메뉴 건너뛰기




Volumn 5, Issue 5, 2014, Pages

High throughput screening for inhibitors of the HECT ubiquitin E3 ligase ITCH identifies antidepressant drugs as regulators of autophagy

Author keywords

Antidepressant; Autophagy; E3 ligase; HECT; Inhibitors; Ubiquitin

Indexed keywords

ANTIDEPRESSANT AGENT; ANTINEOPLASTIC AGENT; CLOMIPRAMINE; GEMCITABINE; HT 1376; ITCH PROTEIN; LIGASE INHIBITOR; MITOMYCIN; NORCLOMIPRAMINE; PROTEIN P73; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; ENZYME INHIBITOR; UBIQUITIN; UBIQUITIN PROTEIN LIGASE;

EID: 84901048406     PISSN: None     EISSN: 20414889     Source Type: Journal    
DOI: 10.1038/cddis.2014.113     Document Type: Article
Times cited : (109)

References (60)
  • 1
    • 23944474593 scopus 로고    scopus 로고
    • Intracellular protein degradation: From a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting
    • Ciechanover A. Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Cell Death Differ 2005; 12: 1178-1190.
    • (2005) Cell Death Differ , vol.12 , pp. 1178-1190
    • Ciechanover, A.1
  • 2
    • 23944471680 scopus 로고    scopus 로고
    • The ubiquitin system for protein degradation and some of its roles in the control of the cell division cycle
    • Hershko A. The ubiquitin system for protein degradation and some of its roles in the control of the cell division cycle. Cell Death Differ 2005; 12: 1191-1197.
    • (2005) Cell Death Differ , vol.12 , pp. 1191-1197
    • Hershko, A.1
  • 3
    • 23944507555 scopus 로고    scopus 로고
    • Discovery of the ubiquitin proteasome system and its involvement in apoptosis
    • Melino G. Discovery of the ubiquitin proteasome system and its involvement in apoptosis. Cell Death Differ 2005; 12: 1155-1157.
    • (2005) Cell Death Differ , vol.12 , pp. 1155-1157
    • Melino, G.1
  • 4
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover A. The ubiquitin-proteasome proteolytic pathway. Cell 1994; 79: 13-21.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 5
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart CM. Mechanisms underlying ubiquitination. Annu Rev Biochem 2001; 70: 503-533.
    • (2001) Annu Rev Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 6
    • 45849153870 scopus 로고    scopus 로고
    • The HECT family of E3 ubiquitin ligases: Multiple players in cancer development
    • 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.
    • (2008) Cancer Cell , vol.14 , pp. 10-21
    • Bernassola, F.1    Karin, M.2    Ciechanover, A.3    Melino, G.4
  • 7
    • 56149122833 scopus 로고    scopus 로고
    • Modeling and molecular dynamics of the interaction between the E3 ubiquitin ligase Itch and the E2 UbcH7
    • Raimondo D, Giorgetti A, Bernassola F, Melino G, Tramontano A. Modeling and molecular dynamics of the interaction between the E3 ubiquitin ligase Itch and the E2 UbcH7. Biochem Pharmacol 2008; 76: 1620-1627.
    • (2008) Biochem Pharmacol , vol.76 , pp. 1620-1627
    • Raimondo, D.1    Giorgetti, A.2    Bernassola, F.3    Melino, G.4    Tramontano, A.5
  • 14
    • 77957006621 scopus 로고    scopus 로고
    • Recognition of p63 by the E3 ligase ITCH: Effect of an ectodermal dysplasia mutant
    • 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: 3730-3739.
    • (2010) Cell Cycle , vol.9 , pp. 3730-3739
    • Bellomaria, A.1    Barbato, G.2    Melino, G.3    Paci, M.4    Melino, S.5
  • 15
    • 79960336511 scopus 로고    scopus 로고
    • Differential altered stability and transcriptional activity of DeltaNp63 mutants in distinct ectodermal dysplasias
    • Browne G, Cipollone R, Lena AM, Serra V, Zhou H, van Bokhoven H et al. Differential altered stability and transcriptional activity of DeltaNp63 mutants in distinct ectodermal dysplasias. J Cell Sci 2011; 124(Pt 13): 2200-2207.
