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Volumn 11, Issue 19, 2012, Pages 3638-3648

Recognition mechanism of p63 by the E3 ligase Itch: Novel strategy in the study and inhibition of this interaction

Author keywords

Cyclization; E3 ubiquitin ligases; HECT; Metal peptide; P53 family; P63; Ubiquitilation

Indexed keywords

PROTEIN P63; PROTEIN P73; UBIQUITIN PROTEIN LIGASE E3; UBIQUITIN PROTEIN LIGASE E3 ITCH; UNCLASSIFIED DRUG;

EID: 84867266706     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.21918     Document Type: Article
Times cited : (40)

References (62)
  • 1
    • 0034296394 scopus 로고    scopus 로고
    • Basic Medical Research Award. The ubiquitin system
    • PMID:11017125
    • Hershko A, Ciechanover A, Varshavsky A. Basic Medical Research Award. The ubiquitin system. Nat Med 2000; 6:1073-81; PMID:11017125; http://dx.doi.org/10. 1038/80384.
    • (2000) Nat Med , vol.6 , pp. 1073-1081
    • Hershko, A.1    Ciechanover, A.2    Varshavsky, A.3
  • 2
    • 83755162631 scopus 로고    scopus 로고
    • HECT-type ubiquitin ligase ITCH targets lysosomal-associated protein multispanning transmembrane 5 (LAPTM5) and prevents LAPTM5-mediated cell death
    • PMID:22009753
    • Ishihara T, Inoue J, Kozaki K, Imoto I, Inazawa J. HECT-type ubiquitin ligase ITCH targets lysosomal-associated protein multispanning transmembrane 5 (LAPTM5) and prevents LAPTM5-mediated cell death. J Biol Chem 2011; 286:44086-94; PMID:22009753; http://dx.doi.org/10.1074/jbc.M111.251694.
    • (2011) J Biol Chem , vol.286 , pp. 44086-44094
    • Ishihara, T.1    Inoue, J.2    Kozaki, K.3    Imoto, I.4    Inazawa, J.5
  • 3
    • 0032524621 scopus 로고    scopus 로고
    • Characterization of human hect domain family members and their interaction with UbcH5 and UbcH7
    • PMID:9575161
    • Schwarz SE, Rosa JL, Scheffner M. Characterization of human hect domain family members and their interaction with UbcH5 and UbcH7. J Biol Chem 1998; 273:12148-54; PMID:9575161; http://dx.doi.org/10.1074/jbc.273.20.12148.
    • (1998) J Biol Chem , vol.273 , pp. 12148-12154
    • Schwarz, S.E.1    Rosa, J.L.2    Scheffner, M.3
  • 4
    • 23344436258 scopus 로고    scopus 로고
    • WW domains provide a platform for the assembly of multiprotein networks
    • PMID:16055720
    • Ingham RJ, Colwill K, Howard C, Dettwiler S, Lim CS, Yu J, et al. WW domains provide a platform for the assembly of multiprotein networks. Mol Cell Biol 2005; 25:7092-106; PMID:16055720; http://dx.doi.org/10.1128/MCB.25.16.7092- 7106.2005.
    • (2005) Mol Cell Biol , vol.25 , pp. 7092-7106
    • Ingham, R.J.1    Colwill, K.2    Howard, C.3    Dettwiler, S.4    Lim, C.S.5    Yu, J.6
  • 5
    • 33749346301 scopus 로고    scopus 로고
    • Modification of proteins by ubiquitin and ubiquitin-like proteins
    • PMID:16753028
    • Kerscher O, Felberbaum R, Hochstrasser M. Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu Rev Cell Dev Biol 2006; 22:159-80; PMID:16753028; http://dx.doi.org/10.1146/annurev.cellbio.22.010605.093503.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 159-180
    • Kerscher, O.1    Felberbaum, R.2    Hochstrasser, M.3
  • 6
    • 0033105864 scopus 로고    scopus 로고
    • Defective regulation of the epithelial Na+ channel by Nedd4 in Liddle's syndrome
    • PMID:10074483
    • Abriel H, Loffing J, Rebhun JF, Pratt JH, Schild L, Horisberger JD, et al. Defective regulation of the epithelial Na+ channel by Nedd4 in Liddle's syndrome. J Clin Invest 1999; 103:667-73; PMID:10074483; http://dx.doi.org/10. 1172/JCI5713.
    • (1999) J Clin Invest , vol.103 , pp. 667-673
    • Abriel, H.1    Loffing, J.2    Rebhun, J.F.3    Pratt, J.H.4    Schild, L.5    Horisberger, J.D.6
  • 7
    • 0033549789 scopus 로고    scopus 로고
    • A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation
    • PMID:10458166
    • Zhu H, Kavsak P, Abdollah S, Wrana JL, Thomsen GH. A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation. Nature 1999; 400:687-93; PMID:10458166; http://dx.doi.org/10.1038/23293.
