Ryan Limbocker

Assistant Professor

United States Military Academy

United States

Research Interests

Explore related searches

Professors in United States

Contact this professor

Get a free first email built on one of their papers, ready for you to edit and send yourself.

About

Ryan Limbocker is an Assistant Professor at the United States Military Academy. His research focuses on protein misfolding diseases, particularly the mechanisms of oligomer formation and the neurotoxic effects of amyloid-β aggregates. Recent articles have explored therapeutic strategies for Alzheimer's disease, the interaction of peptides with cell membranes, and the effects of various metabolites on protein aggregation.

Articles (18)

Year:

2025

Year:

2025

Year:

2024

Year:

2024

Year:

2024

Year:

2023

Year:

2023

Year:

2023

Year:

2023

Year:

2022

Year:

2022

Year:

2022

Year:

2021

Year:

2021

Year:

2021

Year:

2021

Year:

2020

Year:

2020

Collaborators (16)

Melissa Eslinger

Associate Professor

United States Military Academy

UNITED STATES

Ryan Limbocker

Research Interests

Explore related searches

Contact this professor

About

Articles (18)

An aminosterol breaks the autocatalytic cycle of Aβ42 aggregation and protects cell membranes from its soluble aggregates

Polyphenol–Mediated Peptide Assembly Modulates Melittin Toxicity: A Structure–Activity Strategy for Neutralizing the Interface Affinity of Pore–Forming Toxins to Cell Membranes

A Relationship between the Structures and Neurotoxic Effects of Aβ Oligomers Stabilized by Different Metal Ions

Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases

Editorial: Promising therapeutic strategies for Alzheimer's disease: a focus on amyloid-β targeting

Characterization of Pairs of Toxic and Nontoxic Misfolded Protein Oligomers Elucidates the Structural Determinants of Oligomer Toxicity in Protein Misfolding Diseases

Combinations of Vitamin A and Vitamin E Metabolites Confer Resilience against Amyloid-β Aggregation

Quantitative Attribution of the Protective Effects of Aminosterols against Protein Aggregates to Their Chemical Structures and Ability to Modulate Biological Membranes

EGCG inactivates a pore-forming toxin by promoting its oligomerization and decreasing its solvent-exposed hydrophobicity

Utilization of Standardized College Entrance Metrics to Predict Undergraduate Student Success in Chemistry

Squalamine and trodusquemine: two natural products for neurodegenerative diseases, from physical chemistry to the clinic

A Brain-Permeable Aminosterol Regulates Cell Membranes to Mitigate the Toxicity of Diverse Pore-Forming Agents

Comparative Studies in the A30P and A53T α-Synuclein C. elegans Strains to Investigate the Molecular Origins of Parkinson's Disease.

Erratum: Publisher Correction: Two human metabolites rescue a C. elegans model of Alzheimer's disease via a cytosolic unfolded protein response (Communications biology (2021) 4 1 (843))

Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress the Toxicity of Their Oligomers

Two human metabolites rescue a C. elegans model of Alzheimer’s disease via a cytosolic unfolded protein response

Non-Pharmaceutical Interventions and Military Hygiene at the United States Military Academy between 1890 and 1910.

Therapeutic Strategies to Reduce the Toxicity of Misfolded Protein Oligomers

Collaborators (16)

Melissa Eslinger

Peter M. Tessier

Clemens Kaminski

Simuck Yuk

Michele Vendruscolo

Ellen AA Nollen

Francesco Simone Ruggeri

Cristina Cecchi

Pietro Sormanni

Lam Nguyen

Martino Calamai

Fabrizio Chiti

Nunilo Cremades

Justin Toole

Alessandra Bigi

Sara Linse

Make your next move.