2013
DOI: 10.1016/j.bbagen.2013.06.010
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Enzyme dimension of the ribosomal protein S4 across plant and animal kingdoms

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Cited by 6 publications
(8 citation statements)
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“…We have previously reviewed evidence for autologous regulation of most ribosomal proteins of their own translation by means of binding directly to their own mRNA [7], and they include only a summary of that information in Table 3, Table 4, Table 5 and Table 6. The majority of ribosomal proteins, both in prokaryotes and eukaryotes, play additional roles in cellular metabolism, ranging from DNA repair, control of transcription and replication, and histone binding to the regulation of various enzymes and mRNA splicing as summarized in Table 3, Table 4, Table 5 and Table 6 [81,89,90,91,92,93,94,95,96,97,98,99,100,101,102,103,104,105,106,107,108,109,110,111,112]. The degree to which these extra-ribosomal functions are integrated into cellular functions is exemplified by the participation of riboprotein L13a into the GAIT complex in eukaryotes.…”
Section: Resultsmentioning
confidence: 99%
“…We have previously reviewed evidence for autologous regulation of most ribosomal proteins of their own translation by means of binding directly to their own mRNA [7], and they include only a summary of that information in Table 3, Table 4, Table 5 and Table 6. The majority of ribosomal proteins, both in prokaryotes and eukaryotes, play additional roles in cellular metabolism, ranging from DNA repair, control of transcription and replication, and histone binding to the regulation of various enzymes and mRNA splicing as summarized in Table 3, Table 4, Table 5 and Table 6 [81,89,90,91,92,93,94,95,96,97,98,99,100,101,102,103,104,105,106,107,108,109,110,111,112]. The degree to which these extra-ribosomal functions are integrated into cellular functions is exemplified by the participation of riboprotein L13a into the GAIT complex in eukaryotes.…”
Section: Resultsmentioning
confidence: 99%
“…The substrate concentration in these experiments was 20 μM, which is nearly equal to the reported K m value of 19.8 μM. 44 Experiments at a later stage were also performed using 40 μM substrate. The appearance of the profile for the solvent viscosity dependence of the initial velocity (v 0 ) for the substrate cleavage by hS4 at a constant enzyme:substrate ratio (Figure 3) is similar to that for the viscosity dependence of cytochrome c unfolding (Figure 1), and the same Kramers-like empirical relation (eq 2) fits the data best.…”
Section: ■ Resultsmentioning
confidence: 68%
“…In this set of experiments, human ribosomal protein S4 (hS4) that has been recently described as a cysteine protease , was allowed to cleave the synthetic substrate Z-FR↓-AMC (N-CBZ-Phe-Arg-aminomethylcoumarin) at different glycerol contents in 20 mM Tris-HCl and 100 mM NaCl (pH 7.6) at 37 °C. The substrate concentration in these experiments was 20 μM, which is nearly equal to the reported K m value of 19.8 μM . Experiments at a later stage were also performed using 40 μM substrate.…”
Section: Resultsmentioning
confidence: 99%
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