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Proteomes Are of Proteoforms: Embracing the Complexity
| Content Provider | MDPI |
|---|---|
| Author | Carbonara, Katrina Andonovski, Martin Coorssen, Jens R. |
| Copyright Year | 2021 |
| Description | Proteomes are complex—much more so than genomes or transcriptomes. Thus, simplifying their analysis does not simplify the issue. Proteomes are of proteoforms, not canonical proteins. While having a catalogue of amino acid sequences provides invaluable information, this is the Proteome-lite. To dissect biological mechanisms and identify critical biomarkers/drug targets, we must assess the myriad of proteoforms that arise at any point before, after, and between translation and transcription (e.g., isoforms, splice variants, and post-translational modifications [PTM]), as well as newly defined species. There are numerous analytical methods currently used to address proteome depth and here we critically evaluate these in terms of the current ‘state-of-the-field’. We thus discuss both pros and cons of available approaches and where improvements or refinements are needed to quantitatively characterize proteomes. To enable a next-generation approach, we suggest that advances lie in transdisciplinarity via integration of current proteomic methods to yield a unified discipline that capitalizes on the strongest qualities of each. Such a necessary (if not revolutionary) shift cannot be accomplished by a continued primary focus on proteo-genomics/-transcriptomics. We must embrace the complexity. Yes, these are the hard questions, and this will not be easy…but where is the fun in easy? |
| Starting Page | 38 |
| e-ISSN | 22277382 |
| DOI | 10.3390/proteomes9030038 |
| Journal | Proteomes |
| Issue Number | 3 |
| Volume Number | 9 |
| Language | English |
| Publisher | MDPI |
| Publisher Date | 2021-08-31 |
| Access Restriction | Open |
| Subject Keyword | Proteomes Biochemical Research Proteomics Top-down Bottom-up Immunoassay Mass Spectrometry Two-dimensional Gel Electrophoresis Western Blotting |
| Content Type | Text |
| Resource Type | Article |
