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Interplay of folded domains and the disordered low-complexity domain in  mediating hnRNPA1 phase separation | bioRxiv
Interplay of folded domains and the disordered low-complexity domain in mediating hnRNPA1 phase separation | bioRxiv

Molecular structure of an amyloid fibril formed by FUS low-complexity domain  - ScienceDirect
Molecular structure of an amyloid fibril formed by FUS low-complexity domain - ScienceDirect

A. Cartoon of FUS protein topology, showing the tyrosine rich low... |  Download Scientific Diagram
A. Cartoon of FUS protein topology, showing the tyrosine rich low... | Download Scientific Diagram

Tuning levels of low-complexity domain interactions to modulate endogenous  oncogenic transcription - ScienceDirect
Tuning levels of low-complexity domain interactions to modulate endogenous oncogenic transcription - ScienceDirect

Low-complexity domains adhere by reversible amyloid-like interactions  between kinked β-sheets | bioRxiv
Low-complexity domains adhere by reversible amyloid-like interactions between kinked β-sheets | bioRxiv

Imaging dynamic and selective low-complexity domain interactions that  control gene transcription | Science
Imaging dynamic and selective low-complexity domain interactions that control gene transcription | Science

A) Schematic representation of a low complexity region-containing... |  Download Scientific Diagram
A) Schematic representation of a low complexity region-containing... | Download Scientific Diagram

Phosphorylation-Regulated Binding of RNA Polymerase II to Fibrous Polymers  of Low-Complexity Domains: Cell
Phosphorylation-Regulated Binding of RNA Polymerase II to Fibrous Polymers of Low-Complexity Domains: Cell

The low-complexity domain of the FUS RNA binding protein self-assembles via  the mutually exclusive use of two distinct cross-β cores | PNAS
The low-complexity domain of the FUS RNA binding protein self-assembles via the mutually exclusive use of two distinct cross-β cores | PNAS

Assessing the low complexity of protein sequences via the low complexity  triangle | PLOS ONE
Assessing the low complexity of protein sequences via the low complexity triangle | PLOS ONE

Sequence of HasCL10contig2, a repetitive low complexity domain (RLCD)... |  Download Scientific Diagram
Sequence of HasCL10contig2, a repetitive low complexity domain (RLCD)... | Download Scientific Diagram

Imaging dynamic and selective low-complexity domain interactions that  control gene transcription | Science
Imaging dynamic and selective low-complexity domain interactions that control gene transcription | Science

ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in  the TDP-43 Low-Complexity C-Terminal Domain - ScienceDirect
ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain - ScienceDirect

Sequence Determines the Switch in the Fibril Forming Regions in the Low- Complexity FUS Protein and Its Variants | The Journal of Physical Chemistry  Letters
Sequence Determines the Switch in the Fibril Forming Regions in the Low- Complexity FUS Protein and Its Variants | The Journal of Physical Chemistry Letters

Phase separation of low-complexity domains in cellular function and disease  | Experimental & Molecular Medicine
Phase separation of low-complexity domains in cellular function and disease | Experimental & Molecular Medicine

Low complexity and disordered regions of proteins have different structural  and amino acid preferences - Molecular BioSystems (RSC Publishing)  DOI:10.1039/C4MB00425F
Low complexity and disordered regions of proteins have different structural and amino acid preferences - Molecular BioSystems (RSC Publishing) DOI:10.1039/C4MB00425F

Dissecting the role of low-complexity regions in the evolution of  vertebrate proteins | BMC Ecology and Evolution | Full Text
Dissecting the role of low-complexity regions in the evolution of vertebrate proteins | BMC Ecology and Evolution | Full Text

Phosphorylation of the FUS low‐complexity domain disrupts phase separation,  aggregation, and toxicity | The EMBO Journal
Phosphorylation of the FUS low‐complexity domain disrupts phase separation, aggregation, and toxicity | The EMBO Journal

Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly  and Drives Pathological Fibrillization
Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization

Dynamic arrest and aging of biomolecular condensates are modulated by low-complexity  domains, RNA and biochemical activity | Nature Communications
Dynamic arrest and aging of biomolecular condensates are modulated by low-complexity domains, RNA and biochemical activity | Nature Communications

Frontiers | Aberrant Phase Transitions: Side Effects and Novel Therapeutic  Strategies in Human Disease
Frontiers | Aberrant Phase Transitions: Side Effects and Novel Therapeutic Strategies in Human Disease

CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion  to pathogenic amyloid | Nature Communications
CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid | Nature Communications

Phase separation of low-complexity domains in cellular function and disease  | Experimental & Molecular Medicine
Phase separation of low-complexity domains in cellular function and disease | Experimental & Molecular Medicine

Shasha Chong on Twitter: "(3/4) We also provide proof-of-concept  demonstration that single-molecule measurements of protein diffusion rates  can serve as an effective means for detecting phase separation in vivo. We  detected a
Shasha Chong on Twitter: "(3/4) We also provide proof-of-concept demonstration that single-molecule measurements of protein diffusion rates can serve as an effective means for detecting phase separation in vivo. We detected a

Interplay of folded domains and the disordered low-complexity domain in  mediating hnRNPA1 phase separation | bioRxiv
Interplay of folded domains and the disordered low-complexity domain in mediating hnRNPA1 phase separation | bioRxiv