… Pelletier, JN & Michnick, SW A protein complementation assay for detection of protein–…
Remy, I., Wilson, IA & Michnick, SW Erythropoietin receptor activation by a ligand-induced …

Over a century ago, colloidal phase separation of matter into non-membranous bodies was
recognized as a fundamental organizing principal of cell "protoplasm." Recent insights into …

Owing to their crucial roles in regulating protein function, phosphorylation sites (phosphosites)
are expected to be evolutionarily conserved. However, mixed results regarding this …

Drosophila olfactory sensory neurons (OSNs) each express two odorant receptors (ORs): a
divergent member of the OR family and the highly conserved, broadly expressed receptor …

Protein interactions regulate the systems-level behavior of cells; thus, deciphering the structure
and dynamics of protein interaction networks in their cellular context is a central goal in …

Erythropoietin and other cytokine receptors are thought to be activated through hormone-induced
dimerization and autophosphorylation of JAK kinases associated with the receptor …

Protein-fragment complementation assays (PCAs) provide a general strategy to study the
dynamics of protein-protein interactions in vivo and in vitro. The full potential of PCA requires …

We have previously described a strategy for detecting protein–protein interactions based on
protein interaction–assisted folding of rationally designed fragments of enzymes. We call …

Transforming growth factor β (TGF-β) has a major role in cell proliferation, differentiation
and apoptosis in many cell types. Integration of the TGF-β pathway with other signalling …

Reassembly of enzymes from peptide fragments has been used as a strategy for understanding
the evolution, folding, and role of individual subdomains in catalysis and regulation of …