메뉴 건너뛰기




Volumn 22, Issue 10, 2015, Pages 1665-1675

Bak apoptotic pores involve a flexible C-terminal region and juxtaposition of the C-terminal transmembrane domains

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DIMER; OLIGOMER; PROTEIN BAK; PROTEIN BAX;

EID: 84941191862     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/cdd.2015.15     Document Type: Article
Times cited : (52)

References (72)
  • 1
    • 84872006971 scopus 로고    scopus 로고
    • Where killers meet-permeabilization of the outer mitochondrial membrane during apoptosis
    • Bender T, Martinou JC. Where killers meet-permeabilization of the outer mitochondrial membrane during apoptosis. Cold Spring Harb Perspect Biol 2013; 5: a011106.
    • (2013) Cold Spring Harb Perspect Biol , vol.5
    • Bender, T.1    Martinou, J.C.2
  • 2
    • 77956095537 scopus 로고    scopus 로고
    • Mitochondria and cell death: Outer membrane permeabilization and beyond
    • Tait SW, Green DR. Mitochondria and cell death: outer membrane permeabilization and beyond. Nat Rev Mol Cell Biol 2010; 11: 621-632.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 621-632
    • Tait, S.W.1    Green, D.R.2
  • 4
    • 33751544565 scopus 로고    scopus 로고
    • The x-ray structure of a BAK homodimer reveals an inhibitory zinc binding site
    • Moldoveanu T, Liu Q, Tocilj A, Watson MH, Shore G, Gehring K. The x-ray structure of a BAK homodimer reveals an inhibitory zinc binding site. Mol Cell 2006; 24: 677-688.
    • (2006) Mol Cell , vol.24 , pp. 677-688
    • Moldoveanu, T.1    Liu, Q.2    Tocilj, A.3    Watson, M.H.4    Shore, G.5    Gehring, K.6
  • 5
    • 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
  • 6
    • 84907994244 scopus 로고    scopus 로고
    • Bak core and latch domains separate during activation, and freed core domains form symmetric homodimers
    • Brouwer JM, Westphal D, Dewson G, Robin AY, Uren RT, Bartolo R et al. Bak core and latch domains separate during activation, and freed core domains form symmetric homodimers. Mol Cell 2014; 55: 938-946.
    • (2014) Mol Cell , vol.55 , pp. 938-946
    • Brouwer, J.M.1    Westphal, D.2    Dewson, G.3    Robin, A.Y.4    Uren, R.T.5    Bartolo, R.6
  • 7
    • 84873307384 scopus 로고    scopus 로고
    • Bax crystal structures reveal how BH3 domains activate bax and nucleate its oligomerization to induce apoptosis
    • Czabotar PE, Westphal D, Dewson G, Ma S, Hockings C, Fairlie WD et al. Bax crystal structures reveal how BH3 domains activate bax and nucleate its oligomerization to induce apoptosis. Cell 2013; 152: 519-531.
    • (2013) Cell , vol.152 , pp. 519-531
    • Czabotar, P.E.1    Westphal, D.2    Dewson, G.3    Ma, S.4    Hockings, C.5    Fairlie, W.D.6
  • 8
    • 79960235245 scopus 로고    scopus 로고
    • Transient binding of an activator BH3 domain to the Bak BH3-binding groove initiates Bak oligomerization
    • Dai H, Smith A, Meng XW, Schneider PA, Pang YP, Kaufmann SH. Transient binding of an activator BH3 domain to the Bak BH3-binding groove initiates Bak oligomerization. J Cell Biol 2011; 194: 39-48.
    • (2011) J Cell Biol , vol.194 , pp. 39-48
    • Dai, H.1    Smith, A.2    Meng, X.W.3    Schneider, P.A.4    Pang, Y.P.5    Kaufmann, S.H.6
  • 11
    • 0036728834 scopus 로고    scopus 로고
    • Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics
    • Letai A, Bassik MC, Walensky LD, Sorcinelli MD, Weiler S, Korsmeyer SJ. Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. Cancer Cell 2002; 2: 183-192.
