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Volumn 107, Issue 1, 2010, Pages 308-313

Binding of a potent small-molecule inhibitor of six-helix bundle formation requires interactions with both heptad-repeats of the RSV fusion protein

Author keywords

Cocrystal structure; Respiratory syncytial virus; TMC353121; Viral fusion

Indexed keywords

AMINO ACID; ANTIVIRUS AGENT; TMC 353121; UNCLASSIFIED DRUG; VIRUS FUSION PROTEIN;

EID: 76249116900     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0910108106     Document Type: Article
Times cited : (72)

References (52)
  • 1
    • 0037381269 scopus 로고    scopus 로고
    • The structural biology of type I viral membrane fusion
    • Colman PM, Lawrence MC (2003) The structural biology of type I viral membrane fusion. Nat Rev Mol Cell Biol 4:309-319.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 309-319
    • Colman, P.M.1    Lawrence, M.C.2
  • 2
    • 31344432402 scopus 로고    scopus 로고
    • Virus membrane-fusion proteins: More than one way to make a hairpin
    • Kielian M, Rey FA (2006) Virus membrane-fusion proteins: More than one way to make a hairpin. Nat Rev Microbiol 4:67-76.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 67-76
    • Kielian, M.1    Rey, F.A.2
  • 3
    • 34548824835 scopus 로고    scopus 로고
    • Structural basis of viral invasion: Lessons from paramyxovirus F
    • Lamb RA, Jardetzky TS (2007) Structural basis of viral invasion: lessons from paramyxovirus F. Curr Opin Struct Biol 17:427-436.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 427-436
    • Lamb, R.A.1    Jardetzky, T.S.2
  • 4
    • 53549088587 scopus 로고    scopus 로고
    • The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines
    • Kadlec J, Loureiro S, Abrescia NG, Stuart DI, Jones IM (2008) The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines. Nat Struct Mol Biol 15:1024-1030.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1024-1030
    • Kadlec, J.1    Loureiro, S.2    Abrescia, N.G.3    Stuart, D.I.4    Jones, I.M.5
  • 5
  • 6
    • 30144436116 scopus 로고    scopus 로고
    • Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation
    • Yin H-S, Wen X, Paterson RG, Lamb RA, Jardetzky TS (2006) Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation. Nature 439: 38-44.
    • (2006) Nature , vol.439 , pp. 38-44
    • Yin, H.-S.1    Wen, X.2    Paterson, R.G.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 7
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion
    • Melikyan GB, et al. (2000) Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion. J Cell Biol 151: 413-423.
    • (2000) J Cell Biol , vol.151 , pp. 413-423
    • Melikyan, G.B.1
  • 8
    • 0035421959 scopus 로고    scopus 로고
    • Membrane fusion machines of paramyxoviruses: Capture of intermediates of fusion
    • Russell CJ, Jardetzky TS, Lamb RA (2001) Membrane fusion machines of paramyxoviruses: capture of intermediates of fusion. EMBO J 20:4024-4034.
    • (2001) EMBO J , vol.20 , pp. 4024-4034
    • Russell, C.J.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 9
    • 0032433685 scopus 로고    scopus 로고
    • Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target
    • Chan DC, Chutkowski CT, Kim PS (1998) Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target. Proc Natl Acad Sci USA 95: 15613-15617.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15613-15617
    • Chan, D.C.1    Chutkowski, C.T.2    Kim, P.S.3
  • 10
    • 0034687711 scopus 로고    scopus 로고
    • Structural characterization of the human respiratory syncytial virus fusion protein core
    • Zhao X, Singh M, Malashkevich VN, Kim PS (2000) Structural characterization of the human respiratory syncytial virus fusion protein core. Proc Natl Acad Sci USA 97: 14172-14177.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14172-14177
    • Zhao, X.1    Singh, M.2    Malashkevich, V.N.3    Kim, P.S.4
  • 11
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough PA, Hughson FM, Skehel JJ, Wiley DC (1994) Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371:37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 12
    • 0035902564 scopus 로고    scopus 로고
    • The trimer-of-hairpins motif in membrane fusion: Visna virus
    • Malashkevich VN, Singh M, Kim PS (2001) The trimer-of-hairpins motif in membrane fusion: Visna virus. Proc Natl Acad Sci USA 98:8502-8506.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 8502-8506
    • Malashkevich, V.N.1    Singh, M.2    Kim, P.S.3
  • 13
    • 11144237311 scopus 로고    scopus 로고
    • Structure of a proteolytically resistant core from the severe acute respiratory syndrome coronavirus S2 fusion protein
    • Supekar VM, et al. (2004) Structure of a proteolytically resistant core from the severe acute respiratory syndrome coronavirus S2 fusion protein. Proc Natl Acad Sci USA 101: 17958-17963.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 17958-17963
    • Supekar, V.M.1
  • 14
    • 0032214714 scopus 로고    scopus 로고
    • Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain
    • Weissenhorn W, Carfí A, Lee KH, Skehel JJ, Wiley DC (1998) Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain. Mol Cell 2:605-616.
