Proteomics

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System-wide profiling of lysine 5-hydroxylation


ABSTRACT: Lysine 5-hydroxylation (5-Hyl) has been well recognized as an essential protein post-translational modification regulating cellular structural stability, RNA alternative splicing and epigenetic gene expression. System-wide enrichment and quantification of 5-Hyl targets have been challenging due to its chemical inert nature and difficulties in differentiating structural isomers in a complex biological sample. Here, we report the development of an efficient chemical proteomic workflow for affinity enrichment and constitutional isomer specific profiling of endogenous 5-Hyl substrates based on highly selective periodate chemistry.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell

SUBMITTER: Yue Chen  

LAB HEAD: Yue Chen

PROVIDER: PXD054608 | Pride | 2025-04-04

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
20230223_FlagHA_nuclear_rep01.raw Raw
20230223_FlagHA_nuclear_rep02.raw Raw
20230223_FlagHA_nuclear_rep03.raw Raw
20230223_longJMJD6_nuclear_rep01.raw Raw
20230223_longJMJD6_nuclear_rep02.raw Raw
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Publications

A constitutional isomer selective chemical proteomic strategy for system-wide profiling of protein lysine 5-hydroxylation.

Sin Yi-Cheng YC   Park Meeyeon M   Griffin Timothy J TJ   Yong Jeongsik J   Chen Yue Y  

Chemical science 20241008


Lysine 5-hydroxylation (5-Hyl) has been well recognized as an essential protein post-translational modification regulating cellular structural stability, RNA alternative splicing and epigenetic gene expression. System-wide enrichment and quantification of 5-Hyl targets have been challenging due to their chemical inert nature and difficulties in differentiating structural isomers in a complex biological sample. Here, we report the development of an efficient chemical proteomic workflow for affini  ...[more]

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