메뉴 건너뛰기




Volumn 82, Issue 6, 2014, Pages 1035-1047

Antiapoptotic Bcl-2 homolog CED-9 in Caenorhabditis elegans: Dynamics of BH3 and CED-4 binding regions and comparison with mammalian antiapoptotic Bcl-2 proteins

Author keywords

Accessible surface area; Comparative simulations; Flexible and rigid binding regions; Helix bundle protein; Hydrophobic binding groove; Interhelical angle; Programmed cell death; Protein protein interactions in apoptosis

Indexed keywords

APOPTOTIC PROTEASE ACTIVATING FACTOR 1; BCL2 RELATED PROTEIN A1; BH3 PROTEIN; CED 9 PROTEIN; PROTEIN BCL 2; PROTEIN BCL W; PROTEIN BCL XL; PROTEIN MCL 1; UNCLASSIFIED DRUG; CAENORHABDITIS ELEGANS PROTEIN; CED-9 PROTEIN, C ELEGANS; PROTEIN BINDING;

EID: 84900826276     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24476     Document Type: Article
Times cited : (5)

References (77)
  • 1
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR, Reed JC. Mitochondria and apoptosis. Science 1998;281:1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 2
    • 0030947095 scopus 로고    scopus 로고
    • Programmed cell death in animal development
    • Jacobson MD, Weil M, Raff MC. Programmed cell death in animal development. Cell 1997;88:347-354.
    • (1997) Cell , vol.88 , pp. 347-354
    • Jacobson, M.D.1    Weil, M.2    Raff, M.C.3
  • 3
    • 0031046848 scopus 로고    scopus 로고
    • Apoptosis and disease: regulation and clinical relevance of programmed cell death
    • Rudin CM, Thompson CB. Apoptosis and disease: regulation and clinical relevance of programmed cell death. Ann Rev Med 1997;48:267-281.
    • (1997) Ann Rev Med , vol.48 , pp. 267-281
    • Rudin, C.M.1    Thompson, C.B.2
  • 4
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson CB. Apoptosis in the pathogenesis and treatment of disease. Science 1995;267:1456-1462.
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 6
    • 0034710649 scopus 로고    scopus 로고
    • Structural and biochemical basis of apoptotic activation by Smac/DIABLO
    • Chai JJ, Du CY, Wu JW, Kyin S, Wang XD, Shi YG. Structural and biochemical basis of apoptotic activation by Smac/DIABLO. Nature 2000;406:855-862.
    • (2000) Nature , vol.406 , pp. 855-862
    • Chai, J.J.1    Du, C.Y.2    Wu, J.W.3    Kyin, S.4    Wang, X.D.5    Shi, Y.G.6
  • 7
    • 0033193863 scopus 로고    scopus 로고
    • Dark is a Drosophila homologue of Apaf-1/CED-4 and functions in an evolutioarily conserved death pathway
    • Rodriguez A, Oliver H, Zou H, Chen P, Wang XD, Abrams JM. Dark is a Drosophila homologue of Apaf-1/CED-4 and functions in an evolutioarily conserved death pathway. Nature Cell Biol 1999;1:272-279.
    • (1999) Nature Cell Biol , vol.1 , pp. 272-279
    • Rodriguez, A.1    Oliver, H.2    Zou, H.3    Chen, P.4    Wang, X.D.5    Abrams, J.M.6
  • 8
    • 0033231548 scopus 로고    scopus 로고
    • HAC-1, a Drosophila homolog of APAF-1 and CED-4 functions in developmental and radiation-induced apoptosis
    • Zhou L, Song ZW, Tittel J, Steller H. HAC-1, a Drosophila homolog of APAF-1 and CED-4 functions in developmental and radiation-induced apoptosis. Mol Cell 1999;4:745-755.
