T. Pape

Publication List Details

Period

1911 - 2009

Number

35

Co-Authors

Biogeochemistry of a low-activity cold seep in the Larsen B area, western Weddell Sea, Antarctica (2009)

H. Niemann, D. Fischer, D. Graffe, K. Knittel, A. Montiel, O. Heilmayer, ...

First videographic indication of an Antarctic cold seep ecosystem was recently obtained from the collapsed Larsen B ice shelf, western Weddell Sea (Domack et al., 2005). Within the framework of the...

A new species of Sarcofahrtiopsis Hall (Diptera: Sarcophagidae) living in roosts of Spix’s disk-winged bat Thyroptera tricolor Spix (Chiroptera) in Costa Rica. (2002)

Pape, T, Dechmann, D K N, Vonhof, M J

Sarcofahrtiopsisthyropteronthossp. n. is described from Costa Rica. All specimens were bred from faeces taken from young, tubular leaves of musoid plants (genera Heliconia and Calathea) used as...

Microbial reefs in the Black Sea fueled by anaerobic oxidation of methane (2002)

Michaelis, W., Seifert, R., Nauhaus, K., Treude, T., Thiel, V., Blumenberg, M., ...

Massive microbial mats covering up to 4-meter-high carbonate buildups prosper at methane seeps in anoxic waters of the northwestern Black Sea shelf. Strong C-13 depletions indicate an incorporation...

The G222D mutation in elongation factor Tu inhibits the codon-induced conformational changes leading to GTPase activation on the ribosome.

Vorstenbosch, E, Pape, T, Rodnina, M V, Kraal, B, Wintermeyer, W

Elongation factor Tu (EF-Tu) from Escherichia coli carrying the mutation G222D is unable to hydrolyze GTP on the ribosome and to sustain polypeptide synthesis at near physiological Mg2+...

Complete kinetic mechanism of elongation factor Tu-dependent binding of aminoacyl-tRNA to the A site of the E. coli ribosome.

Pape, T, Wintermeyer, W, Rodnina, M V

The kinetic mechanism of elongation factor Tu (EF-Tu)-dependent binding of Phe-tRNAPhe to the A site of poly(U)-programmed Escherichia coli ribosomes has been established by pre-steady-state kinetic...

Induced fit in initial selection and proofreading of aminoacyl-tRNA on the ribosome.

Pape, T, Wintermeyer, W, Rodnina, M

The fidelity of aminoacyl-tRNA (aa-tRNA) selection by the bacterial ribosome is determined by initial selection before and proofreading after GTP hydrolysis by elongation factor Tu. Here we report...

The G222D mutation in elongation factor Tu inhibits the codon-induced conformational changes leading to GTPase activation on the ribosome.

Vorstenbosch, E, Pape, T, Rodnina, M V, Kraal, B, Wintermeyer, W

Elongation factor Tu (EF-Tu) from Escherichia coli carrying the mutation G222D is unable to hydrolyze GTP on the ribosome and to sustain polypeptide synthesis at near physiological Mg2+...

Complete kinetic mechanism of elongation factor Tu-dependent binding of aminoacyl-tRNA to the A site of the E. coli ribosome.

Pape, T, Wintermeyer, W, Rodnina, M V

The kinetic mechanism of elongation factor Tu (EF-Tu)-dependent binding of Phe-tRNAPhe to the A site of poly(U)-programmed Escherichia coli ribosomes has been established by pre-steady-state kinetic...

Induced fit in initial selection and proofreading of aminoacyl-tRNA on the ribosome.

Pape, T, Wintermeyer, W, Rodnina, M

The fidelity of aminoacyl-tRNA (aa-tRNA) selection by the bacterial ribosome is determined by initial selection before and proofreading after GTP hydrolysis by elongation factor Tu. Here we report...