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W Maret

Showing results (31-40 of 53) with videos related to

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Proceedings of the National Academy of Sciences of the United States of America|August 5, 1998
The ATP-metallothionein complexL J Jiang, W Maret, B L Vallee
Proceedings of the National Academy of Sciences of the United States of America|March 18, 1997
Coordination dynamics of biological zinc "clusters" in metallothioneins and in the DNA-binding domain of the transcription factor Gal4W Maret, K S Larsen, B L Vallee
European Journal of Biochemistry|October 1, 1979
Active-site-specific reconstituted cobalt(II) horse-liver alcohol dehydrogenase. Changes of the spectra of the substrate trans-4-(N,N-dimethylamino)-cinnamaldehyde and of the catalytic cobalt ion upon ternary complex formation with NADH and 1,4,5,6-tetrahydronicotinamide--adenine dinucleotideH Dietrich, W Maret, L Wallén, et al.
Biochimica Et Biophysica Acta|April 13, 1994
Human liver aldehyde dehydrogenases: new method of purification of the major mitochondrial and cytosolic enzymes and re-evaluation of their kinetic propertiesL G Rashkovetsky, W Maret, A A Klyosov
European Journal of Biochemistry|March 3, 1986
Binding of ligands to horse liver alcohol dehydrogenase lacking zinc ions at the active sitesJ Kovár, L Matyska, M Zeppezauer, et al.
Journal of Inorganic Biochemistry|July 1, 1981
Active site-specifically reconstituted nickel(II) horse liver alcohol dehydrogenase: optical spectra of binary and ternary complexes with coenzymes, coenzyme analogues, substrates, and inhibitorsH Dietrich, W Maret, H Kozłowski, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 1, 1983
Neutral metal-bound water is the base catalyst in liver alcohol dehydrogenaseM W Makinen, W Maret, M B Yim
Proceedings of the National Academy of Sciences of the United States of America|May 9, 1998
The glutathione redox couple modulates zinc transfer from metallothionein to zinc-depleted sorbitol dehydrogenaseL J Jiang, W Maret, B L Vallee
Progress in Clinical and Biological Research|January 1, 1985
The interaction of catalytic metal ions and ionizing groups in equilibrium studies and in transient intermediates of metal-substituted alcohol dehydrogenasesW Maret, M Gerber, M Zeppezauer, et al.
Journal of Inorganic Biochemistry|June 1, 1980
Active site-specific reconstituted copper(II) horse liver alcohol dehydrogenase: a biological model for type 1 Cu2+ and its changes upon ligand binding and conformational transitionsW Maret, H Dietrich, H H Ruf, et al.
Pageof 6

Showing results (31-40 of 53) with videos related to

Sort By:
Pageof 6
Proceedings of the National Academy of Sciences of the United States of America|August 5, 1998
The ATP-metallothionein complexL J Jiang, W Maret, B L Vallee
Proceedings of the National Academy of Sciences of the United States of America|March 18, 1997
Coordination dynamics of biological zinc "clusters" in metallothioneins and in the DNA-binding domain of the transcription factor Gal4W Maret, K S Larsen, B L Vallee
European Journal of Biochemistry|October 1, 1979
Active-site-specific reconstituted cobalt(II) horse-liver alcohol dehydrogenase. Changes of the spectra of the substrate trans-4-(N,N-dimethylamino)-cinnamaldehyde and of the catalytic cobalt ion upon ternary complex formation with NADH and 1,4,5,6-tetrahydronicotinamide--adenine dinucleotideH Dietrich, W Maret, L Wallén, et al.
Biochimica Et Biophysica Acta|April 13, 1994
Human liver aldehyde dehydrogenases: new method of purification of the major mitochondrial and cytosolic enzymes and re-evaluation of their kinetic propertiesL G Rashkovetsky, W Maret, A A Klyosov
European Journal of Biochemistry|March 3, 1986
Binding of ligands to horse liver alcohol dehydrogenase lacking zinc ions at the active sitesJ Kovár, L Matyska, M Zeppezauer, et al.
Journal of Inorganic Biochemistry|July 1, 1981
Active site-specifically reconstituted nickel(II) horse liver alcohol dehydrogenase: optical spectra of binary and ternary complexes with coenzymes, coenzyme analogues, substrates, and inhibitorsH Dietrich, W Maret, H Kozłowski, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 1, 1983
Neutral metal-bound water is the base catalyst in liver alcohol dehydrogenaseM W Makinen, W Maret, M B Yim
Proceedings of the National Academy of Sciences of the United States of America|May 9, 1998
The glutathione redox couple modulates zinc transfer from metallothionein to zinc-depleted sorbitol dehydrogenaseL J Jiang, W Maret, B L Vallee
Progress in Clinical and Biological Research|January 1, 1985
The interaction of catalytic metal ions and ionizing groups in equilibrium studies and in transient intermediates of metal-substituted alcohol dehydrogenasesW Maret, M Gerber, M Zeppezauer, et al.
Journal of Inorganic Biochemistry|June 1, 1980
Active site-specific reconstituted copper(II) horse liver alcohol dehydrogenase: a biological model for type 1 Cu2+ and its changes upon ligand binding and conformational transitionsW Maret, H Dietrich, H H Ruf, et al.
Pageof 6