    • (1999) Mol Cell , vol.4 , pp. 745-755
    • Zhou, L.1    Song, Z.W.2    Tittel, J.3    Steller, H.4
  • 9
    • 0034651791 scopus 로고    scopus 로고
    • Induction of apoptosis by Drosophila reaper, hid and grim through inhibition of IAP function
    • Goyal L, McCall K, Agapite J, Hartweig E, Steller H. Induction of apoptosis by Drosophila reaper, hid and grim through inhibition of IAP function. EMBO J 2000;19:589-597.
    • (2000) EMBO J , vol.19 , pp. 589-597
    • Goyal, L.1    McCall, K.2    Agapite, J.3    Hartweig, E.4    Steller, H.5
  • 10
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou H, Henzel WJ, Liu XS, Lutschg A, Wang XD. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 1997;90:405-413.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.S.3    Lutschg, A.4    Wang, X.D.5
  • 11
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: the executioners of apoptosis
    • Cohen GM. Caspases: the executioners of apoptosis. Biochem J 1997;326:1-16.
    • (1997) Biochem J , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 12
    • 0033119372 scopus 로고    scopus 로고
    • Bcl-2 gene family and the regulation of programmed cell death
    • Korsmeyer SJ Bcl-2 gene family and the regulation of programmed cell death. Cancer Res 1999;59:S1693-S1700.
    • (1999) Cancer Res , vol.59
    • Korsmeyer, S.J.1
  • 13
    • 0037089068 scopus 로고    scopus 로고
    • BH3-only proteins - evolutionarily conserved proapoptotic Bcl-2 family members essential for initiating programmed cell death
    • Bouillet P, Strasser A. BH3-only proteins - evolutionarily conserved proapoptotic Bcl-2 family members essential for initiating programmed cell death. J Cell Sci 2002;115:1567-1574.
    • (2002) J Cell Sci , vol.115 , pp. 1567-1574
    • Bouillet, P.1    Strasser, A.2
  • 14
    • 68149094266 scopus 로고    scopus 로고
    • Egl-1: a key activator of apoptotic cell death in C. elegans
    • Nehme R, Conradt B. Egl-1: a key activator of apoptotic cell death in C. elegans. Oncogene 2008;27:S30-S40.
    • (2008) Oncogene , vol.27
    • Nehme, R.1    Conradt, B.2
  • 15
    • 0028288277 scopus 로고
    • C. elegans cell survival gene CED-9 encodes a functional homolog of the mammalian protooncogene Bcl-2
    • Hengartner MO, Horvitz HR. C. elegans cell survival gene CED-9 encodes a functional homolog of the mammalian protooncogene Bcl-2. Cell 1994;76:665-676.
    • (1994) Cell , vol.76 , pp. 665-676
    • Hengartner, M.O.1    Horvitz, H.R.2
  • 16
    • 0034193520 scopus 로고    scopus 로고
    • The Drosophila Bcl-2 family member dBorg-1 functions in the apoptotic response to UV-irradiation
    • Brachmann CB, Jassim OW, Wachsmuth BD, Cagan RL. The Drosophila Bcl-2 family member dBorg-1 functions in the apoptotic response to UV-irradiation. Curr Biol 2000;10:547-550.
    • (2000) Curr Biol , vol.10 , pp. 547-550
    • Brachmann, C.B.1    Jassim, O.W.2    Wachsmuth, B.D.3    Cagan, R.L.4
  • 17
    • 0034282917 scopus 로고    scopus 로고
    • Drosophila pro-apoptotic Bcl-2/Bax homologue reveals evolutionary conservation of cell death mechanisms
    • Zhang H, Huang QH, Ke N, Matsuyama S, Hammock B, Godzik A, Reed JC. Drosophila pro-apoptotic Bcl-2/Bax homologue reveals evolutionary conservation of cell death mechanisms. J Biol Chem 2000;275:27303-27306.
