Dr. Edward H Koo M.D.
Neurologist | Neurology
9500 Gilman Dr Mail Code 0691 La Jolla CA, 92093About
Dr. Edward Koo is a distinguished Neurologist in La Jolla, CA. Dr. Koo specializes in diagnosing, treating, and managing disorders of the brain and nervous system. With expertise in handling complex conditions like epilepsy, multiple sclerosis, and migraines, Dr. Koo employs advanced techniques and personalized treatment plans to improve patient outcomes. As a neurologist, Dr. Koo is committed to staying abreast of the latest developments in neurological research and therapies.
Education and Training
Duke University School of Medicine 1980
Board Certification
Psychiatry and NeurologyAmerican Board of Psychiatry and NeurologyABPN
Provider Details
Expert Publications
Data provided by the National Library of Medicine- Presenilin 1 facilitates the constitutive turnover of beta-catenin: differential activity of Alzheimer's disease-linked PS1 mutants in the beta-catenin-signaling pathway.
- Recombinant adenovirus is an appropriate vector for endocytotic protein trafficking studies in cultured neurons.
- Mutagenesis identifies new signals for beta-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Abeta42.
- Amyloid diseases: abnormal protein aggregation in neurodegeneration.
- Expression of beta-amyloid precursor protein-CD3gamma chimeras to demonstrate the selective generation of amyloid beta(1-40) and amyloid beta(1-42) peptides within secretory and endocytic compartments.
- A second cytotoxic proteolytic peptide derived from amyloid beta-protein precursor.
- The nonconserved hydrophilic loop domain of presenilin (PS) is not required for PS endoproteolysis or enhanced abeta 42 production mediated by familial early onset Alzheimer's disease-linked PS variants.
- LDL receptor-related protein (LRP) in Alzheimer's disease: towards a unified theory of pathogenesis.
- Modulation of amyloid beta-protein clearance and Alzheimer's disease susceptibility by the LDL receptor-related protein pathway.
- Presenilin 1 negatively regulates beta-catenin/T cell factor/lymphoid enhancer factor-1 signaling independently of beta-amyloid precursor protein and notch processing.
- The amyloidogenic pathway of amyloid precursor protein (APP) is independent of its cleavage by caspases.
- Loss of presenilin 1 is associated with enhanced beta-catenin signaling and skin tumorigenesis.
- A subset of NSAIDs lower amyloidogenic Abeta42 independently of cyclooxygenase activity.
- The aspartate-257 of presenilin 1 is indispensable for mouse development and production of beta-amyloid peptides through beta-catenin-independent mechanisms.
- Caspase cleavage of members of the amyloid precursor family of proteins.
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