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Volumn 186, Issue , 2008, Pages 407-429

Proline-rich sequence recognition domains (PRD): Ligands, function and inhibition

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND; PROLINE;

EID: 49049108952     PISSN: 01712004     EISSN: 18650325     Source Type: Book Series    
DOI: 10.1007/978-3-540-72843-6_17     Document Type: Article
Times cited : (32)

References (149)
  • 1
    • 0027474991 scopus 로고
    • Left-handed polyproline II helices commonly occur in globular proteins
    • Adzhubei AA, Sternberg MJ (1993) Left-handed polyproline II helices commonly occur in globular proteins. J Mol Biol 229:472-493
    • (1993) J Mol Biol , vol.229 , pp. 472-493
    • Adzhubei, A.A.1    Sternberg, M.J.2
  • 2
    • 33750011457 scopus 로고    scopus 로고
    • Identification of novel proteins induced by estradiol, 4-hydroxytamoxifen and acolbifene in T47D breast cancer cells
    • Al Dhaheri MH, Shah YM, Basrur V, Pind S, Rowan BG (2006) Identification of novel proteins induced by estradiol, 4-hydroxytamoxifen and acolbifene in T47D breast cancer cells. Steroids 71:966-978
    • (2006) Steroids , vol.71 , pp. 966-978
    • Al Dhaheri, M.H.1    Shah, Y.M.2    Basrur, V.3    Pind, S.4    Rowan, B.G.5
  • 3
    • 23044492008 scopus 로고    scopus 로고
    • WW domain-containing proteins, WWOX and YAP, compete for interaction with ErbB-4 and modulate its transcriptional function
    • Aqeilan RI, Donati V, Palamarchuk A, Trapasso F, Kaou M, Pekarsky Y, Sudol M, Croce CM (2005) WW domain-containing proteins, WWOX and YAP, compete for interaction with ErbB-4 and modulate its transcriptional function. Cancer Res 65:6764-6772
    • (2005) Cancer Res , vol.65 , pp. 6764-6772
    • Aqeilan, R.I.1    Donati, V.2    Palamarchuk, A.3    Trapasso, F.4    Kaou, M.5    Pekarsky, Y.6    Sudol, M.7    Croce, C.M.8
  • 4
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • Arkin MR, Wells JA (2004) Small-molecule inhibitors of protein-protein interactions: progressing towards the dream. Nat Rev Drug Discov 3:301-317
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 6
    • 12444347534 scopus 로고    scopus 로고
    • A protein's final ESCRT
    • Babst M (2005) A protein's final ESCRT. Traffic 6:2-9
    • (2005) Traffic , vol.6 , pp. 2-9
    • Babst, M.1
  • 8
    • 15944411375 scopus 로고    scopus 로고
    • First stereoselective synthesis of a pro-pro E-alkene dipeptide isostere
    • Bandur NG, Harms K, Koert U (2005) First stereoselective synthesis of a pro-pro E-alkene dipeptide isostere. Synlett 773-776
    • (2005) Synlett , pp. 773-776
    • Bandur, N.G.1    Harms, K.2    Koert, U.3
  • 10
    • 0030910308 scopus 로고    scopus 로고
    • FBP WW domains and the Abl SH3 domain bind to a specific class of proline-rich ligands
    • Bedford MT, Chan DC, Leder P (1997) FBP WW domains and the Abl SH3 domain bind to a specific class of proline-rich ligands. EMBO J 16:2376-2383
    • (1997) EMBO J , vol.16 , pp. 2376-2383
    • Bedford, M.T.1    Chan, D.C.2    Leder, P.3
  • 11
    • 0034717290 scopus 로고    scopus 로고
    • Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains
    • Bedford MT, Frankel A, Yaffe MB, Clarke S, Leder P, Richard S (2000) Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains. J Biol Chem 275:16030-16036
    • (2000) J Biol Chem , vol.275 , pp. 16030-16036
    • Bedford, M.T.1    Frankel, A.2    Yaffe, M.B.3    Clarke, S.4    Leder, P.5    Richard, S.6
  • 13
    • 27444437758 scopus 로고    scopus 로고
    • Disease-related modifications in tau affect the interaction between Fyn and Tau
    • Bhaskar K, Yen SH, Lee G (2005) Disease-related modifications in tau affect the interaction between Fyn and Tau. J Biol Chem 280:35119-35125
    • (2005) J Biol Chem , vol.280 , pp. 35119-35125
    • Bhaskar, K.1    Yen, S.H.2    Lee, G.3
  • 14
    • 29144474443 scopus 로고    scopus 로고
    • Late budding domains and host proteins in enveloped virus release
    • Bieniasz PD (2006) Late budding domains and host proteins in enveloped virus release. Virology 344:55-63
    • (2006) Virology , vol.344 , pp. 55-63
    • Bieniasz, P.D.1
  • 16
    • 0036035968 scopus 로고    scopus 로고
    • Polyproline II structure in proteins: Identification by chiroptical spectroscopies, stability, and functions
    • Bochicchio B, Tamburro AM (2002) Polyproline II structure in proteins: identification by chiroptical spectroscopies, stability, and functions. Chirality 14:782-792
    • (2002) Chirality , vol.14 , pp. 782-792
    • Bochicchio, B.1    Tamburro, A.M.2
  • 17
    • 7944223078 scopus 로고    scopus 로고
    • Structure and regulation of Src family kinases
    • Boggon TJ, Eck MJ (2004) Structure and regulation of Src family kinases. Oncogene 23:7918-7927
    • (2004) Oncogene , vol.23 , pp. 7918-7927
    • Boggon, T.J.1    Eck, M.J.2
  • 18
    • 0027988814 scopus 로고
    • The WW domain: A signalling site in dystrophin?
