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David P Ballou

Showing results (41-50 of 78) with videos related to

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The Journal of Biological Chemistry|November 10, 2023
Disease-causing cystathionine β-synthase linker mutations impair allosteric regulationJoseph V Roman, Romila Mascarenhas, Karanfil Ceric, et al.
Biochemistry|January 4, 2008
Gamma-glutamyl hydrolase: kinetic characterization of isopeptide hydrolysis using fluorogenic substratesJessica P Alexander, Thomas J Ryan, David P Ballou, et al.
Biochemistry|November 11, 2008
Function of Glu-469' in the acid-base catalysis of thioredoxin reductase from Drosophila melanogasterHsin-Hung Huang, L David Arscott, David P Ballou, et al.
Biochemistry|March 31, 2004
Use of 8-substituted-FAD analogues to investigate the hydroxylation mechanism of the flavoprotein 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenasePimchai Chaiyen, Jeerus Sucharitakul, Jisnuson Svasti, et al.
Journal of Bacteriology|December 25, 2007
LuxG is a functioning flavin reductase for bacterial luminescenceSarayut Nijvipakul, Janewit Wongratana, Chutintorn Suadee, et al.
Biochemistry|June 26, 2002
Role of protein flexibility in the catalytic cycle of p-hydroxybenzoate hydroxylase elucidated by the Pro293Ser mutantBruce A Palfey, Rajit Basu, Kendra King Frederick, et al.
Journal of Biochemistry|September 1, 2007
Luciferase from Vibrio campbellii is more thermostable and binds reduced FMN better than its homologuesChutintorn Suadee, Sarayut Nijvipakul, Jisnuson Svasti, et al.
Biochemistry|June 28, 2007
Kinetics of a two-component p-hydroxyphenylacetate hydroxylase explain how reduced flavin is transferred from the reductase to the oxygenaseJeerus Sucharitakul, Thanawat Phongsak, Barrie Entsch, et al.
Biochemistry|September 6, 2013
The transfer of reduced flavin mononucleotide from LuxG oxidoreductase to luciferase occurs via free diffusionRuchanok Tinikul, Warintra Pitsawong, Jeerus Sucharitakul, et al.
The Journal of Biological Chemistry|February 3, 2007
Kinetic characterization of the disulfide bond-forming enzyme DsbBTimothy L Tapley, Timo Eichner, Stefan Gleiter, et al.
Pageof 8

Showing results (41-50 of 78) with videos related to

Sort By:
Pageof 8
The Journal of Biological Chemistry|November 10, 2023
Disease-causing cystathionine β-synthase linker mutations impair allosteric regulationJoseph V Roman, Romila Mascarenhas, Karanfil Ceric, et al.
Biochemistry|January 4, 2008
Gamma-glutamyl hydrolase: kinetic characterization of isopeptide hydrolysis using fluorogenic substratesJessica P Alexander, Thomas J Ryan, David P Ballou, et al.
Biochemistry|November 11, 2008
Function of Glu-469' in the acid-base catalysis of thioredoxin reductase from Drosophila melanogasterHsin-Hung Huang, L David Arscott, David P Ballou, et al.
Biochemistry|March 31, 2004
Use of 8-substituted-FAD analogues to investigate the hydroxylation mechanism of the flavoprotein 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenasePimchai Chaiyen, Jeerus Sucharitakul, Jisnuson Svasti, et al.
Journal of Bacteriology|December 25, 2007
LuxG is a functioning flavin reductase for bacterial luminescenceSarayut Nijvipakul, Janewit Wongratana, Chutintorn Suadee, et al.
Biochemistry|June 26, 2002
Role of protein flexibility in the catalytic cycle of p-hydroxybenzoate hydroxylase elucidated by the Pro293Ser mutantBruce A Palfey, Rajit Basu, Kendra King Frederick, et al.
Journal of Biochemistry|September 1, 2007
Luciferase from Vibrio campbellii is more thermostable and binds reduced FMN better than its homologuesChutintorn Suadee, Sarayut Nijvipakul, Jisnuson Svasti, et al.
Biochemistry|June 28, 2007
Kinetics of a two-component p-hydroxyphenylacetate hydroxylase explain how reduced flavin is transferred from the reductase to the oxygenaseJeerus Sucharitakul, Thanawat Phongsak, Barrie Entsch, et al.
Biochemistry|September 6, 2013
The transfer of reduced flavin mononucleotide from LuxG oxidoreductase to luciferase occurs via free diffusionRuchanok Tinikul, Warintra Pitsawong, Jeerus Sucharitakul, et al.
The Journal of Biological Chemistry|February 3, 2007
Kinetic characterization of the disulfide bond-forming enzyme DsbBTimothy L Tapley, Timo Eichner, Stefan Gleiter, et al.
Pageof 8