메뉴 건너뛰기




Volumn 20, Issue 12, 2011, Pages 2035-2046

Insights into the structural stability of Bax from molecular dynamics simulations at high temperatures

Author keywords

Apoptosis; Bax; Bcl 2 family; Electrostatic interactions; MD simulations; Protein stability; Thermal unfolding

Indexed keywords

PROTEIN BAX;

EID: 81755172092     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.740     Document Type: Article
Times cited : (12)

References (71)
  • 1
    • 77952576788 scopus 로고    scopus 로고
    • Cell death mechanisms: Cross-talk and role in disease
    • Zhivotovsky B, Orrenius S (2010) Cell death mechanisms: cross-talk and role in disease. Exp Cell Res 316:1374-1383.
    • (2010) Exp Cell Res , vol.316 , pp. 1374-1383
    • Zhivotovsky, B.1    Orrenius, S.2
  • 2
    • 70549107710 scopus 로고    scopus 로고
    • Mitochondrial cell death effectors
    • Brenner D, Mak TW (2009) Mitochondrial cell death effectors. Curr Opin Cell Biol 21:871-877.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 871-877
    • Brenner, D.1    Mak, T.W.2
  • 4
    • 1442359844 scopus 로고    scopus 로고
    • Bcl-2 family members and disease
    • Sorenson CM (2004) Bcl-2 family members and disease. Biochim Biophys Acta 1644:169-177.
    • (2004) Biochim Biophys Acta , vol.1644 , pp. 169-177
    • Sorenson, C.M.1
  • 5
    • 73349091842 scopus 로고    scopus 로고
    • The role of mitochondria in apoptosis
    • Wang C, Youle RJ (2009) The role of mitochondria in apoptosis. Annu Rev Genet 43:95-118.
    • (2009) Annu Rev Genet , vol.43 , pp. 95-118
    • Wang, C.1    Youle, R.J.2
  • 8
    • 77956924838 scopus 로고    scopus 로고
    • Targeting Bcl-2-mediated cell death as a novel therapy in pancreatic cancer
    • Muilenburg DJ, Coates JM, Virudachalam S, Bold RJ (2010) Targeting Bcl-2-mediated cell death as a novel therapy in pancreatic cancer. J Surg Res 163:276-281.
    • (2010) J Surg Res , vol.163 , pp. 276-281
    • Muilenburg, D.J.1    Coates, J.M.2    Virudachalam, S.3    Bold, R.J.4
  • 9
    • 64849113485 scopus 로고    scopus 로고
    • Control of mitochondrial apoptosis by the Bcl-2 family
    • Brunelle JK, Letai A (2009) Control of mitochondrial apoptosis by the Bcl-2 family. J Cell Sci 122:437.
    • (2009) J Cell Sci , vol.122 , pp. 437
    • Brunelle, J.K.1    Letai, A.2
  • 10
    • 78449249926 scopus 로고    scopus 로고
    • Bcl-2 family-regulated apoptosis in health and disease
    • Dewson G, Kluck RM (2010) Bcl-2 family-regulated apoptosis in health and disease. Cell Health Cytoskelet 2:9-22.
    • (2010) Cell Health Cytoskelet , vol.2 , pp. 9-22
    • Dewson, G.1    Kluck, R.M.2
  • 13
    • 33947727119 scopus 로고    scopus 로고
    • Structure of M11L: A myxoma virus structural homolog of the apoptosis inhibitor, Bcl-2
    • DOI 10.1110/ps.062720107
    • Douglas AE, Corbett KD, Berger JM, McFadden G, Handel TM (2007) Structure of M11L: a myxoma virus structural homolog of the apoptosis inhibitor, Bcl-2. Protein Sci 16:695-703. (Pubitemid 46506998)
    • (2007) Protein Science , vol.16 , Issue.4 , pp. 695-703
    • Douglas, A.E.1    Corbett, K.D.2    Berger, J.M.3    Mcfadden, G.4    Handel, T.M.5
  • 14
    • 77951665317 scopus 로고    scopus 로고
    • Ceramide and activated Bax act synergistically to permeabilize the mitochondrial outer membrane
    • Ganesan V, Perera MN, Colombini D, Datskovskiy D, Chadha K, Colombini M (2010) Ceramide and activated Bax act synergistically to permeabilize the mitochondrial outer membrane. Apoptosis 15:553-562.