    • Bork P, Sudol M (1994) The WW domain: a signalling site in dystrophin? Trends Biochem Sci 19:531-533
    • (1994) Trends Biochem Sci , vol.19 , pp. 531-533
    • Bork, P.1    Sudol, M.2
  • 19
    • 84886632310 scopus 로고
    • Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells
    • Carlsson L, Nystrom LE, Sundkvist I, Markey F, Lindberg U (1977) Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells. J Mol Biol 115:465-483
    • (1977) J Mol Biol , vol.115 , pp. 465-483
    • Carlsson, L.1    Nystrom, L.E.2    Sundkvist, I.3    Markey, F.4    Lindberg, U.5
  • 20
    • 4143110407 scopus 로고    scopus 로고
    • Cell cycle arrest and cell death are controlled by p53-dependent and p53-independent mechanisms in Tsg101-deficient cells
    • Carstens MJ, Krempler A, Triplett AA, Van Lohuizen M, Wagner KU (2004) Cell cycle arrest and cell death are controlled by p53-dependent and p53-independent mechanisms in Tsg101-deficient cells. J Biol Chem 279:35984-35994
    • (2004) J Biol Chem , vol.279 , pp. 35984-35994
    • Carstens, M.J.1    Krempler, A.2    Triplett, A.A.3    Van Lohuizen, M.4    Wagner, K.U.5
  • 21
    • 0037138380 scopus 로고    scopus 로고
    • Can we infer peptide recognition specificity mediated by SH3 domains?
    • Cesareni G, Panni S, Nardelli G, Castagnoli L (2002) Can we infer peptide recognition specificity mediated by SH3 domains? FEBS Lett 513:38-44
    • (2002) FEBS Lett , vol.513 , pp. 38-44
    • Cesareni, G.1    Panni, S.2    Nardelli, G.3    Castagnoli, L.4
  • 22
    • 0028933782 scopus 로고
    • A focal adhesion factor directly linking intracellularly motile Listeria monocytogenes and Listeria ivanovii to the actin-based cytoskeleton of mammalian cells
    • Chakraborty T, Ebel F, Domann E, Niebuhr K, Gerstel B, Pistor S, Temm-Grove CJ, Jockusch BM, Reinhard M, Walter U (1995) A focal adhesion factor directly linking intracellularly motile Listeria monocytogenes and Listeria ivanovii to the actin-based cytoskeleton of mammalian cells. EMBO J 14:1314-1321
    • (1995) EMBO J , vol.14 , pp. 1314-1321
    • Chakraborty, T.1    Ebel, F.2    Domann, E.3    Niebuhr, K.4    Gerstel, B.5    Pistor, S.6    Temm-Grove, C.J.7    Jockusch, B.M.8    Reinhard, M.9    Walter, U.10
  • 25
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson T, Wells JA (1995) A hot spot of binding energy in a hormone-receptor interface. Science 267:383-386
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 26
    • 13944275600 scopus 로고    scopus 로고
    • Properties of polyproline II, a secondary structure element implicated in protein-protein interactions
    • Cubellis MV, Caillez F, Blundell TL, Lovell SC (2005) Properties of polyproline II, a secondary structure element implicated in protein-protein interactions. Proteins 58:880-892
    • (2005) Proteins , vol.58 , pp. 880-892
    • Cubellis, M.V.1    Caillez, F.2    Blundell, T.L.3    Lovell, S.C.4
  • 28
    • 0037154214 scopus 로고    scopus 로고
    • Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function
    • Demirov DG, Ono A, Orenstein JM, Freed EO (2002) Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function. Proc Natl Acad Sci USA 99:955-960
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 955-960
    • Demirov, D.G.1    Ono, A.2    Orenstein, J.M.3    Freed, E.O.4
  • 30
    • 0027937223 scopus 로고
    • Isolation of a novel gene mutated in Wiskott-Aldrich syndrome
    • Derry JM, Ochs HD, Francke U (1994) Isolation of a novel gene mutated in Wiskott-Aldrich syndrome. Cell 79:635-644
    • (1994) Cell , vol.79 , pp. 635-644
    • Derry, J.M.1    Ochs, H.D.2    Francke, U.3
  • 32
    • 10444276589 scopus 로고    scopus 로고
    • Making protein interactions druggable: Targeting PDZ domains
    • Dev KK (2004) Making protein interactions druggable: targeting PDZ domains. Nat Rev Drug Discov 3:1047-1056
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 1047-1056
    • Dev, K.K.1
  • 33
    • 27144507874 scopus 로고    scopus 로고
    • Collagen-like triple helix formation of synthetic (Pro-Pro-Gly 10 analogues: (4(S)-hydroxyprolyl-4(R)-hydroxyprolyl-Gly 10, (4(R)-hydroxyprolyl-4(R)-hydroxyprolyl-Gly and (4(S)-fluoroprolyl-4(R)-fluoroprolyl-Gly)10
    • Doi M, Nishi Y, Uchiyama S, Nishiuchi Y, Nishio H, Nakazawa T, Ohkubo T, Kobayashi Y (2005) Collagen-like triple helix formation of synthetic (Pro-Pro-Gly)10 analogues: (4(S)-hydroxyprolyl-4(R)-hydroxyprolyl-Gly)10, (4(R)-hydroxyprolyl-4(R)-hydroxyprolyl-Gly)10 and (4(S)-fluoroprolyl-4(R)-fluoroprolyl-Gly)10. J Pept Sci 11:609-616
    • (2005) J Pept Sci , vol.11 , pp. 609-616
    • Doi, M.1    Nishi, Y.2    Uchiyama, S.3    Nishiuchi, Y.4    Nishio, H.5    Nakazawa, T.6    Ohkubo, T.7    Kobayashi, Y.8
  • 35
    • 3042523534 scopus 로고    scopus 로고
    • Small-molecule inhibitors of the p53 suppressor HDM2: Have protein-protein interactions come of age as drug targets?