    • (2000) J Biol Chem , vol.275 , pp. 27303-27306
    • Zhang, H.1    Huang, Q.H.2    Ke, N.3    Matsuyama, S.4    Hammock, B.5    Godzik, A.6    Reed, J.C.7
  • 18
    • 0041813273 scopus 로고    scopus 로고
    • Buffy, a Drosophila Bcl-2 protein, has anti-apoptotic and cell cycle inhibitory functions
    • Quinn L, Coombe M, Mills K, Daish T, Colussi P, Kumar S, Richardson H. Buffy, a Drosophila Bcl-2 protein, has anti-apoptotic and cell cycle inhibitory functions. EMBO J 2003;22:3568-3579.
    • (2003) EMBO J , vol.22 , pp. 3568-3579
    • Quinn, L.1    Coombe, M.2    Mills, K.3    Daish, T.4    Colussi, P.5    Kumar, S.6    Richardson, H.7
  • 19
    • 0032509238 scopus 로고    scopus 로고
    • Caenorhabditis elegans EGL-1 disrupts the interaction of CED-9 with CED-4 and promotes CED-3 activation
    • del Peso L, Gonzalez VM, Nunez G. Caenorhabditis elegans EGL-1 disrupts the interaction of CED-9 with CED-4 and promotes CED-3 activation. J Biol Chem 1998;273:33495-33500.
    • (1998) J Biol Chem , vol.273 , pp. 33495-33500
    • del Peso, L.1    Gonzalez, V.M.2    Nunez, G.3
  • 20
    • 0032524885 scopus 로고    scopus 로고
    • The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9
    • Conradt B, Horvitz HR. The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9. Cell 1998;93:519-529.
    • (1998) Cell , vol.93 , pp. 519-529
    • Conradt, B.1    Horvitz, H.R.2
  • 21
    • 0032761224 scopus 로고    scopus 로고
    • Apaf1 and the apoptotic machinery
    • Cecconi F. Apaf1 and the apoptotic machinery. Cell Death Differ 1999;6:1087-1098.
    • (1999) Cell Death Differ , vol.6 , pp. 1087-1098
    • Cecconi, F.1
  • 22
    • 0031918223 scopus 로고    scopus 로고
    • Bcl-2 family: regulators of cell death
    • Chao DT, Korsmeyer SJ Bcl-2 family: regulators of cell death. Annu Rev Immunol 1998;16:395-419.
    • (1998) Annu Rev Immunol , vol.16 , pp. 395-419
    • Chao, D.T.1    Korsmeyer, S.J.2
  • 24
    • 37549048249 scopus 로고    scopus 로고
    • The Bcl-2 protein family: opposing activities that mediate cell death
    • Youle RJ, Strasser A. The Bcl-2 protein family: opposing activities that mediate cell death. Nat Rev Mol Cell Biol 2008;9:47-59.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 25
    • 27544446991 scopus 로고    scopus 로고
    • Life in the balance: how BH3-only proteins induce apoptosis
    • Willis SN, Adams JM. Life in the balance: how BH3-only proteins induce apoptosis. Curr Opin Cell Biol 2005;17:617-625.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 617-625
    • Willis, S.N.1    Adams, J.M.2
  • 26
    • 0033635733 scopus 로고    scopus 로고
    • BH3-only proteins: essential initiators of apoptotic cell death
    • Huang DCS, Strasser A. BH3-only proteins: essential initiators of apoptotic cell death. Cell 2000;103:839-842.
    • (2000) Cell , vol.103 , pp. 839-842
    • Huang, D.C.S.1    Strasser, A.2
  • 27
    • 68249106060 scopus 로고    scopus 로고
    • BH3-only proteins in apoptosis and beyond: an overview
    • Lomonosova E, Chinnadurai G. BH3-only proteins in apoptosis and beyond: an overview. Oncogene 2008;27:S2-S19.
    • (2008) Oncogene , vol.27
    • Lomonosova, E.1    Chinnadurai, G.2
  • 28
    • 4644249309 scopus 로고    scopus 로고
    • Structural, biochemical and functional analyses of CED-9 recognition by the pro-apoptotic proteins EGL-1 and CED-4
    • Yan N, Gu L, Kokel D, Chai J, Li W, Han A, Chen L, Xue D, Shi Y. Structural, biochemical and functional analyses of CED-9 recognition by the pro-apoptotic proteins EGL-1 and CED-4. Mol Cell 2004;15:999-1006.