    • (2010) Apoptosis , vol.15 , pp. 553-562
    • Ganesan, V.1    Perera, M.N.2    Colombini, D.3    Datskovskiy, D.4    Chadha, K.5    Colombini, M.6
  • 15
    • 70349524664 scopus 로고    scopus 로고
    • Cardiolipin acts as a mitochondrial signalling platform to launch apoptosis
    • Schug ZT, Gottlieb E (2009) Cardiolipin acts as a mitochondrial signalling platform to launch apoptosis. Biochim Biophys Acta 1788:2022-2031.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 2022-2031
    • Schug, Z.T.1    Gottlieb, E.2
  • 17
    • 77957551452 scopus 로고    scopus 로고
    • Bax is upregulated by p53 signal pathway in the SPE B-induced apoptosis
    • Lee WT, Chang CW (2010) Bax is upregulated by p53 signal pathway in the SPE B-induced apoptosis. Mol Cell Biochem 343:271-279.
    • (2010) Mol Cell Biochem , vol.343 , pp. 271-279
    • Lee, W.T.1    Chang, C.W.2
  • 18
    • 76749131517 scopus 로고    scopus 로고
    • Evaluating bistability of Bax activation switch
    • Sun T, Lin X, Wei Y, Xu Y, Shen P (2010) Evaluating bistability of Bax activation switch. FEBS Lett 584:954-960.
    • (2010) FEBS Lett , vol.584 , pp. 954-960
    • Sun, T.1    Lin, X.2    Wei, Y.3    Xu, Y.4    Shen, P.5
  • 19
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis
    • Hsu YT, Wolter KG, Youle RJ (1997) Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis. Proc Natl Acad Sci USA 94:3668-3672.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3668-3672
    • Hsu, Y.T.1    Wolter, K.G.2    Youle, R.J.3
  • 20
    • 68949099606 scopus 로고    scopus 로고
    • Mitochondrial outer-membrane permeabilization and remodelling in apoptosis
    • Jourdain A, Martinou JC (2009) Mitochondrial outer-membrane permeabilization and remodelling in apoptosis. Int J Biochem Cell Biol 41:1884-1889.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 1884-1889
    • Jourdain, A.1    Martinou, J.C.2
  • 21
    • 33745933456 scopus 로고    scopus 로고
    • The Bax pore in liposomes, Biophysics
    • DOI 10.1038/sj.cdd.4401991, PII 4401991
    • Schlesinger PH, Saito M (2006) The Bax pore in liposomes, biophysics. Cell Death Differ 13:1403-1408. (Pubitemid 44057476)
    • (2006) Cell Death and Differentiation , vol.13 , Issue.8 , pp. 1403-1408
    • Schlesinger, P.H.1    Saito, M.2
  • 22
    • 56249132688 scopus 로고    scopus 로고
    • Structure of transmembrane pore induced by Bax-derived peptide: Evidence for lipidic pores
    • Qian S, Wang W, Yang L, Huang HW (2008) Structure of transmembrane pore induced by Bax-derived peptide: evidence for lipidic pores. Proc Natl Acad Sci USA 105:17379-17383.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 17379-17383
    • Qian, S.1    Wang, W.2    Yang, L.3    Huang, H.W.4
  • 23
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and intracellular localization
    • Suzuki M, Youle RJ, Tjandra N (2000) Structure of Bax: coregulation of dimer formation and intracellular localization. Cell 103:645-654.
