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Volumn 7, Issue 7, 2012, Pages

Recombinant expression and purification of T4 phage Hoc, soc, gp23, gp24 proteins in native conformations with stability studies

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; ENDOTOXIN; GUANIDINE; PROTEIN GP23; PROTEIN GP24; PROTEIN HOC; PROTEIN SOC; UNCLASSIFIED DRUG;

EID: 84863752632     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0038902     Document Type: Article
Times cited : (11)

References (32)
  • 1
    • 49149111138 scopus 로고    scopus 로고
    • The immense journey of bacteriophage T4-from d'Hérelle to Delbrück and then to Darwin and beyond
    • Krisch HM, Comeau AM, (2008) The immense journey of bacteriophage T4-from d'Hérelle to Delbrück and then to Darwin and beyond. Res Microbiol 159(5): 314-24.
    • (2008) Res Microbiol , vol.159 , Issue.5 , pp. 314-324
    • Krisch, H.M.1    Comeau, A.M.2
  • 2
    • 0038808883 scopus 로고    scopus 로고
    • The prospect for bacteriophage therapy in Western medicine
    • Merril CR, Scholl D, Adhya SL, (2003) The prospect for bacteriophage therapy in Western medicine. Nat Rev Drug Discov 2(6): 489-497.
    • (2003) Nat Rev Drug Discov , vol.2 , Issue.6 , pp. 489-497
    • Merril, C.R.1    Scholl, D.2    Adhya, S.L.3
  • 3
    • 0037174681 scopus 로고    scopus 로고
    • Bacteriophage therapy. Stalin's Forgotten Cure
    • Stone R, (2002) Bacteriophage therapy. Stalin's Forgotten Cure. Science 298(5594): 728-731.
    • (2002) Science , vol.298 , Issue.5594 , pp. 728-731
    • Stone, R.1
  • 4
    • 20444503665 scopus 로고    scopus 로고
    • Phage therapy: an attractive option for dealing with antibiotic-resistant bacterial infections
    • Sulakvelidze A, (2005) Phage therapy: an attractive option for dealing with antibiotic-resistant bacterial infections. Drug Discov Today 10(12): 807-809.
    • (2005) Drug Discov Today , vol.10 , Issue.12 , pp. 807-809
    • Sulakvelidze, A.1
  • 5
    • 66849124585 scopus 로고    scopus 로고
    • The bacteriophages in human- and animal body-associated microbial communities
    • Letarov AV, Kulikov E, (2009) The bacteriophages in human- and animal body-associated microbial communities. J Appl Microbiol 107(1): 1-13.
    • (2009) J Appl Microbiol , vol.107 , Issue.1 , pp. 1-13
    • Letarov, A.V.1    Kulikov, E.2
  • 6
    • 84856507333 scopus 로고    scopus 로고
    • Phage therapy pharmacology phage cocktails
    • Chan BK, Abedon ST, (2012) Phage therapy pharmacology phage cocktails. Adv Appl Microbiol 78: 1-23.
    • (2012) Adv Appl Microbiol , vol.78 , pp. 1-23
    • Chan, B.K.1    Abedon, S.T.2
  • 12
    • 15244342831 scopus 로고    scopus 로고
    • The potential role of endogenous bacteriophages in controlling invading pathogens
    • Górski A, Weber-Dabrowska B, (2005) The potential role of endogenous bacteriophages in controlling invading pathogens. Cell Mol Life Sci 62(5): 511-9.
    • (2005) Cell Mol Life Sci , vol.62 , Issue.5 , pp. 511-519
    • Górski, A.1    Weber-Dabrowska, B.2
  • 13
    • 84861904346 scopus 로고    scopus 로고
    • Pathogen associated molecular pattern motifs from Gram-positive and Gram-negative bacteria induce different inflammatory mediator profiles in equine blood
    • doi:10.1016/j.tvjl.2011.09.001
    • Declue AE, Johnson PJ, Day JL, Amorim JR, Honaker AR, (2011) Pathogen associated molecular pattern motifs from Gram-positive and Gram-negative bacteria induce different inflammatory mediator profiles in equine blood. Vet J doi:10.1016/j.tvjl.2011.09.001.