    • (2011) J Cell Sci , vol.124 , Issue.PART.13 , pp. 2200-2207
    • Browne, G.1    Cipollone, R.2    Lena, A.M.3    Serra, V.4    Zhou, H.5    Van Bokhoven, H.6
  • 16
    • 84867266706 scopus 로고    scopus 로고
    • Recognition mechanism of p63 by the E3 ligase Itch: Novel strategy in the study and inhibition of this interaction
    • Bellomaria A, Barbato G, Melino G, Paci M, Melino S. Recognition mechanism of p63 by the E3 ligase Itch: novel strategy in the study and inhibition of this interaction. Cell Cycle 2012; 11: 3638-3648.
    • (2012) Cell Cycle , vol.11 , pp. 3638-3648
    • Bellomaria, A.1    Barbato, G.2    Melino, G.3    Paci, M.4    Melino, S.5
  • 17
    • 79952266588 scopus 로고    scopus 로고
    • Negative regulation of the Hippo pathway by E3 ubiquitin ligase ITCH is sufficient to promote tumorigenicity
    • Salah Z, Melino G, Aqeilan RI. Negative regulation of the Hippo pathway by E3 ubiquitin ligase ITCH is sufficient to promote tumorigenicity. Cancer Res 2011; 71: 2010-2020.
    • (2011) Cancer Res , vol.71 , pp. 2010-2020
    • Salah, Z.1    Melino, G.2    Aqeilan, R.I.3
  • 18
    • 32044447161 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase itch couples JNK activation to TNFalpha-induced cell death by inducing c-FLIP(L) turnover
    • Chang L, Kamata H, Solinas G, Luo JL, Maeda S, Venuprasad K et al. The E3 ubiquitin ligase itch couples JNK activation to TNFalpha-induced cell death by inducing c-FLIP(L) turnover. Cell 2006; 124: 601-613.
    • (2006) Cell , vol.124 , pp. 601-613
    • Chang, L.1    Kamata, H.2    Solinas, G.3    Luo, J.L.4    Maeda, S.5    Venuprasad, K.6
  • 19
    • 77950580572 scopus 로고    scopus 로고
    • The ubiquitin ligase itch regulates apoptosis by targeting thioredoxin-interacting protein for ubiquitin-dependent degradation
    • 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: 8869-8879.
    • (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
    • 76349086181 scopus 로고    scopus 로고
    • The ubiquitin ligase Itch mediates the antiapoptotic activity of epidermal growth factor by promoting the ubiquitylation and degradation of the truncated C-terminal portion of Bid
    • Azakir BA, Desrochers G, Angers A. The ubiquitin ligase Itch mediates the antiapoptotic activity of epidermal growth factor by promoting the ubiquitylation and degradation of the truncated C-terminal portion of Bid. FEBS J 2010; 277: 1319-1330.
    • (2010) FEBS J , vol.277 , pp. 1319-1330
    • Azakir, B.A.1    Desrochers, G.2    Angers, A.3
  • 21
    • 84875878283 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase Itch regulates tumor suppressor protein RASSF5/NORE1 stability in an acetylation-dependent manner
    • Suryaraja R, Anitha M, Anbarasu K, Kumari G, Mahalingam S. The E3 ubiquitin ligase Itch regulates tumor suppressor protein RASSF5/NORE1 stability in an acetylation-dependent manner. Cell Death Dis 2013; 4: e565.
    • (2013) Cell Death Dis , vol.4
    • Suryaraja, R.1    Anitha, M.2    Anbarasu, K.3    Kumari, G.4    Mahalingam, S.5
  • 22
    • 79953204984 scopus 로고    scopus 로고
    • Itch E3 ubiquitin ligase regulates large tumor suppressor 1 stability [corrected]
    • 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 USA 2011; 108: 4870-4875.
    • (2011) Proc Natl Acad Sci USA , 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
  • 23
    • 83755162631 scopus 로고    scopus 로고
    • HECT-type ubiquitin ligase ITCH targets lysosomal-associated protein multispanning transmembrane 5 (LAPTM5) and prevents LAPTM5-mediated cell death
    • 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: 44086-44094.