    • (2002) Cancer Cell , vol.2 , pp. 183-192
    • Letai, A.1    Bassik, M.C.2    Walensky, L.D.3    Sorcinelli, M.D.4    Weiler, S.5    Korsmeyer, S.J.6
  • 14
    • 43049105074 scopus 로고    scopus 로고
    • To trigger apoptosis Bak exposes its BH3 domain and homo-dimerizes via BH3:Grooove interactions
    • Dewson G, Kratina T, Sim HW, Puthalakath H, Adams JM, Colman PM et al. To trigger apoptosis Bak exposes its BH3 domain and homo-dimerizes via BH3:grooove interactions. Mol Cell 2008; 30: 369-380.
    • (2008) Mol Cell , vol.30 , pp. 369-380
    • Dewson, G.1    Kratina, T.2    Sim, H.W.3    Puthalakath, H.4    Adams, J.M.5    Colman, P.M.6
  • 15
    • 0035891057 scopus 로고    scopus 로고
    • Cellular damage signals promote sequential changes at the N-terminus and BH-1 domain of the pro-apoptotic protein Bak
    • Griffiths GJ, Corfe BM, Savory P, Leech S, Esposti MD, Hickman JA et al. Cellular damage signals promote sequential changes at the N-terminus and BH-1 domain of the pro-apoptotic protein Bak. Oncogene 2001; 20: 7668-7676.
    • (2001) Oncogene , vol.20 , pp. 7668-7676
    • Griffiths, G.J.1    Corfe, B.M.2    Savory, P.3    Leech, S.4    Esposti, M.D.5    Hickman, J.A.6
  • 16
    • 0031007644 scopus 로고    scopus 로고
    • Nonionic detergents induce dimerization among members of the Bcl-2 family
    • Hsu YT, Youle RJ. Nonionic detergents induce dimerization among members of the Bcl-2 family. J Biol Chem 1997; 272: 13829-13834.
    • (1997) J Biol Chem , vol.272 , pp. 13829-13834
    • Hsu, Y.T.1    Youle, R.J.2
  • 20
    • 21844464054 scopus 로고    scopus 로고
    • Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis
    • Annis MG, Soucie EL, Dlugosz PJ, Cruz-Aguado JA, Penn LZ, Leber B et al. Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis. EMBO J 2005; 24: 2096-2103.
    • (2005) EMBO J , vol.24 , pp. 2096-2103
    • Annis, M.G.1    Soucie, E.L.2    Dlugosz, P.J.3    Cruz-Aguado, J.A.4    Penn, L.Z.5    Leber, B.6
  • 21
    • 84893480044 scopus 로고    scopus 로고
    • Organization of the mitochondrial apoptotic BAK pore: Oligomerization of the Bak homodimers
    • Aluvila SM, Mandal T, Hustedt E, Fajer P, Choe JY, Oh KJ. Organization of the mitochondrial apoptotic BAK pore: oligomerization of the Bak homodimers. J Biol Chem 2014; 289: 2537-2551.
    • (2014) J Biol Chem , vol.289 , pp. 2537-2551
    • Aluvila, S.M.1    Mandal, T.2    Hustedt, E.3    Fajer, P.4    Choe, J.Y.5    Oh, K.J.6
  • 22
    • 77956523192 scopus 로고    scopus 로고
    • Conformational changes in BAK, a pore-forming proapoptotic Bcl-2 family member, upon membrane insertion and direct evidence for the existence of BH3-BH3 contact interface in BAK homo-oligomers
    • Oh KJ, Singh P, Lee K, Foss K, Lee S, Park M et al. Conformational changes in BAK, a pore-forming proapoptotic Bcl-2 family member, upon membrane insertion and direct evidence for the existence of BH3-BH3 contact interface in BAK homo-oligomers. J Biol Chem 2010; 285: 28924-28937.
