser, K.R.2    Hjerrild, M.3    Lim, D.4
  • 114
    • 80052510197 scopus 로고    scopus 로고
    • Proteomic screening method for phosphopeptide motif binding proteins using peptide libraries
    • Christofk, H. R., Wu, N., Cantley, L. C., Asara, J. M., Proteomic screening method for phosphopeptide motif binding proteins using peptide libraries. J. Proteome Res. 2011, 10, 4158-4164.
    • (2011) J. Proteome Res. , vol.10 , pp. 4158-4164
    • Christofk, H.R.1    Wu, N.2    Cantley, L.C.3    Asara, J.M.4
  • 115
    • 0029157039 scopus 로고
    • Structure-function analysis of SH3 domains: SH3 binding specificity altered by single amino acid substitutions
    • Weng, Z., Rickles, R. J., Feng, S., Richard, S. et al., Structure-function analysis of SH3 domains: SH3 binding specificity altered by single amino acid substitutions. Mol. Cell. Biol. 1995, 15, 5627-5634.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5627-5634
    • Weng, Z.1    Rickles, R.J.2    Feng, S.3    Richard, S.4
  • 116
    • 33748322019 scopus 로고    scopus 로고
    • A high efficiency strategy for binding property characterization of peptide-binding domains
    • Song, E., Gao, S., Tian, R., Ma, S. et al., A high efficiency strategy for binding property characterization of peptide-binding domains. Mol. Cell. Proteomics 2006, 5, 1368-1381.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1368-1381
    • Song, E.1    Gao, S.2    Tian, R.3    Ma, S.4
  • 117
    • 0037059461 scopus 로고    scopus 로고
    • A combined experimental and computational strategy to define protein interaction networks for peptide recognition modules
    • Tong, A. H., Drees, B., Nardelli, G., Bader, G. D. et al., A combined experimental and computational strategy to define protein interaction networks for peptide recognition modules. Science 2002, 295, 321-324.
    • (2002) Science , vol.295 , pp. 321-324
    • Tong, A.H.1    Drees, B.2    Nardelli, G.3    Bader, G.D.4
  • 120
    • 20144372620 scopus 로고    scopus 로고
    • High-throughput mapping of a dynamic signaling network in mammalian cells
    • Barrios-Rodiles, M., Brown, K. R., Ozdamar, B., Bose, R. et al., High-throughput mapping of a dynamic signaling network in mammalian cells. Science 2005, 307, 1621-1625.
    • (2005) Science , vol.307 , pp. 1621-1625
    • Barrios-Rodiles, M.1    Brown, K.R.2    Ozdamar, B.3    Bose, R.4
  • 121
    • 0042622251 scopus 로고    scopus 로고
    • Scansite 2.0: proteome-wide prediction of cell signaling interactions using short sequence motifs
    • Obenauer, J. C., Cantley, L. C., Yaffe, M. B., Scansite 2.0: proteome-wide prediction of cell signaling interactions using short sequence motifs. Nucleic Acids Res. 2003, 31, 3635-3641.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3635-3641
    • Obenauer, J.C.1    Cantley, L.C.2    Yaffe, M.B.3
  • 122
    • 84862688337 scopus 로고    scopus 로고
    • Src homology 2 domain binding sites in insulin, IGF-1 and FGF receptor mediated signaling networks reveal an extensive potential interactome
    • Liu, B. A., Jablonowski, K., Engelmann, B. W., Higginbotham, K. et al., Src homology 2 domain binding sites in insulin, IGF-1 and FGF receptor mediated signaling networks reveal an extensive potential interactome. Publication in preparation 2012.
    • (2012) Publication in preparation
    • Liu, B.A.1    Jablonowski, K.2    Engelmann, B.W.3    Higginbotham, K.4
  • 123
    • 78650861777 scopus 로고    scopus 로고
    • SAINT: probabilistic scoring of affinity purification-mass spectrometry data
    • Choi, H., Larsen, B., Lin, Z. Y., Breitkreutz, A. et al., SAINT: probabilistic scoring of affinity purification-mass spectrometry data. Nat. Methods 2011, 8, 70-73.
