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Table 1.

Fold change for top over expressed proteins per time point.

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Table 1 Expand

Table 2.

Number of reactions catalyzed by essential enzymes according to [7] carrying zero flux.

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Table 2 Expand

Table 3.

Comparison of the MSEP for the proposed method and the E-flux method.

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Table 3 Expand

Fig 1.

Mean squared error of prediction for the proposed method and the E-flux method for three experimental conditions.

The use of proteomics data to define objective functions in FBA yields lower predicion errors.

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Fig 1 Expand

Table 4.

Number of reactions with large flux variability for the proposed proteomics objective function and the E-flux method.

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Table 4 Expand

Fig 2.

Comparison of flux variability between the proposed method and the E-flux method for all experimental conditions (individual replicates).

The use of proteomics data to define objective functions in FBA yields lower mean flux variability due to alternative optimal solutions.

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Fig 2 Expand

Fig 3.

Comparison of fold-change.

Logarithm of fold change of metabolic flux for mefloquine to control condition.

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Fig 3 Expand