메뉴 건너뛰기




Volumn 1804, Issue 11, 2010, Pages 2146-2152

Exploring the positional importance of aromatic residues and lysine in the interactions of peptides with the Plasmodium falciparum Hsp70-1

Author keywords

Apicoplast; Fluorescence; PfHsp70 1; Plasmodium falciparum; Transit peptide

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; HEAT SHOCK PROTEIN 70; LYSINE; NUCLEAR PROTEIN;

EID: 77956651076     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.08.007     Document Type: Article
Times cited : (11)

References (27)
  • 1
    • 0037844597 scopus 로고    scopus 로고
    • Biosynthetic pathways of plastid-derived organelles as potential drug targets against parasitic apicomplexa
    • Seeber F. Biosynthetic pathways of plastid-derived organelles as potential drug targets against parasitic apicomplexa. Curr. Drug Targets Immune. Endocr. Metabol. Disord. 2003, 3:99-109.
    • (2003) Curr. Drug Targets Immune. Endocr. Metabol. Disord. , vol.3 , pp. 99-109
    • Seeber, F.1
  • 2
    • 0035103466 scopus 로고    scopus 로고
    • Nuclear-encoded plastid-targeted genes suggest a single common origin for apicomplexan and dinoflagellate plastids
    • Fast N.M., Kissinger J.C., Roos D.S., Keeling P.J. Nuclear-encoded plastid-targeted genes suggest a single common origin for apicomplexan and dinoflagellate plastids. Mol. Biol. Evol. 2001, 18:418-426.
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 418-426
    • Fast, N.M.1    Kissinger, J.C.2    Roos, D.S.3    Keeling, P.J.4
  • 5
    • 0034678922 scopus 로고    scopus 로고
    • Protein trafficking to the plastid of Plasmodium falciparum is via the secretory pathway
    • Waller R.F., Reed M.B., Cowman A.F., McFadden G.I. Protein trafficking to the plastid of Plasmodium falciparum is via the secretory pathway. EMBO J. 2000, 19:1794-1802.
    • (2000) EMBO J. , vol.19 , pp. 1794-1802
    • Waller, R.F.1    Reed, M.B.2    Cowman, A.F.3    McFadden, G.I.4
  • 6
    • 8444244485 scopus 로고    scopus 로고
    • Evolutionary pressures on apicoplast transit peptides
    • Ralph S.A., Foth B.J., Hall N., McFadden G.I. Evolutionary pressures on apicoplast transit peptides. Mol. Biol. Evol. 2004, 21:2183-2194.
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 2183-2194
    • Ralph, S.A.1    Foth, B.J.2    Hall, N.3    McFadden, G.I.4
  • 7
    • 0035666657 scopus 로고    scopus 로고
    • Deciphering apicoplast targeting signals-feature extraction from nuclear-encoded precursors of Plasmodium falciparum apicoplast proteins
    • Zuegge J., Ralph S., Schmuker M., McFadden G.I., Schneider G. Deciphering apicoplast targeting signals-feature extraction from nuclear-encoded precursors of Plasmodium falciparum apicoplast proteins. Gene 2001, 280:19-26.
    • (2001) Gene , vol.280 , pp. 19-26
    • Zuegge, J.1    Ralph, S.2    Schmuker, M.3    McFadden, G.I.4    Schneider, G.5
  • 10
    • 0030976048 scopus 로고    scopus 로고
    • Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
    • Rudiger S., Germeroth L., Schneider-Mergener J., Bukau B. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 1997, 16:1501-1507.
    • (1997) EMBO J. , vol.16 , pp. 1501-1507
    • Rudiger, S.1    Germeroth, L.2    Schneider-Mergener, J.3    Bukau, B.4
  • 11
    • 0033781954 scopus 로고    scopus 로고
    • Interaction of the targeting sequence of chloroplast precursors with Hsp70 molecular chaperones
    • Rial D.V., Arakaki A.K., Ceccarelli E.A. Interaction of the targeting sequence of chloroplast precursors with Hsp70 molecular chaperones. Eur. J. Biochem. 2000, 267:6239-6248.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6239-6248
    • Rial, D.V.1    Arakaki, A.K.2    Ceccarelli, E.A.3
  • 12
    • 34548461255 scopus 로고    scopus 로고
    • The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum
    • Shonhai A., Boshoff A., Blatch G.L. The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum. Protein Sci. 2007, 16:1803-1818.
    • (2007) Protein Sci. , vol.16 , pp. 1803-1818
    • Shonhai, A.1    Boshoff, A.2    Blatch, G.L.3
  • 13
    • 74549179024 scopus 로고    scopus 로고
    • Plasmodial heat shock proteins: targets for chemotherapy, FEMS
    • Shonhai A. Plasmodial heat shock proteins: targets for chemotherapy, FEMS. Immunol. Med. Microbiol. 2010, 58:61-74.
    • (2010) Immunol. Med. Microbiol. , vol.58 , pp. 61-74
    • Shonhai, A.1
  • 15
    • 67349203991 scopus 로고    scopus 로고
