메뉴 건너뛰기




Volumn 88, Issue 9, 2007, Pages 2619-2626

Amyloid-specific fluorophores for the rapid, sensitive in situ detection of prion contamination on surgical instruments

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; PRION PROTEIN; STAINLESS STEEL; THIAZOLE; THIOFLAVINE;

EID: 34548202342     PISSN: 00221317     EISSN: None     Source Type: Journal    
DOI: 10.1099/vir.0.82228-0     Document Type: Article
Times cited : (30)

References (54)
  • 2
    • 0035140891 scopus 로고    scopus 로고
    • Heat stability of prion rods and recombinant prion protein in water, lipid and lipid-water mixtures
    • Appel, T., Wolff, M., von Rheinbaben, F., Heinzel, M. & Riesner, D. (2001). Heat stability of prion rods and recombinant prion protein in water, lipid and lipid-water mixtures. J Gen Virol 82, 465-473.
    • (2001) J Gen Virol , vol.82 , pp. 465-473
    • Appel, T.1    Wolff, M.2    von Rheinbaben, F.3    Heinzel, M.4    Riesner, D.5
  • 6
    • 0033036115 scopus 로고    scopus 로고
    • The acute inflammatory response in CNS following injection of prion brain homogenate or normal brain homogenate
    • Betmouni, S. & Perry, V. H. (1999). The acute inflammatory response in CNS following injection of prion brain homogenate or normal brain homogenate. Neuropathol Appl Neurobiol 25, 20-28.
    • (1999) Neuropathol Appl Neurobiol , vol.25 , pp. 20-28
    • Betmouni, S.1    Perry, V.H.2
  • 9
    • 0017059781 scopus 로고
    • Cerebral amyloidosis in scrapie in the mouse: Effect of agent strain and mouse genotype
    • Bruce, M. E., Dickinson, A. G. & Fraser, H. (1976). Cerebral amyloidosis in scrapie in the mouse: effect of agent strain and mouse genotype. Neuropathol Appl Neurobiol 2, 471-478.
    • (1976) Neuropathol Appl Neurobiol , vol.2 , pp. 471-478
    • Bruce, M.E.1    Dickinson, A.G.2    Fraser, H.3
  • 10
    • 0014141740 scopus 로고
    • The specificity of the staining of amyloid deposits with thioflavine T
    • Burns, J., Pennock, C. A. & Stoward, P. J. (1967). The specificity of the staining of amyloid deposits with thioflavine T. J Pathol Bacteriol 94, 337-344.
    • (1967) J Pathol Bacteriol , vol.94 , pp. 337-344
    • Burns, J.1    Pennock, C.A.2    Stoward, P.J.3
  • 11
    • 0029664899 scopus 로고    scopus 로고
    • Iatrogenic and zoonotic Creutzfeldt-Jakob disease: The Australian perspective
    • Collins, S. & Masters, C. L. (1996). Iatrogenic and zoonotic Creutzfeldt-Jakob disease: the Australian perspective. Med J Aust 164, 598-602.
    • (1996) Med J Aust , vol.164 , pp. 598-602
    • Collins, S.1    Masters, C.L.2
  • 12
    • 0034930258 scopus 로고    scopus 로고
    • Evaluation of a rapid Western immunoblotting procedure for the diagnosis of bovine spongiform encephalopathy (BSE) in the UK
    • Cooley, W. A., Clark, J. K., Ryder, S. J., Davis, L. A., Farrelly, S. S. & Stack, M. J. (2001). Evaluation of a rapid Western immunoblotting procedure for the diagnosis of bovine spongiform encephalopathy (BSE) in the UK. J Comp Pathol 125, 64-70.
    • (2001) J Comp Pathol , vol.125 , pp. 64-70
    • Cooley, W.A.1    Clark, J.K.2    Ryder, S.J.3    Davis, L.A.4    Farrelly, S.S.5    Stack, M.J.6
  • 13
    • 0002773247 scopus 로고
    • Amino acids and proteins of developing mammalian brain
    • Edited by W. A. Himwich. New York: Marcel Dekker
    • Davis, J. M. & Himwich, W. A. (1973). Amino acids and proteins of developing mammalian brain. In Biochemistry of the Developing Brain, p. 102. Edited by W. A. Himwich. New York: Marcel Dekker.
