This thesis explores the world of conditional protein-protein interactions using combinatorial peptide-phage display and proteomic peptide-phage display (ProP-PD). Large parts of proteins in the human proteome do not fold in to well-defined structures instead they are intrinsically disordered. The disordered parts are enriched in linear binding-motifs that participate in protein-protein interaction. These motifs are 3-12 residue long stretches of proteins where post-translational modifications, like protein phosphorylation, can occur changing the binding preference of the motif. Allosteric changes in a protein or domain due to phosphorylation or binding to second messenger molecules like Ca2+ can also lead conditional interactions. Finding ...
SummaryPhosphorylation is one of the most common posttranslational modifications controlling cellula...
<div><p>A substantial proportion of protein interactions relies on small domains binding to short pe...
A substantial proportion of protein interactions relies on small domains binding to short peptides i...
This thesis explores the world of conditional protein-protein interactions using combinatorial pepti...
Protein-protein interactions (PPIs) orchestrate a variety of cellular events, ranging from signal tr...
The intrinsically disordered regions of eukaryotic proteomes are enriched in short linear motifs (SL...
A key function of reversible protein phosphorylation is to regulate protein–protein interactions, ma...
Phage display is a powerful technique for profiling specificities of peptide binding domains. The me...
Specific protein-protein interactions are central to all processes that underlie cell physiology. Nu...
Phosphorylation is a ubiquitous post-translation modification that regulates protein function by pro...
Background: Sorcin is a calcium sensor that exerts many calcium-related functions in the cells, e.g....
Protein-protein interactions are of vital importance to the cell as they mediate the assembly of pro...
Cellular organization and response to internal and external stimuli are mediated by an intricate web...
Interactions between modular domains and short linear motifs (3-10 amino acids peptide stretches) ar...
SummaryPhosphorylation is one of the most common posttranslational modifications controlling cellula...
<div><p>A substantial proportion of protein interactions relies on small domains binding to short pe...
A substantial proportion of protein interactions relies on small domains binding to short peptides i...
This thesis explores the world of conditional protein-protein interactions using combinatorial pepti...
Protein-protein interactions (PPIs) orchestrate a variety of cellular events, ranging from signal tr...
The intrinsically disordered regions of eukaryotic proteomes are enriched in short linear motifs (SL...
A key function of reversible protein phosphorylation is to regulate protein–protein interactions, ma...
Phage display is a powerful technique for profiling specificities of peptide binding domains. The me...
Specific protein-protein interactions are central to all processes that underlie cell physiology. Nu...
Phosphorylation is a ubiquitous post-translation modification that regulates protein function by pro...
Background: Sorcin is a calcium sensor that exerts many calcium-related functions in the cells, e.g....
Protein-protein interactions are of vital importance to the cell as they mediate the assembly of pro...
Cellular organization and response to internal and external stimuli are mediated by an intricate web...
Interactions between modular domains and short linear motifs (3-10 amino acids peptide stretches) ar...
SummaryPhosphorylation is one of the most common posttranslational modifications controlling cellula...
<div><p>A substantial proportion of protein interactions relies on small domains binding to short pe...
A substantial proportion of protein interactions relies on small domains binding to short peptides i...