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Submission Deadline: November 1, 2020

At Thermo Fisher Scientific, we are committed to lifelong learning and a lifelong partnership with the scientific community. One way we express this committment is by supporting early stage career researchers as they embark on their journeys to become the next generation of leaders in academic research using electron microscopy technology.  

As part of our career achievement and community outreach program at Thermo Fisher Scientific, we are proud to once again open submissions for our Young Investigator Award. This award will be presented in recognition of a young researcher who has recently published work in a scientific journal and whose research meets the criteria of having: significant biological relevance, a high impact on the research community, transparency in materials and methodology for peers, and exemplifies innovation in utilizing  pre-established or new process/methodology in his or her life science research work to become the next generation of leaders in academic reaserch using electron microscopy for life science research.

 

 

Winners will be announced January 15, 2021.

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2017-2018 Young Investigator Life Sciences Award Winner
Congratulations to Anythony W.P. Fitzpatrick of Columbia University

Thank you to everyone who submitted to the Young Investigator Life Sciences Award competition. We were very impressed by the breadth and diversity of innovative paper topics. We would like to congratulate our 2017–18 winner, Anthony W. P. Fitzpatrick of Columbia University, for the paper: Cryo-EM structures of tau filaments from Alzheimer’s disease. Anthony will receive his cash prize and will be featured in a sponsored talk on his subject at the Biophysical Society Show.

 

Dr. Anthony Fitzpatrick is an Assistant Professor of Biochemistry and Molecular Biophysics at the Zuckerman Institute, Columbia University, New York, USA. Previously, Anthony was a Marie Curie International Outgoing Fellow at the Laboratory of Molecular Biology, University of Cambridge (2015–2017) and the California Institute of Technology (2012–2014). He has a biophysics background (PhD with Professor Christopher M. Dobson, University of Cambridge) and undertook postdoctoral training with Professors Helen Saibil in London, Robert G. Griffin at the Massachusetts Institute of Technology, Ahmed H. Zewail (Nobel Laureate) at the California Institute of Technology and Sjors Scheres and Michel Goedert at the Laboratory of Molecular Biology, Cambridge.

The research focus of the Fitzpatrick Lab is to determine the structure and behavior of patient-derived amyloid fibrils and, more generally, to understand the role of protein aggregation in vivo by identifying the cellular changes that occur in response to the formation, clearance and spread of fibrillar inclusions. The methods employed by Anthony’s lab are largely experimental and include cryo-electron microscopy (cryo-EM), mass spectrometry, transcriptomics, microfluidics, magic angle spinning NMR and optical super-resolution microscopy.

Alzheimer’s disease is the most common neurodegenerative disease, and there are no mechanism-based therapies. The disease is defined by the presence of abundant neurofibrillary lesions and neuritic plaques in the cerebral cortex. Neurofibrillary lesions comprise paired helical and straight tau filaments, whereas tau filaments with different morphologies characterize other neurodegenerative diseases. No high-resolution structures of tau filaments are available. Here we present cryo-electron microscopy (cryo-EM) maps at 3.4–3.5 Å resolution and corresponding atomic models of paired helical and straight filaments from the brain of an individual with Alzheimer’s disease. Filament cores are made of two identical protofilaments comprising residues 306–378 of tau protein, which adopt a combined cross-β/β-helix structure and define the seed for tau aggregation. Paired helical and straight filaments differ in their inter-protofilament packing, showing that they are ultrastructural polymorphs. These findings demonstrate that cryo-EM allows atomic characterization of amyloid filaments from patient-derived material, and pave the way for investigation of a range of neurodegenerative diseases. 

Honorable Acknowledgements

Dr. Anthony Fitzpatrick is an Assistant Professor of Biochemistry and Molecular Biophysics at the Zuckerman Institute, Columbia University, New York, USA. Previously, Anthony was a Marie Curie International Outgoing Fellow at the Laboratory of Molecular Biology, University of Cambridge (2015–2017) and the California Institute of Technology (2012–2014). He has a biophysics background (PhD with Professor Christopher M. Dobson, University of Cambridge) and undertook postdoctoral training with Professors Helen Saibil in London, Robert G. Griffin at the Massachusetts Institute of Technology, Ahmed H. Zewail (Nobel Laureate) at the California Institute of Technology and Sjors Scheres and Michel Goedert at the Laboratory of Molecular Biology, Cambridge.

The research focus of the Fitzpatrick Lab is to determine the structure and behavior of patient-derived amyloid fibrils and, more generally, to understand the role of protein aggregation in vivo by identifying the cellular changes that occur in response to the formation, clearance and spread of fibrillar inclusions. The methods employed by Anthony’s lab are largely experimental and include cryo-electron microscopy (cryo-EM), mass spectrometry, transcriptomics, microfluidics, magic angle spinning NMR and optical super-resolution microscopy.

Alzheimer’s disease is the most common neurodegenerative disease, and there are no mechanism-based therapies. The disease is defined by the presence of abundant neurofibrillary lesions and neuritic plaques in the cerebral cortex. Neurofibrillary lesions comprise paired helical and straight tau filaments, whereas tau filaments with different morphologies characterize other neurodegenerative diseases. No high-resolution structures of tau filaments are available. Here we present cryo-electron microscopy (cryo-EM) maps at 3.4–3.5 Å resolution and corresponding atomic models of paired helical and straight filaments from the brain of an individual with Alzheimer’s disease. Filament cores are made of two identical protofilaments comprising residues 306–378 of tau protein, which adopt a combined cross-β/β-helix structure and define the seed for tau aggregation. Paired helical and straight filaments differ in their inter-protofilament packing, showing that they are ultrastructural polymorphs. These findings demonstrate that cryo-EM allows atomic characterization of amyloid filaments from patient-derived material, and pave the way for investigation of a range of neurodegenerative diseases. 

Honorable Acknowledgements

How to apply

Submit your work on our Electron Microscopy community page, created in collaboration with AZoM. Even if you do not receive the award, your work could be promoted in the Electron Microscopy community and distributed through the AZoM Electron Microscopy newsletter which is sent to over 17,000 researchers, engineers and scientists in the industry.

Submit your entry