    • (2010) J Biol Chem , vol.285 , pp. 28924-28937
    • Oh, K.J.1    Singh, P.2    Lee, K.3    Foss, K.4    Lee, S.5    Park, M.6
  • 23
    • 84907573467 scopus 로고    scopus 로고
    • Apoptotic pore formation is associated with in-plane insertion of Bak or Bax central helices into the mitochondrial outer membrane
    • Westphal D, Dewson G, Menard M, Frederick P, Iyer S, Bartolo R et al. Apoptotic pore formation is associated with in-plane insertion of Bak or Bax central helices into the mitochondrial outer membrane. Proc Natl Acad Sci USA 2014; 111: E4076-E4085.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. E4076-E4085
    • Westphal, D.1    Dewson, G.2    Menard, M.3    Frederick, P.4    Iyer, S.5    Bartolo, R.6
  • 24
    • 70449941949 scopus 로고    scopus 로고
    • Bak activation for apoptosis involves oligomerization of dimers via their alpha6 helices
    • Dewson G, Kratina T, Czabotar P, Day CL, Adams JM, Kluck RM. Bak activation for apoptosis involves oligomerization of dimers via their alpha6 helices. Mol Cell 2009; 36: 696-703.
    • (2009) Mol Cell , vol.36 , pp. 696-703
    • Dewson, G.1    Kratina, T.2    Czabotar, P.3    Day, C.L.4    Adams, J.M.5    Kluck, R.M.6
  • 25
    • 84883690023 scopus 로고    scopus 로고
    • Assembly of the Bak apoptotic pore: A critical role for the Bak protein alpha6 helix in the multimerization of homodimers during apoptosis
    • Ma S, Hockings C, Anwari K, Kratina T, Fennell S, Lazarou M et al. Assembly of the Bak apoptotic pore: a critical role for the Bak protein alpha6 helix in the multimerization of homodimers during apoptosis. J Biol Chem 2013; 288: 26027-26038.
    • (2013) J Biol Chem , vol.288 , pp. 26027-26038
    • Ma, S.1    Hockings, C.2    Anwari, K.3    Kratina, T.4    Fennell, S.5    Lazarou, M.6
  • 26
    • 84887840021 scopus 로고    scopus 로고
    • Proapoptotic Bax and Bak proteins form stable protein-permeable pores of tunable size
    • Bleicken S, Landeta O, Landajuela A, Basanez G, Garcia-Saez AJ. Proapoptotic Bax and Bak proteins form stable protein-permeable pores of tunable size. J Biol Chem 2013; 288: 33241-33252.
    • (2013) J Biol Chem , vol.288 , pp. 33241-33252
    • Bleicken, S.1    Landeta, O.2    Landajuela, A.3    Basanez, G.4    Garcia-Saez, A.J.5
  • 27
    • 0034523818 scopus 로고    scopus 로고
    • Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c
    • Korsmeyer SJ, Wei MC, Saito M, Weiler S, Oh KJ, Schlesinger PH. Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c. Cell Death Differ 2000; 7: 1166-1173.
    • (2000) Cell Death Differ , vol.7 , pp. 1166-1173
    • Korsmeyer, S.J.1    Wei, M.C.2    Saito, M.3    Weiler, S.4    Oh, K.J.5    Schlesinger, P.H.6
  • 28
    • 33845685298 scopus 로고    scopus 로고
    • Cytosolic factor- and TOM-independent import of C-tail-anchored mitochondrial outer membrane proteins
    • Setoguchi K, Otera H, Mihara K. Cytosolic factor- and TOM-independent import of C-tail-anchored mitochondrial outer membrane proteins. EMBO J 2006; 25: 5635-5647.
    • (2006) EMBO J , vol.25 , pp. 5635-5647
    • Setoguchi, K.1    Otera, H.2    Mihara, K.3
  • 29
    • 84911412568 scopus 로고    scopus 로고
    • Conformational rearrangements in the pro-apoptotic protein, Bax, as it inserts into mitochondria: A cellular death switch
    • Gahl RF, He Y, Yu S, Tjandra N. Conformational rearrangements in the pro-apoptotic protein, Bax, as it inserts into mitochondria: a cellular death switch. J Biol Chem 2014; 289: 32871-32882.