    • (1999) Nature , vol.400 , pp. 687-693
    • Zhu, H.1    Kavsak, P.2    Abdollah, S.3    Wrana, J.L.4    Thomsen, G.H.5
  • 8
    • 0034517389 scopus 로고    scopus 로고
    • Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation
    • PMID:11163210
    • Kavsak P, Rasmussen RK, Causing CG, Bonni S, Zhu H, Thomsen GH, et al. Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation. Mol Cell 2000; 6:1365-75; PMID:11163210; http://dx.doi.org/10.1016/S1097-2765(00)00134-9.
    • (2000) Mol Cell , vol.6 , pp. 1365-1375
    • Kavsak, P.1    Rasmussen, R.K.2    Causing, C.G.3    Bonni, S.4    Zhu, H.5    Thomsen, G.H.6
  • 9
    • 0038388266 scopus 로고    scopus 로고
    • The role of Nedd4/Nedd4-like dependant ubiquitylation in epithelial transport processes
    • PMID:12698368
    • Flores SY, Debonneville C, Staub O. The role of Nedd4/Nedd4-like dependant ubiquitylation in epithelial transport processes. Pflugers Arch 2003; 446:334-8; PMID:12698368.
    • (2003) Pflugers Arch , vol.446 , pp. 334-338
    • Flores, S.Y.1    Debonneville, C.2    Staub, O.3
  • 10
    • 4444223733 scopus 로고    scopus 로고
    • Itch E3 ligase-mediated regulation of TGF-beta signaling by modulating smad2 phosphorylation
    • PMID:15350225
    • Bai Y, Yang C, Hu K, Elly C, Liu YC. Itch E3 ligase-mediated regulation of TGF-beta signaling by modulating smad2 phosphorylation. Mol Cell 2004; 15:825-31; PMID:15350225; http://dx.doi.org/10.1016/j.molcel.2004.07.021.
    • (2004) Mol Cell , vol.15 , pp. 825-831
    • Bai, Y.1    Yang, C.2    Hu, K.3    Elly, C.4    Liu, Y.C.5
  • 11
    • 35748950163 scopus 로고    scopus 로고
    • Damage-induced ubiquitylation of human RNA polymerase II by the ubiquitin ligase Nedd4, but not Cockayne syndrome proteins or BRCA1
    • PMID:17996703
    • Anindya R, Aygün O, Svejstrup JQ. Damage-induced ubiquitylation of human RNA polymerase II by the ubiquitin ligase Nedd4, but not Cockayne syndrome proteins or BRCA1. Mol Cell 2007; 28:386-97; PMID:17996703; http://dx.doi.org/10.1016/j.molcel.2007.10.008.
    • (2007) Mol Cell , vol.28 , pp. 386-397
    • Anindya, R.1    Aygün, O.2    Svejstrup, J.Q.3
  • 12
    • 34249293370 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase Itch in T cell activation, differentiation, and tolerance
    • PMID:17433711
    • Liu YC. The E3 ubiquitin ligase Itch in T cell activation, differentiation, and tolerance. Semin Immunol 2007; 19:197-205; PMID:17433711; http://dx.doi.org/10.1016/j.smim.2007.02.003.
    • (2007) Semin Immunol , vol.19 , pp. 197-205
    • Liu, Y.C.1
  • 13
    • 45849153870 scopus 로고    scopus 로고
    • The HECT family of E3 ubiquitin ligases: Multiple players in cancer development
    • PMID:18598940
    • Bernassola F, Karin M, Ciechanover A, Melino G. The HECT family of E3 ubiquitin ligases: multiple players in cancer development. Cancer Cell 2008; 14:10-21; PMID:18598940; http://dx.doi.org/10.1016/j.ccr.2008.06.001.
    • (2008) Cancer Cell , vol.14 , pp. 10-21
    • Bernassola, F.1    Karin, M.2    Ciechanover, A.3    Melino, G.4
  • 14
    • 45449094801 scopus 로고    scopus 로고
    • Itch: A HECT-type E3 ligase regulating immunity, skin and cancer
    • PMID:18552861
    • Melino G, Gallagher E, Aqeilan RI, Knight R, Peschiaroli A, Rossi M, et al. Itch: a HECT-type E3 ligase regulating immunity, skin and cancer. Cell Death Differ 2008; 15:1103-12; PMID:18552861; http://dx.doi.org/10.1038/cdd.2008.60.