    • (2011) Vet J
    • Declue, A.E.1    Johnson, P.J.2    Day, J.L.3    Amorim, J.R.4    Honaker, A.R.5
  • 15
    • 24644495576 scopus 로고    scopus 로고
    • Implication of Toll-like receptor and tumor necrosis factor alpha signaling in septic shock
    • Lin WJ, Yeh WC, (2005) Implication of Toll-like receptor and tumor necrosis factor alpha signaling in septic shock. Shock 24(3): 206-9.
    • (2005) Shock , vol.24 , Issue.3 , pp. 206-209
    • Lin, W.J.1    Yeh, W.C.2
  • 17
    • 79961196704 scopus 로고    scopus 로고
    • Structure of the three N-terminal immunoglobulin domains of the highly immunogenic outer capsid protein from a T4-like bacteriophage
    • Fokine A, Islam MZ, Zhang Z, Bowman VD, Rao VB, et al. (2011) Structure of the three N-terminal immunoglobulin domains of the highly immunogenic outer capsid protein from a T4-like bacteriophage. J Virol 85(16): 8141-8.
    • (2011) J Virol , vol.85 , Issue.16 , pp. 8141-8148
    • Fokine, A.1    Islam, M.Z.2    Zhang, Z.3    Bowman, V.D.4    Rao, V.B.5
  • 18
    • 0000956277 scopus 로고
    • Morphogenesis of the T4 Head
    • In: Karam JD, editors, editor
    • Black LW, Showe MK, Steven AC, (1994) Morphogenesis of the T4 Head. In: Karam JD, editors. pp. 218-258 editor. Molecular biology of bacteriophage T4. Washington, DC: American Society for Microbiology.
    • (1994) , pp. 218-258
    • Black, L.W.1    Showe, M.K.2    Steven, A.C.3
  • 20
    • 0032581506 scopus 로고    scopus 로고
    • Phage T4 SOC and HOC display of biologically active, full-length proteins on the viral capsid
    • Ren Z, Black LW, (1998) Phage T4 SOC and HOC display of biologically active, full-length proteins on the viral capsid. Gene 215(2): 439-44.
    • (1998) Gene , vol.215 , Issue.2 , pp. 439-444
    • Ren, Z.1    Black, L.W.2
  • 22
    • 84862782517 scopus 로고    scopus 로고
    • Deletion of the Hoc and Soc capsid proteins affects the surface and cellular uptake properties of bacteriophage T4 derived nanoparticles
    • Robertson K, Furukawa Y, Underwood A, Black L, Liu JL, (2012) Deletion of the Hoc and Soc capsid proteins affects the surface and cellular uptake properties of bacteriophage T4 derived nanoparticles. Biochem Biophys Res Commun 418(3): 537-40.
    • (2012) Biochem Biophys Res Commun , vol.418 , Issue.3 , pp. 537-540
    • Robertson, K.1    Furukawa, Y.2    Underwood, A.3    Black, L.4    Liu, J.L.5
  • 23
    • 0032748895 scopus 로고    scopus 로고
    • Theoretical studies toward quantitative protein circular dichroism calculations
    • Besley NA, Hirst JD, (1999) Theoretical studies toward quantitative protein circular dichroism calculations. J Am Chem Soc 121: 9636-9644.
    • (1999) J Am Chem Soc , vol.121 , pp. 9636-9644
    • Besley, N.A.1    Hirst, J.D.2
  • 24
    • 33846432696 scopus 로고    scopus 로고
    • Computation of the amide I band of polypeptides and proteins with a partial Hessian approach
    • Besley NA, Metcalf KA, (2007) Computation of the amide I band of polypeptides and proteins with a partial Hessian approach. J Chem Phys 126(3): 035101.
