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Volumn 2010, Issue , 2010, Pages

Cysteine-free proteins in the immunobiology of arthropod-borne diseases

Author keywords

[No Author keywords available]

Indexed keywords

BONE MORPHOGENETIC PROTEIN; CYSTEINE; FLICE INHIBITORY PROTEIN; HYDROLASE; LIPOPROTEIN; PEPTIDYLPROLYL ISOMERASE; PERTACTIN; TRYPTOPHAN; BACTERIAL PROTEIN;

EID: 77953691213     PISSN: 11107243     EISSN: 11107251     Source Type: Journal    
DOI: 10.1155/2010/171537     Document Type: Article
Times cited : (2)

References (27)
  • 1
    • 0032975954 scopus 로고    scopus 로고
    • Emerging and resurging vector-borne diseases
    • DOI 10.1146/annurev.ento.44.1.51
    • N. G. Gratz, "Emerging and resurging vector-borne diseases," Annual Review of Entomology, vol. 44, pp. 51-75, 1999. (Pubitemid 29096966)
    • (1999) Annual Review of Entomology , vol.44 , pp. 51-75
    • Gratz, N.G.1
  • 2
    • 1642453833 scopus 로고    scopus 로고
    • Global change and human vulnerability to vector-borne diseases
    • DOI 10.1128/CMR.17.1.136-173.2004
    • R. W. Sutherst, "Global change and human vulnerability to vector-borne diseases," Clinical Microbiology Reviews, vol. 17, no. 1, pp. 136-173, 2004. (Pubitemid 38124454)
    • (2004) Clinical Microbiology Reviews , vol.17 , Issue.1 , pp. 136-173
    • Sutherst, R.W.1
  • 4
    • 9444285923 scopus 로고    scopus 로고
    • Tularaemia: Bioterrorism defence renews interest in Francisella tularensis
    • DOI 10.1038/nrmicro1045
    • P. C. F. Oyston, A. Sjostedt, and R. W. Titball, "Tularaemia: bioterrorism defence renews interest in Francisella tularensis," Nature Reviews Microbiology, vol. 2, no. 12, pp. 967-978, 2004. (Pubitemid 39562535)
    • (2004) Nature Reviews Microbiology , vol.2 , Issue.12 , pp. 967-978
    • Oyston, P.C.F.1    Sjostedt, A.2    Titball, R.W.3
  • 5
    • 34447116311 scopus 로고    scopus 로고
    • Pathogenic rickettsiae as bioterrorism agents
    • DOI 10.1086/518147
    • A. F. Azad, "Pathogenic rickettsiae as bioterrorism agents," Clinical Infectious Diseases, vol. 45, supplement 1, pp. S52-S55, 2007. (Pubitemid 47036026)
    • (2007) Clinical Infectious Diseases , vol.45 , Issue.SUPPL. 1
    • Azad, A.F.1
  • 6
    • 0036839931 scopus 로고    scopus 로고
    • Yellow fever vaccine safety: A reality or a myth?
    • DOI 10.1016/S0264-410X(02)00409-7, PII S0264410X02004097
    • S. C. Arya, "Yellow fever vaccine safety: a reality or a myth?" Vaccine, vol. 20, no. 31-32, pp. 3627-3628, 2002. (Pubitemid 35223388)
    • (2002) Vaccine , vol.20 , Issue.31-32 , pp. 3627-3628
    • Arya, S.C.1
  • 7
    • 0345447480 scopus 로고    scopus 로고
    • Vaccines and animal models for arboviral encephalitides
    • DOI 10.1016/j.antiviral.2003.08.001
    • A. Nalca, P. F. Fellows, and C. A. Whitehouse, "Vaccines and animal models for arboviral encephalitides," Antiviral Research, vol. 60, no. 3, pp. 153-174, 2003. (Pubitemid 37456864)
    • (2003) Antiviral Research , vol.60 , Issue.3 , pp. 153-174
    • Nalca, A.1    Fellows, P.F.2    Whitehouse, C.A.3
  • 9
    • 34447273166 scopus 로고    scopus 로고
    • Polyspeci-ficity of T cell and B cell receptor recognition
    • K. W. Wucherpfennig, P. M. Allen, F. Celada, et al., "Polyspeci- ficity of T cell and B cell receptor recognition," Seminars in Immunology, vol. 19, no. 4, pp. 216-224, 2007.
    • (2007) Seminars in Immunology , vol.19 , Issue.4 , pp. 216-224
    • Wucherpfennig, K.W.1    Allen, P.M.2    Celada, F.3
  • 10
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • DOI 10.1016/S0968-0004(02)02169-2, PII S0968000402021692