    • (2014) J Biol Chem , vol.289 , pp. 32871-32882
    • Gahl, R.F.1    He, Y.2    Yu, S.3    Tjandra, N.4
  • 30
    • 79953276389 scopus 로고    scopus 로고
    • Bcl-x(L) Retrotranslocates Bax from the mitochondria into the cytosol
    • Edlich F, Banerjee S, Suzuki M, Cleland MM, Arnoult D, Wang C et al. Bcl-x(L) Retrotranslocates Bax from the mitochondria into the cytosol. Cell 2011; 145: 104-116.
    • (2011) Cell , vol.145 , pp. 104-116
    • Edlich, F.1    Banerjee, S.2    Suzuki, M.3    Cleland, M.M.4    Arnoult, D.5    Wang, C.6
  • 32
    • 0033522391 scopus 로고    scopus 로고
    • Conformation of the Bax C-terminus regulates subcellular location and cell death
    • Nechushtan A, Smith CL, Hsu YT, Youle RJ. Conformation of the Bax C-terminus regulates subcellular location and cell death. EMBO J 1999; 18: 2330-2341.
    • (1999) EMBO J , vol.18 , pp. 2330-2341
    • Nechushtan, A.1    Smith, C.L.2    Hsu, Y.T.3    Youle, R.J.4
  • 33
    • 84858590503 scopus 로고    scopus 로고
    • Translocation of a Bak C-terminus mutant from cytosol to mitochondria to mediate cytochrome C release: Implications for Bak and Bax apoptotic function
    • Ferrer PE, Frederick P, Gulbis JM, Dewson G, Kluck RM. Translocation of a Bak C-terminus mutant from cytosol to mitochondria to mediate cytochrome C release: implications for Bak and Bax apoptotic function. PLoS One 2012; 7: e31510.
    • (2012) PLoS One , vol.7
    • Ferrer, P.E.1    Frederick, P.2    Gulbis, J.M.3    Dewson, G.4    Kluck, R.M.5
  • 36
    • 73849084212 scopus 로고    scopus 로고
    • VDAC2 is required for truncated BID-induced mitochondrial apoptosis by recruiting BAK to the mitochondria
    • Roy SS, Ehrlich AM, Craigen WJ, Hajnoczky G. VDAC2 is required for truncated BID-induced mitochondrial apoptosis by recruiting BAK to the mitochondria. EMBO Rep 2009; 10: 1341-1347.
    • (2009) EMBO Rep , vol.10 , pp. 1341-1347
    • Roy, S.S.1    Ehrlich, A.M.2    Craigen, W.J.3    Hajnoczky, G.4
  • 38
    • 85027930466 scopus 로고    scopus 로고
    • Bax targets mitochondria by distinct mechanisms before or during apoptotic cell death: A requirement for VDAC2 or Bak for efficient Bax apoptotic function
    • Ma SB, Nguyen TN, Tan I, Ninnis R, Iyer S, Stroud DA et al. Bax targets mitochondria by distinct mechanisms before or during apoptotic cell death: a requirement for VDAC2 or Bak for efficient Bax apoptotic function. Cell Death Differ 2014; 21: 1925-1935.
    • (2014) Cell Death Differ , vol.21 , pp. 1925-1935
    • Ma, S.B.1    Nguyen, T.N.2    Tan, I.3    Ninnis, R.4    Iyer, S.5    Stroud, D.A.6
  • 40
    • 0035928830 scopus 로고    scopus 로고
    • Conformation of the C-terminal domain of the pro-apoptotic protein Bax and mutants and its interaction with membranes
    • del Mar Martinez-Senac M, Corbalan-Garcia S, Gomez-Fernandez JC. Conformation of the C-terminal domain of the pro-apoptotic protein Bax and mutants and its interaction with membranes. Biochemistry 2001; 40: 9983-9992.
