Agar, Jeffrey - Northeastern University

个人简介

Degrees/Education Ph.D., University of Georgia B.S., University of Michigan

研究领域

The Agar group characterizes post-translational modifications of proteins and changes in protein, peptide, and lipid expression that occur during ALS, and then determines which of these changes have structural or toxic consequences. Because ALS begins with the death of a single type of cell, the motor neuron, we have developed numerous methods for the analysis of single cells by mass spectrometry. The Agar group specializes in mass spectrometry, including ultra-high mass resolution “top-down” mass spectrometry and mass spectrometry imaging methods, and has developed both analytical methods (“Matrix solution fixation” introduced by Agar YR 2007, automated funnel-skimmer dissociation, Karabacak 2008 and Cobb 2010, single-cell mass spectrometry imaging of mammalian cells, Agar YR 2010 and Boggio 2011) and computational tools (Karabacak 2008 introduced “Big Mascot” or Mascot TD database search engine, Li 2008 and 2010 introduce isotope calculator, a suite for mass spectrometry imaging applications is functional and to-be-submitted).

近期论文

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The central nervous system transcriptome of the weakly electric brown ghost knifefish (Apteronotus leptorhynchus): de novo assembly, annotation, and proteomics validation. Salisbury JP, Sîrbulescu, RF, Moran BM, Auclair JR, Zupanc, GKH, Agar JN. BMC Genomics. 2015 March 11;16:166. QUDeX-MS: hydrogen/deuterium exchange calculation for mass spectra with resolved isotopic fine structure. Salisbury JP, Liu Q, Agar JN. BMC Bioinformatics. 2014 Dec 11;15(1):403. The first pilot project of the consortium for top-down proteomics: a status report. Dang X, Scotcher J, Wu S, Chu RK, Tolić N, Ntai I, Thomas PM, Fellers RT, Early BP, Zheng Y, Durbin KR, Leduc RD, Wolff JJ, Thompson CJ, Pan J, Han J, Shaw JB, Salisbury JP, Easterling M, Borchers CH, Brodbelt JS, Agar JN, Paša-Tolić L, Kelleher NL, Young NL. Proteomics. 2014 May;14(10):1130-40. Artifacts to avoid while taking advantage of top-down mass spectrometry based detection of protein S-thiolation. Auclair JR, Salisbury JP, Johnson JL, Petsko GA, Ringe D, Bosco DA, Agar NY, Santagata S, Durham HD, Agar JN. Proteomics. 2014 May;14(10):1152-7. Resolving Isotopic Fine Structure to Detect and Quantify Natural Abundance- and Hydrogen/Deuterium Exchange-Derived Isotopomers. Liu Q, Easterling ML, Agar JN. Anal Chem. 2014 Jan 7;86(1):820-5. A rapid MALDI-TOF mass spectrometry workflow for Drosophila melanogaster differential neuropeptidomics. Salisbury JP, Boggio KJ, Hsu YW, Quijada J, Sivachenko A, Gloeckner G, Kowalski PJ, Easterling ML, Rosbash M, Agar JN. Mol Brain. 2013 Dec 27;6(1):60. Molecular imaging of drug transit through the blood-brain barrier with MALDI mass spectrometry imaging. Liu X, Ide JL, Norton I, Marchionni MA, Ebling MC, Wang LY, Davis E, Sauvageot CM, Kesari S, Kellersberger KA, Easterling ML, Santagata S, Stuart DD, Alberta J, Agar JN, Stiles CD, Agar NY. Sci Rep. 2013 Oct 4;3:2859. Post-translational modification by cysteine protects Cu/Zn-superoxide dismutase from oxidative damage. Auclair JR, Johnson JL, Lui Q, Salisbury JP, Rotunno MS, Petsko GA, Ringe D, Brown RH Jr, Bosco DA, Agar JN. Biochemistry. 2013 Sep 10;52(36):6137-44. Structural consequences of cysteinylation of Cu/Zn-superoxide dismutase. Auclair JR, Brodkin HR, D’Aquino JA, Petsko GA, Ringe D, Agar JN. Biochemistry Sep 10;52(36):6145-50. Performance comparisons of Nano-LC systems, electrospray sources and LC-MS-MS platforms. Liu Q, Cobb JS, Johnson JL, Wang Q, Agar JN. J Chromatogr Sci. 2013. Mass spectrometry tools for analysis of intermolecular interactions. Auclair JR, Somasundaran M, Green KM, Evans JE, Schiffer CA, Ringe D, Petsko GA, Agar JN. Methods Mol Biol. 2012;896:387-98. Impaired proteasome function in sporadic amyotrophic lateral sclerosis. Kabashi E, Agar JN, Strong MJ, Durham HD. Amyotroph Lateral Scler. 2012 Jun;13(4):367-71. A soluble α-synuclein construct forms a dynamic tetramer. Wang W, Perovic I, Chittuluru J, Kaganovich A, Nguyen LT, Liao J, Auclair JR, Johnson D, Landeru A, Simorellis AK, Ju S, Cookson MR, Asturias FJ, Agar JN, Webb BN, Kang C, Ringe D, Petsko GA, Pochapsky TC, Hoang QQ. Proc Natl Acad Sci U S A. 2011 Oct 25;108(43):17797-802. Recent advances in single-cell MALDI mass spectrometry imaging and potential clinical impact. Boggio KJ, Obasuyi E, Sugino K, Nelson SB, Agar NY, Agar JN. Expert Rev Proteomics. 2011 Oct;8(5):591-604. Evidence of the participation of remote residues in the catalytic activity of Co-type nitrile hydratase from Pseudomonas putida. Brodkin HR, Novak WR, Milne AC, D’Aquino JA, Karabacak NM, Goldberg IG, Agar JN, Payne MS, Petsko GA, Ondrechen MJ, Ringe D. Biochemistry. 2011 Jun 7;50(22):4923-35. Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis. Auclair JR, Boggio KJ, Petsko GA, Ringe D, Agar JN. Proc Natl Acad Sci U S A. 2010 Dec 14;107(50):21394-9. Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS. Bosco DA, Morfini G, Karabacak NM, Song Y, Gros-Louis F, Pasinelli P, Goolsby H, Fontaine BA, Lemay N, McKenna-Yasek D, Frosch MP, Agar JN, Julien JP, Brady ST, Brown RH Jr. Nat Neurosci. 2010 Nov;13(11):1396-403. Memory-efficient calculation of the isotopic mass states of a molecule. Li L, Karabacak NM, Cobb JS, Wang Q, Hong P, Agar JN. Rapid Commun Mass Spectrom. 2010 Sep;24(18):2689-96. Tissue preparation for the in situ MALDI MS imaging of proteins, lipids, and small molecules at cellular resolution. Agar NY, Kowalski JM, Kowalski PJ, Wong JH, Agar JN.Methods Mol Biol. 2010;656:415-31. Transformative effects of higher magnetic field in Fourier transform ion cyclotron resonance mass spectrometry. Karabacak NM, Easterling ML, Agar NY, Agar JN.J Am Soc Mass Spectrom. 2010 Jul;21(7):1218-22.