    • P. Tompa, "Intrinsically unstructured proteins," Trend sin Biochemical Sciences, vol. 27, no. 10, pp. 527-533, 2002. (Pubitemid 35279598)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.10 , pp. 527-533
    • Tompa, P.1
  • 11
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: Polymorphism and structural disorder in protein-protein interactions
    • P. Tompa and M. Fuxreiter, "Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions," Trends in Biochemical Sciences, vol. 33, no. 1, pp. 2-8, 2008.
    • (2008) Trends in Biochemical Sciences , vol.33 , Issue.1 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 12
    • 22744437069 scopus 로고    scopus 로고
    • Natively disordered proteins: Functions and predictions
    • DOI 10.2165/00822942-200403020-00005
    • P. Romero, Z. Obradovic, and A. K. Dunker, "Natively disordered proteins: functions and predictions," Applied Bioinfor-matics, vol. 3, no. 2-3, pp. 105-113, 2004. (Pubitemid 41032063)
    • (2004) Applied Bioinformatics , vol.3 , Issue.2-3 , pp. 105-113
    • Romero, P.1    Obradovic, Z.2    Dunker, A.K.3
  • 16
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • DOI 10.1016/j.jmb.2004.05.028, PII S0022283604005972
    • J. D. Bendtsen, H. Nielsen, G. von Heijne, and S. Brunak, "Improved prediction of signal peptides: signalP 3.0," Journal of Molecular Biology, vol. 340, no. 4, pp. 783-795, 2004. (Pubitemid 38829638)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.4 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    Von Heijne, G.3    Brunak, S.4
  • 17
    • 0029988488 scopus 로고    scopus 로고
    • Structure of Bordetella pertussis virulence factor P.69 pertactin
    • DOI 10.1038/381090a0
    • P. Emsley, I. G. Charles, N. F. Fairweather, and N. W. Isaacs, "Structure of Bordetella pertussis virulence factor P.69 pertactin," Nature, vol. 381, no. 6577, pp. 90-92, 1996. (Pubitemid 26130010)
    • (1996) Nature , vol.381 , Issue.6577 , pp. 90-92
    • Emsley, P.1    Charles, I.G.2    Fairweather, N.F.3    Isaacs, N.W.4
  • 18
    • 0032169654 scopus 로고    scopus 로고
    • The great escape: Structure and function of the autotransporter proteins
    • DOI 10.1016/S0966-842X(98)01318-3, PII S0966842X98013183
    • I. R. Henderson, F. Navarro-Garcia, and J. P. Nataro, "The great escape: structure and function of the autotransporter proteins," Trends in Microbiology, vol. 6, no. 9, pp. 370-378, 1998. (Pubitemid 28473198)
    • (1998) Trends in Microbiology , vol.6 , Issue.9 , pp. 370-378
    • Henderson, I.R.1    Navarro-Garcia, F.2    Nataro, J.P.3
  • 19
    • 33645108429 scopus 로고    scopus 로고
    • The immunomod-ulatory factors of arthropod saliva and the potential for these factors to serve as vaccine targets to prevent pathogen transmission
    • R. G. Titus, J. V. Bishop, and J. S. Mejia, "The immunomod-ulatory factors of arthropod saliva and the potential for these factors to serve as vaccine targets to prevent pathogen transmission," Parasite Immunology, vol. 28, no. 4, pp. 131-141, 2006.
    • (2006) Parasite Immunology , vol.28 , Issue.4 , pp. 131-141
    • Titus, R.G.1    Bishop, J.V.2    Mejia, J.S.3
  • 20
    • 33746296447 scopus 로고    scopus 로고
    • Is it possible to develop pan-arthropod vaccines?
    • DOI 10.1016/j.pt.2006.06.001, PII S1471492206001309
    • J. S. Mejia, J. V. Bishop, and R. G. Titus, "Is it possible to develop pan-arthropod vaccines?" Trendsin Parasitology , vol. 22, no. 8, pp. 367-370, 2006. (Pubitemid 44108756)
    • (2006) Trends in Parasitology , vol.22 , Issue.8 , pp. 367-370
