Journal
NATURE METHODS
Volume 16, Issue 7, Pages 587-594Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41592-019-0457-0
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Funding
- NIH [R01 NS065263, R01 GM117058, S10 OD018475, 1R01GM120272, R01CA218500, P30DK063491, R01 GM103479, S10 RR028893, S10 OD018504]
- ALSA [18-IIA-420]
- Biopharmaceutical Analysis Training Lab at Northeastern University
- Wisconsin Partnership Funds
- Thermo Fisher Scientific
- SCIEX
- US Department of Energy [DE-FC-02-02ER63421]
- NIH Ruth L. Kirschstein National Research Service Award (NRSA) [T32 GM007185]
- National Resource for Translational and Developmental Proteomics under NIH Grant from the National Institute of General Medical Sciences [P41GM108569]
- Chemistry of Life Processes Predoctoral Training Program at Northwestern University [T32GM105538]
Ask authors/readers for more resources
One gene can give rise to many functionally distinct proteoforms, each of which has a characteristic molecular mass. Top-down mass spectrometry enables the analysis of intact proteins and proteoforms. Here members of the Consortium for Top-Down Proteomics provide a decision tree that guides researchers to robust protocols for mass analysis of intact proteins (antibodies, membrane proteins and others) from mixtures of varying complexity. We also present cross-platform analytical benchmarks using a protein standard sample, to allow users to gauge their proficiency.
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