    • (2008) Cell Death Differ , vol.15 , pp. 1103-1112
    • Melino, G.1    Gallagher, E.2    Aqeilan, R.I.3    Knight, R.4    Peschiaroli, A.5    Rossi, M.6
  • 15
    • 51149088572 scopus 로고    scopus 로고
    • Itchy mice: The identification of a new pathway for the development of autoimmunity
    • PMID:18727493
    • Matesic LE, Copeland NG, Jenkins NA. Itchy mice: the identification of a new pathway for the development of autoimmunity. Curr Top Microbiol Immunol 2008; 321:185-200; PMID:18727493; http://dx.doi.org/10.1007/978-3-540-75203-5-9.
    • (2008) Curr Top Microbiol Immunol , vol.321 , pp. 185-200
    • Matesic, L.E.1    Copeland, N.G.2    Jenkins, N.A.3
  • 16
    • 16344375852 scopus 로고    scopus 로고
    • Ubiquitylation of a melanosomal protein by HECT-E3 ligases serves as sorting signal for lysosomal degradation
    • PMID:15703212
    • Lévy F, Muehlethaler K, Salvi S, Peitrequin AL, Lindholm CK, Cerottini JC, et al. Ubiquitylation of a melanosomal protein by HECT-E3 ligases serves as sorting signal for lysosomal degradation. Mol Biol Cell 2005; 16:1777-87; PMID:15703212; http://dx.doi.org/10.1091/mbc.E04-09-0803.
    • (2005) Mol Biol Cell , vol.16 , pp. 1777-1787
    • Lévy, F.1    Muehlethaler, K.2    Salvi, S.3    Peitrequin, A.L.4    Lindholm, C.K.5    Cerottini, J.C.6
  • 17
    • 41949128060 scopus 로고    scopus 로고
    • Isoform-specific monoubiquitination, endocytosis, and degradation of alternatively spliced ErbB4 isoforms
    • PMID:18334649
    • Sundvall M, Korhonen A, Paatero I, Gaudio E, Melino G, Croce CM, et al. Isoform-specific monoubiquitination, endocytosis, and degradation of alternatively spliced ErbB4 isoforms. Proc Natl Acad Sci USA 2008; 105:4162-7; PMID:18334649; http://dx.doi.org/10.1073/pnas.0708333105.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 4162-4167
    • Sundvall, M.1    Korhonen, A.2    Paatero, I.3    Gaudio, E.4    Melino, G.5    Croce, C.M.6
  • 18
    • 0242362743 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase AIP4 mediates ubiquitination and sorting of the G protein-coupled receptor CXCR4
    • PMID:14602072
    • Marchese A, Raiborg C, Santini F, Keen JH, Stenmark H, Benovic JL. The E3 ubiquitin ligase AIP4 mediates ubiquitination and sorting of the G protein-coupled receptor CXCR4. Dev Cell 2003; 5:709-22; PMID:14602072; http://dx.doi.org/10.1016/S1534-5807(03)00321-6.
    • (2003) Dev Cell , vol.5 , pp. 709-722
    • Marchese, A.1    Raiborg, C.2    Santini, F.3    Keen, J.H.4    Stenmark, H.5    Benovic, J.L.6
  • 19
    • 77950580572 scopus 로고    scopus 로고
    • The ubiquitin ligase itch regulates apoptosis by targeting thioredoxin-interacting protein for ubiquitin-dependent degradation
    • PMID:20068034
    • Zhang P, Wang C, Gao K, Wang D, Mao J, An J, et al. The ubiquitin ligase itch regulates apoptosis by targeting thioredoxin-interacting protein for ubiquitin-dependent degradation. J Biol Chem 2010; 285:8869-79; PMID:20068034; http://dx.doi.org/10.1074/jbc.M109.063321.
    • (2010) J Biol Chem , vol.285 , pp. 8869-8879
    • Zhang, P.1    Wang, C.2    Gao, K.3    Wang, D.4    Mao, J.5    An, J.6
  • 20
    • 54949108684 scopus 로고    scopus 로고
    • ITCH is a putative target for a novel 20q11.22 amplification detected in anaplastic thyroid carcinoma cells by array-based comparative genomic hybridization
    • PMID:19016753
    • Ishihara T, Tsuda H, Hotta A, Kozaki K, Yoshida A, Noh JY, et al. ITCH is a putative target for a novel 20q11.22 amplification detected in anaplastic thyroid carcinoma cells by array-based comparative genomic hybridization. Cancer Sci 2008; 99:1940-9; PMID:19016753.