    • (2011) J Biol Chem , vol.286 , pp. 44086-44094
    • Ishihara, T.1    Inoue, J.2    Kozaki, K.3    Imoto, I.4    Inazawa, J.5
  • 24
    • 41949128060 scopus 로고    scopus 로고
    • Isoform-specific monoubiquitination, endocytosis, and degradation of alternatively spliced ErbB4 isoforms
    • 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: 4162-4167.
    • (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
  • 25
    • 0036197639 scopus 로고    scopus 로고
    • Dysregulation of T lymphocyte function in itchy mice: A role for Itch in TH2 differentiation
    • Fang D, Elly C, Gao B, Fang N, Altman Y, Joazeiro C et al. Dysregulation of T lymphocyte function in itchy mice: a role for Itch in TH2 differentiation. Nat Immunol 2002; 3: 281-287.
    • (2002) Nat Immunol , vol.3 , pp. 281-287
    • Fang, D.1    Elly, C.2    Gao, B.3    Fang, N.4    Altman, Y.5    Joazeiro, C.6
  • 26
    • 12144290293 scopus 로고    scopus 로고
    • Calcineurin imposes T cell unresponsiveness through targeted proteolysis of signaling proteins
    • Heissmeyer V, Macian F, Im SH, Varma R, Feske S, Venuprasad K et al. Calcineurin imposes T cell unresponsiveness through targeted proteolysis of signaling proteins. Nat Immunol 2004; 5: 255-265.
    • (2004) Nat Immunol , vol.5 , pp. 255-265
    • Heissmeyer, V.1    Macian, F.2    Im, S.H.3    Varma, R.4    Feske, S.5    Venuprasad, K.6
  • 27
    • 33645531744 scopus 로고    scopus 로고
    • Convergence of Itch-induced ubiquitination with MEKK1-JNK signaling in Th2 tolerance and airway inflammation
    • Venuprasad K, Elly C, Gao M, Salek-Ardakani S, Harada Y, Luo JL et al. Convergence of Itch-induced ubiquitination with MEKK1-JNK signaling in Th2 tolerance and airway inflammation. J Clin Invest 2006; 116: 1117-1126.
    • (2006) J Clin Invest , vol.116 , pp. 1117-1126
    • Venuprasad, K.1    Elly, C.2    Gao, M.3    Salek-Ardakani, S.4    Harada, Y.5    Luo, J.L.6
  • 28
    • 39449083378 scopus 로고    scopus 로고
    • The E3 ligase Itch negatively regulates inflammatory signaling pathways by controlling the function of the ubiquitin-editing enzyme A20
    • Shembade N, Harhaj NS, Parvatiyar K, Copeland NG, Jenkins NA, Matesic LE et al. The E3 ligase Itch negatively regulates inflammatory signaling pathways by controlling the function of the ubiquitin-editing enzyme A20. Nat Immunol 2008; 9: 254-262.
    • (2008) Nat Immunol , vol.9 , pp. 254-262
    • Shembade, N.1    Harhaj, N.S.2    Parvatiyar, K.3    Copeland, N.G.4    Jenkins, N.A.5    Matesic, L.E.6
  • 29
    • 0034680909 scopus 로고    scopus 로고
    • Recognition and ubiquitination of Notch by Itch, a hect-type E3 ubiquitin ligase
    • Qiu L, Joazeiro C, Fang N, Wang HY, Elly C, Altman Y et al. Recognition and ubiquitination of Notch by Itch, a hect-type E3 ubiquitin ligase. J Biol Chem 2000; 275: 35734-35737.
    • (2000) J Biol Chem , vol.275 , pp. 35734-35737
    • Qiu, L.1    Joazeiro, C.2    Fang, N.3    Wang, H.Y.4    Elly, C.5    Altman, Y.6
  • 30
    • 4444223733 scopus 로고    scopus 로고
    • Itch E3 ligase-mediated regulation of TGF-beta signaling by modulating smad2 phosphorylation
    • 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: 825-831.