    • Fischer PM, Lane DP (2004) Small-molecule inhibitors of the p53 suppressor HDM2: have protein-protein interactions come of age as drug targets? Trends Pharmacol Sci 25:343-346
    • (2004) Trends Pharmacol Sci , vol.25 , pp. 343-346
    • Fischer, P.M.1    Lane, D.P.2
  • 36
    • 0036721834 scopus 로고    scopus 로고
    • The SPOT-synthesis technique. Synthetic peptide arrays on membrane supports-principles and applications
    • Frank R (2002) The SPOT-synthesis technique. Synthetic peptide arrays on membrane supports-principles and applications. J Immunol Methods 267:13-26
    • (2002) J Immunol Methods , vol.267 , pp. 13-26
    • Frank, R.1
  • 37
    • 0032985562 scopus 로고    scopus 로고
    • The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences
    • Freund C, Dotsch V, Nishizawa K, Reinherz EL, Wagner G (1999) The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences. Nat Struct Biol 6:656-660
    • (1999) Nat Struct Biol , vol.6 , pp. 656-660
    • Freund, C.1    Dotsch, V.2    Nishizawa, K.3    Reinherz, E.L.4    Wagner, G.5
  • 38
    • 0037112758 scopus 로고    scopus 로고
    • Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector molecules
    • Freund C, Kuhne R, Yang H, Park S, Reinherz EL, Wagner G (2002) Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector molecules. EMBO J 21:5985-5995
    • (2002) EMBO J , vol.21 , pp. 5985-5995
    • Freund, C.1    Kuhne, R.2    Yang, H.3    Park, S.4    Reinherz, E.L.5    Wagner, G.6
  • 41
    • 0037688240 scopus 로고    scopus 로고
    • Defects in human immunodeficiency virus budding and endosomal sorting induced by TSG101 overexpression
    • Goila-Gaur R, Demirov DG, Orenstein JM, Ono A, Freed EO (2003) Defects in human immunodeficiency virus budding and endosomal sorting induced by TSG101 overexpression. J Virol 77:6507-6519
    • (2003) J Virol , vol.77 , pp. 6507-6519
    • Goila-Gaur, R.1    Demirov, D.G.2    Orenstein, J.M.3    Ono, A.4    Freed, E.O.5
  • 42
    • 0034774728 scopus 로고    scopus 로고
    • The transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1
    • Goldstrohm AC, Albrecht TR, Sune C, Bedford MT, Garcia-Blanco MA (2001) The transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1. Mol Cell Biol 21:7617-7628
    • (2001) Mol Cell Biol , vol.21 , pp. 7617-7628
    • Goldstrohm, A.C.1    Albrecht, T.R.2    Sune, C.3    Bedford, M.T.4    Garcia-Blanco, M.A.5
  • 44
    • 0030575866 scopus 로고    scopus 로고
    • Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2
    • Gorina S, Pavletich NP (1996) Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2. Science 274:1001-1005
    • (1996) Science , vol.274 , pp. 1001-1005
    • Gorina, S.1    Pavletich, N.P.2
  • 45
    • 0026317877 scopus 로고
    • Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release
    • Gottlinger HG, Dorfman T, Sodroski JG, Haseltine WA (1991) Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release. Proc Natl Acad Sci USA 88:3195-3199
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 3195-3199
    • Gottlinger, H.G.1    Dorfman, T.2    Sodroski, J.G.3    Haseltine, W.A.4
  • 46
    • 0037722978 scopus 로고    scopus 로고
    • Molecular basis of phosphorylationinduced activation of the NADPH oxidase
    • Groemping Y, Lapouge K, Smerdon SJ, Rittinger K (2003) Molecular basis of phosphorylationinduced activation of the NADPH oxidase. Cell 113:343-355
    • (2003) Cell , vol.113 , pp. 343-355
    • Groemping, Y.1    Lapouge, K.2    Smerdon, S.J.3    Rittinger, K.4
  • 48
    • 0034740693 scopus 로고    scopus 로고
    • Mechanism and role of PDZ domains in signaling complex assembly
    • Harris BZ, Lim WA (2001) Mechanism and role of PDZ domains in signaling complex assembly. J Cell Sci 114:3219-3231
    • (2001) J Cell Sci , vol.114 , pp. 3219-3231
    • Harris, B.Z.1    Lim, W.A.2
  • 50
    • 0033525582 scopus 로고    scopus 로고
    • Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
    • Hofmann RM, Pickart CM (1999) Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Cell 96:645-653
    • (1999) Cell , vol.96 , pp. 645-653
    • Hofmann, R.M.1    Pickart, C.M.2
  • 54
    • 0028971135 scopus 로고
    • P6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease
    • Huang M, Orenstein JM, Martin MA, Freed EO (1995) p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease. J Virol 69:6810-6818
    • (1995) J Virol , vol.69 , pp. 6810-6818
    • Huang, M.1    Orenstein, J.M.2    Martin, M.A.3    Freed, E.O.4
  • 55
    • 33646010475 scopus 로고    scopus 로고
    • The ESCRT complexes: Structure and mechanism of a membrane-trafficking network
    • Hurley JH, Emr SD (2006) The ESCRT complexes: structure and mechanism of a membrane-trafficking network. Annu Rev Biophys Biomol Struct 35:277-298
    • (2006) Annu Rev Biophys Biomol Struct , vol.35 , pp. 277-298
    • Hurley, J.H.1    Emr, S.D.2
  • 56
    • 0036157980 scopus 로고    scopus 로고
    • The WW domain: Linking cell signalling to the membrane cytoskeleton
    • Ilsley JL, Sudol M, Winder SJ (2002) The WW domain: linking cell signalling to the membrane cytoskeleton. Cell Signal 14:183-189
    • (2002) Cell Signal , vol.14 , pp. 183-189
