VIDOVÁ, Veronika and Zdeněk SPÁČIL. A review on mass spectrometry-based quantitative proteomics: Targeted and data independent acquisition. Analytica Chimica Acta. Amsterdam: Elsevier Science publishers, vol. 964, April, p. 7-23. ISSN 0003-2670. doi:10.1016/j.aca.2017.01.059. 2017.
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Basic information
Original name A review on mass spectrometry-based quantitative proteomics: Targeted and data independent acquisition
Authors VIDOVÁ, Veronika (203 Czech Republic, belonging to the institution) and Zdeněk SPÁČIL (203 Czech Republic, guarantor, belonging to the institution).
Edition Analytica Chimica Acta, Amsterdam, Elsevier Science publishers, 2017, 0003-2670.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10406 Analytical chemistry
Country of publisher Netherlands
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 5.123
RIV identification code RIV/00216224:14310/17:00097721
Organization unit Faculty of Science
Doi http://dx.doi.org/10.1016/j.aca.2017.01.059
UT WoS 000398434700002
Keywords in English Targeted quantitative proteomics tutorial; Selected/multiple reaction monitoring (SRM/MRM); Parallel reaction monitoring (PRM); Tandem mass spectrometry (MS/MS); Data independent acquisition (DIA)
Tags NZ, rivok
Tags International impact, Reviewed
Changed by Changed by: Ing. Nicole Zrilić, učo 240776. Changed: 27/3/2018 21:42.
Abstract
Mass spectrometry (MS) based proteomics have achieved a near- complete proteome coverage in humans and in several other organisms, producing a wealth of information stored in databases and bioinformatics resources. Recent implementation of selected/multiple reaction monitoring (SRM/MRM) technology in targeted proteomics introduced the possibility of quantitatively follow-up specific protein targets in a hypothesis-driven experiment. In contrast to immunoaffinity-based workflows typically used in biological and clinical research for protein quantification, SRM/MRM is characterized by high selectivity, large capacity for multiplexing (approx.200 proteins per analysis) and rapid, cost-effective transition from assay development to deployment. The concept of SRM/MRM utilizes triple quadrupole (QqQ) mass analyzer to provide inherent reproducibility, unparalleled sensitivity and selectivity to efficiently differentiate isoforms, post-translational modifications and mutated forms of proteins. SRMlike targeted acquisitions such as parallel reaction monitoring (PRM) are pioneered on high resolution/accurate mass (HR/AM) platforms based on the quadrupole-orbitrap (Q-orbitrap) mass spectrometer. The expansion of HR/AM also caused development in data independent acquisition (DIA). This review presents a step-by-step tutorial on development of SRM/MRM protein assay intended for researchers without prior experience in proteomics. We discus practical aspects of SRM-based quantitative proteomics workflow, summarize milestones in basic biological and medical research as well as recent trends and emerging techniques.
Links
EF15_003/0000469, research and development projectName: Cetocoen Plus
LM2015051, research and development projectName: Centrum pro výzkum toxických látek v prostředí (Acronym: RECETOX RI)
Investor: Ministry of Education, Youth and Sports of the CR
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