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 24
    • 43949128394 scopus 로고    scopus 로고
    • Prediction of a putative functional region in the human bax protein by computational analysis
    • Sánchez-Aguilar M, Marchat LA, Zamorano A (2007) Prediction of a Putative functional region in the human Bax protein by computational analysis. Am J Infect Dis 3:68-75. (Pubitemid 351699391)
    • (2007) American Journal of Infectious Diseases , vol.3 , Issue.2 , pp. 68-75
    • Sanchez-Aguilar, M.1    Marchat, L.A.2    Zamorano, A.3
  • 25
    • 9744244990 scopus 로고    scopus 로고
    • The first a helix of Bax plays a necessary role in its ligand-induced activation by the BH3-only proteins bid and PUMA
    • DOI 10.1016/j.molcel.2004.10.028, PII S1097276504006537
    • Cartron PF, Gallenne T, Bougras G, Gautier F, Manero F, Vusio P, Meah K, Vallette FM, Juin P (2004) The First a-helix of Bax plays a necessary role in its ligand-induced activation by the BH3-only proteins bid and PUMA. Mol Cell 16:807-818. (Pubitemid 39586538)
    • (2004) Molecular Cell , vol.16 , Issue.5 , pp. 807-818
    • Cartron, P.-F.1    Gallenne, T.2    Bougras, G.3    Gautier, F.4    Manero, F.5    Vusio, P.6    Meflah, K.7    Vallette, F.M.8    Juin, P.9
  • 28
    • 63949086330 scopus 로고    scopus 로고
    • Conformational changes and protein stability of the pro-apoptotic protein Bax
    • Bleicken S, Zeth K (2009) Conformational changes and protein stability of the pro-apoptotic protein Bax. J Bioenerg Biomembr 41:29-40.
    • (2009) J Bioenerg Biomembr , vol.41 , pp. 29-40
    • Bleicken, S.1    Zeth, K.2
  • 29
    • 34247533289 scopus 로고    scopus 로고
    • Bax activation and mitochondrial insertion during apoptosis
    • DOI 10.1007/s10495-007-0749-1, Special Issue on Mitochondria in Apoptosis
    • Lalier L, Cartron PF, Juin P, Nedelkina S, Manon S, Bechinger B, Vallette FM (2007) Bax activation and mitochondrial insertion during apoptosis. Apoptosis 12:887-896. (Pubitemid 46653297)
    • (2007) Apoptosis , vol.12 , Issue.5 , pp. 887-896
    • Lalier, L.1    Cartron, P.-F.2    Juin, P.3    Nedelkina, S.4    Manon, S.5    Bechinger, B.6    Vallette, F.M.7
  • 30
    • 33845982932 scopus 로고    scopus 로고
    • A membrane-targeted BID BCL-2 homology 3 peptide is sufficient for high potency activation of BAX in vitro
    • DOI 10.1074/jbc.M602341200
    • Oh KJ, Barbuto S, Pitter K, Morash J, Walensky LD, Korsmeyer SJ (2006) A membrane-targeted BID BCL-2 homology 3 peptide is sufficient for high potency activation of BAX in vitro. J Biol Chem 281:36999-37008. (Pubitemid 46042170)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.48 , pp. 36999-37008
    • Kyoung, J.O.1    Barbuto, S.2    Pitter, K.3    Morash, J.4    Walensky, L.D.5    Korsmeyer, S.J.6
  • 31
    • 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 (2008) Anti-apoptotic Bcl-XL protein in complex with BH3 peptides of pro-apoptotic Bak, Bad, and Bim proteins: comparative molecular dynamics simulations. Proteins: Struct Funct Bioinf 73:492-514.
    • (2008) Proteins: Struct Funct Bioinf , vol.73 , pp. 492-514
    • Lama, D.1    Sankararamakrishnan, R.2
  • 32
    • 77249169837 scopus 로고    scopus 로고
    • Mcl-1-Bim complexes accommodate surprising point mutations via minor structural changes
    • Fire E, Gullá SV, Grant RA, Keating AE (2010) Mcl-1-Bim complexes accommodate surprising point mutations via minor structural changes. Protein Sci 19:507-519.