    • (2001) Biochemistry , vol.40 , pp. 9983-9992
    • Del Mar Martinez-Senac, M.1    Corbalan-Garcia, S.2    Gomez-Fernandez, J.C.3
  • 41
    • 0036220239 scopus 로고    scopus 로고
    • The structure of the C-terminal domain of the pro-apoptotic protein Bak and its interaction with model membranes
    • Martinez-Senac M, Corbalan-Garcia S, Gomez-Fernandez JC. The structure of the C-terminal domain of the pro-apoptotic protein Bak and its interaction with model membranes. Biophys J 2002; 82: 233-243.
    • (2002) Biophys J , vol.82 , pp. 233-243
    • Martinez-Senac, M.1    Corbalan-Garcia, S.2    Gomez-Fernandez, J.C.3
  • 43
    • 84869434589 scopus 로고    scopus 로고
    • Molecular basis for membrane pore formation by Bax protein carboxyl terminus
    • Tatulian SA, Garg P, Nemec KN, Chen B, Khaled AR. Molecular basis for membrane pore formation by Bax protein carboxyl terminus. Biochemistry 2012; 51: 9406-9419.
    • (2012) Biochemistry , vol.51 , pp. 9406-9419
    • Tatulian, S.A.1    Garg, P.2    Nemec, K.N.3    Chen, B.4    Khaled, A.R.5
  • 44
    • 51549103252 scopus 로고    scopus 로고
    • The interaction of the Bax C-terminal domain with negatively charged lipids modifies the secondary structure and changes its way of insertion into membranes
    • Ausili A, Torrecillas A, Martinez-Senac MM, Corbalan-Garcia S, Gomez-Fernandez JC. The interaction of the Bax C-terminal domain with negatively charged lipids modifies the secondary structure and changes its way of insertion into membranes. J Struct Biol 2008; 164: 146-152.
    • (2008) J Struct Biol , vol.164 , pp. 146-152
    • Ausili, A.1    Torrecillas, A.2    Martinez-Senac, M.M.3    Corbalan-Garcia, S.4    Gomez-Fernandez, J.C.5
  • 45
    • 68749086032 scopus 로고    scopus 로고
    • The interaction of the Bax C-terminal domain with membranes is influenced by the presence of negatively charged phospholipids
    • Ausili A, de Godos A, Torrecillas A, Corbalan-Garcia S, Gomez-Fernandez JC. The interaction of the Bax C-terminal domain with membranes is influenced by the presence of negatively charged phospholipids. Biochim Biophys Acta 2009; 1788: 1924-1932.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1924-1932
    • Ausili, A.1    De Godos, A.2    Torrecillas, A.3    Corbalan-Garcia, S.4    Gomez-Fernandez, J.C.5
  • 47
    • 84870314860 scopus 로고    scopus 로고
    • Transmembrane pore formation by the carboxyl terminus of Bax protein
    • Garg P, Nemec KN, Khaled AR, Tatulian SA. Transmembrane pore formation by the carboxyl terminus of Bax protein. Biochim Biophys Acta 2013; 1828: 732-742.
    • (2013) Biochim Biophys Acta , vol.1828 , pp. 732-742
    • Garg, P.1    Nemec, K.N.2    Khaled, A.R.3    Tatulian, S.A.4
  • 50
    • 2442551481 scopus 로고    scopus 로고
    • During apoptosis bcl-2 changes membrane topology at both the endoplasmic reticulum and mitochondria
    • Kim PK, Annis MG, Dlugosz PJ, Leber B, Andrews DW. During apoptosis bcl-2 changes membrane topology at both the endoplasmic reticulum and mitochondria. Mol Cell 2004; 14: 523-529.
