A simple model of mergers and innovation

We analyze the impact of a merger on firms’ incentives to innovate. We show that the merging parties always decrease their innovation efforts post-merger while the outsiders to the merger respond by increasing their effort. A merger tends to reduce overall innovation. Consumers are always worse off after a merger. Our model calls into question the applicability of the “inverted-U” relationship between innovation and competition to a merger setting

Additional file 5: Figure S2. of In silico identification of essential proteins in Corynebacterium pseudotuberculosis based on protein-protein interaction networks

Homology distribution of Cp essential proteins aligned against hosts. Dark green: proteins homologous to host; Yellow: Proteins with low identity against hosts (identity < 30 %). Dark red: non-host homologous proteins, proteins with low identity and low coverage alignment against hosts (identity x coverage < = 10 %). Dark blue: non-host homologous proteins, proteins with no alignment hits against O. aires and C. hircus. Light blue: non-host homologous proteins, proteins with no alignment hits against the five hosts. The alignment summary is depicted in Additional file 6. (JPG 318 kb

Additional file 4: of In silico identification of essential proteins in Corynebacterium pseudotuberculosis based on protein-protein interaction networks

List of 181 essential proteins. The amino acid sequence of hubs proteins was compared against bacterial proteins sequence from Database of Essential Genes (DEG). (TXT 62 kb

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Compounds/Libraries name, MolDock scores and predicted hydrogen bonds for the selected molecules against NP_939445.1 (DIP1084, Putative iron transport membrane protein, FecCD-family).

<p>Compounds/Libraries name, MolDock scores and predicted hydrogen bonds for the selected molecules against NP_939445.1 (DIP1084, Putative iron transport membrane protein, FecCD-family).</p

Superposition of co-crystallized and Docked ligand; Dark Khaki represents the co crystallized ligand and Dark Cyan the re-docked conformation of the ligand.

<p>Superposition of co-crystallized and Docked ligand; Dark Khaki represents the co crystallized ligand and Dark Cyan the re-docked conformation of the ligand.</p

Compounds/Libraries name, MolDock scores and predicted hydrogen bonds for the selected molecules against NP_938502.1 (bioB, Biotin synthase).

<p>Compounds/Libraries name, MolDock scores and predicted hydrogen bonds for the selected molecules against NP_938502.1 (bioB, Biotin synthase).</p

An integrative <i>in-silico approach</i> for therapeutic target identification in the human pathogen <i>Corynebacterium diphtheriae</i> - Fig 11

<p><b>A-I</b> 3D cartoon representation of the docking analyses for the most druggable protein cavity of <b>NP_939445.1</b> (<b>DIP1084,</b> Putative iron transport membrane protein, FecCD-family) with Jacarandic Acid (CID 73645). <b>A-II:</b> 3D surface representation of the docking analyses for the structure of Jacarandic Acid with <b>DIP1084,</b> Putative iron transport membrane protein. Figs <b>B-I, II, C-I, II</b> & <b>D-1, II D</b> represent same information for compounds 16-hydrazonisosteviol <b>ZINC13142972</b> and <b>ZINC70454922</b> respectively, for the same protein cavity.</p

Strains of <i>C</i>. <i>diphtheriae</i> employed in the pan-modelome study with information on genomes statistics, disease prevalence and location of isolation.

<p>Strains of <i>C</i>. <i>diphtheriae</i> employed in the pan-modelome study with information on genomes statistics, disease prevalence and location of isolation.</p

Compounds/Libraries name, MolDock scores and predicted hydrogen bonds for the selected molecules against NP_939345.1 (DIP0983, hypothetical protein DIP0983).

<p>Compounds/Libraries name, MolDock scores and predicted hydrogen bonds for the selected molecules against NP_939345.1 (DIP0983, hypothetical protein DIP0983).</p