    • (2011) Nat. Methods , vol.8 , pp. 70-73
    • Choi, H.1    Larsen, B.2    Lin, Z.Y.3    Breitkreutz, A.4
  • 124
    • 40349092949 scopus 로고    scopus 로고
    • Probabilistic assembly of human protein interaction networks from label-free quantitative proteomics
    • Sardiu, M. E., Cai, Y., Jin, J., Swanson, S. K. et al., Probabilistic assembly of human protein interaction networks from label-free quantitative proteomics. Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 1454-1459.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 1454-1459
    • Sardiu, M.E.1    Cai, Y.2    Jin, J.3    Swanson, S.K.4
  • 125
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa, M. E., Bennett, E. J., Gygi, S. P., Harper, J. W., Defining the human deubiquitinating enzyme interaction landscape. Cell 2009, 138, 389-403.
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 126
    • 84857854452 scopus 로고    scopus 로고
    • Annotator: post-processing software for generating function-based signatures from quantitative mass spectrometry
    • Sylvester, J. E., Bray, T. S., Kron, S. J., Annotator: post-processing software for generating function-based signatures from quantitative mass spectrometry. J. Proteome Res. 2012 11, 1521-1536.
    • (2012) J. Proteome Res. , vol.11 , pp. 1521-1536
    • Sylvester, J.E.1    Bray, T.S.2    Kron, S.J.3
  • 127
    • 0035836765 scopus 로고    scopus 로고
    • A comprehensive two-hybrid analysis to explore the yeast protein interactome
    • Ito, T., Chiba, T., Ozawa, R., Yoshida, M. et al., A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 4569-4574.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 4569-4574
    • Ito, T.1    Chiba, T.2    Ozawa, R.3    Yoshida, M.4
  • 128
    • 36949000237 scopus 로고    scopus 로고
    • Where have all the interactions gone? Estimating the coverage of two-hybrid protein interaction maps
    • Huang, H., Jedynak, B. M., Bader, J. S., Where have all the interactions gone? Estimating the coverage of two-hybrid protein interaction maps. PLoS Comput. Biol. 2007, 3, e214.
    • (2007) PLoS Comput. Biol. , vol.3
    • Huang, H.1    Jedynak, B.M.2    Bader, J.S.3
  • 129
    • 33847744247 scopus 로고    scopus 로고
    • How complete are current yeast and human protein-interaction networks?
    • Hart, G. T., Ramani, A. K., Marcotte, E. M., How complete are current yeast and human protein-interaction networks? Genome Biol. 2006, 7, 120.
    • (2006) Genome Biol. , vol.7 , pp. 120
    • Hart, G.T.1    Ramani, A.K.2    Marcotte, E.M.3
  • 130
    • 75549085083 scopus 로고    scopus 로고
    • Human protein reference database and human proteinpedia as discovery tools for systems biology
    • Prasad, T. S., Kandasamy, K., Pandey, A., Human protein reference database and human proteinpedia as discovery tools for systems biology. Methods Mol. Biol. 2009, 577, 67-79.
    • (2009) Methods Mol. Biol. , vol.577 , pp. 67-79
    • Prasad, T.S.1    Kandasamy, K.2    Pandey, A.3
  • 133
    • 30544449081 scopus 로고    scopus 로고
    • A quantitative protein interaction network for the ErbB receptors using protein microarrays
    • Jones, R. B., Gordus, A., Krall, J. A., MacBeath, G., A quantitative protein interaction network for the ErbB receptors using protein microarrays. Nature 2006, 439, 168-174.
    • (2006) Nature , vol.439 , pp. 168-174
    • Jones, R.B.1    Gordus, A.2    Krall, J.A.3    MacBeath, G.4
  • 134
    • 79960245388 scopus 로고    scopus 로고
    • Selected reaction monitoring mass spectrometry reveals the dynamics of signaling through the GRB2 adaptor
    • Bisson, N., James, D. A., Ivosev, G., Tate, S. A. et al., Selected reaction monitoring mass spectrometry reveals the dynamics of signaling through the GRB2 adaptor. Nat. Biotechnol. 2011, 29, 653-658.
    • (2011) Nat. Biotechnol. , vol.29 , pp. 653-658
    • Bisson, N.1    James, D.A.2    Ivosev, G.3    Tate, S.A.4
  • 135
    • 77951644400 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis
    • Olsen, J. V., Vermeulen, M., Santamaria, A., Kumar, C. et al., Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci. Signal. 2010, 3, ra3.
