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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2023.3
- 수록면
- 12 - 20 (9page)
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초록· 키워드
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Over the past decade, mass spectrometry-based bottom-up proteomics (BUP) has been widely used to identify and to quantify complete proteomes from a biological system such as a cell, tissue, or organism. However, due to the protein inference problem, BUP approaches have intrinsic limitations for identifying and characterizing intact proteins that underlie complex traits and molecular mechanisms in biology. In contrast to BUP, which measures peptides produced from proteins by proteolytic digestion, top-down proteomics (TDP) is a powerful technology that allows for measuring intact proteins without proteolysis, thus identifying and quantifying proteoforms which provide new insights into molecular mechanisms. A proteoform is a defined form of a protein product from a single gene, including combinatorial coding polymorphisms, alternative RNA splicing events, and post-translational modifications (PTMs) on the same molecule. In this review, we outline some advances in separation, ionization, and fragmentation of intact proteins and data processing for TDP along with the growing power of proteoform-resolved measurements in clinical and translational research and biotechnology.
목차
Abstract
1. INTRODUCTION
2. 바텀업 단백체학 vs 탑다운 단백체학
3. CONCLUSION
REFERENCES
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UCI(KEPA) : I410-ECN-0101-2023-470-001322152