Jans DA - Search Results

1

Structural gene for the phosphate-repressible phosphate-binding protein of Escherichia coli has its own promoter: complete nucleotide sequence of the phoS gene.

Surin BP, Jans DA, Fimmel AL, Shaw DC, Cox GB, Rosenberg H. Surin BP, et al. Among authors: jans da. J Bacteriol. 1984 Mar;157(3):772-8. doi: 10.1128/jb.157.3.772-778.1984. J Bacteriol. 1984. PMID: 6321434 Free PMC article.

2

Complementation between uncF alleles affecting assembly of the F1F0-ATPase complex of Escherichia coli.

Jans DA, Hatch L, Fimmel AL, Gibson F, Cox GB. Jans DA, et al. J Bacteriol. 1985 Apr;162(1):420-6. doi: 10.1128/jb.162.1.420-426.1985. J Bacteriol. 1985. PMID: 2858470 Free PMC article.

3

An acidic or basic amino acid at position 26 of the b subunit of Escherichia coli F1F0-ATPase impairs membrane proton permeability: suppression of the uncF469 nonsense mutation.

Jans DA, Hatch L, Fimmel AL, Gibson F, Cox GB. Jans DA, et al. J Bacteriol. 1984 Nov;160(2):764-70. doi: 10.1128/jb.160.2.764-770.1984. J Bacteriol. 1984. PMID: 6209261 Free PMC article.

4

Mutations in the uncE gene affecting assembly of the c-subunit of the adenosine triphosphatase of Escherichia coli.

Jans DA, Fimmel AL, Langman L, James LB, Downie JA, Senior AE, Ash GR, Gibson F, Cox GB. Jans DA, et al. Biochem J. 1983 Jun 1;211(3):717-26. doi: 10.1042/bj2110717. Biochem J. 1983. PMID: 6309138 Free PMC article.

5

The F1F0-ATPase of Escherichia coli. The substitution of alanine by threonine at position 25 in the c-subunit affects function but not assembly.

Fimmel AL, Jans DA, Hatch L, James LB, Gibson F, Cox GB. Fimmel AL, et al. Among authors: jans da. Biochim Biophys Acta. 1985 Jul 17;808(2):252-8. doi: 10.1016/0005-2728(85)90007-6. Biochim Biophys Acta. 1985. PMID: 2861849

6

An additional acidic residue in the membrane portion of the b-subunit of the energy-transducing adenosine triphosphatase of Escherichia coli affects both assembly and function.

Jans DA, Fimmel AL, Hatch L, Gibson F, Cox GB. Jans DA, et al. Biochem J. 1984 Jul 1;221(1):43-51. doi: 10.1042/bj2210043. Biochem J. 1984. PMID: 6235807 Free PMC article.

7

The F1F0-ATPase of Escherichia coli. Substitution of proline by leucine at position 64 in the c-subunit causes loss of oxidative phosphorylation.

Fimmel AL, Jans DA, Langman L, James LB, Ash GR, Downie JA, Senior AE, Gibson F, Cox GB. Fimmel AL, et al. Among authors: jans da. Biochem J. 1983 Aug 1;213(2):451-8. doi: 10.1042/bj2130451. Biochem J. 1983. PMID: 6193778 Free PMC article.

8

Hypothesis. The mechanism of ATP synthase. Conformational change by rotation of the beta-subunit.

Cox GB, Jans DA, Fimmel AL, Gibson F, Hatch L. Cox GB, et al. Among authors: jans da. Biochim Biophys Acta. 1984 Dec 17;768(3-4):201-8. doi: 10.1016/0304-4173(84)90016-8. Biochim Biophys Acta. 1984. PMID: 6239652 No abstract available.

9

Oxidative phosphorylation by mutant Escherichia coli membranes with impaired proton permeability.

Cox GB, Jans DA, Gibson F, Langman L, Senior AE, Fimmel AL. Cox GB, et al. Among authors: jans da. Biochem J. 1983 Oct 15;216(1):143-50. doi: 10.1042/bj2160143. Biochem J. 1983. PMID: 6316934 Free PMC article.

10

The chloroplast beta-subunit allows assembly of the Escherichia coli F0 portion of the energy transducing adenosine triphosphatase.

Munn AL, Whitfeld PR, Bottomley W, Hudson GS, Jans DA, Gibson F, Cox GB. Munn AL, et al. Among authors: jans da. Biochim Biophys Acta. 1991 Sep 27;1060(1):82-8. doi: 10.1016/s0005-2728(05)80122-7. Biochim Biophys Acta. 1991. PMID: 1655029

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