Maria K. Janowska

ORCID: 0000-0001-8356-9814
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About
Contact & Profiles
Research Areas
  • Parkinson's Disease Mechanisms and Treatments
  • Neurological disorders and treatments
  • Alzheimer's disease research and treatments
  • Neuroscience and Neuropharmacology Research
  • Electron Spin Resonance Studies
  • Advanced NMR Techniques and Applications
  • Click Chemistry and Applications
  • Biochemical and Molecular Research
  • Advanced Neuroimaging Techniques and Applications
  • Organoboron and organosilicon chemistry
  • Protein Structure and Dynamics
  • Synthetic Organic Chemistry Methods
  • Lysosomal Storage Disorders Research
  • RNA and protein synthesis mechanisms
  • Heat shock proteins research

University of Warsaw
2020

Rutgers, The State University of New Jersey
2013-2017

Abstract Pathology in Parkinson’s disease is linked to self-association of α-Synuclein (αS) into pathogenic oligomeric species and highly ordered amyloid fibrils. Developing effective therapeutic strategies against this debilitating critical βS, a pre-synaptic protein that co-localizes with αS, can act as an inhibitor αS assembly. Despite the potential importance βS nature, location specificity molecular interactions between these two proteins unknown. Here we use NMR paramagnetic relaxation...

10.1038/srep15164 article EN cc-by Scientific Reports 2015-10-19

Aggregation of α-synuclein (αSyn), the primary protein component in Lewy body inclusions patients with Parkinson's disease, arises when normally soluble intrinsically disordered converts to amyloid fibrils. In this work, we provide a mechanistic view role N-terminal acetylation on fibrillation by first establishing quantitative relationship between monomer secondary structural propensity and fibril assembly kinetics, secondly demonstrating acetylated form early onset A53T mutation, that...

10.1371/journal.pone.0075018 article EN cc-by PLoS ONE 2013-09-18

β-synuclein (βS) is a homologue of α-synuclein (αS), the major protein component Lewy bodies in patients with Parkinson's disease. In contrast to αS, βS does not form fibrils, mitigates αS toxicity vivo and inhibits fibril formation vitro. Previously missense mutation βS, P123H, was identified Dementia Body The single P123H at C-terminus able convert from nontoxic toxic that also accelerate inclusions when it presence vivo. To elucidate molecular mechanisms these processes, we compare...

10.1002/pro.2798 article EN Protein Science 2015-09-02
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