Defective gamma subunit of ATP synthase (F1F0) from Escherichia coli leads to resistance to aminoglycoside antibiotics.

Por Humbert, R, Altendorf, K
Publicado em 1989

Bacterial adenosine 5'-triphosphate synthase (F1F0): purification and reconstitution of F0 complexes and biochemical and functional characterization of their subunits.

Por Schneider, E, Altendorf, K
Publicado em 1987

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.

Por Schneider, E, Altendorf, K
Publicado em 1984

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

Por Schneider, E, Altendorf, K
Publicado em 1985

Valinomycin-induced cation transport in vesicles does not reflect the activity of K+ transport systems in Escherichia coli.

Por Altendorf, K, Epstein, W, Löhmann, A
Publicado em 1986

Orientation of Membrane Vesicles from Escherichia coli as Detected by Freeze-Cleave Electron Microscopy

Por Altendorf, K. H., Staehelin, L. A.
Publicado em 1974

Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells.

Por Bowman, E J, Siebers, A, Altendorf, K
Publicado em 1988

Low-affinity potassium uptake system in the archaeon Methanobacterium thermoautotrophicum: overproduction of a 31-kilodalton membrane protein during growth on low-potassium medium.

Por Glasemacher, J, Siebers, A, Altendorf, K, Schönheit, P
Publicado em 1996

Isolation and characterization of the high-affinity K(+)-translocating ATPase from Rhodobacter sphaeroides.

Por Abee, T, Siebers, A, Altendorf, K, Konings, W N
Publicado em 1992

The F0 complex of the ATP synthase of Escherichia coli contains a proton pathway with large proton polarizability caused by collective proton fluctuation.

Por Bartl, F, Deckers-Hebestreit, G, Altendorf, K, Zundel, G
Publicado em 1995

Identification of the structural proteins of an ATP-driven potassium transport system in Escherichia coli.

Por Laimins, L A, Rhoads, D B, Altendorf, K, Epstein, W
Publicado em 1978

High-affinity potassium uptake system in Bacillus acidocaldarius showing immunological cross-reactivity with the Kdp system from Escherichia coli.

Por Bakker, E P, Borchard, A, Michels, M, Altendorf, K, Siebers, A
Publicado em 1987

Sequence homology between two membrane transport ATPases, the Kdp-ATPase of Escherichia coli and the Ca2+-ATPase of sarcoplasmic reticulum.

Por Hesse, J E, Wieczorek, L, Altendorf, K, Reicin, A S, Dorus, E, Epstein, W
Publicado em 1984

Replacement of glycine 232 by aspartic acid in the KdpA subunit broadens the ion specificity of the K(+)-translocating KdpFABC complex.

Por Schrader, M, Fendler, K, Bamberg, E, Gassel, M, Epstein, W, Altendorf, K, Dröse, S
Publicado em 2000

KdpD and KdpE, proteins that control expression of the kdpABC operon, are members of the two-component sensor-effector class of regulators.

Por Walderhaug, M O, Polarek, J W, Voelkner, P, Daniel, J M, Hesse, J E, Altendorf, K, Epstein, W
Publicado em 1992

A model of the quaternary structure of the Escherichia coli F1 ATPase from X-ray solution scattering and evidence for structural changes in the delta subunit during ATP hydrolysis.

Por Svergun, D I, Aldag, I, Sieck, T, Altendorf, K, Koch, M H, Kane, D J, Kozin, M B, Grüber, G
Publicado em 1998