Zobrazeno 1 - 10 of 17 pro vyhledávání: '"B D Cain"'
1
Renal expression of the gene encoding the gastric H(+)-K(+)-ATPase beta-subunit
Autor: J. M. Callaghan, S. S. Tan, M. A. Khan, K. A. Curran, W. G. Campbell, A. J. Smolka, B. H. Toh, P. A. Gleeson, C. S. Wingo, B. D. Cain, al. et
Publikováno v: American Journal of Physiology-Renal Physiology. 268:F363-F374
The gastric mucosal parietal cells and cells of the renal collecting duct both possess H(+)-K(+)-adenosinetriphosphatase (H(+)-K(+)-ATPase) activities. In the stomach, the H(+)-K(+)-ATPase (EC 3.6.1.3) is responsible for acidification of luminal cont
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4245ee1441e8176c68708eb5e1f9e30f
https://doi.org/10.1152/ajprenal.1995.268.3.f363
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2
Mutagenic analysis of the F0 stator subunits
Autor: B D, Cain
Publikováno v: Journal of bioenergetics and biomembranes. 32(4)
The a and b subunits constitute the stator elements in the F0 sector of F1F0-ATP synthase. Both subunits have been difficult to study by physical means, so most of the information on structure and function relationships in the a and b subunits has be
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b38d633fba5de59657965db34ae0f40d
https://pubmed.ncbi.nlm.nih.gov/11768298
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3
Molecular identification of the renal H+,K+-ATPases
Autor: T L, Caviston, W G, Campbell, C S, Wingo, B D, Cain
Publikováno v: Seminars in nephrology. 19(5)
The pharmacological properties of H+,K+-ATPase activity described in the kidney were not necessarily consistent with the properties of the well-characterized gastric H+,K+-ATPase. Recent molecular biology experiments suggest that renal H+,K+-ATPase a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::911cc005c8b25391b129d5ce171da1d6
https://pubmed.ncbi.nlm.nih.gov/10511383
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4
Formation of the b subunit dimer is necessary for interaction with F1-ATPase
Autor: P L, Sorgen, M R, Bubb, K A, McCormick, A S, Edison, B D, Cain
Publikováno v: Biochemistry. 37(3)
In earlier work, we [McCormick, K. A., et al. (1993) J. Biol. Chem. 268, 24683-24691] observed that mutations at Ala-79 of the b subunit affect assembly of F1F0 ATP synthase. Polypeptides modeled on the soluble portion of the b subunit (bsol) with su
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a7d50d0133becb4df8bb79611aad858d
https://pubmed.ncbi.nlm.nih.gov/9454582
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5
Second-site suppressor mutations at glycine 218 and histidine 245 in the alpha subunit of F1F0 ATP synthase in Escherichia coli
Autor: P E, Hartzog, B D, Cain
Publikováno v: The Journal of biological chemistry. 269(51)
The alpha-like subunits of F1F0 ATP synthases share primary structural homology in two segments near their carboxyl termini. However, the amino acids at the functionally important positions occupied by alpha Gly-218 and alpha His-245 in Escherichia c
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f9b7a47f127545ce5dc5fe4218f8a063
https://pubmed.ncbi.nlm.nih.gov/7798232
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6
Characterization of mutations in the b subunit of F1F0 ATP synthase in Escherichia coli
Autor: K A, McCormick, G, Deckers-Hebestreit, K, Altendorf, B D, Cain
Publikováno v: The Journal of biological chemistry. 268(33)
Site-directed mutagenesis was used to investigate the restrictions on Ala-79 of the b subunit in F1F0 adenosine triphosphate synthase. This amino acid had been previously identified as particularly sensitive to mutation (McCormick, K. A., and Cain, B
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::3b925ce318bb8490c6806df16e8ec638
https://pubmed.ncbi.nlm.nih.gov/8227028
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7
The aleu207--arg mutation in F1F0-ATP synthase from Escherichia coli. A model for human mitochondrial disease
Autor: P E, Hartzog, B D, Cain
Publikováno v: The Journal of biological chemistry. 268(17)
The mitochondrial ATPase 6 gene encodes a subunit of F1F0 adenosine triphosphate (ATP) synthase. A mutation in the ATPase 6 gene has been genetically linked to two maternally inherited genetic diseases: neurological muscle weakness, ataxia, and retin
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::26e023883c7cc5ef4927d447992e4a63
https://pubmed.ncbi.nlm.nih.gov/8509361
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9
Proton Translocation by the F1FOATPase of Escherichia coli
Autor: B D Cain, Robert D. Simoni
Publikováno v: Journal of Biological Chemistry. 264:3292-3300
Cassette site-directed mutagenesis was employed to generate mutations in the a subunit (uncB (a) gene) of F1F0ATP synthase. Using sequence homology with similar subunits of other F1F0ATP synthases as a guide, 20 mutations were targeted to a region of
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7293a8239dad308914af2d067f8bfc87
https://doi.org/10.1016/s0021-9258(18)94065-2
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10
Interaction between Glu-219 and His-245 within the a subunit of F1F0-ATPase in Escherichia coli
Autor: Robert D. Simoni, B D Cain
Publikováno v: Journal of Biological Chemistry. 263:6606-6612
Oligonucleotide-directed mutagenesis was used to generate mutations in the a subunit gene (uncB) altering the glutamic acid 219 and the histidine 245 codons. Substitutions of aspartic acid, glutamine, histidine, and leucine for glutamic acid at posit
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::286abe642481291c9bbbdef8afb92d51
https://doi.org/10.1016/s0021-9258(18)68684-3
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