LmU and GlmV reactions are carried out by a single bifunctional enzyme called GlmU. The GlmV enzyme of C. trachomatis is not homologous with the Cterminal portion of E. coli GlmU. GlmV exemplifies a case where a high-Trp analog has evolved as a functional replacement of a lowTrp analog. A number of such up-Trp (or down-Trp) replacements are enumerated in this article. The extent to which the GlmV
LmU and GlmV reactions are carried out by a single bifunctional enzyme called GlmU. The GlmV enzyme of C. trachomatis is not homologous with the Cterminal portion of E. coli GlmU. GlmV exemplifies a case where a high-Trp analog has evolved as a functional replacement of a lowTrp analog. A number of such up-Trp (or down-Trp) replacements are enumerated in this article. The extent to which the GlmV
Review studies that contained a total of 38 individual studies. Supplemental File S2 contains the raw data from these eight studies and supplemental Table S1 contains an overview of the individual 38 studies. Data sets from Beck et al. (22) and D'Alessandro et al. (23), which summarized previous published work, were used instead of each individual study reviewed. Data sets were converted to the co
Tide precursors sampled for MS/MS events (Fig. 5B). The base peak intensity of the chromatogram from 5 mM piperidine solvent with 5 DMSO was slightly lower than 5 mM piperidine alone (Fig. 5A), also juxtaposing the trends observed in positive mode. Noticeable, though, is that the greatest number of MS/MS scans was taken with the piperidine/DMSO buffers than with any other system. These results su
At the beginning of the experiment (Fig. 1). The eABR threshold of the respective ears then was used as a reference current level. Electrical stimulation was wide bipolar between the apical-most and the basal-most contact of the implant, covering cochlear positions with characteristic frequencies 10 kHz (Kral et al., 2009). Auditory stimulation. For intracortical recordings, pulses were presented
Utant that we had earlier observed associating with ESCRT-I, the YLPM1 associated proteins, and CPSF6/7. When we purified Halo-TNIP2 196 ?46 associated proteins in the presence of Benzonase? an endonuclease that digests both DNA and RNA, we detected the bait proteins shown in Fig. 5A (light gray bars). There was no significant change in the relative amounts of the subunits of the ESCRT-I complex d