    • Ilsley, J.L.1    Sudol, M.2    Winder, S.J.3
  • 57
    • 1842591240 scopus 로고    scopus 로고
    • The Nedd4 family of E3 ubiquitin ligases: Functional diversity within a common modular architecture
    • Ingham RJ, Gish G, Pawson T (2004) The Nedd4 family of E3 ubiquitin ligases: functional diversity within a common modular architecture. Oncogene 23:1972-1984
    • (2004) Oncogene , vol.23 , pp. 1972-1984
    • Ingham, R.J.1    Gish, G.2    Pawson, T.3
  • 59
    • 27944493098 scopus 로고    scopus 로고
    • Synthesis of N-benzylated-2-aminoquinolines as ligands for the Tec SH3 domain
    • Inglis SR, Jones RK, Booker GW, Pyke SM (2006) Synthesis of N-benzylated-2-aminoquinolines as ligands for the Tec SH3 domain. Bioorg Med Chem Lett 16:387-390
    • (2006) Bioorg Med Chem Lett , vol.16 , pp. 387-390
    • Inglis, S.R.1    Jones, R.K.2    Booker, G.W.3    Pyke, S.M.4
  • 61
    • 0035027506 scopus 로고    scopus 로고
    • Solution structure of a Nedd4 WW domain-ENaC peptide complex
    • Kanelis V, Rotin D, Forman-Kay JD (2001) Solution structure of a Nedd4 WW domain-ENaC peptide complex. Nat Struct Biol 8:407-412
    • (2001) Nat Struct Biol , vol.8 , pp. 407-412
    • Kanelis, V.1    Rotin, D.2    Forman-Kay, J.D.3
  • 64
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains
    • Kay BK, Williamson MP, Sudol M (2000) The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J 14:231-241
    • (2000) FASEB J , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 65
    • 1842500993 scopus 로고    scopus 로고
    • Unfolded state of polyalanine is a segmented polyproline II helix
    • Kentsis A, Mezei M, Gindin T, Osman R (2004) Unfolded state of polyalanine is a segmented polyproline II helix. Proteins 55:493-501
    • (2004) Proteins , vol.55 , pp. 493-501
    • Kentsis, A.1    Mezei, M.2    Gindin, T.3    Osman, R.4
  • 66
    • 0031962106 scopus 로고    scopus 로고
    • Growth factor receptor-bound protein 2 SH2/SH3 domain binding to CD28 and its role in co-signaling
    • Kim HH, Tharayil M, Rudd CE (1998) Growth factor receptor-bound protein 2 SH2/SH3 domain binding to CD28 and its role in co-signaling. J Biol Chem 273:296-301
    • (1998) J Biol Chem , vol.273 , pp. 296-301
    • Kim, H.H.1    Tharayil, M.2    Rudd, C.E.3
  • 67
    • 33645036616 scopus 로고    scopus 로고
    • The GYF domain
    • Kofler MM, Freund C (2006) The GYF domain. FEBS J 273:245-256
    • (2006) FEBS J , vol.273 , pp. 245-256
    • Kofler, M.M.1    Freund, C.2
  • 68
    • 3142579304 scopus 로고    scopus 로고
    • Recognition sequences for the GYF domain reveal a possible spliceosomal function of CD2BP2
    • Kofler M, Heuer K, Zech T, Freund C (2004) Recognition sequences for the GYF domain reveal a possible spliceosomal function of CD2BP2. J Biol Chem 279:28292-28297
    • (2004) J Biol Chem , vol.279 , pp. 28292-28297
    • Kofler, M.1    Heuer, K.2    Zech, T.3    Freund, C.4
  • 69
    • 28644446256 scopus 로고    scopus 로고
    • GYF Domain proteomics reveals interaction sites in known and novel target proteins
    • Kofler M, Motzny K, Freund C (2005) GYF Domain proteomics reveals interaction sites in known and novel target proteins. Mol Cell Proteomics 4:1797-1811
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1797-1811
    • Kofler, M.1    Motzny, K.2    Freund, C.3
  • 70
    • 0029078212 scopus 로고
    • Identification of WASP mutations in patients with Wiskott-Aldrich syndrome and isolated thrombocytopenia reveals allelic heterogeneity at the WAS locus
    • Kolluri R, Shehabeldin A, Peacocke M, Lamhonwah AM, Teichert-Kuliszewska K, Weissman SM, Siminovitch KA (1995) Identification of WASP mutations in patients with Wiskott-Aldrich syndrome and isolated thrombocytopenia reveals allelic heterogeneity at the WAS locus. Hum Mol Genet 4:1119-1126
    • (1995) Hum Mol Genet , vol.4 , pp. 1119-1126
    • Kolluri, R.1    Shehabeldin, A.2    Peacocke, M.3    Lamhonwah, A.M.4    Teichert-Kuliszewska, K.5    Weissman, S.M.6    Siminovitch, K.A.7
  • 71
    • 0042858208 scopus 로고    scopus 로고
    • WW domain-containing protein YAP associates with ErbB-4 and acts as a co-transcriptional activator for the carboxyl-terminal fragment of ErbB-4 that translocates to the nucleus
    • Komuro A, Nagai M, Navin NE, Sudol M (2003) WW domain-containing protein YAP associates with ErbB-4 and acts as a co-transcriptional activator for the carboxyl-terminal fragment of ErbB-4 that translocates to the nucleus. J Biol Chem 278:33334-33341
    • (2003) J Biol Chem , vol.278 , pp. 33334-33341
    • Komuro, A.1    Nagai, M.2    Navin, N.E.3    Sudol, M.4
  • 72
    • 0037044742 scopus 로고    scopus 로고
    • Targeted deletion of the Tsg101 gene results in cell cycle arrest at G1/S and p53-independent cell death
    • Krempler A, Henry MD, Triplett AA, Wagner KU (2002) Targeted deletion of the Tsg101 gene results in cell cycle arrest at G1/S and p53-independent cell death. J Biol Chem 277:43216-43223
    • (2002) J Biol Chem , vol.277 , pp. 43216-43223
    • Krempler, A.1    Henry, M.D.2    Triplett, A.A.3    Wagner, K.U.4
  • 73
    • 17844367582 scopus 로고    scopus 로고
