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Volumn 26, Issue 2, 2005, Pages 243-249

Heterologous expression, characterization and structural studies of a hydrophobic peptide from the HIV-1 p24 protein

Author keywords

Circular dichroism; Fluorescence spectroscopy; p24 HIV 1; Recombinant peptide; Synthetic gene

Indexed keywords

BACTERIAL PROTEIN; CAPSID PROTEIN; GAG PROTEIN; HYBRID PROTEIN; OLIGOMER; RECOMBINANT PROTEIN;

EID: 11144248099     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2004.09.014     Document Type: Article
Times cited : (5)

References (35)
  • 2
    • 0033106192 scopus 로고    scopus 로고
    • Head-to-tail dimers and interdomais flexibility revealed by the crystal structure of HIV-1 capsid protein (p24) complexed with a monoclonal antibody Fab
    • C. Berthet-Colominas, S. Monaco, A. Novelli, G. Sibai, F. Mallet, and S. Cusak Head-to-tail dimers and interdomais flexibility revealed by the crystal structure of HIV-1 capsid protein (p24) complexed with a monoclonal antibody Fab EMBO J 18 1999 1124 1136
    • (1999) EMBO J , vol.18 , pp. 1124-1136
    • Berthet-Colominas, C.1    Monaco, S.2    Novelli, A.3    Sibai, G.4    Mallet, F.5    Cusak, S.6
  • 3
    • 0036635446 scopus 로고    scopus 로고
    • Assembling the human immunodeficiency virus type 1
    • A. Cimarelli, and J.-L. Darlix Assembling the human immunodeficiency virus type 1 Cell Mol Life Sci 59 2002 1166 1184
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1166-1184
    • Cimarelli, A.1    Darlix, J.-L.2
  • 4
    • 0032053024 scopus 로고    scopus 로고
    • Recombinant fusion proteins for the industrial production of disulfide bridge containing peptides: Purification, oxidation without concatamer formation, and selective cleavage
    • H. Dobeli, H. Andres, N. Breyer, N. Draeger, D. Sizmann, and M.T. Zuber Recombinant fusion proteins for the industrial production of disulfide bridge containing peptides: purification, oxidation without concatamer formation, and selective cleavage Protein Expr Purif 12 1998 404 414
    • (1998) Protein Expr Purif , vol.12 , pp. 404-414
    • Dobeli, H.1    Andres, H.2    Breyer, N.3    Draeger, N.4    Sizmann, D.5    Zuber, M.T.6
  • 6
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • D.M. Eckert, and P.S. Kim Mechanisms of viral membrane fusion and its inhibition Annu Rev Biochem 70 2001 777 810
    • (2001) Annu Rev Biochem , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 8
    • 0025232814 scopus 로고
    • Solid-phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl aminoacids
    • G.B. Fields, and R.L. Noble Solid-phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl aminoacids Int J Peptides Protein Res 35 1990 161 214
    • (1990) Int J Peptides Protein Res , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 9
    • 0036094824 scopus 로고    scopus 로고
    • Formation of a human immunodeficiency virus Type 1 core of optimal stability is crucial for viral replication
    • B.M. Forshey, U. von Schwedler, W.I. Sundquist, and C. Aiken Formation of a human immunodeficiency virus Type 1 core of optimal stability is crucial for viral replication J Virol 76 11 2002 5667 5677
    • (2002) J Virol , vol.76 , Issue.11 , pp. 5667-5677
    • Forshey, B.M.1    Von Schwedler, U.2    Sundquist, W.I.3    Aiken, C.4
  • 10
    • 0032506207 scopus 로고    scopus 로고
    • HIV-1 Gag proteins: Diverse functions in the virus life cycle
    • E.O. Freed HIV-1 Gag proteins: diverse functions in the virus life cycle Virology 251 1998 1 15
    • (1998) Virology , vol.251 , pp. 1-15
    • Freed, E.O.1
  • 11
    • 0032485571 scopus 로고    scopus 로고
    • Genetically engineered synthesis of tandem repetitive polypeptides consisting of glycine-rich sequences of spider dragline silk