    • (1998) Mol Cell , vol.2 , pp. 605-616
    • Weissenhorn, W.1    Carfí, A.2    Lee, K.H.3    Skehel, J.J.4    Wiley, D.C.5
  • 15
    • 0031729823 scopus 로고    scopus 로고
    • Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry
    • Kilby JM, et al. (1998) Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry. Nat Med 4:1302-1307.
    • (1998) Nat Med , vol.4 , pp. 1302-1307
    • Kilby, J.M.1
  • 16
    • 9044234408 scopus 로고    scopus 로고
    • Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion
    • Lambert DM, et al. (1996) Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion. Proc Natl Acad Sci USA 93:2186-2191.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2186-2191
    • Lambert, D.M.1
  • 17
    • 33845776569 scopus 로고    scopus 로고
    • Examination of a fusogenic hexameric core from human metapneumovirus and identification of a potent synthetic peptide inhibitor from the heptad repeat 1 region
    • Miller SA, Tollefson S, Crowe JE Jr, Williams JV, Wright DW (2007) Examination of a fusogenic hexameric core from human metapneumovirus and identification of a potent synthetic peptide inhibitor from the heptad repeat 1 region. J Virol 81: 141-149.
    • (2007) J Virol , vol.81 , pp. 141-149
    • Miller, S.A.1    Tollefson, S.2    Crowe Jr, J.E.3    Williams, J.V.4    Wright, D.W.5
  • 18
    • 24944483017 scopus 로고    scopus 로고
    • Inhibition of Henipavirus fusion and infection by heptadderived peptides of the Nipah virus fusion glycoprotein
    • Bossart KN, et al. (2005) Inhibition of Henipavirus fusion and infection by heptadderived peptides of the Nipah virus fusion glycoprotein. Virol J 2:57.
    • (2005) Virol J , vol.2 , pp. 57
    • Bossart, K.N.1
  • 19
    • 0028864218 scopus 로고
    • A synthetic peptide corresponding to a conserved heptad repeat domain is a potent inhibitor of Sendai virus-cell fusion: An emerging similarity with functional domains of other viruses
    • Rapaport D, Ovadia M, Shai Y (1995) A synthetic peptide corresponding to a conserved heptad repeat domain is a potent inhibitor of Sendai virus-cell fusion: an emerging similarity with functional domains of other viruses. EMBO J 14:5524-5531.
    • (1995) EMBO J , vol.14 , pp. 5524-5531
    • Rapaport, D.1    Ovadia, M.2    Shai, Y.3
  • 20
    • 2942590370 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides
    • Bosch BJ, et al. (2004) Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. Proc Natl Acad Sci USA 101:8455-8460.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8455-8460
    • Bosch, B.J.1
  • 21
    • 0033214895 scopus 로고    scopus 로고
    • Inhibiting HIV-1 entry: Discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket
    • Eckert DM, Malashkevich VN, Hong LH, Carr PA, Kim PS (1999) Inhibiting HIV-1 entry: Discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket. Cell 99: 103-115.
    • (1999) Cell , vol.99 , pp. 103-115
    • Eckert, D.M.1    Malashkevich, V.N.2    Hong, L.H.3    Carr, P.A.4    Kim, P.S.5
  • 23
    • 32544456441 scopus 로고    scopus 로고
    • Prospects and strategies for the discovery and development of small-molecule inhibitors of six-helix bundle formation in class 1 viral fusion proteins
    • Debnath AK (2006) Prospects and strategies for the discovery and development of small-molecule inhibitors of six-helix bundle formation in class 1 viral fusion proteins. Curr Opin Investig Drugs 7:118-127.