    • (2004) Mol Cell , vol.15 , pp. 825-831
    • Bai, Y.1    Yang, C.2    Hu, K.3    Elly, C.4    Liu, Y.C.5
  • 31
    • 39449083806 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase Itch regulates expression of transcription factor Foxp3 and airway inflammation by enhancing the function of transcription factor TIEG1
    • Venuprasad K, Huang H, Harada Y, Elly C, Subramaniam M, Spelsberg T et al. The E3 ubiquitin ligase Itch regulates expression of transcription factor Foxp3 and airway inflammation by enhancing the function of transcription factor TIEG1. Nat Immunol 2008; 9: 245-253.
    • (2008) Nat Immunol , vol.9 , pp. 245-253
    • Venuprasad, K.1    Huang, H.2    Harada, Y.3    Elly, C.4    Subramaniam, M.5    Spelsberg, T.6
  • 32
    • 0242362743 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase AIP4 mediates ubiquitination and sorting of the G protein-coupled receptor CXCR4
    • 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: 709-722.
    • (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
  • 36
    • 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
    • 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: 1940-1949.
    • (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
  • 38
    • 77951075391 scopus 로고    scopus 로고
    • Regulation of the polycomb protein Ring1B by self-ubiquitination or by E6-AP may have implications to the pathogenesis of Angelman syndrome
    • Zaaroor-Regev D, de Bie P, Scheffner M, Noy T, Shemer R, Heled M et al. Regulation of the polycomb protein Ring1B by self-ubiquitination or by E6-AP may have implications to the pathogenesis of Angelman syndrome. Proc Natl Acad Sci USA 2010; 107: 6788-6793.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 6788-6793
    • Zaaroor-Regev, D.1    De Bie, P.2    Scheffner, M.3    Noy, T.4    Shemer, R.5    Heled, M.6
  • 39
    • 33947384611 scopus 로고    scopus 로고
    • Regulation of the Drosophila ubiquitin ligase DIAP1 is mediated via several distinct ubiquitin system pathways
    • Herman-Bachinsky Y, Ryoo HD, Ciechanover A, Gonen H. Regulation of the Drosophila ubiquitin ligase DIAP1 is mediated via several distinct ubiquitin system pathways. Cell Death Differ 2007; 14: 861-871.
    • (2007) Cell Death Differ , vol.14 , pp. 861-871
    • Herman-Bachinsky, Y.1    Ryoo, H.D.2    Ciechanover, A.3    Gonen, H.4
  • 40
    • 70350365288 scopus 로고    scopus 로고
    • Desmethylclomipramine induces the accumulation of autophagy markers by blocking autophagic flux
    • Rossi M, Munarriz ER, Bartesaghi S, Milanese M, Dinsdale D, Guerra-Martin MA et al. Desmethylclomipramine induces the accumulation of autophagy markers by blocking autophagic flux. J Cell Sci 2009; 122(Pt 18): 3330-3339.
    • (2009) J Cell Sci , vol.122 , Issue.PART.18 , pp. 3330-3339
    • Rossi, M.1    Munarriz, E.R.2    Bartesaghi, S.3    Milanese, M.4    Dinsdale, D.5    Guerra-Martin, M.A.6
  • 41
    • 69949106925 scopus 로고    scopus 로고
    • The double-edged sword of autophagy modulation in cancer
    • White E, DiPaola RS. The double-edged sword of autophagy modulation in cancer. Clin Cancer Res 2009; 15: 5308-5316.
    • (2009) Clin Cancer Res , vol.15 , pp. 5308-5316
    • White, E.1    Dipaola, R.S.2
  • 42
    • 0034757896 scopus 로고    scopus 로고
    • A novel assay to study autophagy: Regulation of autophagosome vacuole size by amino acid deprivation
    • Munafo DB, Colombo MI. A novel assay to study autophagy: regulation of autophagosome vacuole size by amino acid deprivation. J Cell Sci 2001; 114(Pt 20): 3619-3629.
    • (2001) J Cell Sci , vol.114 , Issue.PART.20 , pp. 3619-3629
    • Munafo, D.B.1    Colombo, M.I.2
  • 43
    • 0000994406 scopus 로고
    • Analysis of combined drug effects: A new look at a very old problem
    • Chou T-C, Talalay P. Analysis of combined drug effects: a new look at a very old problem. Trends Pharmacol Sci 1983; 4: 450-454.
