A five-level classification system for proteoform identifications.

Smith LM, Thomas PM, Shortreed MR, Schaffer LV, Fellers RT, LeDuc RD, Tucholski T, Ge Y, Agar JN, Anderson LC, Chamot-Rooke J, Gault J, Loo JA, Paša-Tolic L, Robinson CV, Schlüter H, Tsybin YO, Vilaseca M, Vizcaíno JA, Danis PO, and Kelleher NL. “A five-level classification system for proteoform identifications.” Nature Methods 2019; 16: 939–940.

Time-Dependent Measurement of Nrf2-Regulated Antioxidant Response to Ionizing Radiation towards Biomarker Development for Acute Radiation Injury.

Liu K, Singer E, Cohn W, Micewicz ED, McBride WH, Whitelegge JP, and Loo JA. “Time-Dependent Measurement of Nrf2-Regulated Antioxidant Response to Ionizing Radiation towards Biomarker Development for Acute Radiation Injury.” Proteomics Clin Appl 2019; 13 (6), e1900035.

Best practices and benchmarks for intact protein analysis for top-down mass spectrometry.

Donnelly DP, Rawlins CM, DeHart CJ, Fornelli L, Schachner LF, Lin Z, Lippens JL, Aluri KC, Sarin R, Chan B, Lantz C, Jung W, Johnson K, Koller A, Wolff J, Campuzano IDG, Auclair JR, Ivanov AR, Whitelegge JP, Paša-Tolić L, Chamot-Rooke J, Danis PO, Smith LM, Tsybin YO, Loo JA, Ge Y, Kelleher NL, and Agar JN. “Best practices and benchmarks for intact protein analysis for top-down mass spectrometry.” Nature Methods 2019; 16: 587–594.

Native and Denaturing MS Protein Deconvolution for Biopharma: mAbs and Antibody-Drug Conjugates to Polydisperse Membrane Proteins and Beyond.

Campuzano IDG, Robinson J, Hui JO, Shi S, Netirojjanakul C, Nshanian M, Lippens JL, Bagal D, Egea P, Loo JA, and Bern M. “Native and Denaturing MS Protein Deconvolution for Biopharma: mAbs and Antibody-Drug Conjugates to Polydisperse Membrane Proteins and Beyond.” Anal Chem 2019; 91: 9472-9480.

Top or middle? Up or down? A standard lexicon for protein top-down and allied mass spectrometry approaches.

Lermyte F, Tsybin YO, O’Connor PB, and Loo JA. “Top or middle? Up or down? A standard lexicon for protein top-down and allied mass spectrometry approaches.” J Am Soc Mass Spectrom 2019; 30: 1149-1157.

Syntrophus aciditrophicus uses the same enzymes in a reversible manner to degrade and synthesize aromatic and alicyclic acids.

James KL, Kung JW, Crable BR, Mouttaki H, Sieber JR, Nguyen HH, Yang Y, Xie Y, Erde J, Wofford NQ, Karr EA, Loo JA, Ogorzalek Loo RR, Gunsalus RP, and McInerney MJ. “Syntrophus aciditrophicus uses the same enzymes in a reversible manner to degrade and synthesize aromatic and alicyclic acids.” Environ Microbiol 2019; 21(5): 1833-1846.

The L-isoaspartate modification within protein fragments in the aging lens can promote protein aggregation.

Warmack RA, Shawa H, Liu K, Lopez K, Loo JA, Horwitz J, and Clarke SG. “The L-isoaspartate modification within protein fragments in the aging lens can promote protein aggregation.” J Biol Chem 2019; 294(32): 12203-12219.

The molecular tweezer CLR01 inhibits aberrant superoxide dismutase 1 (SOD1) self-assembly in vitro and in the G93A-SOD1 mouse model of ALS.

Malik R, Meng H, Wongkongkathep P, Corrales CI, Sepanj N, Atlasi RS, Klärner F-G, Schrader T, Spencer MJ, Loo JA, Wiedau M, and Bitan G. “The molecular tweezer CLR01 inhibits aberrant superoxide dismutase 1 (SOD1) self-assembly in vitro and in the G93A-SOD1 mouse model of ALS.” J Biol Chem 2019; 294: 3501–3513.

Native Top-Down Mass Spectrometry and Ion Mobility Spectrometry of the Interaction of Tau Protein with a Molecular Tweezer Assembly Modulator.

Nshanian M, Lantz C, Wongkongkathep P, Schrader T, Klärner F-G, Blümke A, Despres C, Ehrmann M, Smet-Nocca C, Bitan G, and Loo JA. “Native Top-Down Mass Spectrometry and Ion Mobility Spectrometry of the Interaction of Tau Protein with a Molecular Tweezer Assembly Modulator.” J. Am. Soc. Mass Spectrom. 2019; 30: 16-23.

Top-Down Protein Identification using a Time-of-Flight Mass Spectrometer and Data Independent Acquisition.

Lakshmanan R and and Loo JA. “Top-Down Protein Identification using a Time-of-Flight Mass Spectrometer and Data Independent Acquisition.” Int. J. Mass Spectrom. 2019; 435: 136–144.