    • Y. Fukushima Genetically engineered synthesis of tandem repetitive polypeptides consisting of glycine-rich sequences of spider dragline silk Biopolymers 45 1998 269 279
    • (1998) Biopolymers , vol.45 , pp. 269-279
    • Fukushima, Y.1
  • 12
    • 0031260436 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle
    • S.D. Fuller, T. Wilk, B.E. Gowen, H.-G. Kräusslich, and V.M. Vogt Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle Curr Biol 7 1997 729 738
    • (1997) Curr Biol , vol.7 , pp. 729-738
    • Fuller, S.D.1    Wilk, T.2    Gowen, B.E.3    Kräusslich, H.-G.4    Vogt, V.M.5
  • 13
    • 0030693391 scopus 로고    scopus 로고
    • Structure of the carboxyl-terminal dimerisation domain of the HIV-1 capsid protein
    • T.R. Gamble, S. Yoo, F.F. Vajdos, U.K. Schwedler, D.K. Worthylake, and H. Wang Structure of the carboxyl-terminal dimerisation domain of the HIV-1 capsid protein Science 278 1997 849 853
    • (1997) Science , vol.278 , pp. 849-853
    • Gamble, T.R.1    Yoo, S.2    Vajdos, F.F.3    Schwedler, U.K.4    Worthylake, D.K.5    Wang, H.6
  • 14
    • 2442689040 scopus 로고    scopus 로고
    • The dimerization domain of the HIV-1 capsid protein binds a capsid protein-derived peptide: A biophysical characterization
    • M.T. Garzón, M.C. Lindón-Moya, F.N. Barrera, A. Prieto, J. Gómez, and M.G. Mateu The dimerization domain of the HIV-1 capsid protein binds a capsid protein-derived peptide: a biophysical characterization Protein Sci 13 2004 1512 1523
    • (2004) Protein Sci , vol.13 , pp. 1512-1523
    • Garzón, M.T.1    Lindón-Moya, M.C.2    Barrera, F.N.3    Prieto, A.4    Gómez, J.5    Mateu, M.G.6
  • 15
    • 0014955318 scopus 로고
    • In vivo degradation of nonsense fragments in E. coli
    • R. Goldschmidt In vivo degradation of nonsense fragments in E. coli Nature 288 1970 1151 1154
    • (1970) Nature , vol.288 , pp. 1151-1154
    • Goldschmidt, R.1
  • 16
    • 0028567251 scopus 로고
    • A recombinant human immunodeficiency virus type-1 capsid protein (rp24): Its expression, purification and physical-chemical characterization
    • G. Hausdorf, A. Gewiess, V. Wray, and T.J. Porstmann A recombinant human immunodeficiency virus type-1 capsid protein (rp24): its expression, purification and physical-chemical characterization Virol Methods 50 1994 1 9
    • (1994) Virol Methods , vol.50 , pp. 1-9
    • Hausdorf, G.1    Gewiess, A.2    Wray, V.3    Porstmann, T.J.4
  • 17
    • 0028017482 scopus 로고
    • Production, purification, and cleavage of tandem repeats of recombinant peptides
    • A. Kuliopulos, and C.T. Walsh Production, purification, and cleavage of tandem repeats of recombinant peptides J Am Chem Soc 116 1994 4599 4607
    • (1994) J Am Chem Soc , vol.116 , pp. 4599-4607
    • Kuliopulos, A.1    Walsh, C.T.2
  • 20
    • 0030110770 scopus 로고    scopus 로고
    • Upstream strategies to minimize proteolytic degradation upon recombinant production in Escherichia coli
    • M. Murby, M. Uhlén, and S. Stähl Upstream strategies to minimize proteolytic degradation upon recombinant production in Escherichia coli Protein Expr Purif 7 1996 129 136
    • (1996) Protein Expr Purif , vol.7 , pp. 129-136
    • Murby, M.1    Uhlén, M.2    Stähl, S.3
  • 21
    • 0033178536 scopus 로고    scopus 로고
    • Expression and activity of cyclic and linear analogues of esculletin-1, an antimicrobial peptide from amphibian skin
    • D. Ponti, G. Mignogna, M.L. Mangoni, D. De Biase, M. Simmaco, and D. Barra Expression and activity of cyclic and linear analogues of esculletin-1, an antimicrobial peptide from amphibian skin Eur J Biochem 263 1999 921 927
    • (1999) Eur J Biochem , vol.263 , pp. 921-927
