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Frank Jordan

Showing results (41-50 of 107) with videos related to

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Biochemistry|June 18, 2009
Proton bridging in the interactions of thrombin with small inhibitorsIldiko M Kovach, Paul Kelley, Carol Eddy, et al.
Biochimica Et Biophysica Acta. Bioenergetics|May 13, 2018
Evidence for functional and regulatory cross-talk between the tricarboxylic acid cycle 2-oxoglutarate dehydrogenase complex and 2-oxoadipate dehydrogenase on the l-lysine, l-hydroxylysine and l-tryptophan degradation pathways from studies in vitroNatalia S Nemeria, Gary Gerfen, Luying Yang, et al.
Acta Crystallographica. Section D, Biological Crystallography|October 24, 2006
Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component from Escherichia coli observed at 2.32 A resolutionKrishnamoorthy Chandrasekhar, Palaniappa Arjunan, Martin Sax, et al.
Journal of the American Chemical Society|October 16, 2003
Dual catalytic apparatus of the thiamin diphosphate coenzyme: acid-base via the 1',4'-iminopyrimidine tautomer along with its electrophilic roleFrank Jordan, Natalia S Nemeria, Sheng Zhang, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 25, 2008
Efficient coupling of catalysis and dynamics in the E1 component of Escherichia coli pyruvate dehydrogenase multienzyme complexSachin Kale, Gözde Ulas, Jaeyoung Song, et al.
Bioorganic Chemistry|October 31, 2006
Acetylphosphinate is the most potent mechanism-based substrate-like inhibitor of both the human and Escherichia coli pyruvate dehydrogenase components of the pyruvate dehydrogenase complexNatalia S Nemeria, Lioubov G Korotchkina, Sumit Chakraborty, et al.
Journal of the American Chemical Society|February 4, 2012
Bifunctionality of the thiamin diphosphate cofactor: assignment of tautomeric/ionization states of the 4'-aminopyrimidine ring when various intermediates occupy the active sites during the catalysis of yeast pyruvate decarboxylaseAnand Balakrishnan, Yuhong Gao, Prerna Moorjani, et al.
Biochemistry|March 18, 2014
Identification of charge transfer transitions related to thiamin-bound intermediates on enzymes provides a plethora of signatures useful in mechanistic studiesHetalben Patel, Natalia S Nemeria, Forest H Andrews, et al.
Angewandte Chemie (International Ed. in English)|July 1, 2022
Structures of the Most Twisted Thioamide and Selenoamide: Effect of Higher Chalcogens of Twisted Amides on N-C(X) ResonanceQun Zhao, Guangchen Li, Pradeep Nareddy, et al.
The Journal of Biological Chemistry|December 10, 2009
Nuclear magnetic resonance evidence for the role of the flexible regions of the E1 component of the pyruvate dehydrogenase complex from gram-negative bacteriaJaeyoung Song, Yun-Hee Park, Natalia S Nemeria, et al.
Pageof 11

Showing results (41-50 of 107) with videos related to

Sort By:
Pageof 11
Biochemistry|June 18, 2009
Proton bridging in the interactions of thrombin with small inhibitorsIldiko M Kovach, Paul Kelley, Carol Eddy, et al.
Biochimica Et Biophysica Acta. Bioenergetics|May 13, 2018
Evidence for functional and regulatory cross-talk between the tricarboxylic acid cycle 2-oxoglutarate dehydrogenase complex and 2-oxoadipate dehydrogenase on the l-lysine, l-hydroxylysine and l-tryptophan degradation pathways from studies in vitroNatalia S Nemeria, Gary Gerfen, Luying Yang, et al.
Acta Crystallographica. Section D, Biological Crystallography|October 24, 2006
Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component from Escherichia coli observed at 2.32 A resolutionKrishnamoorthy Chandrasekhar, Palaniappa Arjunan, Martin Sax, et al.
Journal of the American Chemical Society|October 16, 2003
Dual catalytic apparatus of the thiamin diphosphate coenzyme: acid-base via the 1',4'-iminopyrimidine tautomer along with its electrophilic roleFrank Jordan, Natalia S Nemeria, Sheng Zhang, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 25, 2008
Efficient coupling of catalysis and dynamics in the E1 component of Escherichia coli pyruvate dehydrogenase multienzyme complexSachin Kale, Gözde Ulas, Jaeyoung Song, et al.
Bioorganic Chemistry|October 31, 2006
Acetylphosphinate is the most potent mechanism-based substrate-like inhibitor of both the human and Escherichia coli pyruvate dehydrogenase components of the pyruvate dehydrogenase complexNatalia S Nemeria, Lioubov G Korotchkina, Sumit Chakraborty, et al.
Journal of the American Chemical Society|February 4, 2012
Bifunctionality of the thiamin diphosphate cofactor: assignment of tautomeric/ionization states of the 4'-aminopyrimidine ring when various intermediates occupy the active sites during the catalysis of yeast pyruvate decarboxylaseAnand Balakrishnan, Yuhong Gao, Prerna Moorjani, et al.
Biochemistry|March 18, 2014
Identification of charge transfer transitions related to thiamin-bound intermediates on enzymes provides a plethora of signatures useful in mechanistic studiesHetalben Patel, Natalia S Nemeria, Forest H Andrews, et al.
Angewandte Chemie (International Ed. in English)|July 1, 2022
Structures of the Most Twisted Thioamide and Selenoamide: Effect of Higher Chalcogens of Twisted Amides on N-C(X) ResonanceQun Zhao, Guangchen Li, Pradeep Nareddy, et al.
The Journal of Biological Chemistry|December 10, 2009
Nuclear magnetic resonance evidence for the role of the flexible regions of the E1 component of the pyruvate dehydrogenase complex from gram-negative bacteriaJaeyoung Song, Yun-Hee Park, Natalia S Nemeria, et al.
Pageof 11