Results 141 to 150 of about 10,769 (286)

Mesoscale properties of protein clusters determine the size and nature of liquid-liquid phase separation (LLPS)

open access: yes
The observation of Liquid-Liquid Phase Separation (LLPS) in biological cells has dramatically shifted the paradigm that soluble proteins are uniformly dispersed in the cytoplasm or nucleoplasm.
Daniella Goldfarb   +5 more
core   +1 more source

Topology‐Encoded Charge Polarity Governs Multiphase Organization in Intrinsically Disordered Protein Polymer Condensates

open access: yesSmall, EarlyView.
Electrostatic topology is shown to program phase separation and internal organization in thermoresponsive intrinsically disordered protein polymer (IDPP) condensates. By comparing oppositely charged IDPPs with a covalent diblock, chain connectivity is revealed to control charge compensation, dense‐phase micropolarity, miscibility, and apparent acid ...
Julio Fernández‐Fernández   +6 more
wiley   +1 more source

Liquid-liquid phase separation (LLPS) in DNA and chromatin systems from the perspective of colloid physical chemistry

open access: yes
DNA is a highly charged polyelectrolyte and is prone to associative phase separation driven by the presence of multivalent cations, charged surfactants, proteins, polymers and colloids.
Nordenskiöld, Lars   +12 more
core   +1 more source

Symmetry‐Guided Optical Control of Dynamic 1D Protein Self‐Assembly and Precise In Vitro Initiation of Biomolecular Condensation

open access: yesSmall, EarlyView.
A photoreversible 1D protein assembly has been developed by utilizing symmetry matching between StrepTactin and photoswitchable Dronpa145N. The light‐induced modulation of oligomerization allows for precise control over protein connectivity and valency.
Jangwon Bae, Yongwon Jung
wiley   +1 more source

Elucidation of regulation mechanisms of LLPS leading to pathological protein aggregation in neurodegenerative diseases [PDF]

open access: yes
本研究では、ポリグルタミン(PolyQ)病、筋萎縮性側索硬化症(ALS)などの神経変性疾患における原因蛋白質の液-液相分離(LLPS)の制御破綻による凝集メカニズムの解明を目的として、1)Thio-PolyQとTDP-43-MBPの試験管内実験系を樹立し、両蛋白質のLLPS・凝集を阻害する化合物Xを同定した。2)培養細胞において、DCTN1ノックダウンなどの微小管輸送障害によりTDP-43のストレス顆粒からの解離が遅延し、さらにALSモデルショウジョウバエにおいて ...
永井, 義隆   +2 more
core   +1 more source

HS‐AFM Reveals Hierarchical RNA Folding Driving Condensate Assembly and Material States

open access: yesSmall, EarlyView.
High‐speed atomic force microscopy reveals the nanoscale pathway of RNA condensate formation, from individual RNA folding to higher‐order assembly. Quantitative analyses of fusion dynamics and nanomechanical properties distinguish liquid‐like poly A condensates from solid‐like total RNA assemblies, providing a direct link between RNA self‐assembly and ...
S. M. Neaz Mahmud   +5 more
wiley   +1 more source

Self‐Assembly of Hierarchically Structured Materials From Liquid Crystalline Mesophases of Tobacco Mosaic Virus‐Like Particles

open access: yesSmall, EarlyView.
Recombinantly produced Tobacco Mosaic Virus coat protein (TMVcp) helical rods were demonstrated to reproducibly self‐assemble into hierarchically structured macroscopic filaments, driven by a lyotropic liquid crystal (LC) intermediate phase. The results indicate anisotropic molecular alignment of the fluid phase, retention of the native secondary ...
Guido M. Merino   +2 more
wiley   +1 more source

FXF‐OMe Is a Stable Tripeptide Motif for Ultra‐Short Peptide Coacervates That Establishes Structure‐Property‐Function Relationships

open access: yesSmall, EarlyView.
Ultra‐short peptides with a minimal sticker‐spacer structure undergo liquid‐liquid phase separation, resulting in condensates with microenvironments controlled by the hydrophobicity of the spacers. The condensates provide an easily tunable and exceptionally stable scaffold for photocatalytic microreactors in aqueous media, where catalysis efficiency is
Samuel Hamroff, Lucas Caire da Silva
wiley   +1 more source

Age-Related Increases in PDE11A4 Protein Expression Trigger Liquid–Liquid Phase Separation (LLPS) of the Enzyme That Can Be Reversed by PDE11A4 Small Molecule Inhibitors

open access: yes
PDE11A is a little-studied phosphodiesterase sub-family that breaks down cAMP/cGMP, with the PDE11A4 isoform enriched in the memory-related hippocampal formation.
Marie Danaher   +7 more
core   +1 more source

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