메뉴 건너뛰기




Volumn 23, Issue 6, 2007, Pages 1492-1497

Development of a method using image analysis for the measurement of cellulose-binding domains adsorbed onto cellulose fibers

Author keywords

[No Author keywords available]

Indexed keywords

ADSORPTION; CELLULOSE; CONCENTRATION (PROCESS);

EID: 37149025680     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp070026v     Document Type: Article
Times cited : (15)

References (20)
  • 1
    • 0027372765 scopus 로고
    • Role of the interdomain linker peptide of Trichoderma reesei cellobiohydrolase-I in its interaction with crystalline cellulose
    • Srisodsuk, M.; Reinikainen, T.; Penttila, M.; Teeri, T. T. Role of the interdomain linker peptide of Trichoderma reesei cellobiohydrolase-I in its interaction with crystalline cellulose. J. Biol. Chem. 1993, 268, 20756-20761.
    • (1993) J. Biol. Chem , vol.268 , pp. 20756-20761
    • Srisodsuk, M.1    Reinikainen, T.2    Penttila, M.3    Teeri, T.T.4
  • 2
    • 0342437551 scopus 로고
    • Cellulose binding domains and linker sequences potentiate the activity of hemicellulases against complex substrates
    • Black, G. W.; Rixon, J. E.; Clarke, J. H.; Hazlewood, G. P.; Ferreira, L. M. A.; Bolam, D. N.; Gilbert, H. J. Cellulose binding domains and linker sequences potentiate the activity of hemicellulases against complex substrates. J. Biotechnol. 1991, 57, 59-69.
    • (1991) J. Biotechnol , vol.57 , pp. 59-69
    • Black, G.W.1    Rixon, J.E.2    Clarke, J.H.3    Hazlewood, G.P.4    Ferreira, L.M.A.5    Bolam, D.N.6    Gilbert, H.J.7
  • 3
    • 0035917427 scopus 로고    scopus 로고
    • Addition of substrate-binding domains increases substrate-binding capacity and specific activity of a chitinase from Trichoderma harzianum
    • Limón, M. C.; Margolles-Clark, E.; Benitez, T.; Penttila, M. Addition of substrate-binding domains increases substrate-binding capacity and specific activity of a chitinase from Trichoderma harzianum. FEMS Microbiol. Lett. 2001, 198, 57-63.
    • (2001) FEMS Microbiol. Lett , vol.198 , pp. 57-63
    • Limón, M.C.1    Margolles-Clark, E.2    Benitez, T.3    Penttila, M.4
  • 4
    • 37149053831 scopus 로고    scopus 로고
    • Srisodsuk, M. Mode of Action of Trichoderma reesei Cellobiohydrolase 1 on Crystalline Cellulose; VTT Publications: Helsinki, Finland, 1994; 188, pp 1-107.
    • Srisodsuk, M. Mode of Action of Trichoderma reesei Cellobiohydrolase 1 on Crystalline Cellulose; VTT Publications: Helsinki, Finland, 1994; Vol. 188, pp 1-107.
  • 5
    • 0030903073 scopus 로고
    • Interaction between cellohexaose and cellulose binding domains from Trichoderma reesei cellulases
    • Mattinen, M. L.; Linder, M.; Teleman, A.; Annila, A. Interaction between cellohexaose and cellulose binding domains from Trichoderma reesei cellulases. FEBS Lett. 1991, 407, 291-296.
    • (1991) FEBS Lett , vol.407 , pp. 291-296
    • Mattinen, M.L.1    Linder, M.2    Teleman, A.3    Annila, A.4
  • 6
    • 0034641715 scopus 로고    scopus 로고
    • Cellulose-binding domains promote hydrolysis of different sites on crystalline cellulose
    • Carrard, G.; Koivula, A.; Soderlund, H.; Beguin, P. Cellulose-binding domains promote hydrolysis of different sites on crystalline cellulose. Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 10342-10347.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 10342-10347
    • Carrard, G.1    Koivula, A.2    Soderlund, H.3    Beguin, P.4
  • 8
    • 0037386896 scopus 로고    scopus 로고
    • Use of a fuorescence labelled, carbohydrate-binding module from Phanerochaete chrysosporium Cel7D for studying wood cell wall ultrastructure
    • Hilden, L., Daniel, G., Johansson, G. Use of a fuorescence labelled, carbohydrate-binding module from Phanerochaete chrysosporium Cel7D for studying wood cell wall ultrastructure. Biotechnol. Lett. 2003, 25, 553-558.
    • (2003) Biotechnol. Lett , vol.25 , pp. 553-558
    • Hilden, L.1    Daniel, G.2    Johansson, G.3
  • 9
    • 0029636429 scopus 로고
    • Adhesion of mammalian-cells to a recombinant attachment factor, Cbd/Rgd, analyzed by image-analysis
    • Wierzba, A.; Reichl, U.; Turner, R. F. B.; Warren, R. A. J.; Kilburn, D. G. Adhesion of mammalian-cells to a recombinant attachment factor, Cbd/Rgd, analyzed by image-analysis. Biotechnol. Bioeng. 1995, 46, 185-193.
    • (1995) Biotechnol. Bioeng , vol.46 , pp. 185-193
    • Wierzba, A.1    Reichl, U.2    Turner, R.F.B.3    Warren, R.A.J.4    Kilburn, D.G.5
  • 10
    • 0035112799 scopus 로고    scopus 로고
    • Expression, refolding and indirect immobilization of horseradish peroxidase (HRP) to cellulose via a phage-selected peptide and cellulose-binding domain (CBD)
