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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 transhydrogenase
T 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 translocation
Avtar 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 geometries
Tina 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 monomers
U 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 Transhydrogenase
Pius S Padayatti, Josephine H Leung, Paween Mahinthichaichan, et al.
Page
of 3
Search research articles
Search
Showing results (21-30 of 25) with videos related to
Sort By:
Page
of 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 transhydrogenase
T 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 translocation
Avtar 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 geometries
Tina 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 monomers
U 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 Transhydrogenase
Pius S Padayatti, Josephine H Leung, Paween Mahinthichaichan, et al.
Page
of 3