Zobrazeno 1 - 10
of 47
pro vyhledávání: '"R A, Capaldi"'
Publikováno v:
Electrophoresis. 22(5)
As mitochondria play critical roles in both cell life and cell death, there is great interest in obtaining a human mitochondrial proteome map. Such a map could potentially be useful in diagnosing diseases, identifying targets for drug therapy, and in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::710db11bcced2e85c1f4e06f312ac93f
https://pubmed.ncbi.nlm.nih.gov/11332763
https://pubmed.ncbi.nlm.nih.gov/11332763
Publikováno v:
The Journal of biological chemistry. 275(15)
The structure and functioning of the ATP synthase of human fibroblast cell lines with 91 and 100%, respectively, of the T8993G mutation have been studied, with MRC5 human fibroblasts and Rho(0) cells derived from this cell line as controls. ATP hydro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3eb93c66ae614272b9637e0171c3fab5
https://pubmed.ncbi.nlm.nih.gov/10753912
https://pubmed.ncbi.nlm.nih.gov/10753912
Autor:
R A, Capaldi, B, Schulenberg
Publikováno v:
Biochimica et biophysica acta. 1458(2-3)
Recent studies show that the epsilon subunit of bacterial and chloroplast F(1)F(0) ATPases is a component of the central stalk that links the F(1) and F(0) parts. This subunit interacts with alpha, beta and gamma subunits of F(1) and the c subunit ri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8db4513ef96455724e90b86e9585a7ef
https://pubmed.ncbi.nlm.nih.gov/10838042
https://pubmed.ncbi.nlm.nih.gov/10838042
Publikováno v:
Journal of molecular biology. 295(3)
The binding site of the delta subunit in the F(1)F(0)-ATPsynthase from Escherichia coli has been determined by electron microscopy of negatively stained, antibody-decorated enzyme molecules. The images show that the antibody is bound at the very top
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9f42f923e2cb7b3ffc21ac3a5c9e5833
https://pubmed.ncbi.nlm.nih.gov/10623533
https://pubmed.ncbi.nlm.nih.gov/10623533
Publikováno v:
The Journal of biological chemistry. 274(48)
Mutants with a cysteine residue in the gamma subunit at position 207 and the epsilon subunit at position 31 were expressed in combination with a c-dimer construct, which contains a single cysteine at position 42 of the second c subunit. These mutants
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0c8b15c33d0d2f878c0453df707bdc1e
https://pubmed.ncbi.nlm.nih.gov/10567396
https://pubmed.ncbi.nlm.nih.gov/10567396
Autor:
B, Schulenberg, R A, Capaldi
Publikováno v:
The Journal of biological chemistry. 274(40)
Four double mutants in the epsilon subunit were generated, each containing two cysteines, which, based on the NMR structure of this subunit, should form internal disulfide bonds. Two of these were designed to generate interdomain cross-links that loc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a2458e78178c8784e7688271cde4ad5e
https://pubmed.ncbi.nlm.nih.gov/10497194
https://pubmed.ncbi.nlm.nih.gov/10497194
Publikováno v:
Acta physiologica Scandinavica. Supplementum. 643
The ATP synthase F1F0 is the smallest molecular motor yet studied. ATP hydrolysis drives the rotary motion of the primary stalk subunits gamma and epsilon relative to the alpha 3 beta 3 part of F1. Evidence is reviewed to show that the delta and b su
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::dd7c42638791ace52272bb9938daff3d
https://pubmed.ncbi.nlm.nih.gov/9789558
https://pubmed.ncbi.nlm.nih.gov/9789558
Autor:
J J, García, R A, Capaldi
Publikováno v:
The Journal of biological chemistry. 273(26)
Unisite [gamma-32P]ATP hydrolysis was studied in ECF1 from the mutant betaE381C after generating a single disulfide bond between beta and gamma subunits to prevent the rotation of the gamma/epsilon domain. The single beta-gamma cross-link was obtaine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::cbec2f53b4b9d6038b168786b6131d7f
https://pubmed.ncbi.nlm.nih.gov/9632641
https://pubmed.ncbi.nlm.nih.gov/9632641
Publikováno v:
The Journal of biological chemistry. 272(49)
The delta and b subunits are both involved in binding the F1 to the F0 part in the Escherichia coli ATP synthase (ECF1F0). The interaction of the purified delta subunit and the isolated hydrophilic domain of the b subunit (bsol) has been studied here
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c74e33850d77072fed4a4f9939ab7116
https://pubmed.ncbi.nlm.nih.gov/9388256
https://pubmed.ncbi.nlm.nih.gov/9388256
Publikováno v:
The Journal of biological chemistry. 272(31)
A triple mutant of Escherichia coli F1F0-ATP synthase, alphaQ2C/alphaS411C/epsilonS108C, has been generated for studying movements of the gamma and epsilon subunits during functioning of the enzyme. It includes mutations that allow disulfide bond for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4ea120865fa99a690d21f031c76d4c86
https://pubmed.ncbi.nlm.nih.gov/9235970
https://pubmed.ncbi.nlm.nih.gov/9235970