    • (2010) Protein Sci , vol.19 , pp. 507-519
    • Fire, E.1    Gullá, S.V.2    Grant, R.A.3    Keating, A.E.4
  • 33
    • 77956523665 scopus 로고    scopus 로고
    • Bcl-2 and Bax interact via the BH1-3 Groove-BH3 motif interface and a novel interface involving the BH4 motif
    • Ding J, Zhang Z, Roberts GJ, Falcone M, Miao Y, Shao Y, Zhang XC, Andrews DW, Lin J (2010) Bcl-2 and Bax interact via the BH1-3 Groove-BH3 motif interface and a novel interface involving the BH4 motif. J Biol Chem 285:28749-28763.
    • (2010) J Biol Chem , vol.285 , pp. 28749-28763
    • Ding, J.1    Zhang, Z.2    Roberts, G.J.3    Falcone, M.4    Miao, Y.5    Shao, Y.6    Zhang, X.C.7    Andrews, D.W.8    Lin, J.9
  • 36
    • 69049104094 scopus 로고    scopus 로고
    • Activation of Bax by joint action of tBid and mitochondrial outer membrane: Monte Carlo simulations
    • Veresov VG, Davidovskii AI (2009) Activation of Bax by joint action of tBid and mitochondrial outer membrane: Monte Carlo simulations. Eur Biophys J 38:941-960.
    • (2009) Eur Biophys J , vol.38 , pp. 941-960
    • Veresov, V.G.1    Davidovskii, A.I.2
  • 37
    • 31344431883 scopus 로고    scopus 로고
    • Acid destabilization of the solution conformation of Bcl-XL does not drive its pH-dependent insertion into membranes
    • DOI 10.1110/ps.051807706
    • Thuduppathy GR, Hill RB (2006) Acid destabilization of the solution conformation of Bcl-XL does not drive its pH-dependent insertion into membranes. Protein Sci 15:248-257. (Pubitemid 43144997)
    • (2006) Protein Science , vol.15 , Issue.2 , pp. 248-257
    • Thuduppathy, G.R.1    Hill, R.B.2
  • 38
    • 33646904758 scopus 로고    scopus 로고
    • Protein folding-simulation
    • Daggett V (2006) Protein folding-simulation. Chem Rev 106:1898-1916.
    • (2006) Chem Rev , vol.106 , pp. 1898-1916
    • Daggett, V.1
  • 39
    • 77953508894 scopus 로고    scopus 로고
    • Microsecond simulations of the folding/unfolding thermodynamics of the Trp-cage miniprotein
    • Day R, Paschek D, Garcia AE (2010) Microsecond simulations of the folding/unfolding thermodynamics of the Trp-cage miniprotein. Proteins 78:1889-1899.
    • (2010) Proteins , vol.78 , pp. 1889-1899
    • Day, R.1    Paschek, D.2    Garcia, A.E.3
  • 40
    • 77956516916 scopus 로고    scopus 로고
    • 100 ns molecular dynamics simulations to study intramolecular conformational changes in Bax
    • Koshy C, Parthiban M, Sowdhamini R (2010) 100 ns molecular dynamics simulations to study intramolecular conformational changes in Bax. J Biomol Struct Dyn 28:71-83.
    • (2010) J Biomol Struct Dyn , vol.28 , pp. 71-83
    • Koshy, C.1    Parthiban, M.2    Sowdhamini, R.3
  • 41
    • 77955842900 scopus 로고    scopus 로고
    • Temperature-induced unfolding of epidermal growth factor (EGF): Insight from molecular dynamics simulation
    • Yan C, Pattani V, Tunnell JW, Ren P (2010) Temperature-induced unfolding of epidermal growth factor (EGF): insight from molecular dynamics simulation. J Mol Graph Model 29:2-12.