    • (2006) Curr Opin Investig Drugs , vol.7 , pp. 118-127
    • Debnath, A.K.1
  • 24
    • 0345447465 scopus 로고    scopus 로고
    • Substituted benzimidazoles with nanomolar activity against respiratory syncytial virus
    • Andries K, et al. (2003) Substituted benzimidazoles with nanomolar activity against respiratory syncytial virus. Antiviral Res 60:209-219.
    • (2003) Antiviral Res , vol.60 , pp. 209-219
    • Andries, K.1
  • 25
    • 34648834114 scopus 로고    scopus 로고
    • Selection of a respiratory syncytial virus fusion inhibitor clinical candidate, part 1: Improving the pharmacokinetic profile using the structureproperty relationship
    • Bonfanti J-F, et al. (2007) Selection of a respiratory syncytial virus fusion inhibitor clinical candidate, part 1: Improving the pharmacokinetic profile using the structureproperty relationship. J Med Chem 50:4572-4584.
    • (2007) J Med Chem , vol.50 , pp. 4572-4584
    • Bonfanti, J.-F.1
  • 26
    • 39749188747 scopus 로고    scopus 로고
    • Selection of a respiratory syncytial virus fusion inhibitor clinical candidate. 2. Discovery of a morpholinopropylaminobenzimidazole derivative (TMC353121)
    • Bonfanti J-F, et al. (2008) Selection of a respiratory syncytial virus fusion inhibitor clinical candidate. 2. Discovery of a morpholinopropylaminobenzimidazole derivative (TMC353121). J Med Chem 51:875-896.
    • (2008) J Med Chem , vol.51 , pp. 875-896
    • Bonfanti, J.-F.1
  • 27
    • 6344229213 scopus 로고    scopus 로고
    • Targeting a binding pocket within the trimer-of-hairpins: Smallmolecule inhibition of viral fusion
    • Cianci C, et al. (2004) Targeting a binding pocket within the trimer-of-hairpins: Smallmolecule inhibition of viral fusion. Proc Natl Acad Sci USA 101:15046-15051.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 15046-15051
    • Cianci, C.1
  • 28
    • 21144442487 scopus 로고    scopus 로고
    • Small molecules VP-14637 and JNJ-2408068 inhibit respiratory syncytial virus fusion by similarmechanisms
    • Douglas JL, et al. (2005) Small molecules VP-14637 and JNJ-2408068 inhibit respiratory syncytial virus fusion by similarmechanisms. Antimicrob Agents Chemother 49:2460-2466.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 2460-2466
    • Douglas, J.L.1
  • 29
    • 0037126834 scopus 로고    scopus 로고
    • Design of a protein surface antagonist based on alpha-helixmimicry: Inhibition of gp41 assembly and viral fusion
    • Ernst JT, et al. (2002) Design of a protein surface antagonist based on alpha-helixmimicry: Inhibition of gp41 assembly and viral fusion. Angew Chem Int Ed Engl 41:278-281.
    • (2002) Angew Chem Int Ed Engl , vol.41 , pp. 278-281
    • Ernst, J.T.1
  • 30
    • 0034595078 scopus 로고    scopus 로고
    • A salt bridge between an N-terminal coiled coil of gp41 and an antiviral agent targeted to the gp41 core is important for anti-HIV-1 activity
    • Jiang S, Debnath AK (2000) A salt bridge between an N-terminal coiled coil of gp41 and an antiviral agent targeted to the gp41 core is important for anti-HIV-1 activity. Biochem Biophys Res Commun 270:153-157.
    • (2000) Biochem Biophys Res Commun , vol.270 , pp. 153-157
    • Jiang, S.1    Debnath, A.K.2
  • 31
    • 7244253012 scopus 로고    scopus 로고
    • N-substituted pyrrole derivatives as novel human immunodeficiency virus type 1 entry inhibitors that interfere with the gp41 six-helix bundle formation and block virus fusion
    • Jiang S, et al. (2004) N-substituted pyrrole derivatives as novel human immunodeficiency virus type 1 entry inhibitors that interfere with the gp41 six-helix bundle formation and block virus fusion. Antimicrob Agents Chemother 48: 4349-4359.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 4349-4359
    • Jiang, S.1
  • 32
    • 19744379597 scopus 로고    scopus 로고
    • Theaflavin derivatives in black tea and catechin derivatives in green tea inhibit HIV-1 entry by targeting gp41
    • Liu S, et al. (2005) Theaflavin derivatives in black tea and catechin derivatives in green tea inhibit HIV-1 entry by targeting gp41. Biochim Biophys Acta 1723:270-281.
