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Identification and Quantification of Proteoforms by Mass Spectrometry
Author(s) -
Schaffer Leah V.,
Millikin Robert J.,
Miller Rachel M.,
Anderson Lissa C.,
Fellers Ryan T.,
Ge Ying,
Kelleher Neil L.,
LeDuc Richard D.,
Liu Xiaowen,
Payne Samuel H.,
Sun Liangliang,
Thomas Paul M.,
Tucholski Trisha,
Wang Zhe,
Wu Si,
Wu Zhijie,
Yu Dahang,
Shortreed Michael R.,
Smith Lloyd M.
Publication year - 2019
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201800361
Subject(s) - proteomics , computational biology , mass spectrometry , workflow , identification (biology) , top down proteomics , posttranslational modification , computer science , chemistry , bioinformatics , biology , protein mass spectrometry , tandem mass spectrometry , gene , chromatography , biochemistry , database , botany , enzyme
A proteoform is a defined form of a protein derived from a given gene with a specific amino acid sequence and localized post‐translational modifications. In top‐down proteomic analyses, proteoforms are identified and quantified through mass spectrometric analysis of intact proteins. Recent technological developments have enabled comprehensive proteoform analyses in complex samples, and an increasing number of laboratories are adopting top‐down proteomic workflows. In this review, some recent advances are outlined and current challenges and future directions for the field are discussed.