The ubiquitin proteoform problem |
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| Institution: | 1. Institute for Advanced Life Sciences, Hoshi University, 2-4-41 Ebara, Shinagawa-ku, Tokyo 142-8501, Japan;1. Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA;2. Howard Hughes Medical Institute, Chevy Chase, MD 20815, USA |
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| Abstract: | The diversity of ubiquitin modifications is immense. A protein can be monoubiquitylated, multi-monoubiquitylated, and polyubiquitylated with chains varying in size and shape. Ubiquitin itself can be adorned with other ubiquitin-like proteins and smaller functional groups. Considering different combinations of post-translational modifications can give rise to distinct biological outcomes, characterizing ubiquitylated proteoforms of a given protein is paramount. In this Opinion, we review recent advances in detecting and quantifying various ubiquitin proteoforms using mass spectrometry. |
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| Keywords: | Proteoform Ubiquitin Ubiquitin chain Bottom-up proteomics Middle-down proteomics Top-down proteomics |
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