    • (2010) J Mol Graph Model , vol.29 , pp. 2-12
    • Yan, C.1    Pattani, V.2    Tunnell, J.W.3    Ren, P.4
  • 42
    • 60749097994 scopus 로고    scopus 로고
    • Early events in thermal unfolding of apocytochrome b562 and its double-cysteine mutant as revealed by molecular dynamics simulation
    • Lin YW, Ni FY, Ying TL (2009) Early events in thermal unfolding of apocytochrome b562 and its double-cysteine mutant as revealed by molecular dynamics simulation. Theochem 898:82-89.
    • (2009) Theochem , vol.898 , pp. 82-89
    • Lin, Y.W.1    Ni, F.Y.2    Ying, T.L.3
  • 43
    • 43849090358 scopus 로고    scopus 로고
    • Thermal unfolding simulations of bacterial agellin: Insight into its refolding before assembly
    • Chng CP, Kitao A (2008) Thermal unfolding simulations of bacterial agellin: insight into its refolding before assembly. Biophys J 94:3858-3871.
    • (2008) Biophys J , vol.94 , pp. 3858-3871
    • Chng, C.P.1    Kitao, A.2
  • 44
    • 33748037685 scopus 로고    scopus 로고
    • Molecular dynamics simulation and automated docking of the pro-apoptotic Bax protein and its complex with a peptide designed from the Bax-binding domain of anti-apoptotic Ku70
    • DOI 10.1002/jcb.20893
    • Mancinelli F, Caraglia M, Budillon A, Abbruzzese A, Bismuto E (2006) Molecular dynamics simulation and automated docking of the pro-apoptotic Bax protein and its complex with a peptide designed from the Bax-binding domain of anti-apoptotic Ku70. J Cell Biochem 99:305-318. (Pubitemid 44297973)
    • (2006) Journal of Cellular Biochemistry , vol.99 , Issue.1 , pp. 305-318
    • Mancinelli, F.1    Caraglia, M.2    Budillon, A.3    Abbruzzese, A.4    Bismuto, E.5
  • 45
    • 56649083699 scopus 로고    scopus 로고
    • Computing the stability diagram of the Trp-cage miniprotein
    • Paschek D, Hempel S, García AE (2008) Computing the stability diagram of the Trp-cage miniprotein. Proc Natl Acad Sci USA 105:17754-17759.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 17754-17759
    • Paschek, D.1    Hempel, S.2    García, A.E.3
  • 46
    • 0033022072 scopus 로고    scopus 로고
    • Study of the stability and unfolding mechanism of BBA1 by molecular dynamics simulations at different temperatures
    • Wang L, Duan Y, Shortle R, Imperiali B, Kollman PA (1999) Study of the stability and unfolding mechanism of BBA1 by molecular dynamics simulations at different temperatures. Protein Sci 8:1292-1304. (Pubitemid 29264960)
    • (1999) Protein Science , vol.8 , Issue.6 , pp. 1292-1304
    • Wang, L.1    Duan, Y.2    Shortle, R.3    Imperiali, B.4    Kollman, P.A.5
  • 47
    • 79952159221 scopus 로고    scopus 로고
    • Role of glycosylation in structure and stability of Erythrina corallodendron lectin (EcorL): A molecular dynamics study
    • Kaushik S, Mohanty D, Surolia A (2011) Role of glycosylation in structure and stability of Erythrina corallodendron lectin (EcorL): a molecular dynamics study. Protein Sci 20:465-481.
    • (2011) Protein Sci , vol.20 , pp. 465-481
    • Kaushik, S.1    Mohanty, D.2    Surolia, A.3
  • 48
    • 0033852796 scopus 로고    scopus 로고
    • Charge-charge interactions influence the denatured state ensemble and contribute to protein stability
    • Pace CN, Alston RW, Shaw KL (2000) Charge-charge interactions influence the denatured state ensemble and contribute to protein stability. Protein Sci 9: 1395-1398. (Pubitemid 30602294)
    • (2000) Protein Science , vol.9 , Issue.7 , pp. 1395-1398
    • Pace, C.N.1    Alston, R.W.2    Shaw, K.L.3
  • 49
    • 77955691787 scopus 로고    scopus 로고
    • Uncovering specific electrostatic interactions in the denatured states of proteins
    • Shen JK (2010) Uncovering specific electrostatic interactions in the denatured states of proteins. Biophys J 99:924-932.