    • (2008) Cancer Sci , vol.99 , pp. 1940-1949
    • Ishihara, T.1    Tsuda, H.2    Hotta, A.3    Kozaki, K.4    Yoshida, A.5    Noh, J.Y.6
  • 21
    • 79953204984 scopus 로고    scopus 로고
    • Itch E3 ubiquitin ligase regulates large tumor suppressor 1 stability
    • corrected. PMID:21383157
    • Ho KC, Zhou Z, She YM, Chun A, Cyr TD, Yang X. Itch E3 ubiquitin ligase regulates large tumor suppressor 1 stability [corrected]. Proc Natl Acad Sci U S A 2011; 108:4870-5; PMID:21383157; http://dx.doi.org/10.1073/pnas.1101273108.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 4870-4875
    • Ho, K.C.1    Zhou, Z.2    She, Y.M.3    Chun, A.4    Cyr, T.D.5    Yang, X.6
  • 22
    • 80051789515 scopus 로고    scopus 로고
    • p63 is a suppressor of tumorigenesis and metastasis interacting with mutant p53
    • PMID:21760596
    • Melino G. p63 is a suppressor of tumorigenesis and metastasis interacting with mutant p53. Cell Death Differ 2011; 18:1487-99; PMID:21760596; http://dx.doi.org/10.1038/cdd.2011.81.
    • (2011) Cell Death Differ , vol.18 , pp. 1487-1499
    • Melino, G.1
  • 23
  • 24
    • 0031915677 scopus 로고    scopus 로고
    • The itchy locus encodes a novel ubiquitin protein ligase that is disrupted in a18H mice
    • PMID:9462742
    • Perry WL, Hustad CM, Swing DA, O'Sullivan TN, Jenkins NA, Copeland NG. The itchy locus encodes a novel ubiquitin protein ligase that is disrupted in a18H mice. Nat Genet 1998; 18:143-6; PMID:9462742; http://dx.doi.org/10.1038/ ng0298-143.
    • (1998) Nat Genet , vol.18 , pp. 143-146
    • Perry, W.L.1    Hustad, C.M.2    Swing, D.A.3    O'Sullivan, T.N.4    Jenkins, N.A.5    Copeland, N.G.6
  • 25
    • 0037138411 scopus 로고    scopus 로고
    • WW and SH3 domains, two different scaffolds to recognize proline-rich ligands
    • PMID:11911877
    • Macias MJ, Wiesner S, Sudol M. WW and SH3 domains, two different scaffolds to recognize proline-rich ligands. FEBS Lett 2002; 513:30-7; PMID:11911877; http://dx.doi.org/10.1016/S0014-5793(01)03290-2.
    • (2002) FEBS Lett , vol.513 , pp. 30-37
    • Macias, M.J.1    Wiesner, S.2    Sudol, M.3
  • 26
    • 0033900164 scopus 로고    scopus 로고
    • Converging on proline: The mechanism of WW domain peptide recognition
    • PMID:10932238
    • Zarrinpar A, Lim WA. Converging on proline: the mechanism of WW domain peptide recognition. Nat Struct Biol 2000; 7:611-3; PMID:10932238; http://dx.doi.org/10.1038/77891.
    • (2000) Nat Struct Biol , vol.7 , pp. 611-613
    • Zarrinpar, A.1    Lim, W.A.2
  • 27
    • 0034704216 scopus 로고    scopus 로고
    • NeW wrinkles for an old domain
    • PMID:11163176
    • Sudol M, Hunter T. NeW wrinkles for an old domain. Cell 2000; 103:1001-4; PMID:11163176; http://dx.doi.org/10.1016/S0092-8674(00)00203-8.
    • (2000) Cell , vol.103 , pp. 1001-1004
    • Sudol, M.1    Hunter, T.2
  • 28
    • 15444367709 scopus 로고    scopus 로고
    • The ubiquitin-protein ligase Itch regulates p73 stability
    • PMID:15678106
    • Rossi M, De Laurenzi V, Munarriz E, Green DR, Liu YC, Vousden KH, et al. The ubiquitin-protein ligase Itch regulates p73 stability. EMBO J 2005; 24:836-48; PMID:15678106; http://dx.doi.org/10.1038/sj.emboj.7600444.
    • (2005) EMBO J , vol.24 , pp. 836-848
    • Rossi, M.1    De Laurenzi, V.2    Munarriz, E.3    Green, D.R.4    Liu, Y.C.5    Vousden, K.H.6
  • 29
    • 33748585368 scopus 로고    scopus 로고
    • Itch/AIP4 associates with and promotes p63 protein degradation
    • PMID:16861923
    • Rossi M, De Simone M, Pollice A, Santoro R, La Mantia G, Guerrini L, et al. Itch/AIP4 associates with and promotes p63 protein degradation. Cell Cycle 2006; 5:1816-22; PMID:16861923; http://dx.doi.org/10.4161/cc.5.16.2861.
