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Start Over Author "Ryan T. Fellers" Journal nature methods
2 results on '"Ryan T. Fellers"'

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

Author

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

Subjects
Proteomics, Analytical chemistry, Mass spectrometry, Orbitrap, Biochemistry, Multiplexing, Article, Mass Spectrometry, Spectral line, Charge detection, Ion, law.invention, 03 medical and health sciences, Physics::Plasma Physics, law, Humans, Molecular Biology, 030304 developmental biology, Quantitative Biology::Biomolecules, 0303 health sciences, Chemistry, Proteins, Cell Biology, Characterization (materials science), True mass, Biotechnology
Abstract

A new Orbitrap-based ion analysis procedure is shown to be possible by determining the direct charge for numerous individual protein ions to generate true mass spectra. The deployment of an Orbitrap system for charge detection enables the characterization of highly complicated mixtures of proteoforms and their complexes in both denatured and native modes of operation, revealing information not obtainable by traditional measurement of an ensemble of ions.

Published
2020
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2. A five-level classification system for proteoform identifications

Author

Ryan T. Fellers, Carol V. Robinson, Jeffrey N. Agar, Hartmut Schlüter, Marta Vilaseca, Michael R. Shortreed, Paul M. Thomas, Lloyd M. Smith, Juan Antonio Vizcaíno, Julia Chamot-Rooke, Yury O. Tsybin, Neil L. Kelleher, Lissa C. Anderson, Trisha Tucholski, Paul O. Danis, Richard D. LeDuc, Ying Ge, Joseph A. Loo, Leah V. Schaffer, Joseph Gault, Ljiljana Paša-Tolić, University of Wisconsin-Madison, Northwestern University [Evanston], National High Magnetic Field Laboratory (NHMFL), Florida State University [Tallahassee] (FSU), Spectrométrie de Masse pour la Biologie – Mass Spectrometry for Biology (UTechS MSBio), Institut Pasteur [Paris]-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), University of Oxford [Oxford], University of California [Los Angeles] (UCLA), University of California, Pacific Northwest National Laboratory (PNNL), Universitaetsklinikum Hamburg-Eppendorf = University Medical Center Hamburg-Eppendorf [Hamburg] (UKE), Institute for Research in Biomedicine, Spain, European Bioinformatics Institute [Cambridge, UK], This work was supported by grants R35 GM126914 (to L.M.S.) and P41 GM108569 (to N.L.K.) from the NIH National Institute of General Medical Sciences, R21 LM013097 (to P.M.T.) from the National Library of Medicine, and the Sherman Fairchild Foundation (to N.L.K.)., Institut Pasteur [Paris] (IP)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), University of Oxford, and University of California (UC)

Subjects
Proteomics, 0303 health sciences, Proteomics methods, Extramural, Computer science, media_common.quotation_subject, Cell Biology, Ambiguity, Biochemistry, Data science, Article, 03 medical and health sciences, Identification (information), [CHIM.ANAL]Chemical Sciences/Analytical chemistry, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Molecular Biology, 030304 developmental biology, Biotechnology, media_common
Abstract

International audience; To the editorThe term proteoform, introduced in Nature Methods in 2013 (ref. 1), has rapidly gained acceptance in the proteomics community. The challenge and importance of comprehensively identifying proteoforms in complex samples has been recognized, and reports have begun to appear of new platforms towards that end2,3,4,5. However, one interesting central ambiguity has emerged, namely determining precisely what is meant by a ‘proteoform identification’. At present, the only practical approaches for establishing the exact primary structure of a proteoform employ mass spectrometry (MS), and a wide range of MS results claim proteoform identifications6. This seemingly small matter has significant impact, as the ambiguity in what is meant by an ‘identification’ makes it difficult to compare results from different laboratories and approaches. This situation hinders the ability of the community to evaluate technological progress and to efficiently expand biological knowledge.

Published
2019
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