    • (2010) Biophys J , vol.99 , pp. 924-932
    • Shen, J.K.1
  • 50
    • 0035800850 scopus 로고    scopus 로고
    • Activation of the b2-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6
    • Ballesteros JA, Jensen AD, Liapakis G, Rasmussen SGF, Shi L, Gether U, Javitch JA (2001) Activation of the b2-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6. J Biol Chem 276: 29171-29177.
    • (2001) J Biol Chem , vol.276 , pp. 29171-29177
    • Ballesteros, J.A.1    Jensen, A.D.2    Liapakis, G.3    Rasmussen, S.G.F.4    Shi, L.5    Gether, U.6    Javitch, J.A.7
  • 51
    • 77949267165 scopus 로고    scopus 로고
    • The Bax carboxy-terminal helix does not determine organelle-specific targeting but is essential for maintaining Bax in an inactive state and for stable mitochondrial membrane insertion
    • Brock SE, Li C, Wattenberg BW (2010) The Bax carboxy-terminal helix does not determine organelle-specific targeting but is essential for maintaining Bax in an inactive state and for stable mitochondrial membrane insertion. Apoptosis 15:14-27.
    • (2010) Apoptosis , vol.15 , pp. 14-27
    • Brock, S.E.1    Li, C.2    Wattenberg, B.W.3
  • 52
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: A mechanism of protein structure stabilization
    • Burley SK, Petsko GA (1985) Aromatic-aromatic interaction: a mechanism of protein structure stabilization. Science 229:23-28.
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 54
    • 0035044995 scopus 로고    scopus 로고
    • Conformational change of proteins arising from normal mode calculations
    • Tama F, Sanejouand YH (2001) Conformational change of proteins arising from normal mode calculations. Protein Eng 14:1-6. (Pubitemid 32318932)
    • (2001) Protein Engineering , vol.14 , Issue.1 , pp. 1-6
    • Tama, F.1    Sanejouand, Y.-H.2
  • 55
    • 3242875210 scopus 로고    scopus 로고
    • ElNémo: A normal mode web server for protein movement analysis and the generation of templates for molecular replacement
    • DOI 10.1093/nar/gkh368
    • Suhre K, Sanejouand YH (2004) ElNemo: a normal mode web-server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Research 32:W610-W614. (Pubitemid 38997408)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISS.
    • Suhre, K.1    Sanejouand, Y.-H.2
  • 56
    • 0036721233 scopus 로고    scopus 로고
    • Normal mode analysis of macromolecular motions in a database framework: Developing mode concentration as a useful classifying statistic
    • DOI 10.1002/prot.10168
    • Krebs WG, Alexandrov V, Wilson CA, Echols N, Yu H, Gerstein M (2002) Normal mode analysis of macromolecular motions in a database framework: developing mode concentration as a useful classifying statistic. Proteins 48:682-695. (Pubitemid 34925457)
    • (2002) Proteins: Structure, Function and Genetics , vol.48 , Issue.4 , pp. 682-695
    • Krebs, W.G.1    Alexandrov, V.2    Wilson, C.A.3    Echols, N.4    Yu, H.5    Gerstein, M.6
  • 57
    • 0000579428 scopus 로고
    • Molecular dynamics of an alpha-helical polypeptide: Temperature dependence and deviation from harmonic behavior
    • Levy RM, Perahia D, Karplus M (1982) Molecular dynamics of an alpha-helical polypeptide: temperature dependence and deviation from harmonic behavior. Proc Natl Acad Sci USA 79:1346-1350.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 1346-1350
    • Levy, R.M.1    Perahia, D.2    Karplus, M.3
  • 58
    • 21244476053 scopus 로고    scopus 로고
    • Structural conservation of residues in BH1 and BH2 domains of Bcl-2 family proteins