    • (2004) Mol Cell , vol.15 , pp. 999-1006
    • Yan, N.1    Gu, L.2    Kokel, D.3    Chai, J.4    Li, W.5    Han, A.6    Chen, L.7    Xue, D.8    Shi, Y.9
  • 30
    • 77949507320 scopus 로고    scopus 로고
    • Identification of core structural residues in sequentially diverse and structurally homologous Bcl-2 family of proteins
    • Lama D, Sankararamakrishnan R. Identification of core structural residues in sequentially diverse and structurally homologous Bcl-2 family of proteins. Biochemistry 2010;49:2574-2584.
    • (2010) Biochemistry , vol.49 , pp. 2574-2584
    • Lama, D.1    Sankararamakrishnan, R.2
  • 31
    • 0030827971 scopus 로고    scopus 로고
    • BH3 domain of BAD is required for heterodimerization with Bcl-XL and pro-apoptotic activity
    • Zha JP, Harada H, Osipov K, Jockel J, Waksman G, Korsmeyer SJ BH3 domain of BAD is required for heterodimerization with Bcl-XL and pro-apoptotic activity. J Biol Chem 1997;272:24101-24104.
    • (1997) J Biol Chem , vol.272 , pp. 24101-24104
    • Zha, J.P.1    Harada, H.2    Osipov, K.3    Jockel, J.4    Waksman, G.5    Korsmeyer, S.J.6
  • 32
    • 1542616703 scopus 로고    scopus 로고
    • Proteins of the Bcl-2 family in apoptosis signalling: from mechanistic insights to therapeutic opportunities
    • Chan SL, Yu VC. Proteins of the Bcl-2 family in apoptosis signalling: from mechanistic insights to therapeutic opportunities. Clin Exp Pharmacol Physiol 2004;31:119-128.
    • (2004) Clin Exp Pharmacol Physiol , vol.31 , pp. 119-128
    • Chan, S.L.1    Yu, V.C.2
  • 34
    • 0032146987 scopus 로고    scopus 로고
    • Bcl-2-family proteins: the role of the BH3 domain in apoptosis
    • Kelekar A, Thompson CB. Bcl-2-family proteins: the role of the BH3 domain in apoptosis. Trends Cell Biol 1998;8:324-330.
    • (1998) Trends Cell Biol , vol.8 , pp. 324-330
    • Kelekar, A.1    Thompson, C.B.2
  • 35
    • 0036726059 scopus 로고    scopus 로고
    • BH3 domains: intracellular death-ligands critical for initiating apoptosis
    • Chittenden T. BH3 domains: intracellular death-ligands critical for initiating apoptosis. Cancer Cell 2002;2:165-166.
    • (2002) Cancer Cell , vol.2 , pp. 165-166
    • Chittenden, T.1
  • 37
    • 0042220409 scopus 로고    scopus 로고
    • The structure of a Bcl-xL/Bim fragment complex: implications for Bim function
    • Liu X, Dai S, Zhu Y, Marrack P, Kappler JW. The structure of a Bcl-xL/Bim fragment complex: implications for Bim function. Immunity 2003;19:341-352.
    • (2003) Immunity , vol.19 , pp. 341-352
    • Liu, X.1    Dai, S.2    Zhu, Y.3    Marrack, P.4    Kappler, J.W.5
  • 38
    • 45849104776 scopus 로고    scopus 로고
    • Structure of the BH3 domains from the p53-inducible BH3-only proteins Noxa and Puma in complex with Mcl-1
    • Day CL, Smits C, Fan CF, Lee EF, Fairlie WD, Hinds MG. Structure of the BH3 domains from the p53-inducible BH3-only proteins Noxa and Puma in complex with Mcl-1. J Mol Biol 2008;380:958-971.
