Pages that link to "Q42374822"
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The following pages link to β-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfaces. (Q42374822):
Displaying 15 items.
- A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity (Q30838501) (← links)
- Looking at the recent advances in understanding α-synuclein and its aggregation through the proteoform prism. (Q39297100) (← links)
- The Role of Lipids Interacting with α-Synuclein in the Pathogenesis of Parkinson's Disease (Q39410832) (← links)
- Synucleins and Gene Expression: Ramblers in a Crowd or Cops Regulating Traffic? (Q41000436) (← links)
- A pH-dependent switch promotes β-synuclein fibril formation via glutamate residues (Q42285864) (← links)
- Unveiling a Selective Mechanism for the Inhibition of α-Synuclein Aggregation by β-Synuclein (Q48175893) (← links)
- The small heat shock proteins αB-crystallin (HSPB5) and Hsp27 (HSPB1) inhibit the intracellular aggregation of α-synuclein (Q50308537) (← links)
- Oligomer Diversity during the Aggregation of the Repeat Region of Tau (Q57986225) (← links)
- C-terminal truncation of α-synuclein promotes amyloid fibril amplification at physiological pH (Q57986252) (← links)
- Target Proteins in the Dorsal Hippocampal Formation Sustain the Memory-Enhancing and Neuroprotective Effects of (Q60919526) (← links)
- Living in Promiscuity: The Multiple Partners of Alpha-Synuclein at the Synapse in Physiology and Pathology (Q60922145) (← links)
- Lipids at the Crossroad of α-Synuclein Function and Dysfunction: Biological and Pathological Implications (Q64074236) (← links)
- Multi-Pronged Interactions Underlie Inhibition of α-Synuclein Aggregation by β-Synuclein (Q64869800) (← links)
- An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils (Q83229847) (← links)
- Increased Dynamics of α-Synuclein Fibrils by β-Synuclein Leads to Reduced Seeding and Cytotoxicity (Q91474636) (← links)