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Volumn 16, Issue 11, 2009, Pages 1379-1385

Surface plasmon resonance imaging sensor for cathepsin determination based on immobilized cystatin

Author keywords

Biosensor; Blood plasma; Cathepsins; Cystatin; Leukocytes; Surface plasmon resonance imaging

Indexed keywords

CATHEPSIN; CYSTATIN; IMMOBILIZED PROTEIN;

EID: 70349948839     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986609789353754     Document Type: Article
Times cited : (25)

References (27)
  • 1
    • 0036374209 scopus 로고    scopus 로고
    • Lysosomal cathepsins: Structure, role in antigen processing and presentation, and cancer
    • DOI 10.1016/S0065-2571(01)00034-6, PII S0065257101000346
    • Turk, V.; Turk, B.; Gunčar, G.; Turk, D.; Kos, J. Lysosomal cathepsins: structure, role in antigen processing and presentation, and cancer. Advan. Enzyme Regul., 2002, 42, 285-303. (Pubitemid 35033544)
    • (2002) Advances in Enzyme Regulation , vol.42 , pp. 285-303
    • Turk, V.1    Turk, B.2    Guncar, G.3    Turk, D.4    Kos, J.5
  • 2
    • 0028783299 scopus 로고
    • Are bacterial proteinases pathogenic factors?
    • Travis, J.; Potempa, J.; Maeda, H. Are bacterial proteinases pathogenic factors? Trends Microbiol., 1995, 3(10), 405-407.
    • (1995) Trends Microbiol. , vol.3 , Issue.10 , pp. 405-407
    • Travis, J.1    Potempa, J.2    Maeda, H.3
  • 3
    • 70349949603 scopus 로고    scopus 로고
    • http://www.laboratoria.net/pl/modules.php?name=News&file= article&sid= 1947
  • 4
    • 70349940153 scopus 로고    scopus 로고
    • PhD dissertation, Graduate Faculty of North. Carolina State University, Department of Food Science, USA
    • Carvajal-Rondanelli, P. Diffusion of protease inhibitors in the muscle cell, PhD dissertation, Graduate Faculty of North. Carolina State University, Department of Food Science, USA, 2002.
    • (2002) Diffusion of Protease Inhibitors in the Muscle Cell
    • Carvajal-Rondanelli, P.1
  • 5
    • 0026575258 scopus 로고
    • Degradation of extracellular-matrix proteins by human cathepsin B from normal and tumor tissues
    • Buck, M.R.; Karustis, D.G.; Day, N.A.; Honn, K.V.; Sloane, B.F. Degradation of extracellular-matrix proteins by human cathepsin. B from normal and tumor tissues. Biochem. J., 1992, 282, 273-278.
    • (1992) Biochem. J. , vol.282 , pp. 273-278
    • Buck, M.R.1    Karustis, D.G.2    Day, N.A.3    Honn, K.V.4    Sloane, B.F.5
  • 7
    • 2142647373 scopus 로고    scopus 로고
    • Nuclear factor- B mediates up-regulation, of cathepsin b by doxorubicin in tumor cells
    • Bien, S.; Ritter, C. A.; Gratz, M.; Sperker, B.; Sonnemann, J.; Beck, J. F.; Kroemer, H. K. Nuclear factor- b mediates up-regulation, of cathepsin b by doxorubicin in tumor cells. Mol. Pharmacol, 2004, 65(5), 1092-1102.
    • (2004) Mol. Pharmacol , vol.65 , Issue.5 , pp. 1092-1102
    • Bien, S.1    Ritter, C.A.2    Gratz, M.3    Sperker, B.4    Sonnemann, J.5    Beck, J.F.6    Kroemer, H.K.7
  • 8
    • 14844311934 scopus 로고    scopus 로고
    • Candidate-based proteomics in the search for biomarkers of cardiovascular disease
    • DOI 10.1113/jphysiol.2004.080473
    • Leigh, A. Candidate-based proteomics In the search for biomarkers of cardiovascular disease. J. Physiol., 2005, 563(1), 23-60. (Pubitemid 40340365)