    • (2008) J Mol Biol , vol.380 , pp. 958-971
    • Day, C.L.1    Smits, C.2    Fan, C.F.3    Lee, E.F.4    Fairlie, W.D.5    Hinds, M.G.6
  • 39
    • 42949110343 scopus 로고    scopus 로고
    • Structural plasticity underpins promiscuous binding of the prosurvival protein A1
    • Smits C, Czabotar PE, Hinds MG, Day CL. Structural plasticity underpins promiscuous binding of the prosurvival protein A1. Structure 2008;16:818-829.
    • (2008) Structure , vol.16 , pp. 818-829
    • Smits, C.1    Czabotar, P.E.2    Hinds, M.G.3    Day, C.L.4
  • 40
  • 41
    • 0346121671 scopus 로고    scopus 로고
    • Unique structural features of a Bcl-2 family protein CED-9 and biophysical characterization of CED-9/EGL-1 interactions
    • Woo J-S, Jung J-S, Ha N-C, Shin J, Kim K-H, Lee W, Oh B-H. Unique structural features of a Bcl-2 family protein CED-9 and biophysical characterization of CED-9/EGL-1 interactions. Cell Death Differ 2003;10:1310-1319.
    • (2003) Cell Death Differ , vol.10 , pp. 1310-1319
    • Woo, J.-S.1    Jung, J.-S.2    Ha, N.-C.3    Shin, J.4    Kim, K.-H.5    Lee, W.6    Oh, B.-H.7
  • 42
    • 26844485563 scopus 로고    scopus 로고
    • Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans
    • Yan N, Chai J, Lee ES, Gu L, He J, Wu JW, Kokel D, Li H, Hao Q, Xue D, Shi Y. Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans. Nature 2005;437:831-837.
    • (2005) Nature , vol.437 , pp. 831-837
    • Yan, N.1    Chai, J.2    Lee, E.S.3    Gu, L.4    He, J.5    Wu, J.W.6    Kokel, D.7    Li, H.8    Hao, Q.9    Xue, D.10    Shi, Y.11
  • 43
    • 52249106626 scopus 로고    scopus 로고
    • Anti-apoptotic Bcl-XL protein in complex with BH3 peptides of pro-apoptotic Bak, Bad, and Bim proteins: comparative molecular dynamics simulations
    • Lama D, Sankararamakrishnan R. Anti-apoptotic Bcl-XL protein in complex with BH3 peptides of pro-apoptotic Bak, Bad, and Bim proteins: comparative molecular dynamics simulations. Proteins 2008;73:492-514.
    • (2008) Proteins , vol.73 , pp. 492-514
    • Lama, D.1    Sankararamakrishnan, R.2
  • 44
    • 84974716085 scopus 로고    scopus 로고
    • Sankararamakrishnan R. Plasticity of BH3 domain-binding hydrophobic grooves in the anti-apoptotic Mcl-1 and A1 proteins
    • Bansal M, Srinivasan N, editors. IISc. Press and World Scientific., Singapore
    • Modi V, Lama D, Sankararamakrishnan R. Plasticity of BH3 domain-binding hydrophobic grooves in the anti-apoptotic Mcl-1 and A1 proteins. Bansal M, Srinivasan N, editors. Biomolecular forms and function. IISc. Press and World Scientific., Singapore. 2013. pp 468-481.
    • (2013) Biomolecular forms and function , pp. 468-481
    • Modi, V.1    Lama, D.2
  • 45
    • 84874508143 scopus 로고    scopus 로고
    • Behavior of solvent-exposed hydrophobic groove in the anti-apoptotic Bcl-XL proteclues for its ability to bind diverse BH3 ligands from MD simulations
    • Lama D, Modi V, Sankararamakrishnan R. Behavior of solvent-exposed hydrophobic groove in the anti-apoptotic Bcl-XL proteclues for its ability to bind diverse BH3 ligands from MD simulations. PLoS One 2013;8:e54397.
