V. Rangachari

Reversible disulfide bond crosslinks as tunable levers of phase separation in designer biomolecular condensates.

This study investigates the role of cysteine residues in biomolecular condensates, showing they function as covalent nodes that tune phase separation through redox-sensitive disulfide bonds.

α-Synuclein emulsifies TDP-43 prion-like domain - RNA liquid droplets to promote heterotypic amyloid fibrils

This study shows α-synuclein emulsifies TDP-43 prion-like domain-RNA droplets, promoting heterotypic amyloid fibril formation.

Sugar distributions on gangliosides guide the formation and stability of amyloid-β oligomers

This study shows that sugar distributions on gangliosides modulate Aβ oligomerization and stability.

De novo amyloid peptides with subtle sequence variations differ in their self-assembly and nanomechanical properties

Distinct neurotoxic TDP-43 fibril polymorphs can be generated by heterotypic interactions with α-synuclein

This study shows that α-synuclein can generate distinct TDP-43 fibril polymorphs through heterotypic interactions, leading to synaptic dysfunction.

Ganglioside enriched phospholipid vesicles induce cooperative Aβ oligomerization and membrane disruption

This study shows that GM1-enriched liposomes promote toxic Aβ oligomerization and membrane disruption through cooperative processes.

αS oligomers generated from polyunsaturated fatty acid and dopamine metabolite differentially interact with Aβ to enhance neurotoxicity

This study investigates how αS oligomers from DOPAL and DHA interact with Aβ, showing differential effects on Aβ aggregation and toxicity in neuroblastoma cells.

Cytoplasmic Colocalization of Granulins and TDP-43 Prion-like Domain Involves Electrostatically Driven Coacervation Tuned by the Redox State of Cysteines.

This study shows extracellular granulins colocalize with TDP-43 prion-like domain fragments in neuroblastoma cells and undergo phase separation driven by electrostatic interactions and cysteine redox state.

Prion-like C-terminal domain of TDP-43 and α-Synuclein interact synergistically to generate neurotoxic hybrid fibrils

This study investigates the synergistic interaction between TDP-43's prion-like domain and α-synuclein, showing they form toxic hybrid fibrils with increased cytotoxicity.

Are Granulins Copper Sequestering Proteins?

This study investigates whether granulins bind copper ions and finds that GRN-3 and GRN-5 selectively bind Cu(II) under neutral pH, suggesting a potential role in copper sequestration and redox regulation.

Granulins modulate liquid-liquid phase separation and aggregation of TDP-43 C-terminal domain

This study shows GRNs-3 and -5 interact with TDP-43CTD to modulate its aggregation and stress granule formation in vitro, linking PGRN loss to FTLD and ALS.

A game theoretic approach to deciphering the dynamics of amyloid-β aggregation along competing pathways

This paper uses a game theoretic framework based on Nash equilibria to model and simulate competing pathways of amyloid-β aggregation in the presence of fatty acids, showing how rate constants control oligomer formation.

Large Fatty Acid-derived Aβ42 oligomers Form Ring-like Assemblies

This study determines the structures of large fatty acid-derived Aβ42 oligomers using molecular dynamics and biophysical methods, revealing ring-like assemblies with distinct sizes and functional properties.