    • The human U5 snRNP 52 K protein (CD2BP2) interacts with U5-102 K (hPrp6), a U4/U6.U5 tri-snRNP bridging protein, but dissociates upon tri-snRNP formation
    • Laggerbauer B, Liu S, Makarov E, Vornlocher HP, Makarova O, Ingelfinger D, Achsel T, Luhrmann R (2005) The human U5 snRNP 52 K protein (CD2BP2) interacts with U5-102 K (hPrp6), a U4/U6.U5 tri-snRNP bridging protein, but dissociates upon tri-snRNP formation. RNA 11:598-608
    • (2005) RNA , vol.11 , pp. 598-608
    • Laggerbauer, B.1    Liu, S.2    Makarov, E.3    Vornlocher, H.P.4    Makarova, O.5    Ingelfinger, D.6    Achsel, T.7    Luhrmann, R.8
  • 75
    • 29144458287 scopus 로고    scopus 로고
    • Signaling protein inhibitors via the combinatorial modification of peptide scaffolds
    • Lawrence DS (2005) Signaling protein inhibitors via the combinatorial modification of peptide scaffolds. Biochim Biophys Acta 1754:50-57
    • (2005) Biochim Biophys Acta , vol.1754 , pp. 50-57
    • Lawrence, D.S.1
  • 76
    • 0344505849 scopus 로고    scopus 로고
    • Tau interacts with src-family non-receptor tyrosine kinases
    • Lee G, Newman ST, Gard DL, Band H, Panchamoorthy G (1998) Tau interacts with src-family non-receptor tyrosine kinases. J Cell Sci 111( Pt 21):3167-3177
    • (1998) J Cell Sci , vol.111 , Issue.PART 21 , pp. 3167-3177
    • Lee, G.1    Newman, S.T.2    Gard, D.L.3    Band, H.4    Panchamoorthy, G.5
  • 77
    • 24044540256 scopus 로고    scopus 로고
    • Specificity and versatility of SH3 and other proline-recognition domains: Structural basis and implications for cellular signal transduction
    • Li SS (2005) Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction. Biochem J 390:641-653
    • (2005) Biochem J , vol.390 , pp. 641-653
    • Li, S.S.1
  • 78
    • 23944445322 scopus 로고    scopus 로고
    • Acquisition of Fyn-selective SH3 domain ligands via a combinatorial library strategy
    • Li H, Lawrence DS (2005) Acquisition of Fyn-selective SH3 domain ligands via a combinatorial library strategy. Chem Biol 12:905-912
    • (2005) Chem Biol , vol.12 , pp. 905-912
    • Li, H.1    Lawrence, D.S.2
  • 79
    • 0030585431 scopus 로고    scopus 로고
    • Reading between the lines: SH3 recognition of an intact protein
    • Lim WA (1996) Reading between the lines: SH3 recognition of an intact protein. Structure 4:657-659
    • (1996) Structure , vol.4 , pp. 657-659
    • Lim, W.A.1
  • 80
    • 0032584738 scopus 로고    scopus 로고
    • Association of p59(fyn) with the T lymphocyte costimulatory receptor CD2. Binding of the Fyn Src homology (SH) 3 domain is regulated by the Fyn SH2 domain
    • Lin H, Hutchcroft JE, Andoniou CE, Kamoun M, Band H, Bierer BE (1998) Association of p59(fyn) with the T lymphocyte costimulatory receptor CD2. Binding of the Fyn Src homology (SH) 3 domain is regulated by the Fyn SH2 domain. J Biol Chem 273:19914-19921
    • (1998) J Biol Chem , vol.273 , pp. 19914-19921
    • Lin, H.1    Hutchcroft, J.E.2    Andoniou, C.E.3    Kamoun, M.4    Band, H.5    Bierer, B.E.6
  • 81
    • 0037291960 scopus 로고    scopus 로고
    • Structural basis for specific binding of the Gads SH3 domain to an RxxK motif-containing SLP-76 peptide: A novel mode of peptide recognition
    • Liu Q, Berry D, Nash P, Pawson T, McGlade CJ, Li SS (2003) Structural basis for specific binding of the Gads SH3 domain to an RxxK motif-containing SLP-76 peptide: a novel mode of peptide recognition. Mol Cell 11:471-481
    • (2003) Mol Cell , vol.11 , pp. 471-481
    • Liu, Q.1    Berry, D.2    Nash, P.3    Pawson, T.4    McGlade, C.J.5    Li, S.S.6
  • 82
    • 33750905676 scopus 로고    scopus 로고
    • Hydrazone-and hydrazide-containing N-substituted glycines as peptoid surrogates for expedited library synthesis application to the preparation of Tsg101-directed HIV-1 budding antagonists
    • Liu F, Stephen AG, Adamson CS, Gousset K, Aman MJ, Freed EO, Fisher RJ, Burke TR, Jr. (2006) Hydrazone-and hydrazide-containing N-substituted glycines as peptoid surrogates for expedited library synthesis: application to the preparation of Tsg101-directed HIV-1 budding antagonists. Org Lett 8:5165-5168
    • (2006) Org Lett , vol.8 , pp. 5165-5168
    • Liu, F.1    Stephen, A.G.2    Adamson, C.S.3    Gousset, K.4    Aman, M.J.5    Freed, E.O.6    Fisher, R.J.7    Burke Jr., T.R.8
  • 83
    • 0040017910 scopus 로고    scopus 로고
    • Function of WW domains as phosphoserine-or phosphothreonine-binding modules
    • Lu PJ, Zhou XZ, Shen M, Lu KP (1999) Function of WW domains as phosphoserine-or phosphothreonine-binding modules. Science 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
  • 85
    • 0029775570 scopus 로고    scopus 로고
    • Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide
    • Macias MJ, Hyvonen M, Baraldi E, Schultz J, Sudol M, Saraste M, Oschkinat H (1996) Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide. Nature 382:646-649
    • (1996) Nature , vol.382 , pp. 646-649
    • Macias, M.J.1    Hyvonen, M.2    Baraldi, E.3    Schultz, J.4    Sudol, M.5    Saraste, M.6    Oschkinat, H.7
  • 86
    • 0035030510 scopus 로고    scopus 로고
    • SH3 domains: Complexity in moderation
    • Mayer BJ (2001) SH3 domains: complexity in moderation. J Cell Sci 114:1253-1263
