Elizabeth Rhoades

Investigation of Disease-Relevant Lysine Acetylation Sites in α-Synuclein Enabled by Non-canonical Amino Acid Mutagenesis

Marie Shimogawa, Ming-Hao Li, Grace Park, Jennifer Ramirez et autres

Aggregates of α-synuclein (αS) are hallmarks of synucleinopathies, including Parkinson’s Disease (PD) and Multiple System Atrophy (MSA). We have recently shown that αS lysine acetylation in the soluble monomer pool varies between healthy controls, PD, and MSA patients. We used non-canonical amino …

us (code pays fourni par la source)

N-Terminal Amine Chemistry Influences α-Synuclein Interactions with Lipid Bilayers

Emily Brackhahn, Ming-Hao Li, Paola Miranda-Castrodad, Hudson Lee et autres

High Resolution Image Download MS PowerPoint Slide α-Synuclein (αSyn) is an intrinsically disordered protein whose reversible membrane binding via amphipathic α-helix formation is central to its function and may also contribute to the pathology of Parkinson’s disease. In mammals, αSyn is constitutively …

us (code pays fourni par la source)

Genetic Code Expansion, Enzymatic Modification, and C-Terminal Labeling Enable Facile Production of Highly Modified α-Synuclein

Bernard Abakah, Marie Shimogawa, Paola Miranda-Castrodad, Elizabeth Rhoades et autres

α-Synuclein (αS), a protein that plays a central role in Parkinson's disease and related synucleinopathies, is an intrinsically disordered protein (IDP) whose functional interactions and aggregation behavior can be strongly influenced by post-translational modifications (PTMs). Phosphorylation, acetylation, and other PTMs regulate αS's …

us (code pays fourni par la source)

BPS2026 – Comparing phosphomimics and authentic phosphorylation on Tau function

Taylor Tomlinson, Marie Shimogawa, E. James Petersson, Elizabeth Rhoades et autres

us (code pays fourni par la source)

BPS2026 – Investigating the effects of authentic acetylation on Tau using genetic code expansion

Ibrahim G. Saleh, Jennifer Ramirez, E. James Petersson, Elizabeth Rhoades

BPS2026 – Elucidating the effects of site-specific phosphorylation on native α-synuclein structure and function

Paola M. Miranda Castrodad, Emily A.E. Brackhahn, Elizabeth Rhoades

us (code pays fourni par la source)

BPS2026 – Investigating the effect of Tau PTM mimics on microtubule interactions

Polina Holubovska, Elizabeth Rhoades

us (code pays fourni par la source)

Abstract B007: Low-order assemblies drive RTK fusion signaling without condensation

David Gonzalez-Martinez, Thomas R. Mumford, Delaney Wilde, Sofia Wissert et autres

Abstract Receptor tyrosine kinase (RTK) fusions are a diverse class of oncoproteins that have been identified in ∼5% of cancers. RTK fusions are chimeric proteins where the intracellular domain of an RTK is fused to an oligomeric domain from an unrelated protein. …

us (code pays fourni par la source)

Contrasting physiological and pathological tau phosphorylation

Nima Naseri, Taylor L Tomlinson, Marie Shimogawa, E. James Petersson et autres

BACKGROUND: Although phosphorylation to the microtubule-associated protein tau is strongly correlated with its aggregation and neurodegeneration in Alzheimer's disease, tau is also abundantly phosphorylated during normal, physiological development. Yet, tau phosphorylation is not associated with toxicity in developing brains. This divergence in …

us (code pays fourni par la source)

Author response: Investigation of All Disease-Relevant Lysine Acetylation Sites in α-Synuclein Enabled by Non-canonical Amino Acid Mutagenesis

Marie Shimogawa, Minghao Li, Grace Park, Jennifer Ramirez et autres

Aggregates of α-synuclein (αS) are hallmarks of synucleinopathies, including Parkinson’s Disease (PD) and Multiple System Atrophy (MSA). We have recently shown that αS lysine acetylation in the soluble monomer pool varies between healthy controls, PD, and MSA patients. To study the effects …

Investigation of All Disease-Relevant Lysine Acetylation Sites in α-Synuclein Enabled by Non-canonical Amino Acid Mutagenesis

Marie Shimogawa, Minghao Li, Grace Park, Jennifer Ramirez et autres

Aggregates of α-synuclein (αS) are hallmarks of synucleinopathies, including Parkinson’s Disease (PD) and Multiple System Atrophy (MSA). We have recently shown that αS lysine acetylation in the soluble monomer pool varies between healthy controls, PD, and MSA patients. To study the effects …

us (code pays fourni par la source)

Investigation of Disease-Relevant Lysine Acetylation Sites in α-Synuclein Enabled by Non-canonical Amino Acid Mutagenesis

Marie Shimogawa, Minghao Li, Grace Park, Jennifer Ramirez et autres

Aggregates of α-synuclein (αS) are hallmarks of synucleinopathies, including Parkinson’s Disease (PD) and Multiple System Atrophy (MSA). We have recently shown that αS lysine acetylation in the soluble monomer pool varies between healthy controls, PD, and MSA patients. We used non-canonical amino …

us (code pays fourni par la source)