Samuel Strader

ORCID: 0000-0003-4417-3707
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About
Contact & Profiles
Research Areas
  • Parkinson's Disease Mechanisms and Treatments
  • Alzheimer's disease research and treatments
  • Neuroinflammation and Neurodegeneration Mechanisms
  • Lysosomal Storage Disorders Research
  • Axon Guidance and Neuronal Signaling
  • Retinal Development and Disorders
  • Cellular transport and secretion
  • Genetic Neurodegenerative Diseases
  • Microplastics and Plastic Pollution
  • Neurological disorders and treatments
  • Barrier Structure and Function Studies
  • RNA regulation and disease
  • Zebrafish Biomedical Research Applications

Duke University
2019-2024

Duke University Hospital
2021

Duke Medical Center
2021

Recent studies have identified increasing levels of nanoplastic pollution in the environment. Here, we find that anionic contaminants potently precipitate formation and propagation α-synuclein protein fibrils through a high-affinity interaction with amphipathic non-amyloid component (NAC) domains α-synuclein. Nanoplastics can internalize neurons clathrin-dependent endocytosis, causing mild lysosomal impairment slows degradation aggregated In mice, nanoplastics combine to exacerbate spread...

10.1126/sciadv.adi8716 article EN cc-by-nc Science Advances 2023-11-17

The intricate process of α-synuclein aggregation and fibrillization holds pivotal roles in Parkinson's disease (PD) multiple system atrophy (MSA). While mouse can fibrillize vitro, whether these fibrils commonly used research to induce this or form reproduce structures the human brain remains unknown. Here, we report first atomic structure fibrils, which was solved parallel by two independent teams. shows striking similarity MSA-amplified PD-associated E46K fibrils. However, display altered...

10.1126/sciadv.adq3539 article EN cc-by-nc Science Advances 2024-11-01

Abstract Background LRRK2-targeting therapeutics that inhibit LRRK2 kinase activity have advanced to clinical trials in idiopathic Parkinson’s disease (iPD). phosphorylates Rab10 on endolysosomes phagocytic cells promote some types of immunological responses. The identification factors regulate LRRK2-mediated phosphorylation iPD, and whether phosphorylated-Rab10 levels change different states, or with progression, may provide insights into the role iPD help guide therapeutic strategies...

10.1101/2024.04.15.589570 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2024-04-17

Abstract Background LRRK2-targeting therapeutics that inhibit LRRK2 kinase activity have advanced to clinical trials in idiopathic Parkinson’s disease (iPD). phosphorylates Rab10 on endolysosomes phagocytic cells promote some types of immunological responses. The identification factors regulate LRRK2-mediated phosphorylation iPD, and whether phosphorylated-Rab10 levels change different states, or with progression, may provide insights into the role iPD help guide therapeutic strategies...

10.1186/s13024-024-00738-4 article EN cc-by Molecular Neurodegeneration 2024-06-11

Short Abstract The intricate process of α-synuclein aggregation and fibrillization hold pivotal roles in Parkinson’s disease (PD) multiple system atrophy (MSA). While mouse can fibrillize vitro , whether these fibrils commonly used research to induce this or form reproduce structures the human brain remains unknown. Here we report first atomic structure fibrils, which was solved parallel by two independent teams. shows striking similarity MSA-amplified PD-associated E46K fibrils. However,...

10.1101/2024.05.09.593334 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2024-05-09

Abstract Recent studies have identified increasing levels of nanoplastic pollution in the environment. Here we find that anionic contaminants potently precipitate formation and propagation α-synuclein protein fibrils through a high-affinity interaction with amphipathic non-amyloid component (NAC) domains α-synuclein. Nanoplastics can internalize neurons clathrin-dependent endocytosis, causing mild lysosomal impairment slows degradation aggregated In mice, nanoplastics combine to exacerbate...

10.21203/rs.3.rs-3439102/v1 preprint EN cc-by Research Square (Research Square) 2023-10-13

SUMMARY Glial cells regulate synaptic connectivity during development, but whether they selectively instruct the formation of specific circuits is not known. Here we show that major perisynaptic glia retina, Muller (MG), control proper establishment direction-selective (DS) circuit by a synaptogenic protein, Thrombospondin 1 (TSP1). We found TSP1 promotes excitatory synapse specifically in o n- ff D irection- S elective retinal G anglion C ells (ooDSGCs). Lack leads to reduced within inner...

10.1101/866590 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2019-12-09

Glial cells regulate synaptic connectivity during development, but whether they selectively instruct the formation of specific circuits is not known. Here we show that major perisynaptic glia retina, Muller (MG), control proper establishment direction-selective (DS) circuit by a synaptogenic protein, Thrombospondin 1 (TSP1). We found TSP1 promotes excitatory synapse specifically in on-off Direction-Selective retinal Ganglion Cells (ooDSGCs). Lack leads to reduced within inner plexiform...

10.2139/ssrn.3497027 article EN SSRN Electronic Journal 2019-01-01
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