    • (2004) Mol Cell , vol.14 , pp. 523-529
    • Kim, P.K.1    Annis, M.G.2    Dlugosz, P.J.3    Leber, B.4    Andrews, D.W.5
  • 52
    • 34250792303 scopus 로고    scopus 로고
    • Use of site-directed cysteine and disulfide chemistry to probe protein structure and dynamics: Applications to soluble and transmembrane receptors of bacterial chemotaxis
    • Bass RB, Butler SL, Chervitz SA, Gloor SL, Falke JJ. Use of site-directed cysteine and disulfide chemistry to probe protein structure and dynamics: applications to soluble and transmembrane receptors of bacterial chemotaxis. Methods Enzymol 2007; 423: 25-51.
    • (2007) Methods Enzymol , vol.423 , pp. 25-51
    • Bass, R.B.1    Butler, S.L.2    Chervitz, S.A.3    Gloor, S.L.4    Falke, J.J.5
  • 54
    • 36448936085 scopus 로고    scopus 로고
    • An artificial mtochondrial tail signal/anchor sequence confirms a requirement for moderate hydrophobicity for targeting
    • Wattenberg. An artificial mtochondrial tail signal/anchor sequence confirms a requirement for moderate hydrophobicity for targeting. Biosci Rep 2007; 27: 385-401.
    • (2007) Biosci Rep , vol.27 , pp. 385-401
    • Wattenberg1
  • 56
    • 0026686793 scopus 로고
    • Glycophorin A dimerization is driven by specific interactions between transmembrane alpha-helices
    • Lemmon MA, Flanagan JM, Hunt JF, Adair BD, Bormann BJ, Dempsey CE et al. Glycophorin A dimerization is driven by specific interactions between transmembrane alpha-helices. J Biol Chem 1992; 267: 7683-7689.
    • (1992) J Biol Chem , vol.267 , pp. 7683-7689
    • Lemmon, M.A.1    Flanagan, J.M.2    Hunt, J.F.3    Adair, B.D.4    Bormann, B.J.5    Dempsey, C.E.6
  • 57
    • 67049171187 scopus 로고    scopus 로고
    • Structural basis for dimerization of the BNIP3 transmembrane domain
    • Sulistijo ES, Mackenzie KR. Structural basis for dimerization of the BNIP3 transmembrane domain. Biochemistry 2009; 48: 5106-5120.
    • (2009) Biochemistry , vol.48 , pp. 5106-5120
    • Sulistijo, E.S.1    Mackenzie, K.R.2
  • 59
    • 1842474296 scopus 로고    scopus 로고
    • Structure of rat monoamine oxidase A and its specific recognitions for substrates and inhibitors
    • Ma J, Yoshimura M, Yamashita E, Nakagawa A, Ito A, Tsukihara T. Structure of rat monoamine oxidase A and its specific recognitions for substrates and inhibitors. J Mol Biol 2004; 338: 103-114.
    • (2004) J Mol Biol , vol.338 , pp. 103-114
    • Ma, J.1    Yoshimura, M.2    Yamashita, E.3    Nakagawa, A.4    Ito, A.5    Tsukihara, T.6
  • 61
    • 0242579164 scopus 로고    scopus 로고
    • The solution structure of human mitochondria fission protein Fis1 reveals a novel TPR-like helix bundle
    • Suzuki M, Jeong SY, Karbowski M, Youle RJ, Tjandra N. The solution structure of human mitochondria fission protein Fis1 reveals a novel TPR-like helix bundle. J Mol Biol 2003; 334: 445-458.
    • (2003) J Mol Biol , vol.334 , pp. 445-458
    • Suzuki, M.1    Jeong, S.Y.2    Karbowski, M.3    Youle, R.J.4    Tjandra, N.5
  • 62
    • 58149267953 scopus 로고    scopus 로고
    • X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation
    • Bocquet N, Nury H, Baaden M, Le Poupon C, Changeux JP, Delarue M et al. X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation. Nature 2009; 457: 111-114.
    • (2009) Nature , vol.457 , pp. 111-114
    • Bocquet, N.1    Nury, H.2    Baaden, M.3    Le Poupon, C.4    Changeux, J.P.5    Delarue, M.6
  • 63
    • 66649132042 scopus 로고    scopus 로고
    • The structure of a cytolytic alpha-helical toxin pore reveals its assembly mechanism
    • Mueller M, Grauschopf U, Maier T, Glockshuber R, Ban N. The structure of a cytolytic alpha-helical toxin pore reveals its assembly mechanism. Nature 2009; 459: 726-730.