    • (2007) J Chem Phys , vol.126 , Issue.3 , pp. 035101
    • Besley, N.A.1    Metcalf, K.A.2
  • 25
    • 0036130801 scopus 로고    scopus 로고
    • Thermodynamics of single peptide bond cleavage in bovine pancreatic trypsin inhibitor (BPTI)
    • Buczek O, Krowarsch D, Otlewski J, (2002) Thermodynamics of single peptide bond cleavage in bovine pancreatic trypsin inhibitor (BPTI). Protein Sci 11(4): 924-32.
    • (2002) Protein Sci , vol.11 , Issue.4 , pp. 924-932
    • Buczek, O.1    Krowarsch, D.2    Otlewski, J.3
  • 26
    • 0000040655 scopus 로고
    • Molecular Chaperons in T4 Assembly
    • In: Karam JD, editors, editor
    • Georgopoulos CP, Linder CH, (1994) Molecular Chaperons in T4 Assembly. In: Karam JD, editors. pp. 213-317 editor. Molecular biology of bacteriophage T4. Washington, DC: American Society for Microbiology.
    • (1994) , pp. 213-317
    • Georgopoulos, C.P.1    Linder, C.H.2
  • 27
    • 71549132519 scopus 로고    scopus 로고
    • Dissociation kinetics of the GroEL-gp31 chaperonin complex studied with Förster resonance energy transfer
    • Calmat S, Hendriks J, van Heerikhuizen H, Schmidt CF, van der Vies SM, et al. (2009) Dissociation kinetics of the GroEL-gp31 chaperonin complex studied with Förster resonance energy transfer. Biochemistry 48(49): 11692-8.
    • (2009) Biochemistry , vol.48 , Issue.49 , pp. 11692-11698
    • Calmat, S.1    Hendriks, J.2    van Heerikhuizen, H.3    Schmidt, C.F.4    van der Vies, S.M.5
  • 28
    • 67651208925 scopus 로고    scopus 로고
    • Adapting the machine: adaptor proteins for Hsp100/Clp and AAA + proteases
    • Kirstein J, Molière N, Dougan DA, Turgay K, (2009) Adapting the machine: adaptor proteins for Hsp100/Clp and AAA + proteases. Nat Rev Microbiol 7(8): 589-599.
    • (2009) Nat Rev Microbiol , vol.7 , Issue.8 , pp. 589-599
    • Kirstein, J.1    Molière, N.2    Dougan, D.A.3    Turgay, K.4
  • 29
    • 0001189491 scopus 로고
    • General Procedures
    • In: Karam JD, editors, editor
    • Carlson K, Miller ES, (1994) General Procedures. In: Karam JD, editors. pp. 427-437 editor. Molecular biology of bacteriophage T4. Washington, DC: American Society for Microbiology.
    • (1994) , pp. 427-437
    • Carlson, K.1    Miller, E.S.2
  • 30
    • 0026754044 scopus 로고
    • A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range
    • Santoro MM, Bolen DW, (1992) A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range. Biochemistry, 31, 4901-4907.
    • (1992) Biochemistry, 31, 4901-4907
    • Santoro, M.M.1    Bolen, D.W.2
  • 31
    • 0029996162 scopus 로고    scopus 로고
    • Incorporation of non-local interactions in protein secondary structure prediction from the amino acid sequence
    • Frishman D, Argos P, (1996) Incorporation of non-local interactions in protein secondary structure prediction from the amino acid sequence. Protein Eng 9(2): 133-42.
    • (1996) Protein Eng , vol.9 , Issue.2 , pp. 133-142
    • Frishman, D.1    Argos, P.2
  • 32
    • 84855690465 scopus 로고    scopus 로고
    • Prediction of protein secondary structure from circular dichroism using theoretically derived spectra
    • doi:10.1002/prot.23188
    • Louis-Jeune C, Andrade-Navarro MA, Perez-Iratxeta C, (2011) Prediction of protein secondary structure from circular dichroism using theoretically derived spectra. Proteins doi:10.1002/prot.23188.
    • (2011) Proteins
    • Louis-Jeune, C.1    Andrade-Navarro, M.A.2    Perez-Iratxeta, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.