    • (2013) PLoS One , vol.8
    • Lama, D.1    Modi, V.2    Sankararamakrishnan, R.3
  • 48
    • 0032515874 scopus 로고    scopus 로고
    • Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation
    • Hu YM, Benedict MA, Wu DY, Inohara N, Nunez G. Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation. Proc Natl Acad Sci U S A 1998;95:4386-4391.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 4386-4391
    • Hu, Y.M.1    Benedict, M.A.2    Wu, D.Y.3    Inohara, N.4    Nunez, G.5
  • 49
    • 0033774569 scopus 로고    scopus 로고
    • Failure of Bcl-2 family members to interact with Apaf-1 in normal and apoptotic cells
    • Conus S, Rosse T, Borner C. Failure of Bcl-2 family members to interact with Apaf-1 in normal and apoptotic cells. Cell Death Differ 2000;7:947-954.
    • (2000) Cell Death Differ , vol.7 , pp. 947-954
    • Conus, S.1    Rosse, T.2    Borner, C.3
  • 54
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: algorithms for highly efficient, load-balanced and scalable molecular simulation
    • Hess B, Kutzner C, van der Spoel D, Lindahl E. GROMACS 4: algorithms for highly efficient, load-balanced and scalable molecular simulation. J Chem Theory Comput 2008;4:435-447.
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 57
    • 0001751804 scopus 로고    scopus 로고
    • Parametrization of aliphatic CHn united atoms of GROMOS96 force field
    • Daura X, Mark AE, van Gunsteren WF. Parametrization of aliphatic CHn united atoms of GROMOS96 force field. J Comput Chem 1998;19:535-547.
    • (1998) J Comput Chem , vol.19 , pp. 535-547
    • Daura, X.1    Mark, A.E.2    van Gunsteren, W.F.3
  • 60
    • 84864194883 scopus 로고    scopus 로고
    • The UniProt Consortium The universal protein resource (UniProt) 2009
    • The UniProt Consortium The universal protein resource (UniProt) 2009. Nucleic Acids Res 2012;40:D71-D75.
    • (2012) Nucleic Acids Res , vol.40
  • 61
    • 0030447864 scopus 로고    scopus 로고
    • Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol
    • Rohl CA, Chakrabartty A, Baldwin RL. Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol. Protein Sci 1996;5:2623-2637.
    • (1996) Protein Sci , vol.5 , pp. 2623-2637
    • Rohl, C.A.1    Chakrabartty, A.2    Baldwin, R.L.3
  • 62
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983;22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 63
    • 0344608883 scopus 로고    scopus 로고
    • The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity
    • Hinds MG, Lackmann M, Skea GL, Harrison PJ, Huang DCS, Day CL. The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity. EMBO J 2003;22:1497-1507.
    • (2003) EMBO J , vol.22 , pp. 1497-1507
    • Hinds, M.G.1    Lackmann, M.2    Skea, G.L.3    Harrison, P.J.4    Huang, D.C.S.5    Day, C.L.6
  • 65
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: coregulation of dimer formation and intracellular localization
    • Suzuki M, Youle RJ, Tjandra N. Structure of Bax: coregulation of dimer formation and intracellular localization. Cell 2000;103:645-654.
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 66
    • 78650787051 scopus 로고    scopus 로고
    • The C. elegans B-cell lymphoma 2 (bcl-2) homolog cell death abnormal 9 (ced-9) associates with and remodels lipid membranes
    • Tan FJ, Zuckerman JE, Wells RC, Hill RB. The C. elegans B-cell lymphoma 2 (bcl-2) homolog cell death abnormal 9 (ced-9) associates with and remodels lipid membranes. Protein Sci 2011;20:62-74.
    • (2011) Protein Sci , vol.20 , pp. 62-74
    • Tan, F.J.1    Zuckerman, J.E.2    Wells, R.C.3    Hill, R.B.4
  • 67
    • 84555194738 scopus 로고    scopus 로고
    • Dynamics of noncovalent interactions in all-α and all-β class proteins: implications for the stability of amyloid aggregates
    • Jain A, Sankararamakrishnan R. Dynamics of noncovalent interactions in all-α and all-β class proteins: implications for the stability of amyloid aggregates. J Chem Inf Model 2011;51:3208-3216.