    • (1983) Trends Pharmacol Sci , vol.4 , pp. 450-454
    • Chou, T.-C.1    Talalay, P.2
  • 44
    • 84878154617 scopus 로고    scopus 로고
    • Mule/Huwe1/Arf-BP1 suppresses Ras-driven tumorigenesis by preventing c-Myc/Miz1-mediated down-regulation of p21 and p15
    • Inoue S, Hao Z, Elia AJ, Cescon D, Zhou L, Silvester J et al. Mule/Huwe1/Arf-BP1 suppresses Ras-driven tumorigenesis by preventing c-Myc/Miz1-mediated down-regulation of p21 and p15. Gen Dev 2013; 27: 1101-1114.
    • (2013) Gen Dev , vol.27 , pp. 1101-1114
    • Inoue, S.1    Hao, Z.2    Elia, A.J.3    Cescon, D.4    Zhou, L.5    Silvester, J.6
  • 45
    • 84884902595 scopus 로고    scopus 로고
    • The Cul4ADDB1 E3 ubiquitin ligase complex represses p73 transcriptional activity
    • Malatesta M, Peschiaroli A, Memmi EM, Zhang J, Antonov A, Green DR et al. The Cul4ADDB1 E3 ubiquitin ligase complex represses p73 transcriptional activity. Oncogene 2012; 32: 4721-4726.
    • (2012) Oncogene , vol.32 , pp. 4721-4726
    • Malatesta, M.1    Peschiaroli, A.2    Memmi, E.M.3    Zhang, J.4    Antonov, A.5    Green, D.R.6
  • 46
    • 77955648341 scopus 로고    scopus 로고
    • Differential control of TAp73 and DeltaNp73 protein stability by the ring finger ubiquitin ligase PIR2
    • Sayan BS, Yang AL, Conforti F, Tucci P, Piro MC, Browne GJ et al. Differential control of TAp73 and DeltaNp73 protein stability by the ring finger ubiquitin ligase PIR2. Proc Natl Acad Sci USA 2010; 107: 12877-12882.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 12877-12882
    • Sayan, B.S.1    Yang, A.L.2    Conforti, F.3    Tucci, P.4    Piro, M.C.5    Browne, G.J.6
  • 47
    • 77950430911 scopus 로고    scopus 로고
    • The antiapoptotic DeltaNp73 is degraded in a c-Jun-dependent manner upon genotoxic stress through the antizyme-mediated pathway
    • Dulloo I, Gopalan G, Melino G, Sabapathy K. The antiapoptotic DeltaNp73 is degraded in a c-Jun-dependent manner upon genotoxic stress through the antizyme-mediated pathway. Proc Natl Acad Sci USA 2010; 107: 4902-4907.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 4902-4907
    • Dulloo, I.1    Gopalan, G.2    Melino, G.3    Sabapathy, K.4
  • 48
    • 69849083542 scopus 로고    scopus 로고
    • The F-box protein FBXO45 promotes the proteasome-dependent degradation of p73
    • Peschiaroli A, Scialpi F, Bernassola F, Pagano M, Melino G. The F-box protein FBXO45 promotes the proteasome-dependent degradation of p73. Oncogene 2009; 28: 3157-3166.
    • (2009) Oncogene , vol.28 , pp. 3157-3166
    • Peschiaroli, A.1    Scialpi, F.2    Bernassola, F.3    Pagano, M.4    Melino, G.5
  • 51
    • 77949265991 scopus 로고    scopus 로고
    • The ubiquitin-specific protease USP47 is a novel beta-TRCP interactor regulating cell survival
    • Peschiaroli A, Skaar JR, Pagano M, Melino G. The ubiquitin-specific protease USP47 is a novel beta-TRCP interactor regulating cell survival. Oncogene 2010; 29: 1384-1393.
