Kiersten M. Ruff

The paper designs synthetic scaffold proteins that form cell-cell interfaces with switch-like condensation behaviors, enabling selective and specific intercellular interactions.

The paper shows that alpha-synuclein phase separation can form Lewy body-like structures without pre-existing seeds, suggesting a new mechanism for neurodegeneration.

ASAP-ID reduces steric disruption in proximity labelling by using small tags and antibodies, identifying new lamin interactors and showing mutant-specific aggregation patterns.

This paper maps the critical regime of an intrinsically disordered protein using simulations and finite-size scaling, identifying three distinct phase behavior regimes.

The paper shows that SRSF1 and TDP-43 form microphases through protein interactions, and MALAT1 enhances this process by binding to SRSF1 microphases.

This study shows YAP and Mediator form transcriptionally active condensates through charge patterning, enabling signal integration in stem cells.

This study investigates the functional role of the I-II linker in Nav1.5 channels, finding that a point mutation significantly affects channel gating while deletions have minimal impact.

The paper shows that separable interactions in A1-LCD allow tunable metastability of condensates, which can suppress amyloid fibril formation even with ALS mutations.

The paper introduces GIN, a resource that decodes molecular grammars of human intrinsically disordered regions (IDRs) and identifies their functional roles in biological processes and disease.

This study identifies sequence-encoded molecular grammars in synapsin-1 IDRs that drive condensation and generate pH gradients relevant for synaptic function.

The paper identifies inert and seed-competent tau monomers, showing structural differences that influence aggregation potential.