    • (2006) Cell Cycle , vol.5 , pp. 1816-1822
    • Rossi, M.1    De Simone, M.2    Pollice, A.3    Santoro, R.4    La Mantia, G.5    Guerrini, L.6
  • 30
    • 77957006621 scopus 로고    scopus 로고
    • Recognition of p63 by the E3 ligase ITCH: Effect of an ectodermal dysplasia mutant
    • PMID:20855944
    • Bellomaria A, Barbato G, Melino G, Paci M, Melino S. Recognition of p63 by the E3 ligase ITCH: Effect of an ectodermal dysplasia mutant. Cell Cycle 2010; 9:3730-9; PMID:20855944; http://dx.doi.org/10.4161/cc.9.18.12933.
    • (2010) Cell Cycle , vol.9 , pp. 3730-3739
    • Bellomaria, A.1    Barbato, G.2    Melino, G.3    Paci, M.4    Melino, S.5
  • 31
    • 0026158667 scopus 로고
    • An efficient 3D NMR technique for correlating the proton and 15N backbone amide resonances with the alpha-carbon of the preceding residue in uniformly 15N/13C enriched proteins
    • PMID:1668719
    • Bax A, Ikura M. An efficient 3D NMR technique for correlating the proton and 15N backbone amide resonances with the alpha-carbon of the preceding residue in uniformly 15N/13C enriched proteins. J Biomol NMR 1991; 1:99-104; PMID:1668719; http://dx.doi.org/10.1007/BF01874573.
    • (1991) J Biomol NMR , vol.1 , pp. 99-104
    • Bax, A.1    Ikura, M.2
  • 32
    • 0026275542 scopus 로고
    • Multidimensional triple resonance NMR spectroscopy of isotopically uniformly enriched proteins: A powerful new strategy for structure determination
    • discussion 119-35; PMID:1814691
    • Bax A, Ikura M, Kay LE, Barbato G, Spera S. Multidimensional triple resonance NMR spectroscopy of isotopically uniformly enriched proteins: a powerful new strategy for structure determination. Ciba Found Symp 1991; 161:108-19, discussion 119-35; PMID:1814691.
    • (1991) Ciba Found Symp , vol.161 , pp. 108-119
    • Bax, A.1    Ikura, M.2    Kay, L.E.3    Barbato, G.4    Spera, S.5
  • 33
    • 0028393784 scopus 로고
    • The 13C chemical-shift index: A simple method for the identification of protein secondary structure using 13C chemical-shift data
    • PMID:8019132
    • Wishart DS, Sykes BD. The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 1994; 4:171-80; PMID:8019132; http://dx.doi.org/10.1007/ BF00175245.
    • (1994) J Biomol NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 34
    • 0034699496 scopus 로고    scopus 로고
    • Synthesis, stability, antiviral activity, and protease-bound structures of substrate-mimicking constrained macrocyclic inhibitors of HIV-1 protease
    • PMID:11000004
    • Tyndall JD, Reid RC, Tyssen DP, Jardine DK, Todd B, Passmore M, et al. Synthesis, stability, antiviral activity, and protease-bound structures of substrate-mimicking constrained macrocyclic inhibitors of HIV-1 protease. J Med Chem 2000; 43:3495-504; PMID:11000004; http://dx.doi.org/10.1021/jm000013n.
    • (2000) J Med Chem , vol.43 , pp. 3495-3504
    • Tyndall, J.D.1    Reid, R.C.2    Tyssen, D.P.3    Jardine, D.K.4    Todd, B.5    Passmore, M.6
  • 35
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • PMID:13650640
    • Ellman GL. Tissue sulfhydryl groups. Arch Biochem Biophys 1959; 82:70-7; PMID:13650640; http://dx.doi.org/10.1016/0003-9861(59)90090-6.
    • (1959) Arch Biochem Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 36
    • 0020695584 scopus 로고
    • Reassessment of Ellman's reagent
    • PMID:6855597
    • Riddles PW, Blakeley RL, Zerner B. Reassessment of Ellman's reagent. Methods Enzymol 1983; 91:49-60; PMID:6855597; http://dx.doi.org/10.1016/S0076- 6879(83)91010-8.
    • (1983) Methods Enzymol , vol.91 , pp. 49-60
    • Riddles, P.W.1    Blakeley, R.L.2    Zerner, B.3
  • 37
    • 0343320717 scopus 로고
    • Coordinating properties of the amide bond: Stability and structure of metal ion complexes of peptides and related ligands
    • Sigel H, Martin RB. Coordinating properties of the amide bond: Stability and structure of metal ion complexes of peptides and related ligands. Chem Rev 1982; 82:385-426; http://dx.doi.org/10.1021/cr00050a003.
