Schoner W - Search Results

1

How do MgATP analogues differentially modify high-affinity and low-affinity ATP binding sites of Na+/K(+)-ATPase?

Serpersu EH, Bunk S, Schoner W. Serpersu EH, et al. Among authors: schoner w. Eur J Biochem. 1990 Jul 31;191(2):397-404. doi: 10.1111/j.1432-1033.1990.tb19135.x. Eur J Biochem. 1990. PMID: 2166662 Free article.

2

Affinity labelling with MgATP analogues reveals coexisting Na+ and K+ forms of the alpha-subunits of Na+/K+-ATPase.

Antolovic R, Hamer E, Serpersu EH, Kost H, Linnertz H, Kovarik Z, Schoner W. Antolovic R, et al. Among authors: schoner w. Eur J Biochem. 1999 Apr;261(1):181-9. doi: 10.1046/j.1432-1327.1999.00260.x. Eur J Biochem. 1999. PMID: 10103049 Free article.

3

Epitope mapping by amino-acid-sequence-specific antibodies reveals that both ends of the alpha subunit of Na+/K(+)-ATPase are located on the cytoplasmic side of the membrane.

Antolovic R, Brüller HJ, Bunk S, Linder D, Schoner W. Antolovic R, et al. Among authors: schoner w. Eur J Biochem. 1991 Jul 1;199(1):195-202. doi: 10.1111/j.1432-1033.1991.tb16109.x. Eur J Biochem. 1991. PMID: 1712297 Free article.

4

Chromium(III)ATP inactivating (Na+ + K+)-ATPase supports Na+-Na+ and Rb+-Rb+ exchanges in everted red blood cells but not Na+,K+ transport.

Pauls H, Serpersu EH, Kirch U, Schoner W. Pauls H, et al. Among authors: schoner w. Eur J Biochem. 1986 Jun 16;157(3):585-95. doi: 10.1111/j.1432-1033.1986.tb09706.x. Eur J Biochem. 1986. PMID: 2424757 Free article.

5

Comparative studies on the ATPase-binding sites in Ca2+-ATPase and (Na+ + K+)-ATPase by the use of ATP-analogues.

Schoner W, Serpersu EH, Pauls H, Patzelt-Wenczler R, Kreickmann H, Rempeters G. Schoner W, et al. Z Naturforsch C Biosci. 1982 Jul-Aug;37(7-8):692-705. Z Naturforsch C Biosci. 1982. PMID: 6291269

6

Demonstration of a stable occluded form of Ca2+ by the use of the chromium complex of ATP in the Ca2+-ATPase of sarcoplasmic reticulum.

Serpersu EH, Kirch U, Schoner W. Serpersu EH, et al. Among authors: schoner w. Eur J Biochem. 1982 Feb;122(2):347-54. doi: 10.1111/j.1432-1033.1982.tb05887.x. Eur J Biochem. 1982. PMID: 6460621 Free article. No abstract available.

7

Modification of the E1ATP binding site of Na+/K(+)-ATPase by the chromium complex of adenosine 5'-[beta,gamma-methylene]triphosphate blocks the overall reaction but not the partial activities of the E2 conformation.

Hamer E, Schoner W. Hamer E, et al. Among authors: schoner w. Eur J Biochem. 1993 Apr 15;213(2):743-8. doi: 10.1111/j.1432-1033.1993.tb17815.x. Eur J Biochem. 1993. PMID: 8386635 Free article.

8

Binding of the Co(NH3)4 derivative of (2')3'-O-[N-methyl-anthraniloyl]-ATP to the E2ATP site of Na+/K+-transporting ATPase lowers the conformational flexibility of its E1ATP site.

Schoner W, Mertens W, Helms M, Fortes G. Schoner W, et al. Eur J Biochem. 1998 Apr 1;253(1):245-50. doi: 10.1046/j.1432-1327.1998.2530245.x. Eur J Biochem. 1998. PMID: 9578483 Free article.

Na+/K+-activated ATP hydrolysis by the sodium pump is catalyzed by the interaction of high-affinity and low-affinity ATP-binding sites [Thoenges, D. & Schoner, W. (1997) J. Biol. Chem. 272, 16315-16321]. To explore how binding of ATP to the low-affinity E2ATP si …

Na+/K+-activated ATP hydrolysis by the sodium pump is catalyzed by the interaction of high-affinity and low-affinity ATP-binding sites [Thoe …

9

Na+/K(+)-ATPase with a blocked E1ATP site still allows backdoor phosphorylation of the E2ATP site.

Linnertz H, Thönges D, Schoner W. Linnertz H, et al. Among authors: schoner w. Eur J Biochem. 1995 Sep 1;232(2):420-4. doi: 10.1111/j.1432-1033.1995.tb20827.x. Eur J Biochem. 1995. PMID: 7556190 Free article.

Evidently, ATP sites coexist in Na+/K(+)-ATPase, and binding of ATP to one site affects the property of the other site [Scheiner-Bobis, G., Esmann, M. & Schoner, W. (1989) Eur. J. Biochem. 183, 173-178]. Although the enzyme can be phosphorylated from both ATP si …

Evidently, ATP sites coexist in Na+/K(+)-ATPase, and binding of ATP to one site affects the property of the other site [Scheiner-Bobis, G., …

10

Blocking of Na+/K+ transport by the MgPO4 complex analogue Co(NH3)4PO4 leaves the Na+/Na(+)-exchange reaction of the sodium pump unaltered and shifts its high-affinity ATP-binding site to a Na(+)-like form.

Buxbaum E, Schoner W. Buxbaum E, et al. Among authors: schoner w. Eur J Biochem. 1990 Oct 24;193(2):355-60. doi: 10.1111/j.1432-1033.1990.tb19346.x. Eur J Biochem. 1990. PMID: 1699757 Free article.

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