1983
DOI: 10.1093/mj/3.3.309
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The Rabbinical Conferences of the 1850's and the Quest for Liturgical Unity

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Cited by 3 publications
(2 citation statements)
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“…108,109 Interestingly, the ESRP motifs (Glu218-Ser219-Arg220-Pro221 in Sa-PDT and Glu319-Ser320-Arg321-Pro322 in AtADT2) and the GXLX motifs in Sa-PDT (Gly198, Leu199, Leu200, Ala201) and AtADT2 (Gly299, Val300, Leu301, Phe302) are both located at the interface between the two ACT regulatory domains in the dimers (Figure 8(c)). Indeed, mutational and isothermal calorimetric analyses indicated that mutations of residues comprising the ESRP, as well as the GXLX, motifs in the P-protein reduced sensitivity to Phe (1)-mediated feedback regulation.…”
Section: Bacterial Prephenate Dehydratases and Plant Arogenate Dehydrmentioning
confidence: 99%
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“…108,109 Interestingly, the ESRP motifs (Glu218-Ser219-Arg220-Pro221 in Sa-PDT and Glu319-Ser320-Arg321-Pro322 in AtADT2) and the GXLX motifs in Sa-PDT (Gly198, Leu199, Leu200, Ala201) and AtADT2 (Gly299, Val300, Leu301, Phe302) are both located at the interface between the two ACT regulatory domains in the dimers (Figure 8(c)). Indeed, mutational and isothermal calorimetric analyses indicated that mutations of residues comprising the ESRP, as well as the GXLX, motifs in the P-protein reduced sensitivity to Phe (1)-mediated feedback regulation.…”
Section: Bacterial Prephenate Dehydratases and Plant Arogenate Dehydrmentioning
confidence: 99%
“…The catalytic zinc was ligated to four amino acid residues, Cys47, His69, Glu70, and Cys163, in a tetrahedral orientation in both the apo form and the binary complex (Figures 34(b) and 34(c)). By contrast, the structural zinc ion was tetrahedrally coordinated with four cysteine residues, Cys100, Cys103, Cys106, and Cys114, being located in a short -helixcontaining loop (residues [98][99][100][101][102][103][104][105][106][107][108][109][110][111][112][113][114][115][116] (Figure 34(b)). By contrast, the structural zinc ion was tetrahedrally coordinated with four cysteine residues, Cys100, Cys103, Cys106, and Cys114, being located in a short -helixcontaining loop (residues [98][99][100][101][102][103][104][105][106][107][108][109][110][111][112][113][114][115][116] (Figure 34(b)).…”
Section: Cinnamyl Alcohol Dehydrogenase: Comparison To Horse Liver Almentioning
confidence: 99%