    • (2010) Sci. Signal. , vol.3
    • Olsen, J.V.1    Vermeulen, M.2    Santamaria, A.3    Kumar, C.4
  • 136
    • 78650466243 scopus 로고    scopus 로고
    • A tissue-specific atlas of mouse protein phosphorylation and expression
    • Huttlin, E. L., Jedrychowski, M. P., Elias, J. E., Goswami, T. et al., A tissue-specific atlas of mouse protein phosphorylation and expression. Cell 2010, 143, 1174-1189.
    • (2010) Cell , vol.143 , pp. 1174-1189
    • Huttlin, E.L.1    Jedrychowski, M.P.2    Elias, J.E.3    Goswami, T.4
  • 137
    • 64349110975 scopus 로고    scopus 로고
    • Systems-level interactions between insulin-EGF networks amplify mitogenic signaling
    • Borisov, N., Aksamitiene, E., Kiyatkin, A., Legewie, S. et al., Systems-level interactions between insulin-EGF networks amplify mitogenic signaling. Mol. Syst. Biol. 2009, 5, 256.
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 256
    • Borisov, N.1    Aksamitiene, E.2    Kiyatkin, A.3    Legewie, S.4
  • 138
    • 0035996750 scopus 로고    scopus 로고
    • Probing the phosphopeptide specificities of protein tyrosine phosphatases, SH2 and PTB domains with combinatorial library methods
    • Vetter, S. W., Zhang, Z. Y., Probing the phosphopeptide specificities of protein tyrosine phosphatases, SH2 and PTB domains with combinatorial library methods. Curr. Protein Pept. Sci. 2002, 3, 365-397.
    • (2002) Curr. Protein Pept. Sci. , vol.3 , pp. 365-397
    • Vetter, S.W.1    Zhang, Z.Y.2
  • 139
    • 0028351583 scopus 로고
    • Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav
    • Songyang, Z., Shoelson, S. E., McGlade, J., Olivier, P. et al., Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav. Mol. Cell. Biol. 1994, 14, 2777-2785.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2777-2785
    • Songyang, Z.1    Shoelson, S.E.2    McGlade, J.3    Olivier, P.4
  • 140
    • 34250748507 scopus 로고    scopus 로고
    • Identifying specificity profiles for peptide recognition modules from phage-displayed peptide libraries
    • Tonikian, R., Zhang, Y., Boone, C., Sidhu, S. S., Identifying specificity profiles for peptide recognition modules from phage-displayed peptide libraries. Nat. Protoc. 2007, 2, 1368-1386.
    • (2007) Nat. Protoc. , vol.2 , pp. 1368-1386
    • Tonikian, R.1    Zhang, Y.2    Boone, C.3    Sidhu, S.S.4
  • 142
    • 0028181441 scopus 로고
    • Hidden Markov models in computational biology. Applications to protein modeling
    • Krogh, A., Brown, M., Mian, I. S., Sjolander, K. et al., Hidden Markov models in computational biology. Applications to protein modeling. J. Mol. Biol. 1994, 235, 1501-1531.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1501-1531
    • Krogh, A.1    Brown, M.2    Mian, I.S.3    Sjolander, K.4
  • 143
    • 0031813130 scopus 로고    scopus 로고
    • Pfam: multiple sequence alignments and HMM-profiles of protein domains
    • Sonnhammer, E. L., Eddy, S. R., Birney, E., Bateman, A. et al., Pfam: multiple sequence alignments and HMM-profiles of protein domains. Nucleic Acids Res. 1998, 26, 320-322.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 320-322
    • Sonnhammer, E.L.1    Eddy, S.R.2    Birney, E.3    Bateman, A.4
  • 144
    • 77951209627 scopus 로고    scopus 로고
    • Predicting conserved protein motifs with sub-HMMs
    • Horan, K., Shelton, C. R., Girke, T., Predicting conserved protein motifs with sub-HMMs. BMC Bioinformatics 2010, 11, 205.
    • (2010) BMC Bioinformatics , vol.11 , pp. 205
    • Horan, K.1    Shelton, C.R.2    Girke, T.3
  • 145
    • 0042622252 scopus 로고    scopus 로고
    • ELM server: a new resource for investigating short functional sites in modular eukaryotic proteins
    • Puntervoll, P., Linding, R., Gemund, C., Chabanis-Davidson, S. et al., ELM server: a new resource for investigating short functional sites in modular eukaryotic proteins. Nucleic Acids Res. 2003, 31, 3625-3630.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3625-3630
    • Puntervoll, P.1    Linding, R.2    Gemund, C.3    Chabanis-Davidson, S.4
  • 146
    • 78650406559 scopus 로고    scopus 로고
    • Combining peptide recognition specificity and context information for the prediction of the 14-3-3-mediated interactome in S. cerevisiae and H. sapiens
    • Panni, S., Montecchi-Palazzi, L., Kiemer, L., Cabibbo, A. et al., Combining peptide recognition specificity and context information for the prediction of the 14-3-3-mediated interactome in S. cerevisiae and H. sapiens. Proteomics 2011, 11, 128-143.