    • Ponti, D.1    Mignogna, G.2    Mangoni, M.L.3    De Biase, D.4    Simmaco, M.5    Barra, D.6
  • 22
    • 0017681196 scopus 로고
    • DNA sequencing with chain-terminating inhibitors
    • F. Sanger, S. Nicklen, and R. Coulson DNA sequencing with chain-terminating inhibitors Proc Natl Acad Sci USA 74 1977 5463 5467
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 5463-5467
    • Sanger, F.1    Nicklen, S.2    Coulson, R.3
  • 23
    • 0345665954 scopus 로고
    • Multiple joined genes prevent product degradation in Escherichia coli
    • S.-H. Shen Multiple joined genes prevent product degradation in Escherichia coli Proc Natl Acad Sci USA 81 1984 4627 4631
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 4627-4631
    • Shen, S.-H.1
  • 25
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy
    • N. Sreerama, S.Y. Venyaminov, and R.W. Woody Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy Protein Sci 8 1999 370 380
    • (1999) Protein Sci , vol.8 , pp. 370-380
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 26
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • N. Sreerama, and R.W. Woody A self-consistent method for the analysis of protein secondary structure from circular dichroism Anal Biochem 209 1993 32 44
    • (1993) Anal Biochem , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 29
    • 0033534386 scopus 로고    scopus 로고
    • Structural biology of HIV
    • B.G. Turner, and M.F. Summers Structural biology of HIV J Mol Biol 285 1999 1 32
    • (1999) J Mol Biol , vol.285 , pp. 1-32
    • Turner, B.G.1    Summers, M.F.2
  • 30
    • 0025365143 scopus 로고
    • Gene fusions for purpose of expression: An introduction
    • M. Uhlén, and T. Moks Gene fusions for purpose of expression: an introduction Methods Enzymol 185 1990 129 144
    • (1990) Methods Enzymol , vol.185 , pp. 129-144
    • Uhlén, M.1    Moks, T.2
  • 32
    • 0025306162 scopus 로고
    • Secondary structure of substance P bound to liposomes in organic solvents and in solution from Raman and CD spectroscopy
    • R.W. Williams, and J.L. Weave Secondary structure of substance P bound to liposomes in organic solvents and in solution from Raman and CD spectroscopy J Biol Chem 265 1990 2505 2513
    • (1990) J Biol Chem , vol.265 , pp. 2505-2513
    • Williams, R.W.1    Weave, J.L.2
  • 33
    • 0033949131 scopus 로고    scopus 로고
    • Expression and purification of recombinant neurotensin in Escherichia coli
    • Williamson PTF, J.F. Roth, T. Haddingham, and A. Watts Expression and purification of recombinant neurotensin in Escherichia coli Protein Expr Purif 19 2000 271 275
    • (2000) Protein Expr Purif , vol.19 , pp. 271-275
    • Ptf, W.1    Roth, J.F.2    Haddingham, T.3    Watts, A.4
  • 34
    • 0037058903 scopus 로고    scopus 로고
    • Recent developments in the electronic spectroscopy of amides and α-helical polypeptides
    • R.W. Woody, and A. Koslowski Recent developments in the electronic spectroscopy of amides and α-helical polypeptides Biophys Chem 101/102 2002 535 551
    • (2002) Biophys Chem , vol.101 , Issue.102 , pp. 535-551
    • Woody, R.W.1    Koslowski, A.2
  • 35
    • 0032577940 scopus 로고    scopus 로고
    • Determinants of recombinant production of antimicrobial cationic peptides and creation of peptide variants in bacteria
    • L. Zhang, T. Falla, M. Wu, S. Fidai, J. Burian, and W. Kay Determinants of recombinant production of antimicrobial cationic peptides and creation of peptide variants in bacteria Biochem Biophys Res Commun 247 1998 674 680
    • (1998) Biochem Biophys Res Commun , vol.247 , pp. 674-680
    • Zhang, L.1    Falla, T.2    Wu, M.3    Fidai, S.4    Burian, J.5    Kay, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.