    • (2011) J Chem Inf Model , vol.51 , pp. 3208-3216
    • Jain, A.1    Sankararamakrishnan, R.2
  • 68
    • 38349178200 scopus 로고    scopus 로고
    • A structural model of the erythrocyte spectrin heterodimer initiation site determined using homology modeling and chemical cross-linking
    • Li D, Tang H-Y, Speicher DW. A structural model of the erythrocyte spectrin heterodimer initiation site determined using homology modeling and chemical cross-linking. J Biol Chem 2008;283:1553-1562.
    • (2008) J Biol Chem , vol.283 , pp. 1553-1562
    • Li, D.1    Tang, H.-Y.2    Speicher, D.W.3
  • 69
    • 0032481346 scopus 로고    scopus 로고
    • The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4
    • Huang DCS, Adams JM, Cory S. The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4. EMBO J 1998;17:1029-1039.
    • (1998) EMBO J , vol.17 , pp. 1029-1039
    • Huang, D.C.S.1    Adams, J.M.2    Cory, S.3
  • 70
    • 0033575142 scopus 로고    scopus 로고
    • NH2-terminal BH4 domain of Bcl-2 is functional for heterodimerization with Bax and inhibition of apoptosis
    • Hirotani M, Zhang YK, Fujita N, Naito M, Tsuruo T. NH2-terminal BH4 domain of Bcl-2 is functional for heterodimerization with Bax and inhibition of apoptosis. J Biol Chem 1999;274:20415-20420.
    • (1999) J Biol Chem , vol.274 , pp. 20415-20420
    • Hirotani, M.1    Zhang, Y.K.2    Fujita, N.3    Naito, M.4    Tsuruo, T.5
  • 72
    • 84880107585 scopus 로고    scopus 로고
    • Small molecule drug screening in Drosophila identifies the 5HT2A receptor as a feeding modulation target
    • Gasque G, Conway S, Huang J, Rao Y, Vosshall LB. Small molecule drug screening in Drosophila identifies the 5HT2A receptor as a feeding modulation target. Sci Rep 2013;3:2120.
    • (2013) Sci Rep , vol.3 , pp. 2120
    • Gasque, G.1    Conway, S.2    Huang, J.3    Rao, Y.4    Vosshall, L.B.5
  • 73
    • 33745223646 scopus 로고    scopus 로고
    • Finding function in novel targets: C. elegans as model organism
    • Kaletta T, Hengartner MO. Finding function in novel targets: C. elegans as model organism. Nat Rev Drug Dis 2006;5:387-398.
    • (2006) Nat Rev Drug Dis , vol.5 , pp. 387-398
    • Kaletta, T.1    Hengartner, M.O.2
  • 74
    • 0037373633 scopus 로고    scopus 로고
    • Dying for a cause: invertebrate genetics takes on human neurodegeneration
    • Driscoll M, Gerstbrein B. Dying for a cause: invertebrate genetics takes on human neurodegeneration. Nat Rev Genet 2003;4:181-194.
    • (2003) Nat Rev Genet , vol.4 , pp. 181-194
    • Driscoll, M.1    Gerstbrein, B.2
  • 75
    • 34248598584 scopus 로고    scopus 로고
    • Invertebrate animal models of diseases as screening tools in drug discovery
    • Segalat L. Invertebrate animal models of diseases as screening tools in drug discovery. ACS Chem Biol 2007;2:231-236.
    • (2007) ACS Chem Biol , vol.2 , pp. 231-236
    • Segalat, L.1
  • 76
    • 77951672406 scopus 로고    scopus 로고
    • High-throughput screening and small animal models, where are we?
    • Giacomotto J, Segalat L. High-throughput screening and small animal models, where are we? Brit J Pharmacol 2010;160:204-216.
    • (2010) Brit J Pharmacol , vol.160 , pp. 204-216
    • Giacomotto, J.1    Segalat, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.