    • Hsp70-1 from Plasmodium falciparum: protein stability, domain analysis and chaperone activity
    • Misra G., Ramachandran R. Hsp70-1 from Plasmodium falciparum: protein stability, domain analysis and chaperone activity. Biophys. Chem. 2009, 142:55-64.
    • (2009) Biophys. Chem. , vol.142 , pp. 55-64
    • Misra, G.1    Ramachandran, R.2
  • 16
    • 0033999271 scopus 로고    scopus 로고
    • Overcoming codon bias: a method for high-level overexpression of Plasmodium and other AT-rich parasite genes in Escherichia coli
    • Baca A.M., Hol W.G. Overcoming codon bias: a method for high-level overexpression of Plasmodium and other AT-rich parasite genes in Escherichia coli. Int. J. Parasitol. 2000, 30:113-118.
    • (2000) Int. J. Parasitol. , vol.30 , pp. 113-118
    • Baca, A.M.1    Hol, W.G.2
  • 17
    • 50849130329 scopus 로고    scopus 로고
    • GraphPad Prism, data analysis, and scientific graphing
    • Swift M.L. GraphPad Prism, data analysis, and scientific graphing. J. Chem. Inf. Comput. Sci. 1997, 37:411-412.
    • (1997) J. Chem. Inf. Comput. Sci. , vol.37 , pp. 411-412
    • Swift, M.L.1
  • 18
    • 0037738615 scopus 로고    scopus 로고
    • The apicoplast: a plastid in Plasmodium falciparum and other apicomplexan parasites
    • Foth B.J., McFadden G.I. The apicoplast: a plastid in Plasmodium falciparum and other apicomplexan parasites. Int. Rev. Cytol. 2003, 224:57-110.
    • (2003) Int. Rev. Cytol. , vol.224 , pp. 57-110
    • Foth, B.J.1    McFadden, G.I.2
  • 19
    • 0142148040 scopus 로고    scopus 로고
    • The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG
    • Stevens S.Y., Cai S., Pellecchia M., Zuiderweg E.R. The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG. Protein Sci. 2003, 12:2588-2596.
    • (2003) Protein Sci. , vol.12 , pp. 2588-2596
    • Stevens, S.Y.1    Cai, S.2    Pellecchia, M.3    Zuiderweg, E.R.4
  • 21
    • 54249123736 scopus 로고    scopus 로고
    • Structure-function study of a Plasmodium falciparum Hsp70 using three dimensional modelling and in vitro analyses
    • Shonhai A., Botha M., de Beer T.A.P., Boshoff A., Blatch G.L. Structure-function study of a Plasmodium falciparum Hsp70 using three dimensional modelling and in vitro analyses. Protein Pept. Lett. 2008, 15:1117-1125.
    • (2008) Protein Pept. Lett. , vol.15 , pp. 1117-1125
    • Shonhai, A.1    Botha, M.2    de Beer, T.A.P.3    Boshoff, A.4    Blatch, G.L.5
  • 22
  • 23
    • 34047268015 scopus 로고    scopus 로고
    • Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker
    • Swain J.F., Dinler G., Sivendran R., Montgomery D.L., Stotz M., Gierasch L.M. Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker. Mol. Cell 2007, 26:27-39.
    • (2007) Mol. Cell , vol.26 , pp. 27-39
    • Swain, J.F.1    Dinler, G.2    Sivendran, R.3    Montgomery, D.L.4    Stotz, M.5    Gierasch, L.M.6
  • 24
    • 0033968437 scopus 로고    scopus 로고
    • In vivo and in vitro interaction of DnaK and a chloroplast transit peptide
    • Ivey R.A., Bruce B.D. In vivo and in vitro interaction of DnaK and a chloroplast transit peptide. Cell Stress Chaperones 2000, 5:62-71.
    • (2000) Cell Stress Chaperones , vol.5 , pp. 62-71
    • Ivey, R.A.1    Bruce, B.D.2
  • 25
    • 0026063035 scopus 로고
    • Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding
    • Palleros D.R., Welch W.J., Fink A.L. Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding. Proc. Natl. Acad. Sci. 1991, 88:5719-5723.
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 5719-5723
    • Palleros, D.R.1    Welch, W.J.2    Fink, A.L.3
  • 26
    • 0028151509 scopus 로고
    • The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE
    • Szabo A., Langer T., Schroder H., Flanagan J., Bukau B., Hartl F.U. The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE. Proc. Natl Acad. Sci. USA 1994, 91:10345-10349.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10345-10349
    • Szabo, A.1    Langer, T.2    Schroder, H.3    Flanagan, J.4    Bukau, B.5    Hartl, F.U.6
  • 27
    • 33745610915 scopus 로고    scopus 로고
    • Structural determinants of HscA peptide-binding specificity
    • Tapley T.L., Cupp-Vickery R.J., Vickery L.E. Structural determinants of HscA peptide-binding specificity. Biochemistry 2006, 45:8058-8066.
    • (2006) Biochemistry , vol.45 , pp. 8058-8066
    • Tapley, T.L.1    Cupp-Vickery, R.J.2    Vickery, L.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.