    • (2001) J Cell Sci , vol.114 , pp. 1253-1263
    • Mayer, B.J.1
  • 87
    • 1842500992 scopus 로고    scopus 로고
    • Polyproline II helix is the preferred conformation for unfolded polyalanine in water
    • Mezei M, Fleming PJ, Srinivasan R, Rose GD (2004) Polyproline II helix is the preferred conformation for unfolded polyalanine in water. Proteins 55:502-507
    • (2004) Proteins , vol.55 , pp. 502-507
    • Mezei, M.1    Fleming, P.J.2    Srinivasan, R.3    Rose, G.D.4
  • 88
    • 0031766401 scopus 로고    scopus 로고
    • HOMSTRAD: A database of protein structure alignments for homologous families
    • Mizuguchi K, Deane CM, Blundell TL, Overington JP (1998) HOMSTRAD: a database of protein structure alignments for homologous families. Protein Sci 7:2469-2471
    • (1998) Protein Sci , vol.7 , pp. 2469-2471
    • Mizuguchi, K.1    Deane, C.M.2    Blundell, T.L.3    Overington, J.P.4
  • 89
    • 0037467384 scopus 로고    scopus 로고
    • Miniature homeodomains: High specificity without an N-terminal arm
    • Montclare JK, Schepartz A (2003) Miniature homeodomains: high specificity without an N-terminal arm. J Am Chem Soc 125:3416-3417
    • (2003) J Am Chem Soc , vol.125 , pp. 3416-3417
    • Montclare, J.K.1    Schepartz, A.2
  • 91
    • 0028485085 scopus 로고
    • High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides
    • Musacchio A, Saraste M, Wilmanns M (1994a) High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides. Nat Struct Biol 1:546-551
    • (1994) Nat Struct Biol , vol.1 , pp. 546-551
    • Musacchio, A.1    Saraste, M.2    Wilmanns, M.3
  • 93
    • 0033555648 scopus 로고    scopus 로고
    • Identification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylase
    • Myllyharju J, Kivirikko KI (1999) Identification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylase. EMBO J 18:306-312
    • (1999) EMBO J , vol.18 , pp. 306-312
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 95
    • 0032509175 scopus 로고    scopus 로고
    • Exploiting the basis of proline recognition by SH3 and WW domains: Design of N-substituted inhibitors
    • Nguyen JT, Turck CW, Cohen FE, Zuckermann RN, Lim WA (1998) Exploiting the basis of proline recognition by SH3 and WW domains: design of N-substituted inhibitors. Science 282:2088-2092
    • (1998) Science , vol.282 , pp. 2088-2092
    • Nguyen, J.T.1    Turck, C.W.2    Cohen, F.E.3    Zuckermann, R.N.4    Lim, W.A.5
  • 97
    • 0035824391 scopus 로고    scopus 로고
    • Gamma-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase
    • Ni CY, Murphy MP, Golde TE, Carpenter G (2001) gamma-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase. Science 294:2179-2181
    • (2001) Science , vol.294 , pp. 2179-2181
    • Ni, C.Y.1    Murphy, M.P.2    Golde, T.E.3    Carpenter, G.4
  • 98
    • 0030864520 scopus 로고    scopus 로고
    • A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family
    • Niebuhr K, Ebel F, Frank R, Reinhard M, Domann E, Carl UD, Walter U, Gertler FB, Wehland J, Chakraborty T (1997) A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family. EMBO J 16:5433-5444
    • (1997) EMBO J , vol.16 , pp. 5433-5444
    • Niebuhr, K.1    Ebel, F.2    Frank, R.3    Reinhard, M.4    Domann, E.5    Carl, U.D.6    Walter, U.7    Gertler, F.B.8    Wehland, J.9    Chakraborty, T.10
  • 99
    • 34248581189 scopus 로고    scopus 로고
    • Structural basis for the bifunctionality of the U5 snRNP 52 K protein (CD2BP2)
    • Nielsen TK, Liu S, Luhrmann R, Ficner R (2007) Structural basis for the bifunctionality of the U5 snRNP 52 K protein (CD2BP2). J Mol Biol 369:902-908
    • (2007) J Mol Biol , vol.369 , pp. 902-908
    • Nielsen, T.K.1    Liu, S.2    Luhrmann, R.3    Ficner, R.4
  • 100
    • 17644365140 scopus 로고    scopus 로고
    • Different effects of 4-hydroxyproline and 4-fluoroproline on the stability of collagen triple helix
    • Nishi Y, Uchiyama S, Doi M, Nishiuchi Y, Nakazawa T, Ohkubo T, Kobayashi Y (2005) Different effects of 4-hydroxyproline and 4-fluoroproline on the stability of collagen triple helix. Biochemistry 44:6034-6042
    • (2005) Biochemistry , vol.44 , pp. 6034-6042
    • Nishi, Y.1    Uchiyama, S.2    Doi, M.3    Nishiuchi, Y.4    Nakazawa, T.5    Ohkubo, T.6    Kobayashi, Y.7
  • 101
    • 0032441151 scopus 로고    scopus 로고
    • Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation
    • Nishizawa K, Freund C, Li J, Wagner G, Reinherz EL (1998) Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation. Proc Natl Acad Sci USA 95:14897-14902
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14897-14902
    • Nishizawa, K.1    Freund, C.2    Li, J.3    Wagner, G.4    Reinherz, E.L.5
  • 102
    • 0032516873 scopus 로고    scopus 로고
    • Grb2 forms an inducible protein complex with CD28 through a Src homology 3 domain-proline interaction
    • Okkenhaug K, Rottapel R (1998) Grb2 forms an inducible protein complex with CD28 through a Src homology 3 domain-proline interaction. J Biol Chem 273:21194-21202
    • (1998) J Biol Chem , vol.273 , pp. 21194-21202
    • Okkenhaug, K.1    Rottapel, R.2
  • 104
    • 0037150229 scopus 로고    scopus 로고