    • (2005) Biochim Biophys Acta , vol.1723 , pp. 270-281
    • Liu, S.1
  • 33
    • 0032876381 scopus 로고    scopus 로고
    • Selection of gp41-mediated HIV-1 cell entry inhibitors from biased combinatorial libraries of non-natural binding elements
    • Ferrer M, et al. (1999) Selection of gp41-mediated HIV-1 cell entry inhibitors from biased combinatorial libraries of non-natural binding elements. Nat Struct Biol 6:953-960.
    • (1999) Nat Struct Biol , vol.6 , pp. 953-960
    • Ferrer, M.1
  • 34
    • 17944384967 scopus 로고    scopus 로고
    • The structure of an HIV-1 specific cell entry inhibitor in complex with the HIV-1 gp41 trimeric core
    • Zhou G, et al. (2000) The structure of an HIV-1 specific cell entry inhibitor in complex with the HIV-1 gp41 trimeric core. Bioorg Med Chem 8:2219-2227.
    • (2000) Bioorg Med Chem , vol.8 , pp. 2219-2227
    • Zhou, G.1
  • 35
    • 24144473658 scopus 로고    scopus 로고
    • Design of a small-molecule entry inhibitor with activity against primary measles virus strains
    • Plemper RK, et al. (2005) Design of a small-molecule entry inhibitor with activity against primary measles virus strains. Antimicrob Agents Chemother 49:3755-3761.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 3755-3761
    • Plemper, R.K.1
  • 36
    • 11144357828 scopus 로고    scopus 로고
    • A target site for template-based design of measles virus entry inhibitors
    • Plemper RK, et al. (2004) A target site for template-based design of measles virus entry inhibitors. Proc Natl Acad Sci USA 101:5628-5633.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 5628-5633
    • Plemper, R.K.1
  • 37
    • 55249103905 scopus 로고    scopus 로고
    • pH-induced activation of arenavirus membrane fusion is antagonized by small-molecule inhibitors
    • York J, Dai D, Amberg SM, Nunberg JH (2008) pH-induced activation of arenavirus membrane fusion is antagonized by small-molecule inhibitors. J Virol 82: 10932-10939.
    • (2008) J Virol , vol.82 , pp. 10932-10939
    • York, J.1    Dai, D.2    Amberg, S.M.3    Nunberg, J.H.4
  • 38
    • 0027523625 scopus 로고
    • Inhibition of the fusion-inducing conformational change of influenza hemagglutinin by benzoquinones and hydroquinones
    • Bodian DL, et al. (1993) Inhibition of the fusion-inducing conformational change of influenza hemagglutinin by benzoquinones and hydroquinones. Biochemistry 32: 2967-2978.
    • (1993) Biochemistry , vol.32 , pp. 2967-2978
    • Bodian, D.L.1
  • 39
    • 57649155175 scopus 로고    scopus 로고
    • Rationally designed anti-HIV peptides containing multifunctional domains as molecule probes for studying the mechanisms of action of the first and second generation HIV fusion inhibitors
    • Qi Z, et al. (2008) Rationally designed anti-HIV peptides containing multifunctional domains as molecule probes for studying the mechanisms of action of the first and second generation HIV fusion inhibitors. J Biol Chem 283:30376-30384.
    • (2008) J Biol Chem , vol.283 , pp. 30376-30384
    • Qi, Z.1
  • 40
    • 53749101563 scopus 로고    scopus 로고
    • Sequestering of the prehairpin intermediate of gp41 by peptide N36Mut(e,g) potentiates the human immunodeficiency virus type 1 neutralizing activity of monoclonal antibodies directed against the N-terminal helical repeat of gp41
    • Gustchina E, Bewley CA, Clore GM (2008) Sequestering of the prehairpin intermediate of gp41 by peptide N36Mut(e,g) potentiates the human immunodeficiency virus type 1 neutralizing activity of monoclonal antibodies directed against the N-terminal helical repeat of gp41. J Virol 82:10032-10041.
