ArticleScientific reports2017
Methylated-antibody affinity purification to improve proteomic identification of plant RNA polymerase Pol V complex and the interacting proteins.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Preliminary Proteomic and Metabolomic Analyses Reveal Potential Serum Biomarkers for Identifying Alveolar Echinococcosis in Mice.Veterinary sciences · 2025Article
- Light regulates nuclear detainment of intron-retained transcripts through COP1-spliceosome to modulate photomorphogenesis.Nature communications · 2024Article
- Syntaxin of plants71 plays essential roles in plant development and stress response via regulating pH homeostasis.Frontiers in plant science · 2023Article
- Deciphering Spatial Protein-Protein Interactions in Brain Using Proximity Labeling.Molecular & cellular proteomics : MCP · 2022Review
- AtSEC22 Regulates Cell Morphogenesis via Affecting Cytoskeleton Organization and Stabilities.Frontiers in plant science · 2021Article
- Listening to the Whispers in Neuroimmune Crosstalk: A Comprehensive Workflow to Investigate Neurotrophin Receptor p75NTR Under Endogenous, Low Abundance Conditions.Frontiers in immunology · 2021Article
- Histone acetylation recruits the SWR1 complex to regulate active DNA demethylation inProceedings of the National Academy of Sciences of the United States of America · 2019Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Affinity purification followed by enzymatic digestion and mass spectrometry has been widely utilized for the sensitive detection of interacting proteins and protein complexes in various organisms. In plants, the method is technically challenging due to the low abundance proteins, non-specific binding and difficulties of eluting interacting proteins from antibody beads. In this report, we describe a strategy to modify antibodies by reductive methylation of lysines without affecting their binding properties, followed by on-bead digestion of bound proteins with endoproteinase Lys-C. By this method, the antibody remains intact and does not interfere with the downstream identification of interacting proteins. Non-specific binding proteins were excluded using
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