메뉴 건너뛰기




Volumn 23, Issue 1, 2015, Pages 139-148

BAX-induced apoptosis can be initiated through a conformational selection mechanism

Author keywords

[No Author keywords available]

Indexed keywords

BH3 PROTEIN; CYTOCHROME C; LIGAND; MONOMER; OLIGOMER; PROTEIN BAX; BAX PROTEIN (53-86); ONCOPROTEIN; PEPTIDE FRAGMENT; PROTEIN BINDING;

EID: 84920943487     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2014.10.016     Document Type: Article
Times cited : (30)

References (37)
  • 2
    • 0035853811 scopus 로고    scopus 로고
    • Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells
    • B. Antonsson, S. Montessuit, B. Sanchez, and J.C. Martinou Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells J. Biol. Chem. 276 2001 11615 11623
    • (2001) J. Biol. Chem. , vol.276 , pp. 11615-11623
    • Antonsson, B.1    Montessuit, S.2    Sanchez, B.3    Martinou, J.C.4
  • 3
    • 36849095428 scopus 로고    scopus 로고
    • Substitutions of potentially phosphorylatable serine residues of Bax reveal how they may regulate its interaction with mitochondria
    • H. Arokium, H. Ouerfelli, G. Velours, N. Camougrand, F.M. Vallette, and S. Manon Substitutions of potentially phosphorylatable serine residues of Bax reveal how they may regulate its interaction with mitochondria J. Biol. Chem. 282 2007 35104 35112
    • (2007) J. Biol. Chem. , vol.282 , pp. 35104-35112
    • Arokium, H.1    Ouerfelli, H.2    Velours, G.3    Camougrand, N.4    Vallette, F.M.5    Manon, S.6
  • 5
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • D.D. Boehr, R. Nussinov, and P.E. Wright The role of dynamic conformational ensembles in biomolecular recognition Nat. Chem. Biol. 5 2009 789 796
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 6
    • 34250841296 scopus 로고    scopus 로고
    • Measuring distances by pulsed dipolar ESR spectroscopy: Spin-labeled histidine kinases
    • P.P. Borbat, and J.H. Freed Measuring distances by pulsed dipolar ESR spectroscopy: spin-labeled histidine kinases Methods Enzymol. 423 2007 52 116
    • (2007) Methods Enzymol. , vol.423 , pp. 52-116
    • Borbat, P.P.1    Freed, J.H.2
  • 8
    • 11344285129 scopus 로고    scopus 로고
    • The determination of pair distance distributions by pulsed ESR using Tikhonov regularization
    • Y.W. Chiang, P.P. Borbat, and J.H. Freed The determination of pair distance distributions by pulsed ESR using Tikhonov regularization J. Magn. Reson. 172 2005 279 295
    • (2005) J. Magn. Reson. , vol.172 , pp. 279-295
    • Chiang, Y.W.1    Borbat, P.P.2    Freed, J.H.3
  • 9
    • 28044472953 scopus 로고    scopus 로고
    • Maximum entropy: A complement to Tikhonov regularization for determination of pair distance distributions by pulsed ESR
    • Y.W. Chiang, P.P. Borbat, and J.H. Freed Maximum entropy: a complement to Tikhonov regularization for determination of pair distance distributions by pulsed ESR J. Magn. Reson. 177 2005 184 196
    • (2005) J. Magn. Reson. , vol.177 , pp. 184-196
    • Chiang, Y.W.1    Borbat, P.P.2    Freed, J.H.3
  • 11
    • 79953192533 scopus 로고    scopus 로고
    • Mutation to Bax beyond the BH3 domain disrupts interactions with pro-survival proteins and promotes apoptosis
    • P.E. Czabotar, E.F. Lee, G.V. Thompson, A.Z. Wardak, W.D. Fairlie, and P.M. Colman Mutation to Bax beyond the BH3 domain disrupts interactions with pro-survival proteins and promotes apoptosis J. Biol. Chem. 286 2011 7123 7131
    • (2011) J. Biol. Chem. , vol.286 , pp. 7123-7131
    • Czabotar, P.E.1    Lee, E.F.2    Thompson, G.V.3    Wardak, A.Z.4    Fairlie, W.D.5    Colman, P.M.6
