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Biomolecular condensates – extant relics or evolving microcompartments?

Communications biology, 2023-06, Vol.6 (1), p.656-656, Article 656

Rangachari, Vijayaraghavan

2023

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Are granulins copper sequestering proteins?

Proteins, structure, function, and bioinformatics, 2021-04, Vol.89 (4), p.450-461

2021

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

Soft matter, 2023-07, Vol.19 (27), p.5150-5159

2023

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Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity

Proceedings of the National Academy of Sciences - PNAS, 2009-05, Vol.106 (18), p.7607-7612

2009

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Accumulation of Pathological Tau Species and Memory Loss in a Conditional Model of Tauopathy

The Journal of neuroscience, 2007-04, Vol.27 (14), p.3650-3662

2007

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Dopamine‐induced α‐synuclein oligomers show self‐ and cross‐propagation properties

Protein science, 2014-10, Vol.23 (10), p.1369-1379

2014

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

Communications biology, 2023-12, Vol.6 (1), p.1227-1227, Article 1227

2023

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Fatty Acid Concentration and Phase Transitions Modulate Aβ Aggregation Pathways

Scientific reports, 2017-09, Vol.7 (1), p.10370-16, Article 10370

2017

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

Communications biology, 2024-01, Vol.7 (1), p.74-74, Article 74

2024

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Large fatty acid-derived Aβ42 oligomers form ring-like assemblies

The Journal of chemical physics, 2019-02, Vol.150 (7), p.075101-075101

2019

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Non-esterified fatty acids generate distinct low-molecular weight amyloid-β (Aβ42) oligomers along pathway different from fibril formation

PloS one, 2011-04, Vol.6 (4), p.e18759

2011

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Aqueous RAFT Synthesis of Low Molecular Weight Anionic Polymers for Determination of Structure/Binding Interactions with Gliadin

Macromolecular bioscience, 2020-08, Vol.20 (8), p.e2000125-n/a

2020

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Self-propagative replication of Aβ oligomers suggests potential transmissibility in Alzheimer disease

PloS one, 2014-11, Vol.9 (11), p.e111492

2014

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

Royal Society open science, 2020-04, Vol.7 (4), p.191814-191814

2020

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A modified Stokes-Einstein equation for Aβ aggregation

BMC bioinformatics, 2011-10, Vol.12 Suppl 10 (S10), p.S13-S13, Article S13

2011

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Dynamics of protofibril elongation and association involved in Aβ42 peptide aggregation in Alzheimer's disease

BMC bioinformatics, 2010-10, Vol.11 Suppl 6 (S6), p.S24-S24, Article S24

2010

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Ganglioside-Enriched Phospholipid Vesicles Induce Cooperative Aβ Oligomerization and Membrane Disruption

Biochemistry (Easton), 2022-10, Vol.61 (20), p.2206-2220

2022

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Granulins modulate liquid–liquid phase separation and aggregation of the prion-like C-terminal domain of the neurodegeneration-associated protein TDP-43

The Journal of biological chemistry, 2020-02, Vol.295 (8), p.2506-2519

2020

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Cause and consequence of Aβ – Lipid interactions in Alzheimer disease pathogenesis

Biochimica et biophysica acta. Biomembranes, 2018-09, Vol.1860 (9), p.1652-1662

2018

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Prion-like C-Terminal Domain of TDP-43 and α-Synuclein Interact Synergistically to Generate Neurotoxic Hybrid Fibrils

Journal of molecular biology, 2021-05, Vol.433 (10), p.166953-166953, Article 166953

2021

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Cloning, expression and purification of the low-complexity region of RanBP9 protein

Protein expression and purification, 2020-08, Vol.172, p.105630-105630, Article 105630

2020

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Disorder and cysteines in proteins: A design for orchestration of conformational see-saw and modulatory functions

Progress in molecular biology and translational science, 2020, Vol.174, p.331-373

2020

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Distinct neurotoxic TDP-43 fibril polymorphs are generated by heterotypic interactions with α-Synuclein

The Journal of biological chemistry, 2022-11, Vol.298 (11), p.102498, Article 102498

2022

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Charge and redox states modulate granulin—TDP-43 coacervation toward phase separation or aggregation

Biophysical journal, 2022-06, Vol.121 (11), p.2107-2126

2022

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

Soft matter, 2023-07, Vol.19 (27), p.515-5159

2023

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Biomolecular condensates – extant relics or evolving microcompartments?

Are granulins copper sequestering proteins?

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

Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity

Accumulation of Pathological Tau Species and Memory Loss in a Conditional Model of Tauopathy

Dopamine‐induced α‐synuclein oligomers show self‐ and cross‐propagation properties

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

Fatty Acid Concentration and Phase Transitions Modulate Aβ Aggregation Pathways

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

Large fatty acid-derived Aβ42 oligomers form ring-like assemblies

Non-esterified fatty acids generate distinct low-molecular weight amyloid-β (Aβ42) oligomers along pathway different from fibril formation

Aqueous RAFT Synthesis of Low Molecular Weight Anionic Polymers for Determination of Structure/Binding Interactions with Gliadin

Self-propagative replication of Aβ oligomers suggests potential transmissibility in Alzheimer disease

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

A modified Stokes-Einstein equation for Aβ aggregation

Dynamics of protofibril elongation and association involved in Aβ42 peptide aggregation in Alzheimer's disease

Ganglioside-Enriched Phospholipid Vesicles Induce Cooperative Aβ Oligomerization and Membrane Disruption

Granulins modulate liquid–liquid phase separation and aggregation of the prion-like C-terminal domain of the neurodegeneration-associated protein TDP-43

Cause and consequence of Aβ – Lipid interactions in Alzheimer disease pathogenesis

Prion-like C-Terminal Domain of TDP-43 and α-Synuclein Interact Synergistically to Generate Neurotoxic Hybrid Fibrils

Cloning, expression and purification of the low-complexity region of RanBP9 protein

Disorder and cysteines in proteins: A design for orchestration of conformational see-saw and modulatory functions

Distinct neurotoxic TDP-43 fibril polymorphs are generated by heterotypic interactions with α-Synuclein

Charge and redox states modulate granulin—TDP-43 coacervation toward phase separation or aggregation

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

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