Emanuele Lamberti

Amyloid-β modulates the phase separation and aggregation of α-synuclein www.pnas.org/doi/10.1073/...

M6A-dependent RNA condensation underlies FUS autoregulation and can be harnessed for ALS therapy development www.science.org/doi/10.1126/...

Direct binding of TDP-43 and Tau drives their co-condensation, but suppresses Tau fibril formation and seeding www.biorxiv.org/content/10.1...

Atomic resolution map of the solvent interactions driving SOD1 unfolding in CAPRIN1 condensates | PNAS Biomolecules can be sequestered into membrane-less compartments, referred to as biomolecular condensates. Experimental and computational methods ha...

www.pnas.org/doi/10.1073/...

How short peptides disassemble tau fibrils in Alzheimer’s disease - Nature Cryo-electron and atomic force microscopy shed light on how fibrils of the protein tau, which accumulate in the brain of people with Alzheimer’s disease, can be disassembled by short peptides, providing a possible route towards developing treatments.

Nature research paper: How short peptides disassemble tau fibrils in Alzheimer’s disease

go.nature.com/44Bsian

Chemically active wetting | PNAS Wetting of liquid droplets on passive surfaces is ubiquitous in our daily lives, and the governing physical laws are well understood. When surfaces...

Chemically active wetting www.pnas.org/doi/abs/10.1...

Homotypic RNA clustering accompanies a liquid-to-solid transition inside the core of multi-component biomolecular condensates - Nature Chemistry Pathological aggregation of repeat-expanded RNA is implicated in neurodegeneration. Now results demonstrate that biomolecular condensates can promote irreversible clustering of GC-rich repeat RNAs fac...

Homotypic RNA clustering accompanies a liquid-to-solid transition inside the core of multi-component biomolecular condensates www.nature.com/articles/s41...

Global kinetic model of lipid-induced α-synuclein aggregation and its inhibition by small molecules | PNAS The aggregation of α-synuclein into amyloid fibrils is a hallmark of Parkinson’s disease. This process has been shown to directly involve interacti...

Global kinetic model of lipid-induced α-synuclein aggregation and its inhibition by small molecules
www.pnas.org/doi/10.1073/...

Network-forming phase separation of oppositely charged polyelectrolytes forming coacervates in a solvent Nature Communications - The formation of coacervates through phase separation of oppositely charged polyelectrolytes (PEs) is critical for understanding biological condensates and developing...

rdcu.be/eq4Od

Manipulation of coacervate droplets with an electric field | PNAS Many biopolymers are highly charged, and as in the case of many polymer mixtures, they tend to phase separate as a natural consequence of chain con...

Manipulation of coacervate droplets with an electric field doi.org/10.1073/pnas...

Macrocyclic β-arch peptides that mimic the structure and function of disease-associated tau folds rdcu.be/enCNK

Small-molecule dissolution of stress granules by redox modulation benefits ALS models rdcu.be/emsBr

Spatiotemporal deciphering of dynamic the FUS interactome during liquid-liquid phase separation in living cells - Nature Communications CLAPM uses proximity labeling mass spectrometry to monitor proteomes within phase-separated droplets. This approach identifies condensate-specific proteins to assess proteome dynamics in various cell ...

Spatiotemporal deciphering of dynamic the FUS interactome during liquid-liquid phase separation in living cells #NatCommun #MassSpec www.nature.com/articles/s41...

TAF15 amyloid filaments in frontotemporal lobar degeneration Nature - Cryogenic electron microscopy structures of amyloid filaments extracted from patient brains reveal that the protein TAF15 forms filaments that characterize certain cases of frontotemporal...

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Nuclear speckle proteins form intrinsic and MALAT1-dependent microphases Nuclear speckles are enriched in serine / arginine rich splicing factors (SRSFs), such as SRSF1. Splicing factors and proteins such as TDP43 concentrate into distinct speckle territories to enable pre...

www.biorxiv.org/content/10.1...

MOAG-4 promotes the aggregation of α-synuclein by competing with self-protective electrostatic interactions - Journal of Biological Chemistry www.jbc.org/article/S002...

Simple Model of the Effect of Solution Conditions on the Nucleation of Amyloid Fibrils | The Journal of Physical Chemistry B pubs.acs.org/doi/10.1021/...

www.researchsquare.com/article/rs-3...

The interface of condensates of the hnRNPA1 low-complexity domain promotes formation of amyloid fibrils Nature Chemistry - Understanding of the molecular mechanisms underlying the maturation of protein condensates into amyloid fibrils associated with neurodegenerative diseases has so far remained...

rdcu.be/d56UU

Interface of biomolecular condensates modulates redox reactions Biomolecular condensates mediate diverse cellular processes. The density-transition process of condensate formation results in the selective partition…

Interface of biomolecular condensates modulates redox reactions www.sciencedirect.com/science/arti...

Structures of filaments from Pick’s disease reveal a novel tau protein fold Nature - The structures of tau filaments from patients with the neurodegenerative disorder Pick’s disease show that the filament fold is different from that of the tau filaments found in...

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Loss of Dynamic RNA Interaction and Aberrant Phase Separation Induced by Two Distinct Types of ALS/FTD-Linked FUS Mutations FUS aggregation is pathogenic hallmark of incurable neurodegenerative diseases, including ALS and FTD. Niaki et al. demonstrate that two classes of ALS/FTD-linked mutations display distinct molecular phenotypes. Arginine mutations lead to defective RNA binding, whereas glycine mutations induce quick loss of fluidity, underpinning potentially disparate pathogenic pathways of disease-linked FUS mutants.

Loss of Dynamic RNA Interaction and Aberrant Phase Separation Induced by Two Distinct Types of ALS/FTD-Linked FUS Mutations: Molecular Cell www.cell.com/molecular-ce...