  • 16
    • 78149449341 scopus 로고    scopus 로고
    • BH3-triggered structural reorganization drives the activation of proapoptotic BAX
    • E. Gavathiotis, D.E. Reyna, M.L. Davis, G.H. Bird, and L.D. Walensky BH3-triggered structural reorganization drives the activation of proapoptotic BAX Mol. Cell 40 2010 481 492
    • (2010) Mol. Cell , vol.40 , pp. 481-492
    • Gavathiotis, E.1    Reyna, D.E.2    Davis, M.L.3    Bird, G.H.4    Walensky, L.D.5
  • 17
    • 84858332577 scopus 로고    scopus 로고
    • Effect of freezing conditions on distances and their distributions derived from Double Electron Resonance (DEER): A study of doubly-spin-labeled T4 lysozyme
    • E.R. Georgieva, A.S. Roy, V.M. Grigoryants, P.P. Borbat, K.A. Earle, C.P. Scholes, and J.H. Freed Effect of freezing conditions on distances and their distributions derived from Double Electron Resonance (DEER): a study of doubly-spin-labeled T4 lysozyme J. Magn. Reson. 216 2012 69 77
    • (2012) J. Magn. Reson. , vol.216 , pp. 69-77
    • Georgieva, E.R.1    Roy, A.S.2    Grigoryants, V.M.3    Borbat, P.P.4    Earle, K.A.5    Scholes, C.P.6    Freed, J.H.7
  • 19
    • 84857917265 scopus 로고    scopus 로고
    • MtsslWizard: In Silico Spin-Labeling and Generation of Distance Distributions in PyMOL
    • G. Hagelueken, R. Ward, J.H. Naismith, and O. Schiemann MtsslWizard: In Silico Spin-Labeling and Generation of Distance Distributions in PyMOL Appl. Magn. Reson. 42 2012 377 391
    • (2012) Appl. Magn. Reson. , vol.42 , pp. 377-391
    • Hagelueken, G.1    Ward, R.2    Naismith, J.H.3    Schiemann, O.4
  • 20
    • 80052158470 scopus 로고    scopus 로고
    • Mesopores provide an amorphous state suitable for studying biomolecular structures at cryogenic temperatures
    • Y.W. Huang, Y.C. Lai, C.J. Tsai, and Y.W. Chiang Mesopores provide an amorphous state suitable for studying biomolecular structures at cryogenic temperatures Proc. Natl. Acad. Sci. USA 108 2011 14145 14150
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 14145-14150
    • Huang, Y.W.1    Lai, Y.C.2    Tsai, C.J.3    Chiang, Y.W.4
  • 21
    • 0038148710 scopus 로고    scopus 로고
    • Conformational diversity and protein evolution - A 60-year-old hypothesis revisited
    • L.C. James, and D.S. Tawfik Conformational diversity and protein evolution - a 60-year-old hypothesis revisited Trends Biochem. Sci. 28 2003 361 368
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 361-368
    • James, L.C.1    Tawfik, D.S.2
  • 22
    • 84859888767 scopus 로고    scopus 로고
    • DEER distance measurements on proteins
    • G. Jeschke DEER distance measurements on proteins Annu. Rev. Phys. Chem. 63 2012 419 446
    • (2012) Annu. Rev. Phys. Chem. , vol.63 , pp. 419-446
    • Jeschke, G.1
  • 23
    • 0030843113 scopus 로고    scopus 로고
    • An automated approach for defining core atoms and domains in an ensemble of NMR-derived protein structures
    • L.A. Kelley, S.P. Gardner, and M.J. Sutcliffe An automated approach for defining core atoms and domains in an ensemble of NMR-derived protein structures Protein Eng. 10 1997 737 741
    • (1997) Protein Eng. , vol.10 , pp. 737-741
    • Kelley, L.A.1    Gardner, S.P.2    Sutcliffe, M.J.3
  • 24
    • 84887584800 scopus 로고    scopus 로고
    • Concurrent observation of bulk and protein hydration water by spin-label ESR under nanoconfinement
    • Y.H. Kuo, Y.R. Tseng, and Y.W. Chiang Concurrent observation of bulk and protein hydration water by spin-label ESR under nanoconfinement Langmuir 29 2013 13865 13872
    • (2013) Langmuir , vol.29 , pp. 13865-13872
