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Sami Barmada on Muck Rack

Sami Barmada

As seen in: Nature, Frontiers, MDPI, EurekAlert!, Science Magazine, Cell Press, Dialnet - Universidad de La Rioja, JoVE- Journal of Visualized Experiments, The Journal of Clinical Investigation
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Articles

PINN-based resolution of inverse non-linear magnetostatic problems

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By Sami Barmada, Alessandro Formisano, Shayan Dodge
| Dialnet - Universidad de La Rioja
Purpose This paper aims to propose a Physics Informed Neural Network (PINN) based method for the solution of inverse problems in magnetics, when the nonlinear characteristics of magnetic materials are included. Design/methodology/approach The proposed method is designed to estimate the current sources from a set of magnetic field measurement, in presence of nonlinear magnetic materials.
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Isoform-specific steric zippers drive aberrant assembly and mislocalization of shortened TDP-43

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By Ashley Murphy, Federico Masiero, Katie E. Copley, Megan Dykstra, Morgan Miller, Miriam Linsenmeier, Longsheng Lai, Yuanhang Wang, Yi-Wei Chang, Sami Barmada, James Shorter
| Science Magazine Verified
Abstract INTRODUCTION RESULTS DISCUSSION MATERIALS AND METHODS Acknowledgments Supplementary Materials REFERENCES Information & Authors Metrics & Citations View Options References Figures Tables Media Share Abstract Prion-like domain (PrLD)–mediated aggregation and concomitant dysfunction of the essential RNA-binding protein transactive response (TAR) DNA-binding protein of 43 kilodaltons (TDP-43) is a common feature of multiple debilitating neurodegenerative disorders, including amyotrophic...
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Splicing the narrative: alternative TARDBP splicing and its relation to neurodegeneration in ALS and FTD

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By Morgan Miller, Megan Dykstra, Sami Barmada
| The Journal of Clinical Investigation
Abstract Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) are progressive neurodegenerative diseases characterized by the nuclear clearance and cytoplasmic aggregation of transactive response DNA/RNA-binding protein of 43 kDa (TDP43). Alternative splicing of TARDBP, the gene encoding TDP43, leads to a surprising diversity of RNA and protein isoforms with unique functions and potential implications for disease pathogenesis.
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