Top-down proteomics
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Top-down proteomics is uniquely positioned to quantify proteoform distributions without enzymatic digestion, thereby linking SDS-PAGE bands/SEC peaks to specific chemical variants and enabling causality rather than correlation in structure-function relationships.
“Top-down proteomics is uniquely positioned to quantify proteo form distributions without enzymatic digestion, thereby linking SDS-PAGE bands/SEC peaks to specific chemical variants and enabling causality rather than correlation in structure-function relationships (Roberts et al., 2024).”
From Structure-function design of amaranth, buckwheat and quinoa proteins as hydrocolloids for emulsion and gel structuring (2027) · cites this paper as Roberts et al., 2024
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200 of 294 shown
Cited by
Sorted by citations
Yan, X., & Zhu, F. (2027) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.113137
- Authors
- Roberts, D. S., Loo, J. A., Tsybin, Y. O., Liu, X., Wu, S., Chamot-Rooke, J., Agar, J. N., Paša-Tolić, L., Smith, L. M., & Ge, Y.
- ORCID
- Venue
- Nature Reviews Methods Primers
- Published
- 2024-06-13
- Volume
- 4
- Issue
- 1
- ISSN
- 2662-8449
- PMC
- PMC11242913
- Cited by
- 154
- References
- 61
- Language
- en
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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