    • (2005) Journal of Physiology , vol.563 , Issue.1 , pp. 23-60
    • Anderon, L.1
  • 10
    • 33745006609 scopus 로고    scopus 로고
    • Dual role of cathepsin D: Ligand and protease
    • Fusek, M.; Větviǐka, V. Dual role of cathepsin D: ligand and protease. Biomed. Papers, 2005, 149(1), 43-50.
    • (2005) Biomed. Papers , vol.149 , Issue.1 , pp. 43-50
    • Fusek, M.1    Větviǐka, V.2
  • 11
    • 0029877274 scopus 로고    scopus 로고
    • Expression of cathepsin D during the progression of human gliomas
    • DOI 10.1016/0304-3940(96)12584-2
    • Sivaparvathi, M.; Sawaya, R.; Chintala, S.K.; Go, Y.; Gokaslan, Z.L.; Rao, J.S. Expression of cathepsin D during the progression of human gliomas. Neurosci. Lett., 1996, 208,171-174. (Pubitemid 26140149)
    • (1996) Neuroscience Letters , vol.208 , Issue.3 , pp. 171-174
    • Sivaparvathi, M.1    Sawaya, R.2    Chintala, S.K.3    Go, Y.4    Gokaslan, Z.L.5    Rao, J.S.6
  • 12
    • 70349958722 scopus 로고    scopus 로고
    • Extracellular matrix proteases & protein technical guide; Calbiochem
    • Preston, A. Extracellular matrix proteases & protein technical guide; Calbiochem, Oncog. Res. Prod., 2002,VoI. 2, pp. 1-20.
    • (2002) Oncog. Res. Prod. , vol.2 , pp. 1-20
    • Preston, A.1
  • 13
    • 33748445168 scopus 로고    scopus 로고
    • Tripeptydylo-peplydaza i - Wystçpowanie, biogeneza i mechanizmy aktywacji
    • Golabek, A.A. Tripeptydylo-peplydaza I - wystçpowanie, biogeneza i mechanizmy aktywacji. Postepy Biochemii (Poland), 2006, 52(1), 16-23.
    • (2006) Postepy Biochemii (Poland) , vol.52 , Issue.1 , pp. 16-23
    • Golabek, A.A.1
  • 15
    • 0025050764 scopus 로고
    • Identification of the primary antimicrobial domains in human neutrophil cathepsin G
    • Bangalore, N.; Travis, J.; Onunka, V.C.; Pohl, J.; Shafer, W.M. Identification of the primary antimicrobial domains in human neutrophil cathepsin G. J. Biol. Chem., 1990, 265(23), 13584-13588 (Pubitemid 20252209)
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.23 , pp. 13584-13588
    • Bangalore, N.1    Travis, J.2    Onunka, V.C.3    Pohl, J.4    Shafer, W.M.5
  • 16
    • 0032727822 scopus 로고    scopus 로고
    • Capillary electrophoretic determination of cathepsin D activity using Oregon green-labeled hemoglobin
    • DOI 10.1002/(SICI)1522-2683(19991001)20:14<2945::AID-ELPS2945>3.0. CO;2-1
    • Chu, Q.; Jones, S.; Zeece, M. Capillary electrophoretic determination of cathepsin D actvity using Oregon Green-labeled hemoglobin. Electrophoresis, 1999, 20(14), 2945-2951 (Pubitemid 29517226)
    • (1999) Electrophoresis , vol.20 , Issue.14 , pp. 2945-2951
    • Chu, Q.1    Jones, S.2    Zeece, M.3
  • 17
    • 70349960503 scopus 로고    scopus 로고
    • http://en.wikipedia.org/wiki/Cathepsin-G
  • 18
    • 14844311944 scopus 로고    scopus 로고
    • Biotinylated fluorescent peptide substrates for the sensitive and specific determination of cathespin D activity
    • DOI 10.1002/psc.607
    • Baechle, D.; Cansier, A.; Fischer, R.; Brandenburg, J.; Burster, T.; Driessen, C.; Kalbacher, H. Biotinylated fluorescent peptide substrates for the sensitive and specific determination of cathepsin D activity. J. Pept. Sci., 2004, 11(3), 166-174. (Pubitemid 40347549)
    • (2005) Journal of Peptide Science , vol.11 , Issue.3 , pp. 166-174
