S B Vik|R A Capaldi - JoVE Visualize

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FEBS Letters|December 20, 2000

The T9176G mutation of human mtDNA gives a fully assembled but inactive ATP synthase when modeled in Escherichia coliR Carrozzo, J Murray, F M Santorelli, et al.

Archives of Biochemistry and Biophysics|August 1, 1992

Epitope mapping of monoclonal antibodies to the Escherichia coli F1 ATPase alpha subunit in relation to activity effects and location in the enzyme complex based on cryoelectron microscopyR Aggeler, R A Capaldi, S Dunn, et al.

Biochemistry|May 30, 1989

Cryoelectron microscopy of Escherichia coli F1 adenosinetriphosphatase decorated with monoclonal antibodies to individual subunits of the complexE P Gogol, R Aggeler, M Sagermann, et al.

Biochemistry|September 5, 1978

Cross-linking of ubiquinone cytochrome c reductase (complex III) with periodate-cleavable bifunctional reagentsR J Smith, R A Capaldi, D Muchmore, et al.

Proceedings of the National Academy of Sciences of the United States of America|December 1, 1990

Ligand-dependent structural variations in Escherichia coli F1 ATPase revealed by cryoelectron microscopyE P Gogol, E Johnston, R Aggeler, et al.

Archives of Biochemistry and Biophysics|October 1, 1990

Mutagenesis of the a subunit of the F1F0-ATP synthase from Escherichia coli in the region of Asn-192S B Vik, D Lee, C E Curtis, et al.

Biochimica Et Biophysica Acta|December 2, 1991

The most conserved nuclear-encoded polypeptide of cytochrome c oxidase is the putative zinc-binding subunit: primary structure of subunit V from the slime mold Dictyostelium discoideumR Rizzuto, D Sandonà, M Brini, et al.

Biochemistry|March 15, 1983

Electron transfer in monomeric forms of beef and shark heart cytochrome c oxidaseG Georgevich, V M Darley-Usmar, F Malatesta, et al.

Biochemical and Biophysical Research Communications|June 15, 1994

TFPACD, a novel bifunctional reagent for reacting with DCCD sites in proteins: studies using Escherichia coli ATP synthaseA S Phadke, R Aggeler, J F Keana, et al.

Proceedings of the National Academy of Sciences of the United States of America|November 26, 1999

Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by x-ray crystallographyA C Hausrath, G Grüber, B W Matthews, et al.

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Showing results (111-120 of 160) with videos related to

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Pageof 16

FEBS Letters|December 20, 2000

The T9176G mutation of human mtDNA gives a fully assembled but inactive ATP synthase when modeled in Escherichia coliR Carrozzo, J Murray, F M Santorelli, et al.

Archives of Biochemistry and Biophysics|August 1, 1992

Epitope mapping of monoclonal antibodies to the Escherichia coli F1 ATPase alpha subunit in relation to activity effects and location in the enzyme complex based on cryoelectron microscopyR Aggeler, R A Capaldi, S Dunn, et al.

Biochemistry|May 30, 1989

Cryoelectron microscopy of Escherichia coli F1 adenosinetriphosphatase decorated with monoclonal antibodies to individual subunits of the complexE P Gogol, R Aggeler, M Sagermann, et al.

Biochemistry|September 5, 1978

Cross-linking of ubiquinone cytochrome c reductase (complex III) with periodate-cleavable bifunctional reagentsR J Smith, R A Capaldi, D Muchmore, et al.

Proceedings of the National Academy of Sciences of the United States of America|December 1, 1990

Ligand-dependent structural variations in Escherichia coli F1 ATPase revealed by cryoelectron microscopyE P Gogol, E Johnston, R Aggeler, et al.

Archives of Biochemistry and Biophysics|October 1, 1990

Mutagenesis of the a subunit of the F1F0-ATP synthase from Escherichia coli in the region of Asn-192S B Vik, D Lee, C E Curtis, et al.

Biochimica Et Biophysica Acta|December 2, 1991

The most conserved nuclear-encoded polypeptide of cytochrome c oxidase is the putative zinc-binding subunit: primary structure of subunit V from the slime mold Dictyostelium discoideumR Rizzuto, D Sandonà, M Brini, et al.

Biochemistry|March 15, 1983

Electron transfer in monomeric forms of beef and shark heart cytochrome c oxidaseG Georgevich, V M Darley-Usmar, F Malatesta, et al.

Biochemical and Biophysical Research Communications|June 15, 1994

TFPACD, a novel bifunctional reagent for reacting with DCCD sites in proteins: studies using Escherichia coli ATP synthaseA S Phadke, R Aggeler, J F Keana, et al.

Proceedings of the National Academy of Sciences of the United States of America|November 26, 1999

Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by x-ray crystallographyA C Hausrath, G Grüber, B W Matthews, et al.

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