    • (1973) Biochemistry of the Developing Brain , pp. 102
    • Davis, J.M.1    Himwich, W.A.2
  • 14
    • 18744402716 scopus 로고    scopus 로고
    • Early behavioural changes in mice infected with BSE and scrapie: Automated home cage monitoring reveals prion strain differences
    • Dell'Omo, G., Vannoni, E., Vyssotski, A. L., Di Bari, M. A., Nonno, R., Agrimi, U. & Lipp, H. P. (2002). Early behavioural changes in mice infected with BSE and scrapie: automated home cage monitoring reveals prion strain differences. Eur J Neurosci 16, 735-742.
    • (2002) Eur J Neurosci , vol.16 , pp. 735-742
    • Dell'Omo, G.1    Vannoni, E.2    Vyssotski, A.L.3    Di Bari, M.A.4    Nonno, R.5    Agrimi, U.6    Lipp, H.P.7
  • 15
    • 34548223240 scopus 로고    scopus 로고
    • Folch Pi, J. (1955). In Biochemistry and the Developing Nervous System, pp. 121-133. Edited by H. Waelsch. New York. Academic Press.
    • Folch Pi, J. (1955). In Biochemistry and the Developing Nervous System, pp. 121-133. Edited by H. Waelsch. New York. Academic Press.
  • 17
    • 0026569388 scopus 로고
    • An improved thioflavine S method for staining neurofibrillary tangles and senile plaques in Alzheimer's disease
    • Guntern, R., Bouras, C., Hof, P. R. & Vallet, P. G. (1992). An improved thioflavine S method for staining neurofibrillary tangles and senile plaques in Alzheimer's disease. Experientia 48, 8-10.
    • (1992) Experientia , vol.48 , pp. 8-10
    • Guntern, R.1    Bouras, C.2    Hof, P.R.3    Vallet, P.G.4
  • 18
    • 33845933773 scopus 로고    scopus 로고
    • The possible role of protein X, a putative auxiliary factor in pathological prion replication, in regulating a physiological endoproteolytic cleavage of cellular prion protein
    • Hachiya, N. S., Imagawa, M. & Kaneko, K. (2007). The possible role of protein X, a putative auxiliary factor in pathological prion replication, in regulating a physiological endoproteolytic cleavage of cellular prion protein. Med Hypotheses 68, 670-673.
    • (2007) Med Hypotheses , vol.68 , pp. 670-673
    • Hachiya, N.S.1    Imagawa, M.2    Kaneko, K.3
  • 21
    • 33645957674 scopus 로고    scopus 로고
    • Variant Creutzfeldt-Jakob disease: Risk of transmission by blood transfusion and blood therapies
    • Suppl. 1, 8-15
    • Ironside, J. W. (2006). Variant Creutzfeldt-Jakob disease: risk of transmission by blood transfusion and blood therapies. Haemophilia 12 (Suppl. 1), 8-15.
    • (2006) Haemophilia , vol.12
    • Ironside, J.W.1
  • 22
    • 2942672633 scopus 로고    scopus 로고
    • Amyloid imaging probes are useful for detection of prion plaques and treatment of transmissible spongiform encephalopathies
    • Ishikawa, K., Doh-ura, K., Kudo, Y., Nishida, N., Murakami-Kubo, I., Ando, Y., Sawada, T. & Iwaki, T. (2004). Amyloid imaging probes are useful for detection of prion plaques and treatment of transmissible spongiform encephalopathies. J Gen Virol 85, 1785-1790.
    • (2004) J Gen Virol , vol.85 , pp. 1785-1790
    • Ishikawa, K.1    Doh-ura, K.2    Kudo, Y.3    Nishida, N.4    Murakami-Kubo, I.5    Ando, Y.6    Sawada, T.7    Iwaki, T.8
  • 24
    • 0037271487 scopus 로고    scopus 로고
    • Rapid detection of biofilms and adherent pathogens using scanning confocal microscopy and episcopic differential interference contrast microscopy
    • Keevil, C. W. (2003). Rapid detection of biofilms and adherent pathogens using scanning confocal microscopy and episcopic differential interference contrast microscopy. Water Sci Technol 47, 105-116.
    • (2003) Water Sci Technol , vol.47 , pp. 105-116
    • Keevil, C.W.1
  • 25
    • 0035902875 scopus 로고    scopus 로고
    • Uncharged thioflavin-T derivatives bind to amyloid-beta protein with high affinity and readily enter the brain
    • Klunk, W. E., Wang, Y., Huang, G. F., Debnath, M. L., Holt, D. P. & Mathis, C. A. (2001). Uncharged thioflavin-T derivatives bind to amyloid-beta protein with high affinity and readily enter the brain. Life Sci 69, 1471-1484.