    • Baechle, D.1    Cansier, A.2    Fischer, R.3    Brandenburg, J.4    Burster, T.5    Driessen, C.6    Kalbacher, H.7
  • 19
    • 0030903497 scopus 로고
    • Correlation of two methods for determination of cathepsin D in breast carcinoma (immunohistochemistry and ELISA in cytosol)
    • (6).
    • Razumović, U.J.; Stojković, R.R.; Petrovećki, M.;Gamulin S. Correlation of two methods for determination of cathepsin D in breast carcinoma (immunohistochemistry and ELISA in cytosol). Breast Cancer Res. Treat., 1991, 43(2), 117-122(6).
    • (1991) Breast Cancer Res. Treat. , vol.43 , Issue.2 , pp. 117-122
    • Razumović, U.J.1    Stojković, R.R.2    Petrovećki, M.3    Gamulin, S.4
  • 20
    • 0041743253 scopus 로고    scopus 로고
    • Determination of cathepsin D activity in mcf-7 cells by capillary zone electrophoresis with, on -column sample stacking
    • Fu, S.; Chu, S. G.; Qin, Z. F.; Xu, X. B. Determination of cathepsin D activity in mcf-7 cells by capillary zone electrophoresis with, on -column sample stacking. Chromatographia, 2003, 58 (1-2), 7378.
    • (2003) Chromatographia , vol.58 , Issue.1-2 , pp. 7378
    • Fu, S.1    Chu, S.G.2    Qin, Z.F.3    Xu, X.B.4
  • 21
    • 10444283096 scopus 로고    scopus 로고
    • Surface plasmon resonance imaging
    • Steiner, G. Surface plasmon resonance imaging. Anal. Bioanal. Chem., 2004, 379, 328-331.
    • (2004) Anal. Bioanal. Chem. , vol.379 , pp. 328-331
    • Steiner, G.1
  • 23
    • 34249713258 scopus 로고    scopus 로고
    • The surface plasmon resonance imaging sensor for papain based on immobilized cystatin
    • DOI 10.2174/092986607780782803
    • Gorodkiewicz, E. The surface plasmone resonance imaging sensor for papain based on immobilized cystatin. Protein Pept. Lett., 2007, 14, 443-445. (Pubitemid 46833870)
    • (2007) Protein and Peptide Letters , vol.14 , Issue.5 , pp. 443-445
    • Gorodkiewicz, E.1
  • 24
    • 33748663332 scopus 로고    scopus 로고
    • Systematic evaluation of a Surface Plasmon Resonance Imaging biochip reader: Study of gold surface modifications
    • Gorodkiewicz, E.; Fernández-González, A.; Akkoyun, A.; Steiner, G.; Salzer, R. Systematic evaluation of a spr imaging biochip reader: study of gold surface modifications. Chem. Anal. (Warsaw), 2005, 50, 103-115. (Pubitemid 44383577)
    • (2005) Chemia Analityczna , vol.50 , Issue.1 , pp. 103-116
    • Gorodkiewicz, E.1    Fernandez-Gonzalez, A.2    Akkoyun, A.3    Steiner, G.4    Salzer, R.5
  • 26
    • 0028220189 scopus 로고
    • Differential changes in the association and dissociation rate constants for binding of cystatins to target proteinases occurring on N-terminal truncation of the inhibitors indicate that the interaction mechanism varies with different enzymes
    • Björk, I,; Pol, E.; Raub-Segall, E.; Abrahamson, M.; Rowan, A.D.; Mort, J.S. Differential changes in the association and dissociation rate constants for binding of cystatins to target proteinases occurring on N-terminal truncation of the inhibitors indicate that the interaction mechanism varies with different enzymes. Biochem J., 1994, 299(Pt 1), 219-225. (Pubitemid 24106313)
    • (1994) Biochemical Journal , vol.299 , Issue.1 , pp. 219-225
    • Bjork, I.1    Pol, E.2    Raub-Segall, E.3    Abrahamson, M.4    Rowan, A.D.5    Mort, J.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.