Hoppe J - Search Results

1

Photolabeling of the phosphate binding site of mitochondrial F1-ATPase by [32P]azidonitrophenyl phosphate. Identification of the photolabeled amino acid residues.

Garin J, Michel L, Dupuis A, Issartel JP, Lunardi J, Hoppe J, Vignais P. Garin J, et al. Among authors: hoppe j. Biochemistry. 1989 Feb 21;28(4):1442-8. doi: 10.1021/bi00430a003. Biochemistry. 1989. PMID: 2524209

2

Mapping of the nucleotide-binding sites in the ADP/ATP carrier of beef heart mitochondria by photolabeling with 2-azido[alpha-32P]adenosine diphosphate.

Dalbon P, Brandolin G, Boulay F, Hoppe J, Vignais PV. Dalbon P, et al. Among authors: hoppe j. Biochemistry. 1988 Jul 12;27(14):5141-9. doi: 10.1021/bi00414a029. Biochemistry. 1988. PMID: 2844252

3

Amino acid sequence of the proteolipid subunit of the proton-translocating ATPase complex from the thermophilic bacterium PS-3.

Hoppe J, Sebald W. Hoppe J, et al. Eur J Biochem. 1980;107(1):57-65. doi: 10.1111/j.1432-1033.1980.tb04624.x. Eur J Biochem. 1980. PMID: 6447066 Free article.

4

Labeling of individual amino acid residues in the membrane-embedded F0 part of the F1 F0 ATP synthase from Neurospora crassa. Influence of oligomycin and dicyclohexylcarbodiimide.

Hoppe J, Gatti D, Weber H, Sebald W. Hoppe J, et al. Eur J Biochem. 1986 Mar 3;155(2):259-64. doi: 10.1111/j.1432-1033.1986.tb09484.x. Eur J Biochem. 1986. PMID: 2869944 Free article.

5

F0 part of the ATP synthase from Escherichia coli. Influence of subunits a, and b, on the structure of subunit c.

Steffens K, Hoppe J, Altendorf K. Steffens K, et al. Among authors: hoppe j. Eur J Biochem. 1988 Jan 4;170(3):627-30. doi: 10.1111/j.1432-1033.1988.tb13743.x. Eur J Biochem. 1988. PMID: 2892677 Free article.

Only liposomes containing intact F0 or all subunits of F0 were active in proton translocation and F1 binding [Schneider, E. and Altendorf, K. (1985) EMBO J. 4, 515-518]. The conformation of subunit c in the different preparations was analyzed by labelling the proteoliposom …

Only liposomes containing intact F0 or all subunits of F0 were active in proton translocation and F1 binding [Schneider, E. and Altendorf, K …

6

Structure of the membrane-embedded F0 part of F1F0 ATP synthase from Escherichia coli as inferred from labeling with 3-(Trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine.

Hoppe J, Brunner J, Jørgensen BB. Hoppe J, et al. Biochemistry. 1984 Nov 6;23(23):5610-6. doi: 10.1021/bi00318a035. Biochemistry. 1984. PMID: 6210106

7

Localization of the high-affinity ATP site in adenosine-3':5'-monophosphate-dependent protein kinase type I. Photoaffinity labelling studies with 8-azidoadenosine 5'-triphosphate.

Hoppe J, Freist W. Hoppe J, et al. Eur J Biochem. 1979 Jan 2;93(1):141-6. doi: 10.1111/j.1432-1033.1979.tb12804.x. Eur J Biochem. 1979. PMID: 220043 Free article.

8

An antibody-binding site in the native enzyme between amino acid residues 205-287 of the gamma-subunit of F1 from Escherichia coli.

Ehrig K, Hoppe J, Friedl P, Schairer HU. Ehrig K, et al. Among authors: hoppe j. Biochem Biophys Res Commun. 1986 May 29;137(1):468-73. doi: 10.1016/0006-291x(86)91233-7. Biochem Biophys Res Commun. 1986. PMID: 2424448

9

A model for the chemical interactions of adenosine 3':5'-monophosphate with the R subunit of protein kinase type I. Refinement of the cyclic phosphate binding moiety of protein kinase type I.

Jastorff B, Hoppe J, Morr M. Jastorff B, et al. Among authors: hoppe j. Eur J Biochem. 1979 Nov;101(2):555-61. doi: 10.1111/j.1432-1033.1979.tb19750.x. Eur J Biochem. 1979. PMID: 230034 Free article.

10

Assignment of conserved amino acid residues to the ATP site in the protein kinase domain of the receptor for epidermal growth factor.

Vogel S, Freist W, Hoppe J. Vogel S, et al. Among authors: hoppe j. Eur J Biochem. 1986 Feb 3;154(3):529-32. doi: 10.1111/j.1432-1033.1986.tb09430.x. Eur J Biochem. 1986. PMID: 3004981 Free article.

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