    • Mejia, J.S.1    Bishop, J.V.2    Titus, R.G.3
  • 21
    • 33845999485 scopus 로고    scopus 로고
    • Evolution of arthropod disease vector
    • W. C. Marquardt, et al., Ed. Elsevier, London, UK, 2nd edition
    • W. C. Black IV and B. C. Kondratieff, "Evolution of arthropod disease vector," in Biology of Disease Vectors, W. C. Marquardt, et al., Ed., pp. 9-23, Elsevier, London, UK, 2nd edition, 2005.
    • (2005) Biology of Disease Vectors , pp. 9-23
    • Black IV, W.C.1    Kondratieff, B.C.2
  • 22
    • 34250792303 scopus 로고    scopus 로고
    • Use of site-directed cysteine and disulfide chemistry to probe protein structure and dynamics: Applications to soluble and transmembrane receptors of bacterial chemotaxis
    • DOI 10.1016/S0076-6879(07)23002-2, PII S0076687907230022, Two Component Signaling Systems, Part B
    • R. B. Bass, S. L. Butler, S. A. Chervitz, S. L. Gloor, and J. J. Falke, "Use of site-directed cysteine and disulfide chemistry to probe protein structure and dynamics: applications to soluble and transmembrane receptors of bacterial chemotaxis," Methods in Enzymology, vol. 423, pp. 25-51, 2007. (Pubitemid 46991090)
    • (2007) Methods in Enzymology , vol.423 , pp. 25-51
    • Bass, R.B.1    Butler, S.L.2    Chervitz, S.A.3    Gloor, S.L.4    Falke, J.J.5
  • 23
    • 0029909653 scopus 로고    scopus 로고
    • Membrane-penetrating domain of streptolysin O identified by cysteine scanning mutagenesis
    • DOI 10.1074/jbc.271.43.26664
    • M. Palmer, P. Saweljew, I. Vulicevic, A. Valeva, M. Kehoe, and S. Bhakdi, "Membrane-penetrating domain of streptolysin O identified by cysteine scanning mutagenesis," Journal of Biological Chemistry, vol. 271, no. 43, pp. 26664-26667, 1996. (Pubitemid 26359071)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.43 , pp. 26664-26667
    • Palmer, M.1    Saweljew, P.2    Vulicevic, I.3    Valeva, A.4    Kehoe, M.5    Bhakdi, S.6
  • 25
    • 4744357458 scopus 로고    scopus 로고
    • The surface-mosaic model in host-parasite relationships
    • DOI 10.1016/j.pt.2004.08.005, PII S1471492204002119
    • J. S. Mejia, F. Moreno, C. Muskus, I. D. Véez, and R. G. Titus, "The surface-mosaic model in host-parasite relationships," Trendsin Parasitology , vol. 20, no. 11, pp. 508-511, 2004. (Pubitemid 39313088)
    • (2004) Trends in Parasitology , vol.20 , Issue.11 , pp. 508-511
    • Mejia, J.S.1    Moreno, F.2    Muskus, C.3    Velez, I.D.4    Titus, R.G.5
  • 26
    • 41049091705 scopus 로고    scopus 로고
    • Intrinsic disorder in pathogenic and non-pathogenic microbes: Discovering and analyzing the unfoldomes of early-branching eukaryotes
    • DOI 10.1039/b719168e
    • A. Mohan, W. J. Sullivan Jr., P. Radivojac, A. K. Dunker, and V. N. Uversky, "Intrinsec disorder in pathogenic and non-pathogenic microbes: discovering and analyzing the unfoldomes of early-branching eukaryotes," Molecular BioSystems, vol. 4, no. 4, pp. 328-340, 2008. (Pubitemid 351422588)
    • (2008) Molecular BioSystems , vol.4 , Issue.4 , pp. 328-340
    • Mohan, A.1    Sullivan Jr., W.J.2    Radivojac, P.3    Dunker, A.K.4    Uversky, V.N.5
  • 27
    • 0024333351 scopus 로고
    • α-Macroglobulins: structure, shape, and mechanism of proteinase complex formation
    • L. Sottrup-Jensen, "α-macroglobulins: structure, shape, and mechanism of proteinase complex formation," Journal of Biological Chemistry, vol. 264, no. 20, pp. 11539-11542, 1989. (Pubitemid 19185316)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.20 , pp. 11539-11542
    • Sottrup-Jensen, L.1


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