    • Kuo, Y.H.1    Tseng, Y.R.2    Chiang, Y.W.3
  • 25
    • 0033522391 scopus 로고    scopus 로고
    • Conformation of the Bax C-terminus regulates subcellular location and cell death
    • A. Nechushtan, C.L. Smith, Y.T. Hsu, and R.J. Youle Conformation of the Bax C-terminus regulates subcellular location and cell death EMBO J. 18 1999 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
  • 27
    • 49649084492 scopus 로고    scopus 로고
    • Dynamic energy landscape view of coupled binding and protein conformational change: Induced-fit versus population-shift mechanisms
    • K. Okazaki, and S. Takada Dynamic energy landscape view of coupled binding and protein conformational change: induced-fit versus population-shift mechanisms Proc. Natl. Acad. Sci. USA 105 2008 11182 11187
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 11182-11187
    • Okazaki, K.1    Takada, S.2
  • 28
    • 0034132251 scopus 로고    scopus 로고
    • Dead-time free measurement of dipole-dipole interactions between electron spins
    • M. Pannier, S. Veit, A. Godt, G. Jeschke, and H.W. Spiess Dead-time free measurement of dipole-dipole interactions between electron spins J. Magn. Reson. 142 2000 331 340
    • (2000) J. Magn. Reson. , vol.142 , pp. 331-340
    • Pannier, M.1    Veit, S.2    Godt, A.3    Jeschke, G.4    Spiess, H.W.5
  • 30
    • 0037452957 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid prevents Bax-induced membrane perturbation and cytochrome C release in isolated mitochondria
    • C.M.P. Rodrigues, S. Solá, J.C. Sharpe, J.J.G. Moura, and C.J. Steer Tauroursodeoxycholic acid prevents Bax-induced membrane perturbation and cytochrome C release in isolated mitochondria Biochemistry 42 2003 3070 3080
    • (2003) Biochemistry , vol.42 , pp. 3070-3080
    • Rodrigues, C.M.P.1    Solá, S.2    Sharpe, J.C.3    Moura, J.J.G.4    Steer, C.J.5
  • 31
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and intracellular localization
    • M. Suzuki, R.J. Youle, and N. Tjandra Structure of Bax: coregulation of dimer formation and intracellular localization Cell 103 2000 645 654
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 32
    • 64849101493 scopus 로고    scopus 로고
    • Protein dynamism and evolvability
    • N. Tokuriki, and D.S. Tawfik Protein dynamism and evolvability Science 324 2009 203 207
    • (2009) Science , vol.324 , pp. 203-207
    • Tokuriki, N.1    Tawfik, D.S.2
  • 33
    • 47249105254 scopus 로고    scopus 로고
    • Bax targeting to mitochondria occurs via both tail anchor-dependent and -independent mechanisms
    • A.J. Valentijn, J.P. Upton, N. Bates, and A.P. Gilmore Bax targeting to mitochondria occurs via both tail anchor-dependent and -independent mechanisms Cell Death Differ. 15 2008 1243 1254
    • (2008) Cell Death Differ. , vol.15 , pp. 1243-1254
    • Valentijn, A.J.1    Upton, J.P.2    Bates, N.3    Gilmore, A.P.4
  • 35
    • 82355181105 scopus 로고    scopus 로고
    • BAX unleashed: The biochemical transformation of an inactive cytosolic monomer into a toxic mitochondrial pore
    • L.D. Walensky, and E. Gavathiotis BAX unleashed: the biochemical transformation of an inactive cytosolic monomer into a toxic mitochondrial pore Trends Biochem. Sci. 36 2011 642 652
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 642-652
    • Walensky, L.D.1    Gavathiotis, E.2
  • 37
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • R.J. Youle, and A. Strasser The BCL-2 protein family: opposing activities that mediate cell death Nat. Rev. Mol. Cell Biol. 9 2008 47 59
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.