Eduardo Ramirez

ORCID: 0000-0002-3079-3844
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About
Contact & Profiles
Research Areas
  • Alzheimer's disease research and treatments
  • Parkinson's Disease Mechanisms and Treatments
  • Genetic Neurodegenerative Diseases
  • Synthesis and Characterization of Heterocyclic Compounds
  • Plant Stress Responses and Tolerance
  • Neurological diseases and metabolism
  • Neuroscience and Neuropharmacology Research
  • Biotin and Related Studies
  • Plant Parasitism and Resistance
  • Drug Transport and Resistance Mechanisms
  • RNA Interference and Gene Delivery
  • Cholinesterase and Neurodegenerative Diseases
  • Dendrimers and Hyperbranched Polymers
  • Amyloidosis: Diagnosis, Treatment, Outcomes
  • Plant-Microbe Interactions and Immunity

Purdue University West Lafayette
2022-2024

University of California, San Diego
2019

Protein misfolding results in a plethora of known diseases such as Alzheimer’s disease, Parkinson’s Huntington’s transthyretin-related amyloidosis, type 2 diabetes, Lewy body dementia, and spongiform encephalopathy. To provide diverse portfolio therapeutic small molecules with the ability to reduce protein misfolding, we evaluated set 13 compounds: 4-(benzo[d]thiazol-2-yl)aniline (BTA) its derivatives containing urea (1), thiourea (2), sulfonamide (3), triazole (4), triazine (5) linker. In...

10.1021/acsomega.3c02668 article EN cc-by ACS Omega 2023-05-23

Insight into how plants simultaneously cope with multiple stresses, for example, when challenged biotic stress from pathogen infection and abiotic drought, is important both understanding evolutionary trade-offs optimizing crop responses to these stresses. Mechanisms by which initial plant immune signaling antagonizes abscisic acid (ABA) signal transduction require further investigation. Using a chemical genetics approach, the small molecule...

10.1111/tpj.14232 article EN The Plant Journal 2019-01-19

AA amyloidosis is the result of overproduction and aberrant processing acute-phase serum amyloid A1 (SAA1) by hepatocytes. Proteolytic cleavage SAA1 believed to play a central role in formation. The protein undergoes 18 residues consisting signal peptide at N-terminal region. To better understand mechanism behind systemic protein, we studied misfolding propensity We first examined amino acid SAA derived from different animal species. A library 16 peptides was designed evaluate aggregation....

10.1016/j.bbrep.2022.101284 article EN cc-by Biochemistry and Biophysics Reports 2022-05-30

Alzheimer's disease (AD) is a multifactorial, chronic neurodegenerative characterized by the presence of extracellular β-amyloid (Aβ) plaques, intraneuronal neurofibrillary tangles (NFTs), activated microglial cells, and an inflammatory state (involving reactive oxygen species production) in brain. NFTs are comprised misfolded hyperphosphorylated forms microtubule-binding protein tau. Interestingly, trimeric form 2N4R splice isoform tau has been found to be more toxic than 1N4R neuron...

10.1016/j.rechem.2023.100938 article EN cc-by Results in Chemistry 2023-01-01

Alzheimer's disease (AD) is the most prevalent neurodegenerative disorder underlying dementia in geriatric population. AD manifests by two pathological hallmarks: extracellular amyloid-β (Aβ) peptide-containing senile plaques and intraneuronal neurofibrillary tangles comprised of aggregated hyperphosphorylated tau protein (p-tau). However, more than half cases also display presence α-synuclein (α-syn)-containing Lewy bodies. Conversely, bodies disorders have been reported to concomitant Aβ...

10.1021/acschemneuro.3c00464 article EN cc-by-nc-nd ACS Chemical Neuroscience 2023-10-11

Parkinson's disease (PD) is the second most common neurodegenerative disease, affecting elderly population worldwide. In PD, misfolding of α-synuclein (α-syn) results in formation inclusions referred to as Lewy bodies (LB) midbrain neurons substantia nigra and other specific brain localizations, which associated with neurodegeneration. There are no approved strategies reduce LB patients PD. Our drug discovery program focuses on synthesis urea thiourea compounds coupled aminoindole moieties...

10.1021/acsomega.3c07453 article EN cc-by-nc-nd ACS Omega 2023-12-19
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