    • (1982) Chem Rev , vol.82 , pp. 385-426
    • Sigel, H.1    Martin, R.B.2
  • 38
    • 0021755638 scopus 로고
    • Characterization of the copper(II)- and nickel(II)-transport site of human serum albumin. Studies of copper(II) and nickel(II) binding to peptide 1-24 of human serum albumin by 13C and 1H NMR spectroscopy
    • PMID:6547847
    • Laussac JP, Sarkar B. Characterization of the copper(II)- and nickel(II)-transport site of human serum albumin. Studies of copper(II) and nickel(II) binding to peptide 1-24 of human serum albumin by 13C and 1H NMR spectroscopy. Biochemistry 1984; 23:2832-8; PMID:6547847; http://dx.doi.org/10. 1021/bi00307a046.
    • (1984) Biochemistry , vol.23 , pp. 2832-2838
    • Laussac, J.P.1    Sarkar, B.2
  • 39
    • 0025674536 scopus 로고
    • Metal ion-catalyzed oxidation of proteins: Biochemical mechanism and biological consequences
    • PMID:2283087
    • Stadtman ER. Metal ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences. Free Radic Biol Med 1990; 9:315-25; PMID:2283087; http://dx.doi.org/10.1016/0891-5849(90)90006-5.
    • (1990) Free Radic Biol Med , vol.9 , pp. 315-325
    • Stadtman, E.R.1
  • 40
    • 75349103046 scopus 로고    scopus 로고
    • Reticulon RTN1-C(CT) peptide: A potential nuclease and inhibitor of histone deacetylase enzymes
    • PMID:20000484
    • Nepravishta R, Bellomaria A, Polizio F, Paci M, Melino S. Reticulon RTN1-C(CT) peptide: a potential nuclease and inhibitor of histone deacetylase enzymes. Biochemistry 2010; 49:252-8; PMID:20000484; http://dx.doi.org/10.1021/ bi9012676.
    • (2010) Biochemistry , vol.49 , pp. 252-258
    • Nepravishta, R.1    Bellomaria, A.2    Polizio, F.3    Paci, M.4    Melino, S.5
  • 41
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • PMID:8352601
    • Stadtman ER. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu Rev Biochem 1993; 62:797-821; PMID:8352601; http://dx.doi.org/10.1146/annurev.bi.62.070193.004053.
    • (1993) Annu Rev Biochem , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 42
    • 0029775570 scopus 로고    scopus 로고
    • Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide
    • PMID:8757138
    • Macias MJ, Hyvönen M, Baraldi E, Schultz J, Sudol M, Saraste M, et al. Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide. Nature 1996; 382:646-9; PMID:8757138; http://dx.doi.org/ 10.1038/382646a0.
    • (1996) Nature , vol.382 , pp. 646-649
    • Macias, M.J.1    Hyvönen, M.2    Baraldi, E.3    Schultz, J.4    Sudol, M.5    Saraste, M.6
  • 43
    • 0035861991 scopus 로고    scopus 로고
    • Solution structures of the YAP65 WW domain and the variant L30 K in complex with the peptides GTPPPPYTVG, N-(n-octyl)- GPPPY and PLPPY and the application of peptide libraries reveal a minimal binding epitope
    • PMID:11743730
    • Pires JR, Taha-Nejad F, Toepert F, Ast T, Hoffmüller U, Schneider-Mergener J, et al. Solution structures of the YAP65 WW domain and the variant L30 K in complex with the peptides GTPPPPYTVG, N-(n-octyl)- GPPPY and PLPPY and the application of peptide libraries reveal a minimal binding epitope. J Mol Biol 2001; 314:1147-56; PMID:11743730; http://dx.doi.org/10.1006/jmbi. 2000.5199.
    • (2001) J Mol Biol , vol.314 , pp. 1147-1156
    • Pires, J.R.1    Taha-Nejad, F.2    Toepert, F.3    Ast, T.4    Hoffmüller, U.5    Schneider-Mergener, J.6
  • 44
    • 0343081091 scopus 로고    scopus 로고
    • Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan
    • PMID:10932245
    • Huang X, Poy F, Zhang R, Joachimiak A, Sudol M, Eck MJ. Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan. Nat Struct Biol 2000; 7:634-8; PMID:10932245; http://dx.doi.org/10.1038/77923.
    • (2000) Nat Struct Biol , vol.7 , pp. 634-638
    • Huang, X.1    Poy, F.2    Zhang, R.3    Joachimiak, A.4    Sudol, M.5    Eck, M.J.6
  • 45
    • 0035027506 scopus 로고    scopus 로고
    • Solution structure of a Nedd4 WW domain-ENaC peptide complex
    • PMID:11323714
    • Kanelis V, Rotin D, Forman-Kay JD. Solution structure of a Nedd4 WW domain-ENaC peptide complex. Nat Struct Biol 2001; 8:407-12; PMID:11323714; http://dx.doi.org/10.1038/87562.
