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Table 1. Summary of results for selected motif candidates.
2002
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Table 3 - Conserved motif counts and motif processing Conserved Motif counts
2008
"... In PAGE 6: ... Strategy 2 uses all available alignment information (pairwise and multiple alignments) whereas strategy 3 does not use any alignment information in the actual motif discovery process. Table3 summarizes the different stages in the motif discovery process for each strategy.... In PAGE 7: ... We prune the list of motif candidates by removing degenerate motifs based on their Z-score and P-values. This step halves the number of motif candidates (see Table3 ). An overview of the entire processing pipeline is given in Figure 3.... ..."
(Table 2; Figure 3). These data strongly suggest that these gene clusters are part of the catabolite control regulon that is controlled by the central regulator CcpA. To further sub- stantiate this, a MAST-motif search was performed to identify putative CRE sites, for binding of CcpA [43,44], within the csc gene clusters and their upstream regions. Putative CRE sites could be identified for six out of the seven up-regulated csc clusters, generally upstream of the first gene of the cluster and in three clusters also inside csc genes (Figure 1, Table 3). In contrast, no significant CRE- like sites could be identified within or upstream of the residual csc gene clusters, supporting a functional role of the identified CRE-site candidate sequences in regulation of these clusters.
2006
Table 2. Numbers of candidates analyzed by the Apriori-like algorithm
"... In PAGE 8: ... Table2 presents numbers of candidates analyzed by the Apriori-like algorithm for different numbers of event attributes (denoted as NATR) and their domain sizes ... ..."
Table 3. Most prevalent KDEL-like carboxy-terminal motifs of soluble kernel ER proteins.
2004
"... In PAGE 14: ...2% of the soluble proteins contain the signal. Table3 shows the most prevalent carboxy-terminal KDEL-like motifs in kernel ER proteins. Among the remaining 73.... ..."
Table 4. Accuracy of various weight matrix and HMM regimes for detecting AATAAA motifs
2004
"... In PAGE 5: ... Since cleavage sites are imprecise, we calculated the accuracy based on identifying the correct AATAAA motif and not the cleavage site. Table4 shows that a crude scan for all exact matches to AATAAA within 1000 nt of the stop codon cor- rectly identifies 56% of signals, though 46% of the total pre- dictions are spurious. If we propose that the 50-most exact match to AATAAA is the signal, the proportion of signals detected correctly is reduced by 5% but there is an 8% increase in specificity.... In PAGE 6: ... For each gene, we used our HMM to search the 1000 bases 30 of each annotated stop codon, and annotated the most likely cleavage site as deter- mined by the Viterbi algorithm (available in the supplement- ary data). We expect 70% of these to be correct, from our previous experiments ( Table4 ). Figure 4 shows the frequency distribution of the distance between WormBase 30-UTRs and the Viterbi prediction for each of their 30-UTR candidates.... In PAGE 7: ... In these experi- ments, we modified the HMM by including 3 coding states which correspond to the nucleotide frequencies observed in first, second and third positions within codons. Table4 shows that the weight matrix methods find a large number of false positives in the coding sequence. However, the specificity of the HMM degrades only slightly, and the performance differ- ence of the posterior decoding is particularly small.... ..."
Table 3.2: Ability of the model to learn motifs that are as likely as the true structure in synthetic data.
Table 1. Nucleotide substitution rates in motifs
2006
"... In PAGE 6: ... Specifically, we calculated the likelihood of each nucleotide substituting for every other in each motif in the dataset. These frequencies are shown in Table1 . For details of how the table was generated see Materials and Methods.... In PAGE 7: ... QNS(b1,b2) (the nucleotide substitution parameter) is the appropriate value from our nucleotide substitution matrix, where b1 (the nucleotide in the candidate k-mer) is substitu- ting for b2 (the nucleotide in the motif k-mer). If d is greater than 1, then QNS(b1,b2) is the average of all of the substitution probabilities (given in Table1 , a and c). Pseudo-k-mers.... ..."
Table 1. Nucleotide substitution rates in motifs
2006
"... In PAGE 6: ... Specifically, we calculated the likelihood of each nucleotide substituting for every other in each motif in the dataset. These frequencies are shown in Table1 . For details of how the table was generated see Materials and Methods.... In PAGE 7: ... QNS(b1,b2) (the nucleotide substitution parameter) is the appropriate value from our nucleotide substitution matrix, where b1 (the nucleotide in the candidate k-mer) is substitu- ting for b2 (the nucleotide in the motif k-mer). If d is greater than 1, then QNS(b1,b2) is the average of all of the substitution probabilities (given in Table1 , a and c). Pseudo-k-mers.... ..."
Table 1. Nucleotide substitution rates in motifs
2006
"... In PAGE 6: ... Specifically, we calculated the likelihood of each nucleotide substituting for every other in each motif in the dataset. These frequencies are shown in Table1 . For details of how the table was generated see Materials and Methods.... In PAGE 7: ... QNS(b1,b2) (the nucleotide substitution parameter) is the appropriate value from our nucleotide substitution matrix, where b1 (the nucleotide in the candidate k-mer) is substitu- ting for b2 (the nucleotide in the motif k-mer). If d is greater than 1, then QNS(b1,b2) is the average of all of the substitution probabilities (given in Table1 , a and c). Pseudo-k-mers.... ..."
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