Work

Multiplexed mass spectrometry of individual ions improves measurement of proteoforms and their complexes

Year: 2020

Type: article

Source: Nature Methods

DOI: 10.1038/s41592-020-0764-5

Authors: Jared O. Kafader, Rafael D. Melani, Kenneth R. Durbin, Bon Ikwuagwu, Bryan P. Early, Ryan T. Fellers, Steven C. Beu, Vlad Zabrouskov, Alexander A. Makarov, Joshua T. Maze, Deven L. Shinholt, Ping F. Yip, Danielle Tullman-Ercek, Michael W. Senko, Philip D. Compton, Neil L. Kelleher

Institutions: Northwestern University, Chemistry of Life Processes Institute, Thermo Fisher Scientific (United States), Thermo Fisher Scientific (Germany)

Language: English

Topic: Mass Spectrometry Techniques and Applications

Subfield: Spectroscopy

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: U.S. Department of Health and Human Services, Sherman Fairchild Foundation, National Institutes of Health, NIH Office of the Director, National Institute of General Medical Sciences

Awards: G2124791380, National Resource for Translational and Developmental Proteomics, G2775350984, G5091946335, Acquisition of a Thermo Fisher Scientific Q Exactive UHMR mass spectrometer, Chemistry of Life Processes Predoctoral Training Program, G9000345326

OpenAlex ID: W3009899209

FWCI: 9.397

Cites: 26

Cited by: 194

Related to: 10