    • (2011) Proteomics , vol.11 , pp. 128-143
    • Panni, S.1    Montecchi-Palazzi, L.2    Kiemer, L.3    Cabibbo, A.4
  • 147
    • 78650964531 scopus 로고    scopus 로고
    • Recognition and specificity determinants of the human cbx chromodomains
    • Kaustov, L., Ouyang, H., Amaya, M., Lemak, A. et al., Recognition and specificity determinants of the human cbx chromodomains. J. Biol. Chem. 2011, 286, 521-529.
    • (2011) J. Biol. Chem. , vol.286 , pp. 521-529
    • Kaustov, L.1    Ouyang, H.2    Amaya, M.3    Lemak, A.4
  • 148
    • 34848856343 scopus 로고    scopus 로고
    • Dynamic scaffolding in a G protein-coupled signaling system
    • Mishra, P., Socolich, M., Wall, M. A., Graves, J. et al., Dynamic scaffolding in a G protein-coupled signaling system. Cell 2007, 131, 80-92.
    • (2007) Cell , vol.131 , pp. 80-92
    • Mishra, P.1    Socolich, M.2    Wall, M.A.3    Graves, J.4
  • 149
    • 84855756033 scopus 로고    scopus 로고
    • The protein interaction network mediated by human SH3 domains
    • Carducci, M., Perfetto, L., Briganti, L., Paoluzi, S. et al., The protein interaction network mediated by human SH3 domains. Biotechnol. Adv. 2012 30, 4-15.
    • (2012) Biotechnol. Adv. , vol.30 , pp. 4-15
    • Carducci, M.1    Perfetto, L.2    Briganti, L.3    Paoluzi, S.4
  • 150
    • 70350404403 scopus 로고    scopus 로고
    • Bayesian modeling of the yeast SH3 domain interactome predicts spatiotemporal dynamics of endocytosis proteins
    • Tonikian, R., Xin, X., Toret, C. P., Gfeller, D. et al., Bayesian modeling of the yeast SH3 domain interactome predicts spatiotemporal dynamics of endocytosis proteins. PLoS Biol. 2009, 7, e1000218.
    • (2009) PLoS Biol. , vol.7
    • Tonikian, R.1    Xin, X.2    Toret, C.P.3    Gfeller, D.4
  • 151
    • 78649327383 scopus 로고    scopus 로고
    • A genome-wide study of PDZ-domain interactions in C. elegans reveals a high frequency of non-canonical binding
    • Lenfant, N., Polanowska, J., Bamps, S., Omi, S. et al., A genome-wide study of PDZ-domain interactions in C. elegans reveals a high frequency of non-canonical binding. BMC Genomics 2010, 11, 671.
    • (2010) BMC Genomics , vol.11 , pp. 671
    • Lenfant, N.1    Polanowska, J.2    Bamps, S.3    Omi, S.4
  • 152
    • 33750987920 scopus 로고    scopus 로고
    • Screening for PTB domain binding partners and ligand specificity using proteome-derived NPXY peptide arrays
    • Smith, M. J., Hardy, W. R., Murphy, J. M., Jones, N. et al., Screening for PTB domain binding partners and ligand specificity using proteome-derived NPXY peptide arrays. Mol. Cell. Biol. 2006, 26, 8461-8474.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 8461-8474
    • Smith, M.J.1    Hardy, W.R.2    Murphy, J.M.3    Jones, N.4
  • 153
    • 12144287536 scopus 로고    scopus 로고
    • A map of WW domain family interactions
    • Hu, H., Columbus, J., Zhang, Y., Wu, D. et al., A map of WW domain family interactions. Proteomics 2004, 4, 643-655.
    • (2004) Proteomics , vol.4 , pp. 643-655
    • Hu, H.1    Columbus, J.2    Zhang, Y.3    Wu, D.4


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