Schneider E - Search Results

1

Chemical modification of the F0 part of the ATP synthase (F1F0) from Escherichia coli. Effects on proton conduction and F1 binding.

Steffens K, Schneider E, Herkenhoff B, Schmid R, Altendorf K. Steffens K, et al. Among authors: schneider e. Eur J Biochem. 1984 Feb 1;138(3):617-22. doi: 10.1111/j.1432-1033.1984.tb07959.x. Eur J Biochem. 1984. PMID: 6319139 Free article.

2

Modification of subunit b of the F0 complex from Escherichia coli ATP synthase by a hydrophobic maleimide and its effects on F0 functions.

Schneider E, Altendorf K. Schneider E, et al. Eur J Biochem. 1985 Nov 15;153(1):105-9. doi: 10.1111/j.1432-1033.1985.tb09274.x. Eur J Biochem. 1985. PMID: 2866095 Free article.

3

ATP synthetase (F1F0) of Escherichia coli K-12. High-yield preparation of functional F0 by hydrophobic affinity chromatography.

Schneider E, Altendorf K. Schneider E, et al. Eur J Biochem. 1982 Aug;126(1):149-53. doi: 10.1111/j.1432-1033.1982.tb06759.x. Eur J Biochem. 1982. PMID: 6290212 Free article.

4

All three subunits are required for the reconstitution of an active proton channel (F0) of Escherichia coli ATP synthase (F1F0).

Schneider E, Altendorf K. Schneider E, et al. EMBO J. 1985 Feb;4(2):515-8. doi: 10.1002/j.1460-2075.1985.tb03658.x. EMBO J. 1985. PMID: 2410260 Free PMC article.

5

Fo portion of Escherichia coli ATP synthase. Further resolution of trypsin-generated fragments from subunit b.

Steffens K, Schneider E, Deckers-Hebestreit G, Altendorf K. Steffens K, et al. Among authors: schneider e. J Biol Chem. 1987 Apr 25;262(12):5866-9. J Biol Chem. 1987. PMID: 2883181 Free article.

By these techniques 3 degradation products with apparent molecular masses of about 16 kDa could be detected in accordance with previous findings (Perlin, D.S., and Senior, A.E. (1985) Arch. Biochem. Biophys. 236, 603-611). Labeling of isolated trypsin-treated Fo fractions …

By these techniques 3 degradation products with apparent molecular masses of about 16 kDa could be detected in accordance with previous find …

6

Subunit b of the membrane moiety (F0) of ATP synthase (F1F0) from Escherichia coli is indispensable for H+ translocation and binding of the water-soluble F1 moiety.

Schneider E, Altendorf K. Schneider E, et al. Proc Natl Acad Sci U S A. 1984 Dec;81(23):7279-83. doi: 10.1073/pnas.81.23.7279. Proc Natl Acad Sci U S A. 1984. PMID: 6209711 Free PMC article.

7

Molecular properties of the ATP synthetase from Escherichia coli.

Paradies HH, Mertens G, Schmid R, Schneider E, Altendorf K. Paradies HH, et al. Among authors: schneider e. Biochem Biophys Res Commun. 1981 Feb 12;98(3):595-606. doi: 10.1016/0006-291x(81)91156-6. Biochem Biophys Res Commun. 1981. PMID: 6261744 No abstract available.

8

ATP-synthetase complex (F1F0) from Escherichia coli. Purification and characterization of subunits A and B of the F0 part.

Steffens K, Kiltz HH, Schneider E, Schmid R, Altendorf K. Steffens K, et al. Among authors: schneider e. FEBS Lett. 1982 Jun 1;142(1):151-4. doi: 10.1016/0014-5793(82)80240-8. FEBS Lett. 1982. PMID: 6286344 Free article. No abstract available.

9

Proton-conducting portion (F0) from Escherichia coli ATP synthase: preparation, dissociation into subunits, and reconstitution of an active complex.

Schneider E, Altendorf K. Schneider E, et al. Methods Enzymol. 1986;126:569-78. doi: 10.1016/s0076-6879(86)26059-0. Methods Enzymol. 1986. PMID: 2908466 No abstract available.

10

Reconstitution of the purified proton conductor (F0) of the adenosine triphosphatase complex from Escherichia coli.

Schneider E, Altendorf K. Schneider E, et al. FEBS Lett. 1980 Jul 28;116(2):173-6. doi: 10.1016/0014-5793(80)80636-3. FEBS Lett. 1980. PMID: 6447620 Free article. No abstract available.

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