Carlos A. Castañeda

The paper uses charge detection mass spectrometry to detect protein nanoclusters, revealing their mass dispersion and polydispersity as intermediates in phase separation.

The paper investigates how tubulin C-terminal tails respond to pH changes and shows their role in regulating microtubule interactions through protonation of glutamate residues.

The paper investigates how intramolecular interactions between folded and disordered regions of ubiquilin proteins influence their structure and function across different species.

This study identifies distinct roles of STI1 domains in UBQLN2's phase separation and stress-induced condensate formation in human cells.

This study identifies the STI1 domain's role in driving Dsk2 self-association and phase separation through interactions with transient helices in disordered regions, with implications for proteasome condensate formation.

This study shows that polyubiquitinated substrates modulate UBQLN2 phase separation in a linkage-dependent manner, affecting proteasome activity and deubiquitination.

This study shows that the N-terminal disordered regions and proline-rich domain regulate phase separation in UBQLN1, UBQLN2, and UBQLN4, with distinct temperature dependencies.