    • (2001) Life Sci , vol.69 , pp. 1471-1484
    • Klunk, W.E.1    Wang, Y.2    Huang, G.F.3    Debnath, M.L.4    Holt, D.P.5    Mathis, C.A.6
  • 26
    • 0036132894 scopus 로고    scopus 로고
    • Immunohistochemistry for the prion protein: Comparison of different monoclonal antibodies in human prion disease subtypes
    • Kovacs, G. G., Head, M. W., Hegyi, I., Bunn, T. J., Flicker, H., Hainfellner, J. A., McCardle, L., Laszlo, L., Jarius, C. & other authors (2002). Immunohistochemistry for the prion protein: comparison of different monoclonal antibodies in human prion disease subtypes. Brain Pathol 12, 1-11.
    • (2002) Brain Pathol , vol.12 , pp. 1-11
    • Kovacs, G.G.1    Head, M.W.2    Hegyi, I.3    Bunn, T.J.4    Flicker, H.5    Hainfellner, J.A.6    McCardle, L.7    Laszlo, L.8    Jarius, C.9
  • 27
    • 0035037753 scopus 로고    scopus 로고
    • A direct relationship between the partitioning of the pathogenic prion protein and transmissible spongiform encephalopathy infectivity during the purification of plasma proteins
    • Lee, D. C., Stenland, C. J., Miller, J. L., Cai, K., Ford, E. K., Gilligan, K. J., Hartwell, R. C., Terry, J. C., Rubenstein, R. & other authors (2001). A direct relationship between the partitioning of the pathogenic prion protein and transmissible spongiform encephalopathy infectivity during the purification of plasma proteins. Transfusion 41, 449-455.
    • (2001) Transfusion , vol.41 , pp. 449-455
    • Lee, D.C.1    Stenland, C.J.2    Miller, J.L.3    Cai, K.4    Ford, E.K.5    Gilligan, K.J.6    Hartwell, R.C.7    Terry, J.C.8    Rubenstein, R.9
  • 28
    • 33749319496 scopus 로고    scopus 로고
    • The sensitivity of approved ninhydrin and Biuret tests in the assessment of protein contamination on surgical steel as an aid to prevent iatrogenic prion transmission
    • Lipscomb, I. P., Pinchin, H. E., Collin, R., Harris, K. & Keevil, C. W. (2006a). The sensitivity of approved ninhydrin and Biuret tests in the assessment of protein contamination on surgical steel as an aid to prevent iatrogenic prion transmission. J Hosp Infect 64, 288-292.
    • (2006) J Hosp Infect , vol.64 , pp. 288-292
    • Lipscomb, I.P.1    Pinchin, H.E.2    Collin, R.3    Harris, K.4    Keevil, C.W.5
  • 29
    • 30344434303 scopus 로고    scopus 로고
    • Rapid method for the sensitive detection of protein contamination on surgical instruments
    • Lipscomb, I. P., Sihota, A. K., Botham, M., Harris, K. L. & Keevil, C. W. (2006b). Rapid method for the sensitive detection of protein contamination on surgical instruments. J Hosp Infect 62, 141-148.
    • (2006) J Hosp Infect , vol.62 , pp. 141-148
    • Lipscomb, I.P.1    Sihota, A.K.2    Botham, M.3    Harris, K.L.4    Keevil, C.W.5
  • 30
    • 34248642838 scopus 로고    scopus 로고
    • Comparative study of surgical instruments from sterile-service departments for presence of residual gram-negative endotoxin and proteinaceous deposits
    • Lipscomb, I. P., Sihota, A. K. & Keevil, C. W. (2006c). Comparative study of surgical instruments from sterile-service departments for presence of residual gram-negative endotoxin and proteinaceous deposits. J Clin Microbiol 44, 3728-3733.
    • (2006) J Clin Microbiol , vol.44 , pp. 3728-3733
    • Lipscomb, I.P.1    Sihota, A.K.2    Keevil, C.W.3
  • 31
    • 33750573183 scopus 로고    scopus 로고
    • Diathermy forceps and pencils: Reservoirs for protein and prion contamination?