    • UCS15A, a novel small molecule, SH3 domain-mediated protein-protein interaction blocking drug
    • Oneyama C, Nakano H, Sharma SV (2002) UCS15A, a novel small molecule, SH3 domain-mediated protein-protein interaction blocking drug. Oncogene 21:2037-2050
    • (2002) Oncogene , vol.21 , pp. 2037-2050
    • Oneyama, C.1    Nakano, H.2    Sharma, S.V.3
  • 106
    • 0037223126 scopus 로고    scopus 로고
    • Dynamin at the actin-membrane interface
    • Orth JD, McNiven MA (2003) Dynamin at the actin-membrane interface. Curr Opin Cell Biol 15:31-39
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 31-39
    • Orth, J.D.1    McNiven, M.A.2
  • 108
    • 0036829172 scopus 로고    scopus 로고
    • Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein
    • Pornillos O, Alam SL, Davis DR, Sundquist WI (2002a) Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein. Nat Struct Biol 9:812-817
    • (2002) Nat Struct Biol , vol.9 , pp. 812-817
    • Pornillos, O.1    Alam, S.L.2    Davis, D.R.3    Sundquist, W.I.4
  • 111
    • 0033553508 scopus 로고    scopus 로고
    • Structure of the enabled/VASP homology 1 domain-peptide complex: A key component in the spatial control of actin assembly
    • Prehoda KE, Lee DJ, Lim WA (1999) Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly. Cell 97:471-480
    • (1999) Cell , vol.97 , pp. 471-480
    • Prehoda, K.E.1    Lee, D.J.2    Lim, W.A.3
  • 113
    • 0344984420 scopus 로고    scopus 로고
    • T-cell costimulatory pathways in allograft rejection and tolerance
    • Rothstein DM, Sayegh MH (2003) T-cell costimulatory pathways in allograft rejection and tolerance. Immunol Rev 196:85-108
    • (2003) Immunol Rev , vol.196 , pp. 85-108
    • Rothstein, D.M.1    Sayegh, M.H.2
  • 114
    • 0344443346 scopus 로고    scopus 로고
    • Molecular recognition of protein surfaces: High affinity ligands for the CBP KIX domain
    • Rutledge SE, Volkman HM, Schepartz A (2003) Molecular recognition of protein surfaces: high affinity ligands for the CBP KIX domain. J Am Chem Soc 125:14336-14347
    • (2003) J Am Chem Soc , vol.125 , pp. 14336-14347
    • Rutledge, S.E.1    Volkman, H.M.2    Schepartz, A.3
  • 116
    • 0030761367 scopus 로고    scopus 로고
    • The role of the PH domain and SH3 binding domains in dynamin function
    • Scaife RM, Margolis RL (1997) The role of the PH domain and SH3 binding domains in dynamin function. Cell Signal 9:395-401
    • (1997) Cell Signal , vol.9 , pp. 395-401
    • Scaife, R.M.1    Margolis, R.L.2
  • 117
    • 0029948974 scopus 로고    scopus 로고
    • Identification of a PY motif in the epithelial Na channel subunits as a target sequence for mutations causing channel activation found in Liddle syndrome
    • Schild L, Lu Y, Gautschi I, Schneeberger E, Lifton RP, Rossier BC (1996) Identification of a PY motif in the epithelial Na channel subunits as a target sequence for mutations causing channel activation found in Liddle syndrome. EMBO J 15:2381-2387
    • (1996) EMBO J , vol.15 , pp. 2381-2387
    • Schild, L.1    Lu, Y.2    Gautschi, I.3    Schneeberger, E.4    Lifton, R.P.5    Rossier, B.C.6
  • 120
    • 0028276812 scopus 로고
    • Arrest of Listeria movement in host cells by a bacterial ActA analogue: Implications for actin-based motility
    • Southwick FS, Purich DL (1994) Arrest of Listeria movement in host cells by a bacterial ActA analogue: implications for actin-based motility. Proc Natl Acad Sci USA 91:5168-5172
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5168-5172
    • Southwick, F.S.1    Purich, D.L.2
  • 121
    • 0032811196 scopus 로고    scopus 로고
    • Molecular dynamics simulations of polypeptide conformations in water: A comparison of alpha, beta, and poly(pro)II conformations
    • Sreerama N, Woody RW (1999) Molecular dynamics simulations of polypeptide conformations in water: A comparison of alpha, beta, and poly(pro)II conformations. Proteins 36:400-406
    • (1999) Proteins , vol.36 , pp. 400-406
    • Sreerama, N.1    Woody, R.W.2
  • 123
    • 0029874436 scopus 로고    scopus 로고
    • WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle's syndrome
    • Staub O, Dho S, Henry P, Correa J, Ishikawa T, McGlade J, Rotin D (1996) WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle's syndrome. EMBO J 15:2371-2380
    • (1996) EMBO J , vol.15 , pp. 2371-2380
    • Staub, O.1    Dho, S.2    Henry, P.3    Correa, J.4    Ishikawa, T.5    McGlade, J.6    Rotin, D.7
  • 124
    • 0030424581 scopus 로고    scopus 로고
    • Structure and function of the WW domain
    • Sudol M (1996) Structure and function of the WW domain. Prog Biophys Mol Biol 65:113-132
    • (1996) Prog Biophys Mol Biol , vol.65 , pp. 113-132
    • Sudol, M.1
  • 125
    • 0035895599 scopus 로고    scopus 로고
    • Functions of WW domains in the nucleus
    • Sudol M, Sliwa K, Russo T (2001) Functions of WW domains in the nucleus. FEBS Lett 490:190-195
    • (2001) FEBS Lett , vol.490 , pp. 190-195
    • Sudol, M.1    Sliwa, K.2    Russo, T.3
  • 127
  • 129
    • 0022409564 scopus 로고
    • Poly(L-proline)-binding proteins from chick embryos are a profilin and a profilactin
