Since its establishment in 2005, the New York University Protein Mass Spectrometry Core Facility for neuroscience has provided cutting edge mass spectrometry-based protein analysis to molecular neuroscientists at the New York University School of Medicine. The purpose of this grant is to provide continued funding to enable neuroscientists at NYU to take advantage of sophisticated and involved protein mass spectrometry and proteomics that would otherwise not be available to them, and guarantee them access to the technology. The proposed Protein Mass Spectrometry Core Facility for Neuroscience would enable NINDS- and other NIH- funded neuroscientists at New York University to identify from one to thousands of proteins of interest, to characterize posttranslational modifications of these proteins such as phosphorylation, glycosylation, proteolysis and modification by lipids, to perform functional proteomics studies to identify the proteins involved in key signal transduction processes in neurons, to characterize protein-protein interactions by surface plasmon resonance and to perform automated RNAi experiments. Research areas that would greatly benefit from this core facility include nerve growth and regeneration, neuromuscular junction formation, cancer metastasis, axon guidance, axon domain assembly, lesion induced synaptic plasticity, potassium channel function, Alzheimer's and other amyloid diseases, brain development, aging, brain cancer, and neurotransmitter receptor trafficking.
The NYU Mass Spectrometry Core Facility for Neuroscience ensures that neuroscientists have access to cutting edge mass spectrometry technology to enable their basic research in such key areas as nerve growth and regeneration, neuromuscular disorders, cerebral hemorrhagic stroke, nervous system development, synaptic plasticity, affective disorders such as depression, Alzheimer's and other amyloid diseases, and aging.
|Rosen, Rebecca F; Tomidokoro, Yasushi; Farberg, Aaron S et al. (2016) Comparative pathobiology of Î²-amyloid and the unique susceptibility of humans to Alzheimer's disease. Neurobiol Aging 44:185-96|
|Xu, Yang; Phoon, Colin K L; Berno, Bob et al. (2016) Loss of protein association causes cardiolipin degradation in Barth syndrome. Nat Chem Biol 12:641-7|
|Huang, Zhifeng; Marsiglia, William M; Basu Roy, Upal et al. (2016) Two FGF Receptor Kinase Molecules Act in Concert to Recruit and Transphosphorylate Phospholipase CÎ³. Mol Cell 61:98-110|
|Bowling, Heather; Bhattacharya, Aditi; Zhang, Guoan et al. (2016) BONLAC: A combinatorial proteomic technique to measure stimulus-induced translational profiles in brain slices. Neuropharmacology 100:76-89|
|McIntee, Farron L; Giannoni, Patrizia; Blais, Steven et al. (2016) In vivo Differential Brain Clearance and Catabolism of Monomeric and Oligomeric Alzheimer's AÎ² protein. Front Aging Neurosci 8:223|
|Luque-Garcia, Jose L; Neubert, Thomas A (2015) Analysis of Electroblotted Proteins by Mass Spectrometry. Methods Mol Biol 1314:243-53|
|Hernandez-Guillamon, Mar; Mawhirt, Stephanie; Blais, Steven et al. (2015) Sequential Amyloid-Î² Degradation by the Matrix Metalloproteases MMP-2 and MMP-9. J Biol Chem 290:15078-91|
|Deng, Jingjing; Zhang, Guoan; Huang, Fang-Ke et al. (2015) Identification of protein N-termini using TMPP or dimethyl labeling and mass spectrometry. Methods Mol Biol 1295:249-58|
|Jami, Mohammad-Saeid; Salehi-Najafabadi, Zahra; Ahmadinejad, Fereshteh et al. (2015) Edaravone leads to proteome changes indicative of neuronal cell protection in response to oxidative stress. Neurochem Int 90:134-41|
|Ai, Minrong; Mills, Holly; Kanai, Makoto et al. (2015) Green-to-Red Photoconversion of GCaMP. PLoS One 10:e0138127|
Showing the most recent 10 out of 61 publications