Reductive methylation labeling, from quantitative to structural proteomics

Z. Liu; Ye Zhou; Jing Liu; Jin Chen; Albert J.R. Heck; Fangjun Wang

doi:10.1016/j.trac.2019.07.009

Reductive methylation labeling, from quantitative to structural proteomics

Z. Liu, Ye Zhou, Jing Liu, Jin Chen, Albert J.R. Heck, Fangjun Wang^*

^*Corresponding author for this work

Research output: Contribution to journal › Review article › peer-review

Abstract

Reductive methylation is a highly reactive and selective chemical labeling method and plays an important role in proteomic analysis. Various applications of reductive methylation have been developed and have substantially promoted the scope of proteomic analysis to date. Aside from a well-known method for introducing isotopes, this reaction could also be conducted under biological conditions and has little structural perturbations. In this paper, we reviewed the recent developments and applications of reductive methylation in quantitative proteomics and protein N-terminal profiling, along with the emerging applications in structural proteomics for monitoring protein structural/conformational changes under various conditions.

Original language	English
Pages (from-to)	771-778
Number of pages	8
Journal	TrAC - Trends in Analytical Chemistry
Volume	118
DOIs	https://doi.org/10.1016/j.trac.2019.07.009
Publication status	Published - Sept 2019

Bibliographical note

Funding Information:
Financial supports are gratefully acknowledged for the National Key R&D Program of China ( 2016YFF0200504 ), the National Natural Science Foundation of China ( 91853101 , 21675152 and 81702995 ) and the grant from DICP ( ZZBS201603 ).

Publisher Copyright:
© 2019 Elsevier B.V.

Funding

Financial supports are gratefully acknowledged for the National Key R&D Program of China ( 2016YFF0200504 ), the National Natural Science Foundation of China ( 91853101 , 21675152 and 81702995 ) and the grant from DICP ( ZZBS201603 ).

Keywords

Lysine reactivity profiling
Mass spectrometry
N-termini profiling
Quantitative proteomics
Reductive methylation
Stable isotope dimethyl labeling
Structural proteomics

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10.1016/j.trac.2019.07.009

1-s2.0-S0165993619302936-mainFinal published version, 1.43 MBLicence: Taverne

Cite this

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title = "Reductive methylation labeling, from quantitative to structural proteomics",

abstract = "Reductive methylation is a highly reactive and selective chemical labeling method and plays an important role in proteomic analysis. Various applications of reductive methylation have been developed and have substantially promoted the scope of proteomic analysis to date. Aside from a well-known method for introducing isotopes, this reaction could also be conducted under biological conditions and has little structural perturbations. In this paper, we reviewed the recent developments and applications of reductive methylation in quantitative proteomics and protein N-terminal profiling, along with the emerging applications in structural proteomics for monitoring protein structural/conformational changes under various conditions.",

keywords = "Lysine reactivity profiling, Mass spectrometry, N-termini profiling, Quantitative proteomics, Reductive methylation, Stable isotope dimethyl labeling, Structural proteomics",

author = "Z. Liu and Ye Zhou and Jing Liu and Jin Chen and Heck, {Albert J.R.} and Fangjun Wang",

note = "Funding Information: Financial supports are gratefully acknowledged for the National Key R&D Program of China ( 2016YFF0200504 ), the National Natural Science Foundation of China ( 91853101 , 21675152 and 81702995 ) and the grant from DICP ( ZZBS201603 ). Publisher Copyright: {\textcopyright} 2019 Elsevier B.V.",

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doi = "10.1016/j.trac.2019.07.009",

language = "English",

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AU - Zhou, Ye

AU - Liu, Jing

AU - Chen, Jin

AU - Heck, Albert J.R.

AU - Wang, Fangjun

N1 - Funding Information: Financial supports are gratefully acknowledged for the National Key R&D Program of China ( 2016YFF0200504 ), the National Natural Science Foundation of China ( 91853101 , 21675152 and 81702995 ) and the grant from DICP ( ZZBS201603 ). Publisher Copyright: © 2019 Elsevier B.V.

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N2 - Reductive methylation is a highly reactive and selective chemical labeling method and plays an important role in proteomic analysis. Various applications of reductive methylation have been developed and have substantially promoted the scope of proteomic analysis to date. Aside from a well-known method for introducing isotopes, this reaction could also be conducted under biological conditions and has little structural perturbations. In this paper, we reviewed the recent developments and applications of reductive methylation in quantitative proteomics and protein N-terminal profiling, along with the emerging applications in structural proteomics for monitoring protein structural/conformational changes under various conditions.

AB - Reductive methylation is a highly reactive and selective chemical labeling method and plays an important role in proteomic analysis. Various applications of reductive methylation have been developed and have substantially promoted the scope of proteomic analysis to date. Aside from a well-known method for introducing isotopes, this reaction could also be conducted under biological conditions and has little structural perturbations. In this paper, we reviewed the recent developments and applications of reductive methylation in quantitative proteomics and protein N-terminal profiling, along with the emerging applications in structural proteomics for monitoring protein structural/conformational changes under various conditions.

KW - Lysine reactivity profiling

KW - Mass spectrometry

KW - N-termini profiling

KW - Quantitative proteomics

KW - Reductive methylation

KW - Stable isotope dimethyl labeling

KW - Structural proteomics

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U2 - 10.1016/j.trac.2019.07.009

DO - 10.1016/j.trac.2019.07.009

M3 - Review article

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SN - 0165-9936

VL - 118

SP - 771

EP - 778

JO - TrAC - Trends in Analytical Chemistry

JF - TrAC - Trends in Analytical Chemistry

ER -

Reductive methylation labeling, from quantitative to structural proteomics

Abstract

Bibliographical note

Funding

Keywords

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