    • Lipscomb, I. P., Sihota, A. K. & Keevil, C. W. (2006d). Diathermy forceps and pencils: reservoirs for protein and prion contamination? J Hosp Infect 64, 193-194.
    • (2006) J Hosp Infect , vol.64 , pp. 193-194
    • Lipscomb, I.P.1    Sihota, A.K.2    Keevil, C.W.3
  • 32
    • 0041743826 scopus 로고    scopus 로고
    • Immunohistochemical comparison of anti-prion protein (PrP) antibodies in the CNS of mice infected with scrapie
    • Liu, W. G., Brown, D. A. & Fraser, J. R. (2003). Immunohistochemical comparison of anti-prion protein (PrP) antibodies in the CNS of mice infected with scrapie. J Histochem Cytochem 51, 1065-1071.
    • (2003) J Histochem Cytochem , vol.51 , pp. 1065-1071
    • Liu, W.G.1    Brown, D.A.2    Fraser, J.R.3
  • 34
    • 14844303913 scopus 로고    scopus 로고
    • Evidence for the presence of three distinct binding sites for the thioflavin T class of Alzheimer's disease PET imaging agents on β-amyloid peptide fibrils
    • Lockhart, A., Ye, L., Judd, D. B., Merritt, A. T., Lowe, P. N., Morgenstern, J. L., Hong, G., Gee, A. D. & Brown, J. (2005). Evidence for the presence of three distinct binding sites for the thioflavin T class of Alzheimer's disease PET imaging agents on β-amyloid peptide fibrils. J Biol Chem 280, 7677-7684.
    • (2005) J Biol Chem , vol.280 , pp. 7677-7684
    • Lockhart, A.1    Ye, L.2    Judd, D.B.3    Merritt, A.T.4    Lowe, P.N.5    Morgenstern, J.L.6    Hong, G.7    Gee, A.D.8    Brown, J.9
  • 35
    • 0023782403 scopus 로고
    • Immunostaining of scrapie cerebral amyloid plaques with antisera raised to scrapie-associated fibrils (SAF)
    • McBride, P. A., Bruce, M. E. & Fraser, H. (1988). Immunostaining of scrapie cerebral amyloid plaques with antisera raised to scrapie-associated fibrils (SAF). Neuropathol Appl Neurobiol 14, 325-336.
    • (1988) Neuropathol Appl Neurobiol , vol.14 , pp. 325-336
    • McBride, P.A.1    Bruce, M.E.2    Fraser, H.3
  • 38
    • 34548242329 scopus 로고    scopus 로고
    • NHS Estates (1997). Washer-Disinfectors: Validation and Verification. Health Technical Memorandum 2030. Edited by NHS Estates. London: The Stationery Office. http://195.92.246.148/ knowledge_network/documents/ HTM2030%20Washer-disinfectors%20Operational%20management% 202003123145743890.pdf
    • NHS Estates (1997). Washer-Disinfectors: Validation and Verification. Health Technical Memorandum 2030. Edited by NHS Estates. London: The Stationery Office. http://195.92.246.148/ knowledge_network/documents/ HTM2030%20Washer-disinfectors%20Operational%20management% 202003123145743890.pdf
  • 40
    • 25144472636 scopus 로고    scopus 로고
    • Tissue safety in view of CJD and variant CJD
    • Pauli, G. (2005). Tissue safety in view of CJD and variant CJD. Cell Tissue Bank 6, 191-200.
    • (2005) Cell Tissue Bank , vol.6 , pp. 191-200
    • Pauli, G.1
  • 41
    • 4043157677 scopus 로고    scopus 로고
    • Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient
    • Peden, A. H., Head, M. W., Ritchie, D. L., Bell, J. E. & Ironside, J. W. (2004). Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient. Lancet 364, 527-529.
    • (2004) Lancet , vol.364 , pp. 527-529
    • Peden, A.H.1    Head, M.W.2    Ritchie, D.L.3    Bell, J.E.4    Ironside, J.W.5
  • 42
    • 33644651130 scopus 로고    scopus 로고
    • Sc in the skeletal muscle of patients with variant, iatrogenic, and sporadic forms of Creutzfeldt-Jakob disease
    • Sc in the skeletal muscle of patients with variant, iatrogenic, and sporadic forms of Creutzfeldt-Jakob disease. Am J Pathol 168, 927-935.
