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The Journal of Membrane Biology
|
May 1, 1996
Mechanisms of active transport in the FOF1 ATP synthase
R K Nakamoto
The Journal of Biological Chemistry
|
March 10, 1984
Studies of the interactions of 2',3'-O-(2,4,6-trinitrocyclohexyldienylidine)adenosine nucleotides with the sarcoplasmic reticulum (Ca2+ + Mg2+)-ATPase active site
R K Nakamoto, G Inesi
FEBS Letters
|
January 6, 1986
Retention of ellipticity between enzymatic states of the Ca2+-ATPase of sarcoplasmic reticulum
R K Nakamoto, G Inesi
Journal of Bioenergetics and Biomembranes
|
October 1, 1989
Molecular properties of the fungal plasma-membrane [H+]-ATPase
R K Nakamoto, C W Slayman
Biochemistry
|
September 20, 2000
Catalytic control and coupling efficiency of the Escherichia coli FoF1 ATP synthase: influence of the Fo sector and epsilon subunit on the catalytic transition state
Y B Peskova, R K Nakamoto
The Biochemical Journal
|
April 19, 2000
Intragenic and intergenic suppression of the Escherichia coli ATP synthase subunit a mutation of Gly-213 to Asn: functional interactions between residues in the proton transport site
P H Kuo, R K Nakamoto
The Journal of Biological Chemistry
|
August 26, 1998
A mutation in the Escherichia coli F0F1-ATP synthase rotor, gammaE208K, perturbs conformational coupling between transport and catalysis
C J Ketchum, R K Nakamoto
Methods in Enzymology
|
October 19, 2000
Expression and purification of Rho/RhoGDI complexes
P W Read, R K Nakamoto
The Journal of Biological Chemistry
|
January 15, 1993
The gamma subunit of the Escherichia coli ATP synthase. Mutations in the carboxyl-terminal region restore energy coupling to the amino-terminal mutant gamma Met-23-->Lys
R K Nakamoto, M Maeda, M Futai
Biochemistry
|
October 23, 1997
Mechanism of energy coupling in the FOF1-ATP synthase: the uncoupling mutation, gammaM23K, disrupts the use of binding energy to drive catalysis
M K Al-Shawi, R K Nakamoto
Page
of 4
Search research articles
Search
Showing results (1-10 of 40) with videos related to
Sort By:
Page
of 4
The Journal of Membrane Biology
|
May 1, 1996
Mechanisms of active transport in the FOF1 ATP synthase
R K Nakamoto
The Journal of Biological Chemistry
|
March 10, 1984
Studies of the interactions of 2',3'-O-(2,4,6-trinitrocyclohexyldienylidine)adenosine nucleotides with the sarcoplasmic reticulum (Ca2+ + Mg2+)-ATPase active site
R K Nakamoto, G Inesi
FEBS Letters
|
January 6, 1986
Retention of ellipticity between enzymatic states of the Ca2+-ATPase of sarcoplasmic reticulum
R K Nakamoto, G Inesi
Journal of Bioenergetics and Biomembranes
|
October 1, 1989
Molecular properties of the fungal plasma-membrane [H+]-ATPase
R K Nakamoto, C W Slayman
Biochemistry
|
September 20, 2000
Catalytic control and coupling efficiency of the Escherichia coli FoF1 ATP synthase: influence of the Fo sector and epsilon subunit on the catalytic transition state
Y B Peskova, R K Nakamoto
The Biochemical Journal
|
April 19, 2000
Intragenic and intergenic suppression of the Escherichia coli ATP synthase subunit a mutation of Gly-213 to Asn: functional interactions between residues in the proton transport site
P H Kuo, R K Nakamoto
The Journal of Biological Chemistry
|
August 26, 1998
A mutation in the Escherichia coli F0F1-ATP synthase rotor, gammaE208K, perturbs conformational coupling between transport and catalysis
C J Ketchum, R K Nakamoto
Methods in Enzymology
|
October 19, 2000
Expression and purification of Rho/RhoGDI complexes
P W Read, R K Nakamoto
The Journal of Biological Chemistry
|
January 15, 1993
The gamma subunit of the Escherichia coli ATP synthase. Mutations in the carboxyl-terminal region restore energy coupling to the amino-terminal mutant gamma Met-23-->Lys
R K Nakamoto, M Maeda, M Futai
Biochemistry
|
October 23, 1997
Mechanism of energy coupling in the FOF1-ATP synthase: the uncoupling mutation, gammaM23K, disrupts the use of binding energy to drive catalysis
M K Al-Shawi, R K Nakamoto
Page
of 4