    • (2010) Oncogene , vol.29 , pp. 1384-1393
    • Peschiaroli, A.1    Skaar, J.R.2    Pagano, M.3    Melino, G.4
  • 52
    • 72149107116 scopus 로고    scopus 로고
    • Insights into ubiquitin transfer cascades from a structure of a UbcH5B approximately ubiquitin- HECT(NEDD4L) complex
    • Kamadurai HB, Souphron J, Scott DC, Duda DM, Miller DJ, Stringer D et al. Insights into ubiquitin transfer cascades from a structure of a UbcH5B approximately ubiquitin- HECT(NEDD4L) complex. Mol Cell 2009; 36: 1095-1102.
    • (2009) Mol Cell , vol.36 , pp. 1095-1102
    • Kamadurai, H.B.1    Souphron, J.2    Scott, D.C.3    Duda, D.M.4    Miller, D.J.5    Stringer, D.6
  • 54
    • 38449106894 scopus 로고    scopus 로고
    • HECT E3s and human disease
    • Scheffner M, Staub O. HECT E3s and human disease. BMC Biochem 2007; 8(Suppl 1): S6.
    • (2007) BMC Biochem , vol.8 , Issue.SUPPL.1
    • Scheffner, M.1    Staub, O.2
  • 55
    • 33751515474 scopus 로고    scopus 로고
    • The polycomb protein Ring1B generates self atypical mixed ubiquitin chains required for its in vitro histone H2A ligase activity
    • Ben-Saadon R, Zaaroor D, Ziv T, Ciechanover A. The polycomb protein Ring1B generates self atypical mixed ubiquitin chains required for its in vitro histone H2A ligase activity. Mol Cell 2006; 24: 701-711.
    • (2006) Mol Cell , vol.24 , pp. 701-711
    • Ben-Saadon, R.1    Zaaroor, D.2    Ziv, T.3    Ciechanover, A.4
  • 56
    • 84901032230 scopus 로고    scopus 로고
    • MolSoft, LLC: La Jolla, CA
    • ICM Version 3.7.2 ed. MolSoft, LLC: La Jolla, CA, 2012.
    • (2012) ICM Version 3.7.2
  • 57
    • 70249098305 scopus 로고    scopus 로고
    • 2,3-Dihydro- 1-benzofuran derivatives as a series of potent selective cannabinoid receptor 2 agonists: Design, synthesis, and binding mode prediction through ligand-steered modeling
    • Diaz P, Phatak SS, Xu J, Fronczek FR, Astruc-Diaz F, Thompson CM et al. 2,3-Dihydro- 1-benzofuran derivatives as a series of potent selective cannabinoid receptor 2 agonists: design, synthesis, and binding mode prediction through ligand-steered modeling. Chem Med Chem 2009; 4: 1615-1629.
    • (2009) Chem Med Chem , vol.4 , pp. 1615-1629
    • Diaz, P.1    Phatak, S.S.2    Xu, J.3    Fronczek, F.R.4    Astruc-Diaz, F.5    Thompson, C.M.6
  • 58
    • 58449114054 scopus 로고    scopus 로고
    • The binding mode of petrosaspongiolide M to the human group IIA phospholipase A(2): Exploring the role of covalent and noncovalent interactions in the inhibition process
    • Monti MC, Casapullo A, Cavasotto CN, Tosco A, Dal Piaz F, Ziemys A et al. The binding mode of petrosaspongiolide M to the human group IIA phospholipase A(2): exploring the role of covalent and noncovalent interactions in the inhibition process. Chem-Eur J 2009; 15: 1155-1163.
    • (2009) Chem-Eur J , vol.15 , pp. 1155-1163
    • Monti, M.C.1    Casapullo, A.2    Cavasotto, C.N.3    Tosco, A.4    Dal Piaz, F.5    Ziemys, A.6
  • 59
    • 78650701635 scopus 로고    scopus 로고
    • Ligand-steered modeling and docking: A benchmarking study in class a g-protein-coupled receptors
    • Phatak SS, Gatica EA, Cavasotto CN. Ligand-steered modeling and docking: A benchmarking study in Class A G-Protein-Coupled Receptors. J Chem Inf Model 2010; 50: 2119-2128.
    • (2010) J Chem Inf Model , vol.50 , pp. 2119-2128
    • Phatak, S.S.1    Gatica, E.A.2    Cavasotto, C.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.