    • Tanaka M, Shibata H (1985) Poly(L-proline)-binding proteins from chick embryos are a profilin and a profilactin. Eur J Biochem 151:291-297
    • (1985) Eur J Biochem , vol.151 , pp. 291-297
    • Tanaka, M.1    Shibata, H.2
  • 130
    • 0014378447 scopus 로고
    • Circular dichroism of poly-l-proline in an unordered conformation
    • Tiffany ML, Krimm S (1968) Circular dichroism of poly-l-proline in an unordered conformation. Biopolymers 6:1767-1770
    • (1968) Biopolymers , vol.6 , pp. 1767-1770
    • Tiffany, M.L.1    Krimm, S.2
  • 131
    • 0037167028 scopus 로고    scopus 로고
    • An oligomeric ser-pro dipeptide mimetic assuming the polyproline II helix conformation
    • Tremmel P, Geyer A (2002) An oligomeric ser-pro dipeptide mimetic assuming the polyproline II helix conformation. J Am Chem Soc 124:8548-8549
    • (2002) J Am Chem Soc , vol.124 , pp. 8548-8549
    • Tremmel, P.1    Geyer, A.2
  • 132
    • 0035875079 scopus 로고    scopus 로고
    • Molecular insights into polyubiquitin chain assembly: Crystal structure of the Mms2/Ubc13 heterodimer
    • VanDemark AP, Hofmann RM, Tsui C, Pickart CM, Wolberger C (2001) Molecular insights into polyubiquitin chain assembly: crystal structure of the Mms2/Ubc13 heterodimer. Cell 105:711-720
    • (2001) Cell , vol.105 , pp. 711-720
    • Vandemark, A.P.1    Hofmann, R.M.2    Tsui, C.3    Pickart, C.M.4    Wolberger, C.5
  • 135
    • 0035996750 scopus 로고    scopus 로고
    • Probing the phosphopeptide specificities of protein tyrosine phosphatases. SH2 and PTB domains with combinatorial library methods
    • Vetter SW, Zhang ZY (2002) Probing the phosphopeptide specificities of protein tyrosine phosphatases, SH2 and PTB domains with combinatorial library methods. Curr Protein Pept Sci 3:365-397
    • (2002) Curr Protein Pept Sci , vol.3 , pp. 365-397
    • Vetter, S.W.1    Zhang, Z.Y.2
  • 137
    • 0037112347 scopus 로고    scopus 로고
    • Structure of the N-WASP EVH1 domain-WIP complex: Insight into the molecular basis of Wiskott-Aldrich Syndrome
    • Volkman BF, Prehoda KE, Scott JA, Peterson FC, Lim WA (2002) Structure of the N-WASP EVH1 domain-WIP complex: insight into the molecular basis of Wiskott-Aldrich Syndrome. Cell 111:565-576
    • (2002) Cell , vol.111 , pp. 565-576
    • Volkman, B.F.1    Prehoda, K.E.2    Scott, J.A.3    Peterson, F.C.4    Lim, W.A.5
  • 139
    • 34247342216 scopus 로고    scopus 로고
    • The emerging shape of the ESCRT machinery
    • Review
    • Williams RL, Urbé S (2007) The emerging shape of the ESCRT machinery. Nat Rev Mol Cell Biol 8:355-368. Review.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 355-368
    • Williams, R.L.1    Urbé, S.2
  • 141
    • 0032542077 scopus 로고    scopus 로고
    • Design and synthesis of SH3 domain binding ligands: Modifications of the consensus sequence XPpXP
    • Witter DJ, Famiglietti SJ, Cambier JC, Castelhano AL (1998) Design and synthesis of SH3 domain binding ligands: modifications of the consensus sequence XPpXP. Bioorg Med Chem Lett 8:3137-3142
    • (1998) Bioorg Med Chem Lett , vol.8 , pp. 3137-3142
    • Witter, D.J.1    Famiglietti, S.J.2    Cambier, J.C.3    Castelhano, A.L.4
  • 143
    • 0033001789 scopus 로고    scopus 로고
    • Crystal structures of c-Src reveal features of its autoinhibitory mechanism
    • Xu W, Doshi A, Lei M, Eck MJ, Harrison SC (1999) Crystal structures of c-Src reveal features of its autoinhibitory mechanism. Mol Cell 3:629-638
    • (1999) Mol Cell , vol.3 , pp. 629-638
    • Xu, W.1    Doshi, A.2    Lei, M.3    Eck, M.J.4    Harrison, S.C.5
  • 144
  • 146
    • 0346555269 scopus 로고    scopus 로고
    • Optimization of specificity in a cellular protein interaction network by negative selection
    • Zarrinpar A, Park SH, Lim WA (2003b) Optimization of specificity in a cellular protein interaction network by negative selection. Nature 426:676-680
    • (2003) Nature , vol.426 , pp. 676-680
    • Zarrinpar, A.1    Park, S.H.2    Lim, W.A.3
  • 147
    • 0034680311 scopus 로고    scopus 로고
    • Evidence that dim1 associates with proteins involved in pre-mRNA splicing, and delineation of residues essential for dim1 interactions with hnRNP F and Npw38/PQBP-1
    • Zhang Y, Lindblom T, Chang A, Sudol M, Sluder AE, Golemis EA (2000) Evidence that dim1 associates with proteins involved in pre-mRNA splicing, and delineation of residues essential for dim1 interactions with hnRNP F and Npw38/PQBP-1. Gene 257:33-43
    • (2000) Gene , vol.257 , pp. 33-43
    • Zhang, Y.1    Lindblom, T.2    Chang, A.3    Sudol, M.4    Sluder, A.E.5    Golemis, E.A.6
  • 148
    • 0030804315 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome/X-linked thrombocytopenia: WASP gene mutations, protein expression, and phenotype
    • Zhu Q, Watanabe C, Liu T, Hollenbaugh D, Blaese RM, Kanner SB, Aruffo A, Ochs HD (1997) Wiskott-Aldrich syndrome/X-linked thrombocytopenia: WASP gene mutations, protein expression, and phenotype. Blood 90:2680-2689
    • (1997) Blood , vol.90 , pp. 2680-2689
    • Zhu, Q.1    Watanabe, C.2    Liu, T.3    Hollenbaugh, D.4    Blaese, R.M.5    Kanner, S.B.6    Aruffo, A.7    Ochs, H.D.8


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