Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Filters

Priit Väljamäe

Showing results (1-10 of 34) with videos related to

Pageof 4
Sort By:
The Journal of Biological Chemistry|November 6, 2010
Processivity of cellobiohydrolases is limited by the substrateMihhail Kurasin, Priit Väljamäe
Biotechnology for Biofuels|July 26, 2013
Selecting β-glucosidases to support cellulases in cellulose saccharificationHele Teugjas, Priit Väljamäe
Biotechnology for Biofuels|January 6, 2017
When substrate inhibits and inhibitor activates: implications of β-glucosidasesSilja Kuusk, Priit Väljamäe
The Journal of Biological Chemistry|October 1, 2021
Kinetics of H<sub>2</sub>O<sub>2</sub>-driven catalysis by a lytic polysaccharide monooxygenase from the fungus Trichoderma reeseiSilja Kuusk, Priit Väljamäe
Plos One|September 30, 2014
Multi-mode binding of Cellobiohydrolase Cel7A from Trichoderma reesei to celluloseJürgen Jalak, Priit Väljamäe
Biotechnology for Biofuels|July 26, 2013
Product inhibition of cellulases studied with 14C-labeled cellulose substratesHele Teugjas, Priit Väljamäe
Biotechnology and Bioengineering|May 28, 2010
Mechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysisJürgen Jalak, Priit Väljamäe
Mitochondrion|September 3, 2010
Yeast mitochondrial DNA polymerase is a highly processive single-subunit enzymeKatrin Viikov, Priit Väljamäe, Juhan Sedman
Plos One|January 28, 2017
Human Chitotriosidase Is an Endo-Processive EnzymeSilja Kuusk, Morten Sørlie, Priit Väljamäe
Archives of Biochemistry and Biophysics|February 21, 2024
Dye-decolorizing peroxidase of Thermobifida halotolerance displays complex kinetics with both substrate inhibition and apparent positive cooperativityHegne Pupart, Tiit Lukk, Priit Väljamäe
Pageof 4

Showing results (1-10 of 34) with videos related to

Sort By:
Pageof 4
The Journal of Biological Chemistry|November 6, 2010
Processivity of cellobiohydrolases is limited by the substrateMihhail Kurasin, Priit Väljamäe
Biotechnology for Biofuels|July 26, 2013
Selecting β-glucosidases to support cellulases in cellulose saccharificationHele Teugjas, Priit Väljamäe
Biotechnology for Biofuels|January 6, 2017
When substrate inhibits and inhibitor activates: implications of β-glucosidasesSilja Kuusk, Priit Väljamäe
The Journal of Biological Chemistry|October 1, 2021
Kinetics of H<sub>2</sub>O<sub>2</sub>-driven catalysis by a lytic polysaccharide monooxygenase from the fungus Trichoderma reeseiSilja Kuusk, Priit Väljamäe
Plos One|September 30, 2014
Multi-mode binding of Cellobiohydrolase Cel7A from Trichoderma reesei to celluloseJürgen Jalak, Priit Väljamäe
Biotechnology for Biofuels|July 26, 2013
Product inhibition of cellulases studied with 14C-labeled cellulose substratesHele Teugjas, Priit Väljamäe
Biotechnology and Bioengineering|May 28, 2010
Mechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysisJürgen Jalak, Priit Väljamäe
Mitochondrion|September 3, 2010
Yeast mitochondrial DNA polymerase is a highly processive single-subunit enzymeKatrin Viikov, Priit Väljamäe, Juhan Sedman
Plos One|January 28, 2017
Human Chitotriosidase Is an Endo-Processive EnzymeSilja Kuusk, Morten Sørlie, Priit Väljamäe
Archives of Biochemistry and Biophysics|February 21, 2024
Dye-decolorizing peroxidase of Thermobifida halotolerance displays complex kinetics with both substrate inhibition and apparent positive cooperativityHegne Pupart, Tiit Lukk, Priit Väljamäe
Pageof 4