    • (2001) Nat Struct Biol , vol.8 , pp. 407-412
    • Kanelis, V.1    Rotin, D.2    Forman-Kay, J.D.3
  • 46
    • 80155206873 scopus 로고    scopus 로고
    • Biophysical analysis of binding of WW domains of the YAP2 transcriptional regulator to PPXY motifs within WBP1 and WBP2 adaptors
    • PMID:21981024
    • McDonald CB, McIntosh SK, Mikles DC, Bhat V, Deegan BJ, Seldeen KL, et al. Biophysical analysis of binding of WW domains of the YAP2 transcriptional regulator to PPXY motifs within WBP1 and WBP2 adaptors. Biochemistry 2011; 50:9616-27; PMID:21981024; http://dx.doi.org/10.1021/bi201286p.
    • (2011) Biochemistry , vol.50 , pp. 9616-9627
    • McDonald, C.B.1    McIntosh, S.K.2    Mikles, D.C.3    Bhat, V.4    Deegan, B.J.5    Seldeen, K.L.6
  • 47
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains
    • PMID:10657980
    • Kay BK, Williamson MP, Sudol M. The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J 2000; 14:231-41; PMID:10657980.
    • (2000) FASEB J , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 48
    • 0030851955 scopus 로고    scopus 로고
    • Using molecular repertoires to identify high-affinity peptide ligands of the WW domain of human and mouse YAP
    • PMID:9224934
    • Linn H, Ermekova KS, Rentschler S, Sparks AB, Kay BK, Sudol M. Using molecular repertoires to identify high-affinity peptide ligands of the WW domain of human and mouse YAP. Biol Chem 1997; 378:531-7; PMID:9224934; http://dx.doi.org/10.1515/bchm.1997.378.6.531.
    • (1997) Biol Chem , vol.378 , pp. 531-537
    • Linn, H.1    Ermekova, K.S.2    Rentschler, S.3    Sparks, A.B.4    Kay, B.K.5    Sudol, M.6
  • 49
    • 0034493023 scopus 로고    scopus 로고
    • Evolution of binding affinity in a WW domain probed by phage display
    • PMID:11206058
    • Dalby PA, Hoess RH, DeGrado WF. Evolution of binding affinity in a WW domain probed by phage display. Protein Sci 2000; 9:2366-76; PMID:11206058.
    • (2000) Protein Sci , vol.9 , pp. 2366-2376
    • Dalby, P.A.1    Hoess, R.H.2    DeGrado, W.F.3
  • 50
    • 79955101793 scopus 로고    scopus 로고
    • Structural features and ligand binding properties of tandem WW domains from YAP and TAZ, nuclear effectors of the Hippo pathway
    • PMID:21417403
    • Webb C, Upadhyay A, Giuntini F, Eggleston I, Furutani-Seiki M, Ishima R, et al. Structural features and ligand binding properties of tandem WW domains from YAP and TAZ, nuclear effectors of the Hippo pathway. Biochemistry 2011; 50:3300-9; PMID:21417403; http://dx.doi.org/10.1021/bi2001888.
    • (2011) Biochemistry , vol.50 , pp. 3300-3309
    • Webb, C.1    Upadhyay, A.2    Giuntini, F.3    Eggleston, I.4    Furutani-Seiki, M.5    Ishima, R.6
  • 51
    • 0032539578 scopus 로고    scopus 로고
    • The structural aspects of limited proteolysis of native proteins
    • PMID:9540791
    • Hubbard SJ. The structural aspects of limited proteolysis of native proteins. Biochim Biophys Acta 1998; 1382:191-206; PMID:9540791; http://dx.doi.org/10.1016/S0167-4838(97)00175-1.
    • (1998) Biochim Biophys Acta , vol.1382 , pp. 191-206
    • Hubbard, S.J.1
  • 52
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • PMID:18075579
    • Wells JA, McClendon CL. Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature 2007; 450:1001-9; PMID:18075579; http://dx.doi.org/10.1038/nature06526.
    • (2007) Nature , vol.450 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 53
    • 44949154279 scopus 로고    scopus 로고
    • Small molecular weight protein-protein interaction antagonists: An insurmountable challenge?
    • PMID:18501203
    • Dömling A. Small molecular weight protein-protein interaction antagonists: an insurmountable challenge? Curr Opin Chem Biol 2008; 12:281-91; PMID:18501203; http://dx.doi.org/10.1016/j.cbpa.2008.04.603.