    • DOI 10.1016/j.febslet.2005.05.015, PII S0014579305006137
    • Gurudutta GU, Verma YK, Singh VK, Gupta P, Raj HG, Sharma RK, Chandra R (2005) Structural conservation of residues in BH1 and BH2 domains of Bcl-2 family proteins. FEBS Lett 579:3503-3507. (Pubitemid 40897684)
    • (2005) FEBS Letters , vol.579 , Issue.17 , pp. 3503-3507
    • Gurudutta, G.U.1    Verma, Y.Kr.2    Singh, V.K.3    Gupta, P.4    Raj, H.G.5    Sharma, R.K.6    Chandra, R.7
  • 59
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for Highly E-cient, Load-Balanced, and Scalable Molecular Simulation
    • Hess B, Kutzner C, van der Spoel D, Lindahl E (2008) GROMACS 4: algorithms for Highly E-cient, Load-Balanced, and Scalable Molecular Simulation. J Chem Theory Comput 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
  • 60
    • 33645941402 scopus 로고    scopus 로고
    • The OPLS potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin
    • Jorgensen WL, Tirado-Rives J (1998) The OPLS potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin. J Am Chem Soc 110:1657-1666.
    • (1998) J Am Chem Soc , vol.110 , pp. 1657-1666
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 61
    • 84986519235 scopus 로고
    • Parametrization and evaluation of a flexible water model
    • Ferguson DM (1995) Parametrization and evaluation of a flexible water model. J Comp Chem 16:501-511.
    • (1995) J Comp Chem , vol.16 , pp. 501-511
    • Ferguson, D.M.1
  • 63
    • 84977266737 scopus 로고
    • Die Berechnung optischer und elektrostatischer Gitterpotentiale
    • Ewald PP (1921) Die Berechnung optischer und elektrostatischer Gitterpotentiale. Ann Phys 64:253-287.
    • (1921) Ann Phys , vol.64 , pp. 253-287
    • Ewald, P.P.1
  • 64
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N-log(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L (1993) Particle mesh Ewald: an N-log(N) method for Ewald sums in large systems. J Chem Phys 98:10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 66
    • 84943502952 scopus 로고
    • A molecular dynamics method for simulations in the canonical ensemble
    • Nosé S (1984) A molecular dynamics method for simulations in the canonical ensemble. Mol Phys 52:255-268.
    • (1984) Mol Phys , vol.52 , pp. 255-268
    • Nosé, S.1
  • 67
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • Hoover WG (1985) Canonical dynamics: equilibrium phase-space distributions. Phys Rev A 31:1695-1697.
    • (1985) Phys Rev A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 68
    • 0019707626 scopus 로고
    • POLYMORPHIC TRANSITIONS IN SINGLE CRYSTALS: A NEW MOLECULAR DYNAMICS METHOD.
    • DOI 10.1063/1.328693
    • Parrinello M, Rahman A (1981) Polymorphic transitions in single crystals: a new molecular dynamics method. J Appl Phys 52:7182-7190. (Pubitemid 12456820)
    • (1981) Journal of Applied Physics , vol.52 , Issue.12 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 69
    • 84926811618 scopus 로고
    • Constant pressure molecular dynamics for molecular systems
    • Nosé S, Klein ML (1983) Constant pressure molecular dynamics for molecular systems. Mol Phys 50: 1055-1076.
    • (1983) Mol Phys , vol.50 , pp. 1055-1076
    • Nosé, S.1    Klein, M.L.2
  • 70
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogenbonded and geometrical features
    • Kabsch W, Sander C (1983) Dictionary of protein secondary structure: pattern recognition of hydrogenbonded and geometrical features. Biopolymers 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.