    • Levy, I.; Shoseyov, O. Expression, refolding and indirect immobilization of horseradish peroxidase (HRP) to cellulose via a phage-selected peptide and cellulose-binding domain (CBD). J. Pept. Sci. 2001, 7, 50-57.
    • (2001) J. Pept. Sci , vol.7 , pp. 50-57
    • Levy, I.1    Shoseyov, O.2
  • 11
    • 33747131733 scopus 로고    scopus 로고
    • Large-scale production of cellulose-binding domains. Adsorption studies using CBD-FITC conjugates
    • Pinto, R.; Carvalho, J.; Mota, M.; Gama, M. Large-scale production of cellulose-binding domains. Adsorption studies using CBD-FITC conjugates. Cellulose 2006, 13, 557-569.
    • (2006) Cellulose , vol.13 , pp. 557-569
    • Pinto, R.1    Carvalho, J.2    Mota, M.3    Gama, M.4
  • 12
    • 0035920275 scopus 로고    scopus 로고
    • Effect of metal ions on the degradation and adsorption of two cellobiohydrolases on microcrystalline cellulose
    • Kim, D. W.; Jang, Y. H.; Kim, C. S.; Lee, N. S. Effect of metal ions on the degradation and adsorption of two cellobiohydrolases on microcrystalline cellulose. Bull. Korean Chem. Soc. 2001, 22, 716-720.
    • (2001) Bull. Korean Chem. Soc , vol.22 , pp. 716-720
    • Kim, D.W.1    Jang, Y.H.2    Kim, C.S.3    Lee, N.S.4
  • 13
    • 0035169890 scopus 로고    scopus 로고
    • Artefacts in restored images due to intensity loss in three-dimensional fluorescence microscopy
    • Markham, J.; Conchello, J. A. Artefacts in restored images due to intensity loss in three-dimensional fluorescence microscopy. J. Microsc. (Oxford) 2001, 204, 93-98.
    • (2001) J. Microsc. (Oxford) , vol.204 , pp. 93-98
    • Markham, J.1    Conchello, J.A.2
  • 14
    • 85151273943 scopus 로고    scopus 로고
    • Ghauharali, R. I.; Brakenhoff, G. J. Fluorescence photobleaching-based image standardization for fluorescence microscopy. J. Microsc. (Oxford) 2000, 198, 88-100.
    • Ghauharali, R. I.; Brakenhoff, G. J. Fluorescence photobleaching-based image standardization for fluorescence microscopy. J. Microsc. (Oxford) 2000, 198, 88-100.
  • 15
    • 0030966142 scopus 로고    scopus 로고
    • Influence of fluorochrome labeling density on the photobleaching kinetics of fluorescein in microscopy
    • Song, L. L.; vanGijlswijk, R. P. M.; Young, I. T.; Tanke, H. J. Influence of fluorochrome labeling density on the photobleaching kinetics of fluorescein in microscopy. Cytometry 1997, 27, 213-223.
    • (1997) Cytometry , vol.27 , pp. 213-223
    • Song, L.L.1    vanGijlswijk, R.P.M.2    Young, I.T.3    Tanke, H.J.4
  • 17
    • 0021956248 scopus 로고
    • Digital Imaging fluorescence microscopy - Spatial heterogeneity of photobleaching rate constants in individual cells
    • Benson, D. M.; Bryan, J.; Plant, A. L.; Gotto, A. M.; Smith, L. C. Digital Imaging fluorescence microscopy - Spatial heterogeneity of photobleaching rate constants in individual cells. J. Cell Biol. 1985, 100, 1309-1323.
    • (1985) J. Cell Biol , vol.100 , pp. 1309-1323
    • Benson, D.M.1    Bryan, J.2    Plant, A.L.3    Gotto, A.M.4    Smith, L.C.5
  • 18
    • 85151301362 scopus 로고    scopus 로고
    • Ghauharali, R. I.; Hofstraat, J. W.; Brakenhoff, G. J. Fluorescence photobleaching-based shading correction for fluorescence microscopy. J. Microsc. (Oxford) 1998, 192, 99-113.
    • Ghauharali, R. I.; Hofstraat, J. W.; Brakenhoff, G. J. Fluorescence photobleaching-based shading correction for fluorescence microscopy. J. Microsc. (Oxford) 1998, 192, 99-113.
  • 19
    • 0024962351 scopus 로고
    • Determination of the 3-dimensional solution structure of the C-terminal domain of cellobiohydrolase-I from Trichoderma reesei - A study using nuclear magnetic-resonance and hybrid distance geometry dynamical simulated annealing
    • Kraulis, P. J.; Clore, G. M.; Nilges, M.; Jones, T. A.; Pettersson, G.; Knowles, J.; Gronenborn, A. M. Determination of the 3-dimensional solution structure of the C-terminal domain of cellobiohydrolase-I from Trichoderma reesei - A study using nuclear magnetic-resonance and hybrid distance geometry dynamical simulated annealing. Biochemistry 1989, 28, 7241-7257.
    • (1989) Biochemistry , vol.28 , pp. 7241-7257
    • Kraulis, P.J.1    Clore, G.M.2    Nilges, M.3    Jones, T.A.4    Pettersson, G.5    Knowles, J.6    Gronenborn, A.M.7
  • 20
    • 0033979485 scopus 로고    scopus 로고
    • The mechanism of cellulase action on cotton fibers: Evidence from atomic force microscopy
    • Lee, I.; Evans, B. R.; Woodward, J. The mechanism of cellulase action on cotton fibers: evidence from atomic force microscopy. Ultramicroscopy 2000, 82, 213-221.
    • (2000) Ultramicroscopy , vol.82 , pp. 213-221
    • Lee, I.1    Evans, B.R.2    Woodward, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.