    • (2006) Am J Pathol , vol.168 , pp. 927-935
    • Peden, A.H.1    Ritchie, D.L.2    Head, M.W.3    Ironside, J.W.4
  • 43
    • 0031859927 scopus 로고    scopus 로고
    • The prion diseases
    • Prusiner, S. B. (1998). The prion diseases. Brain Pathol 8, 499-513.
    • (1998) Brain Pathol , vol.8 , pp. 499-513
    • Prusiner, S.B.1
  • 44
    • 33751352055 scopus 로고    scopus 로고
    • Cell biology: Infectious Alzheimer's disease?
    • Riek, R. (2006). Cell biology: infectious Alzheimer's disease? Nature 444, 429-431.
    • (2006) Nature , vol.444 , pp. 429-431
    • Riek, R.1
  • 45
    • 4344684277 scopus 로고    scopus 로고
    • Advances in the detection of prion protein in peripheral tissues of variant Creutzfeldt-Jakob disease patients using paraffin-embedded tissue blotting
    • Ritchie, D. L., Head, M. W. & Ironside, J. W. (2004). Advances in the detection of prion protein in peripheral tissues of variant Creutzfeldt-Jakob disease patients using paraffin-embedded tissue blotting. Neuropathol Appl Neurobiol 30, 360-368.
    • (2004) Neuropathol Appl Neurobiol , vol.30 , pp. 360-368
    • Ritchie, D.L.1    Head, M.W.2    Ironside, J.W.3
  • 46
    • 0014086078 scopus 로고
    • Thioflavin-T for amyloid detection
    • Saeed, S. M. & Fine, G. (1967). Thioflavin-T for amyloid detection. Am J Clin Pathol 47, 588-593.
    • (1967) Am J Clin Pathol , vol.47 , pp. 588-593
    • Saeed, S.M.1    Fine, G.2
  • 48
    • 30344467886 scopus 로고    scopus 로고
    • Spongiform Encephalopathy Advisory Committee
    • Spongiform Encephalopathy Advisory Committee (2005). Minutes of the open session of the 86th meeting. http://www.seac.gov.uk/minutes/ final86.pdf
    • (2005) Minutes of the open session of the 86th meeting
  • 49
    • 33749822624 scopus 로고    scopus 로고
    • The emerging principles of mammalian prion propagation and transmissibility barriers: Insight from studies in vitro
    • Surewicz, W. K., Jones, E. M. & Apetri, A. C. (2006). The emerging principles of mammalian prion propagation and transmissibility barriers: insight from studies in vitro. Acc Chem Res 39, 654-662.
    • (2006) Acc Chem Res , vol.39 , pp. 654-662
    • Surewicz, W.K.1    Jones, E.M.2    Apetri, A.C.3
  • 50
    • 34548211950 scopus 로고    scopus 로고
    • UK CJD Surveillance Unit (2006). Creutzfeldt-Jakob disease surveillance in the UK. Fourteenth annual report. http://www.cjd.ed.ac.uk/report14.pdf
    • UK CJD Surveillance Unit (2006). Creutzfeldt-Jakob disease surveillance in the UK. Fourteenth annual report. http://www.cjd.ed.ac.uk/report14.pdf
  • 51
    • 0035928432 scopus 로고    scopus 로고
    • Tissue distribution of protease resistant prion protein in variant Creutzfeldt-Jakob disease using a highly sensitive immunoblotting assay
    • Wadsworth, J. D., Joiner, S., Hill, A. F., Campbell, T. A., Desbruslais, M., Luthert, P. J. & Collinge, J. (2001). Tissue distribution of protease resistant prion protein in variant Creutzfeldt-Jakob disease using a highly sensitive immunoblotting assay. Lancet 358, 171-180.
    • (2001) Lancet , vol.358 , pp. 171-180
    • Wadsworth, J.D.1    Joiner, S.2    Hill, A.F.3    Campbell, T.A.4    Desbruslais, M.5    Luthert, P.J.6    Collinge, J.7
  • 54
    • 0033066555 scopus 로고    scopus 로고
    • Infectivity of scrapie prions bound to a stainless steel surface
    • Zobeley, E., Flechsig, E., Cozzio, A., Enari, M. & Weissmann, C. (1999). Infectivity of scrapie prions bound to a stainless steel surface. Mol Med 5, 240-243.
    • (1999) Mol Med , vol.5 , pp. 240-243
    • Zobeley, E.1    Flechsig, E.2    Cozzio, A.3    Enari, M.4    Weissmann, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.