    • (2008) J Virol , vol.82 , pp. 10032-10041
    • Gustchina, E.1    Bewley, C.A.2    Clore, G.M.3
  • 41
    • 76249109526 scopus 로고    scopus 로고
    • Polycyclic agents for the treatment of respiratory syncytial virus infections
    • Bond S, et al. (2005) Polycyclic agents for the treatment of respiratory syncytial virus infections. WO2005061513 A1.
    • (2005) WO2005061513 A1
    • Bond, S.1
  • 42
    • 9144234679 scopus 로고    scopus 로고
    • Orally active fusion inhibitor of respiratory syncytial virus
    • Cianci C, et al. (2004) Orally active fusion inhibitor of respiratory syncytial virus. Antimicrob Agents Chemother 48:413-422.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 413-422
    • Cianci, C.1
  • 43
    • 0345686528 scopus 로고    scopus 로고
    • Development of a photoaffinity label for respiratory syncytial virus inhibitors
    • Dischino DD, et al. (2003) Development of a photoaffinity label for respiratory syncytial virus inhibitors. J Labelled Comp Radiopharm 46:1105-1116.
    • (2003) J Labelled Comp Radiopharm , vol.46 , pp. 1105-1116
    • Dischino, D.D.1
  • 44
    • 0032509096 scopus 로고    scopus 로고
    • Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried polar residues
    • Eckert DM, Malashkevich VN, Kim PS (1998) Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried polar residues. J Mol Biol 284:859-865.
    • (1998) J Mol Biol , vol.284 , pp. 859-865
    • Eckert, D.M.1    Malashkevich, V.N.2    Kim, P.S.3
  • 45
    • 31144472894 scopus 로고    scopus 로고
    • Two domains that control prefusion stability and transport competence of the measles virus fusion protein
    • Doyle J, et al. (2006) Two domains that control prefusion stability and transport competence of the measles virus fusion protein. J Virol 80:1524-1536.
    • (2006) J Virol , vol.80 , pp. 1524-1536
    • Doyle, J.1
  • 46
    • 56649120628 scopus 로고    scopus 로고
    • Structure of influenza hemagglutinin in complex with an inhibitor of membrane fusion
    • Russell RJ, et al. (2008) Structure of influenza hemagglutinin in complex with an inhibitor of membrane fusion. Proc Natl Acad Sci USA 105:17736-17741.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 17736-17741
    • Russell, R.J.1
  • 47
    • 58149151220 scopus 로고    scopus 로고
    • Measles virus entry inhibitors: A structural proposal for mechanism of action and the development of resistance
    • Prussia AJ, Plemper RK, Snyder JP (2008) Measles virus entry inhibitors: A structural proposal for mechanism of action and the development of resistance. Biochemistry 47:13573-13583.
    • (2008) Biochemistry , vol.47 , pp. 13573-13583
    • Prussia, A.J.1    Plemper, R.K.2    Snyder, J.P.3
  • 48
    • 33846821758 scopus 로고    scopus 로고
    • Respiratory syncytial virus fusion inhibitors. Part 4: Optimization for oral bioavailability
    • Yu K-L, et al. (2007) Respiratory syncytial virus fusion inhibitors. Part 4: Optimization for oral bioavailability. Bioorg Med Chem Lett 17:895-901.
    • (2007) Bioorg Med Chem Lett , vol.17 , pp. 895-901
    • Yu, K.-L.1
  • 49
    • 0033766989 scopus 로고    scopus 로고
    • Glycosaminoglycan sulfation requirements for respiratory syncytial virus infection
    • Hallak LK, Spillmann D, Collins PL, Peeples ME (2000) Glycosaminoglycan sulfation requirements for respiratory syncytial virus infection. J Virol 74:10508-10513.
    • (2000) J Virol , vol.74 , pp. 10508-10513
    • Hallak, L.K.1    Spillmann, D.2    Collins, P.L.3    Peeples, M.E.4
  • 50
    • 0033638223 scopus 로고    scopus 로고
    • Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast
    • Mossessova E, Lima CD (2000) Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast. Mol Cell 5:865-876.
    • (2000) Mol Cell , vol.5 , pp. 865-876
    • Mossessova, E.1    Lima, C.D.2
  • 51
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read RJ (1986) Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr A 42:140-149.
    • (1986) Acta Crystallogr A , vol.42 , pp. 140-149
    • Read, R.J.1


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