A5027882588- Parkinson's Disease Mechanisms and Treatments
- Cellular transport and secretion
- CRISPR and Genetic Engineering
- Autophagy in Disease and Therapy
- Genetic Neurodegenerative Diseases
- RNA Research and Splicing
- Alzheimer's disease research and treatments
- Blood properties and coagulation
- 14-3-3 protein interactions
- RNA regulation and disease
- Neurobiology and Insect Physiology Research
- Machine Learning in Bioinformatics
- Genetics, Bioinformatics, and Biomedical Research
- Periodontal Regeneration and Treatments
- Aquaculture disease management and microbiota
- Microbial Metabolic Engineering and Bioproduction
- Bacterial biofilms and quorum sensing
- Neuroinflammation and Neurodegeneration Mechanisms
- Prion Diseases and Protein Misfolding
- Metabolomics and Mass Spectrometry Studies
- Vibrio bacteria research studies
- Nuclear Receptors and Signaling
- Heat shock proteins research
- S100 Proteins and Annexins
- PI3K/AKT/mTOR signaling in cancer
Johns Hopkins University
2020-2024
Johns Hopkins Medicine
2020-2024
Orthopaedic Research Foundation
2022-2024
Stowers Institute for Medical Research
2012-2016
University of Kansas Medical Center
2012-2015
Mutations in PINK1 and parkin cause autosomal recessive Parkinson's disease (PD). Evidence placing common pathways regulating multiple aspects of mitochondrial quality control is burgeoning. However, compelling evidence to causatively link specific PINK1/parkin dependent dopamine neuron degeneration PD lacking. Although are known regulate mitophagy, emerging data suggest that defects mitophagy unlikely be pathological relevance. Mitochondrial functions also tied their proteasomal regulation...
Pathologic α-synuclein plays an important role in the pathogenesis of α-synucleinopathies such as Parkinson’s disease (PD). Disruption proteostasis is thought to be central pathologic toxicity; however, molecular mechanism this deregulation poorly understood. Complementary proteomic approaches cellular and animal models PD were used identify characterize interactome. We report that highest biological processes interacted with mice included RNA processing translation initiation. Regulation...
In recent years, research into Parkinson's disease and similar neurodegenerative disorders has increasingly suggested that these conditions are synonymous with failures in proteostasis. However, the spotlight of this remained firmly focused on tail end proteostasis, primarily aggregation, misfolding, degradation, protein translation being comparatively overlooked. Now, there is an increasing body evidence supporting a potential role for pathogenesis PD, its dysregulation already established...
Ischemic strokes result in the death of brain tissue and a wave downstream effects, often leading to lifelong disabilities or death. However, underlying mechanisms ischemic damage repair systems remain largely unknown. In order better understand these mechanisms, TMT-isobaric mass tagging spectrometry were conducted on cortex extracts from mice subjected one hour middle cerebral artery occlusion (MCAO) after reperfusion. total, 2,690 proteins identified quantified, out which 65% top 5% up-...
The mechanistic target of rapamycin (mTOR) signals through the mTOR complex 1 (mTORC1) and 2 to maintain cellular organismal homeostasis. Failure finely tune activity results in metabolic dysregulation disease. While there is substantial understanding molecular events leading mTORC1 activation at lysosome, remarkably little known about what terminates signaling. Here, we show that AAA + ATPase Thorase directly binds mTOR, thereby orchestrating disassembly inactivation mTORC1. disrupts...
Pathologic α-syn destabilizes the TSC 1 and 2 complex leading to mTORC1 activation, enhanced protein translation neurodegeneration in PD. Abstract: Pathological α-synuclein (α-syn) plays an important role pathogenesis of α-synucleinopathies such as Parkinson’s disease (PD). Disruption homeostasis is thought be central PD pathogenesis, however molecular mechanism this deregulation poorly understood. Here we report that pathologic binds tuberous sclerosis (TSC) TSC1-TSC2 activation mechanistic...