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 281-291
    • Dömling, A.1
  • 54
    • 20444459812 scopus 로고    scopus 로고
    • DNA cleavage by copper-ATCUN complexes. Factors influencing cleavage mechanism and linearization of dsDNA
    • PMID:15941274
    • Jin Y, Cowan JA. DNA cleavage by copper-ATCUN complexes. Factors influencing cleavage mechanism and linearization of dsDNA. J Am Chem Soc 2005; 127:8408-15; PMID:15941274; http://dx.doi.org/10.1021/ja0503985.
    • (2005) J Am Chem Soc , vol.127 , pp. 8408-8415
    • Jin, Y.1    Cowan, J.A.2
  • 55
    • 0032167555 scopus 로고    scopus 로고
    • Selective recognition and cleavage of RNA loop structures by Ni(II).Xaa-Gly-His metallopeptides
    • PMID:9724523
    • Brittain IJ, Huang X, Long EC. Selective recognition and cleavage of RNA loop structures by Ni(II).Xaa-Gly-His metallopeptides. Biochemistry 1998; 37:12113-20; PMID:9724523; http://dx.doi.org/10.1021/bi9806605.
    • (1998) Biochemistry , vol.37 , pp. 12113-12120
    • Brittain, I.J.1    Huang, X.2    Long, E.C.3
  • 56
    • 33845921608 scopus 로고    scopus 로고
    • Metal-binding and nuclease activity of an antimicrobial peptide analogue of the salivary histatin 5
    • PMID:17176059
    • Melino S, Gallo M, Trotta E, Mondello F, Paci M, Petruzzelli R. Metal-binding and nuclease activity of an antimicrobial peptide analogue of the salivary histatin 5. Biochemistry 2006; 45:15373-83; PMID:17176059; http://dx.doi.org/10.1021/bi0615137.
    • (2006) Biochemistry , vol.45 , pp. 15373-15383
    • Melino, S.1    Gallo, M.2    Trotta, E.3    Mondello, F.4    Paci, M.5    Petruzzelli, R.6
  • 57
    • 69749101546 scopus 로고    scopus 로고
    • Metallotherapeutics: Novel strategies in drug design
    • PMID:19685535
    • Hocharoen L, Cowan JA. Metallotherapeutics: novel strategies in drug design. Chemistry 2009; 15:8670-6; PMID:19685535; http://dx.doi.org/10.1002/ chem.200900821.
    • (2009) Chemistry , vol.15 , pp. 8670-8676
    • Hocharoen, L.1    Cowan, J.A.2
  • 58
    • 0034992645 scopus 로고    scopus 로고
    • A method for efficient isotopic labeling of recombinant proteins
    • PMID:11430757
    • Marley J, Lu M, Bracken C. A method for efficient isotopic labeling of recombinant proteins. J Biomol NMR 2001; 20:71-5; PMID:11430757; http://dx.doi.org/10.1023/A:1011254402785.
    • (2001) J Biomol NMR , vol.20 , pp. 71-75
    • Marley, J.1    Lu, M.2    Bracken, C.3
  • 59
    • 0029303455 scopus 로고
    • A new 3D HCACO pulse sequence with optimized resolution and sensitivity. Application to the 21 kDa protein human interleukin-6
    • PMID:7599953
    • Bazzo R, Cicero DO, Barbato G. A new 3D HCACO pulse sequence with optimized resolution and sensitivity. Application to the 21 kDa protein human interleukin-6. J Magn Reson B 1995; 107:189-91; PMID:7599953; http://dx.doi.org/10.1006/jmrb.1995.1077.
    • (1995) J Magn Reson B , vol.107 , pp. 189-191
    • Bazzo, R.1    Cicero, D.O.2    Barbato, G.3
  • 60
    • 0009650222 scopus 로고    scopus 로고
    • A new 3D pulse sequence for correlating intraresidue NH, N and CO chemical shifts in C-13 N-15 labeled proteins. Application to the protein human interleukin 6
    • Bazzo R, Cicero DO, Barbato G. A new 3D pulse sequence for correlating intraresidue NH, N and CO chemical shifts in C-13 N-15 labeled proteins. Application to the protein human interleukin 6. J Magn Reson B 1996; 110:65-8; http://dx.doi.org/10.1006/jmrb.1996.0008.
    • (1996) J Magn Reson B , vol.110 , pp. 65-68
    • Bazzo, R.1    Cicero, D.O.2    Barbato, G.3
  • 61
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • PMID:8520220
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 1995; 6:277-93; PMID:8520220; http://dx.doi.org/10.1007/BF00197809.
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 62
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • PMID:15318002
    • Johnson BA. Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol Biol 2004; 278:313-52; PMID:15318002.
    • (2004) Methods Mol Biol , vol.278 , pp. 313-352
    • Johnson, B.A.1


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