Tale of amyloid filaments in neurodegenerative diseases скачать в хорошем качестве

Tale of amyloid filaments in neurodegenerative diseases

Presented By: Abhay Kotecha, PhD, Sofia Lövestam, and Yang Shi Speaker Biography: Abhay received his PhD in Structural Biology at the University of Oxford, UK. He spent further time at Oxford as a post-doc continuing to a position as Senior Research Scientist. Abhay has been with Thermo Fisher Scientific for over two years and in expert in single particle analysis, MicroED and cryo-electron tomography. I was born in Sweden, raised in Belgium and continued to do a BSc and Mres in Biochemistry at Imperial College of London. During my BSc and Mres, I started studying amyloids in the Lab of Alfonso De Simone using cryo-EM and Nuclear Magnetic Resonance (NMR). In 2019, I joined Sjors Scheres and Michel Goederts lab to reconstitute ex vivo amyloid structures in vitro and to understand their molecular diversity. Yang Shi got his PHD degree from the Institute of Biophysics of the Chinese Academy of Sciences. During his PHD, he determined cryo-EM structures of light harvesting and reaction center core complex and alternative complex III from Roseiflexus castenholzii, and developed an approach to ultra-structurally map subcellular localization of proteins in 3D. In 2018, he joined Michel Goedert's group as a postdoctoral researcher and was also supervised by Sjors Scheres. In the LMB, He focused on cryo-EM structure determination of amyloid filaments from human brain, and have solved many structures of tau, alpha-synuclein and other filaments at high-resolution (the record is 1.9 Å), and also identified the binding sites of a PET ligand on tau filament from Alzheimer's disease. Webinar: Tale of amyloid filaments in neurodegenerative diseases Webinar Abstract: Abnormal accumulation of misfolded tau protein in filaments characterizes more than 20 neurodegenerative diseases—collectively called tauopathies. Most of these diseases can be attributed to mutations in tau gene. Cryo-electron microscopy (cryo-EM) has been used to solve the structures of tau filaments extracted from diseased brain tissue of neuropathologically confirmed cases of Alzheimer's disease, primary age-related tauopathy (PART), chronic traumatic encephalopathy (CTE), Pick's disease, and corticobasal degeneration (CBD). This study led to over 40 high resolution structures of tau filaments found in all these different tauopathies. On top of the previously studied diseases, we have also determined the structures of tau filaments from a further eight tauopathies including progressive supranuclear palsy (PSP) and argyrophilic grain disease (AGD). These cryo-EM findings suggest a hierarchical classification of tauopathies on the basis of their filament folds, which complements clinical diagnosis and neuropathology and also allows the identification of new tauopathies. Different diseases are distinguished by different tau folds. To understand the relevance of these folds we require better model systems which can recapitulate this in vitro. This study led to the high-resolution structure determination 76 structures of recombinant tau filaments assembled in vitro, providing a new database for the greater amyloid field. Understanding their molecular mechanism holds important implications for future diagnostic and treatment approaches. Earn PACE Credits: 1. Make sure you're a registered member of LabRoots (Link to Microsite) 2. Watch the webinar on the LabRoots Website (Link to Microsite) 3. Click Here to get your PACE credits (Expiration date – 2 years webinar date): (PACE Link) This link will be located in the CMS in the webinar CE tab – please enable third party PACE link LabRoots on Social: Facebook:   / labrootsinc   Twitter:   / labroots   LinkedIn:   / labroots   Instagram:   / labrootsinc   Pinterest:   / labroots   SnapChat: labroots_inc