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T T Teeri

Showing results (31-40 of 46) with videos related to

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The Year in Immunology|January 1, 1993
High-level production of an active single-chain Fv fragment in the culture supernatant of Escherichia coliD Sizmann, K Takkinen, M L Laukkanen, et al.
Journal of Chromatography. A|August 25, 2001
Efficient enantioselective separation of drug enantiomers by immobilised antibody fragmentsT K Nevanen, L Söderholm, K Kukkonen, et al.
Proteins|December 1, 1992
Investigation of the function of mutated cellulose-binding domains of Trichoderma reesei cellobiohydrolase IT Reinikainen, L Ruohonen, T Nevanen, et al.
Science (New York, N.Y.)|July 22, 1994
The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reeseiC Divne, J Ståhlberg, T Reinikainen, et al.
FEBS Letters|November 26, 1990
Site-directed mutagenesis of the putative catalytic residues of Trichoderma reesei cellobiohydrolase I and endoglucanase IY Mitsuishi, S Nitisinprasert, M Saloheimo, et al.
FEBS Letters|July 14, 1998
Tryptophan 272: an essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6AA Koivula, T Kinnari, V Harjunpää, et al.
Protein Engineering|February 1, 1995
Introduction of lysine residues on the light chain constant domain improves the labelling properties of a recombinant Fab fragmentA Hemminki, A M Hoffrén, K Takkinen, et al.
Protein Engineering|October 1, 1991
An active single-chain antibody containing a cellulase linker domain is secreted by Escherichia coliK Takkinen, M L Laukkanen, D Sizmann, et al.
Gene|January 1, 1988
EGIII, a new endoglucanase from Trichoderma reesei: the characterization of both gene and enzymeM Saloheimo, P Lehtovaara, M Penttilä, et al.
Structure (London, England : 1993)|October 6, 1999
Crystallographic evidence for substrate ring distortion and protein conformational changes during catalysis in cellobiohydrolase Ce16A from trichoderma reeseiJ y Zou, G J Kleywegt, J Ståhlberg, et al.
Pageof 5

Showing results (31-40 of 46) with videos related to

Sort By:
Pageof 5
The Year in Immunology|January 1, 1993
High-level production of an active single-chain Fv fragment in the culture supernatant of Escherichia coliD Sizmann, K Takkinen, M L Laukkanen, et al.
Journal of Chromatography. A|August 25, 2001
Efficient enantioselective separation of drug enantiomers by immobilised antibody fragmentsT K Nevanen, L Söderholm, K Kukkonen, et al.
Proteins|December 1, 1992
Investigation of the function of mutated cellulose-binding domains of Trichoderma reesei cellobiohydrolase IT Reinikainen, L Ruohonen, T Nevanen, et al.
Science (New York, N.Y.)|July 22, 1994
The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reeseiC Divne, J Ståhlberg, T Reinikainen, et al.
FEBS Letters|November 26, 1990
Site-directed mutagenesis of the putative catalytic residues of Trichoderma reesei cellobiohydrolase I and endoglucanase IY Mitsuishi, S Nitisinprasert, M Saloheimo, et al.
FEBS Letters|July 14, 1998
Tryptophan 272: an essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6AA Koivula, T Kinnari, V Harjunpää, et al.
Protein Engineering|February 1, 1995
Introduction of lysine residues on the light chain constant domain improves the labelling properties of a recombinant Fab fragmentA Hemminki, A M Hoffrén, K Takkinen, et al.
Protein Engineering|October 1, 1991
An active single-chain antibody containing a cellulase linker domain is secreted by Escherichia coliK Takkinen, M L Laukkanen, D Sizmann, et al.
Gene|January 1, 1988
EGIII, a new endoglucanase from Trichoderma reesei: the characterization of both gene and enzymeM Saloheimo, P Lehtovaara, M Penttilä, et al.
Structure (London, England : 1993)|October 6, 1999
Crystallographic evidence for substrate ring distortion and protein conformational changes during catalysis in cellobiohydrolase Ce16A from trichoderma reeseiJ y Zou, G J Kleywegt, J Ståhlberg, et al.
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