The seven 14-3-3 isoforms are highly abundant human proteins encoded by similar yet
distinct genes. 14-3-3 proteins recognize phosphorylated motifs within numerous human and …

Human protein networks have been widely explored but most binding affinities remain
unknown, hindering quantitative interactome-function studies. Yet interactomes rely on minimal …

Protein-protein interaction motifs are often alterable by post-translational modifications. For
example, 19% of predicted human PDZ domain-binding motifs (PBMs) have been …

The degradation of p53 is a hallmark of high-risk human papillomaviruses (HPVs) of the alpha
genus and HPV-related carcinogenicity. The oncoprotein E6 forms a ternary complex with …

Phosphorylation of short linear peptide motifs is a widespread process for the dynamic
regulation of protein–protein interactions. However, the global impact of phosphorylation events …

Bivalent V H Hs have been shown to display better functional affinity compared with their
monovalent counterparts. Bivalency can be achieved either by inserting a hinge region …

Protein domains often recognize short linear protein motifs composed of a core conserved
consensus sequence surrounded by less critical, modulatory positions. PTEN, a lipid …

The accurate description and subsequent modeling of protein interactomes requires
quantification of their affinities at proteome-wide scale. Here we develop and validate the Holdup …

Many protein-protein interactions are mediated by short linear peptide motifs binding to
cognate proteins or protein domains. Such interactions often display affinities in the mid-…

The human PDZome represents one of the largest globular domain families in the human
proteome, with 266 instances. These globular domains typically interact with C-terminal …