    • (2009) Nature , vol.459 , pp. 726-730
    • Mueller, M.1    Grauschopf, U.2    Maier, T.3    Glockshuber, R.4    Ban, N.5
  • 65
    • 84862667284 scopus 로고    scopus 로고
    • micro-Calpain conversion of antiapoptotic Bfl-1 (BCL2A1) into a prodeath factor reveals two distinct alpha-helices inducing mitochondria-mediated apoptosis
    • Valero JG, Cornut-Thibaut A, Juge R, Debaud AL, Gimenez D, Gillet G et al. micro-Calpain conversion of antiapoptotic Bfl-1 (BCL2A1) into a prodeath factor reveals two distinct alpha-helices inducing mitochondria-mediated apoptosis. PLoS One 2012; 7: e38620.
    • (2012) PLoS One , vol.7
    • Valero, J.G.1    Cornut-Thibaut, A.2    Juge, R.3    Debaud, A.L.4    Gimenez, D.5    Gillet, G.6
  • 66
    • 79951826260 scopus 로고    scopus 로고
    • Bax-derived membrane-active peptides act as potent and direct inducers of apoptosis in cancer cells
    • Valero JG, Sancey L, Kucharczak J, Guillemin Y, Gimenez D, Prudent J et al. Bax-derived membrane-active peptides act as potent and direct inducers of apoptosis in cancer cells. J Cell Sci 2011; 124: 556-564.
    • (2011) J Cell Sci , vol.124 , pp. 556-564
    • Valero, J.G.1    Sancey, L.2    Kucharczak, J.3    Guillemin, Y.4    Gimenez, D.5    Prudent, J.6
  • 68
    • 0026489631 scopus 로고
    • Thermal motions of surface alpha-helices in the D-galactose chemosensory receptor. Detection by disulfide trapping
    • Careaga CL, Falke JJ. Thermal motions of surface alpha-helices in the D-galactose chemosensory receptor. Detection by disulfide trapping. J Mol Biol 1992; 226: 1219-1235.
    • (1992) J Mol Biol , vol.226 , pp. 1219-1235
    • Careaga, C.L.1    Falke, J.J.2
  • 69
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • Cole C, Barber JD, Barton GJ. The Jpred 3 secondary structure prediction server. Nucleic Acids Res 2008; 36: W197-W201.
    • (2008) Nucleic Acids Res , vol.36 , pp. W197-W201
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 70
    • 84941177784 scopus 로고    scopus 로고
    • Tripos International, St. Louis, MO, USA
    • Tripos Inc. SYBYL-X 1.2, Tripos International, St. Louis, MO, USA. 2005. http://www.certara.com.
    • (2005) SYBYL-X 1.2
    • Tripos Inc.1
  • 71
    • 0342980358 scopus 로고    scopus 로고
    • Biochemical and genetic evidence for three transmembrane domains in the class I holin, lambda S
    • Grundling A, Blasi U, Young R. Biochemical and genetic evidence for three transmembrane domains in the class I holin, lambda S. J Biol Chem 2000; 275: 769-776.
    • (2000) J Biol Chem , vol.275 , pp. 769-776
    • Grundling, A.1    Blasi, U.2    Young, R.3
  • 72
    • 0035895421 scopus 로고    scopus 로고
    • Non-alpha-helical elements modulate polytopic membrane protein architecture
    • Riek RP, Rigoutsos I, Novotny J, Graham RM. Non-alpha-helical elements modulate polytopic membrane protein architecture. J Mol Biol 2001; 306: 349-362.
    • (2001) J Mol Biol , vol.306 , pp. 349-362
    • Riek, R.P.1    Rigoutsos, I.2    Novotny, J.3    Graham, R.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.