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J Baz Jackson

Showing results (21-30 of 25) with videos related to

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The Journal of Biological Chemistry|March 15, 2006
The role of invariant amino acid residues at the hydride transfer site of proton-translocating transhydrogenaseT Harma C Brondijk, Gijs I van Boxel, Owen C Mather, et al.
The Journal of Biological Chemistry|June 7, 2003
Interactions between transhydrogenase and thio-nicotinamide Analogues of NAD(H) and NADP(H) underline the importance of nucleotide conformational changes in coupling to proton translocationAvtar Singh, Jamie D Venning, Philip G Quirk, et al.
Biochemistry|February 28, 2007
Structures of the dI2dIII1 complex of proton-translocating transhydrogenase with bound, inactive analogues of NADH and NADPH reveal active site geometriesTina Bhakta, Simon J Whitehead, John S Snaith, et al.
The Journal of Biological Chemistry|October 4, 2007
Substitution of tyrosine 146 in the dI component of proton-translocating transhydrogenase leads to reversible dissociation of the active dimer into inactive monomersU Mirian Obiozo, T Harma C Brondijk, Andrew J White, et al.
Structure (London, England : 1993)|June 27, 2017
Critical Role of Water Molecules in Proton Translocation by the Membrane-Bound TranshydrogenasePius S Padayatti, Josephine H Leung, Paween Mahinthichaichan, et al.
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Showing results (21-30 of 25) with videos related to

Sort By:
Pageof 3
You have reached the last page of results.This site can display upto 25 results.
The Journal of Biological Chemistry|March 15, 2006
The role of invariant amino acid residues at the hydride transfer site of proton-translocating transhydrogenaseT Harma C Brondijk, Gijs I van Boxel, Owen C Mather, et al.
The Journal of Biological Chemistry|June 7, 2003
Interactions between transhydrogenase and thio-nicotinamide Analogues of NAD(H) and NADP(H) underline the importance of nucleotide conformational changes in coupling to proton translocationAvtar Singh, Jamie D Venning, Philip G Quirk, et al.
Biochemistry|February 28, 2007
Structures of the dI2dIII1 complex of proton-translocating transhydrogenase with bound, inactive analogues of NADH and NADPH reveal active site geometriesTina Bhakta, Simon J Whitehead, John S Snaith, et al.
The Journal of Biological Chemistry|October 4, 2007
Substitution of tyrosine 146 in the dI component of proton-translocating transhydrogenase leads to reversible dissociation of the active dimer into inactive monomersU Mirian Obiozo, T Harma C Brondijk, Andrew J White, et al.
Structure (London, England : 1993)|June 27, 2017
Critical Role of Water Molecules in Proton Translocation by the Membrane-Bound TranshydrogenasePius S Padayatti, Josephine H Leung, Paween Mahinthichaichan, et al.
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