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Immunoprecipitation of proteins containing Lys48-linked polyUb chains in wild-type C. elegans at day 5 of adulthood

ABSTRACT: We performed immunoprecipitation experiments in young worms using an antibody against Lys48-linked polyUb followed by single shot label-free proteomics.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Caenorhabditis Elegans

TISSUE(S): Whole Body

SUBMITTER: David Vilchez

LAB HEAD: David Vilchez

PROVIDER: PXD024093 | Pride | 2021-05-26

REPOSITORIES: Pride

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			Action	DRS
	1882.xlsx	Xlsx
	20190916_Q1_AWH_ColID_869c_ProjID_1882_Vilchez_sample_04_N2_D5_FLAG-1.raw	Raw
	20190916_Q1_AWH_ColID_869c_ProjID_1882_Vilchez_sample_05_N2_D5_FLAG-2.raw	Raw
	20190916_Q1_AWH_ColID_869c_ProjID_1882_Vilchez_sample_06_N2_D5_FLAG-3.raw	Raw
	20190916_Q1_AWH_ColID_869c_ProjID_1882_Vilchez_sample_13_N2_D5_K48-1.raw	Raw

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Publications

Rewiring of the ubiquitinated proteome determines ageing in C. elegans.

Koyuncu Seda S Loureiro Rute R Lee Hyun Ju HJ Wagle Prerana P Krueger Marcus M Vilchez David D

Nature 20210728 7871

Ageing is driven by a loss of cellular integrity<sup>1</sup>. Given the major role of ubiquitin modifications in cell function<sup>2</sup>, here we assess the link between ubiquitination and ageing by quantifying whole-proteome ubiquitin signatures in Caenorhabditis elegans. We find a remodelling of the ubiquitinated proteome during ageing, which is ameliorated by longevity paradigms such as dietary restriction and reduced insulin signalling. Notably, ageing causes a global loss of ubiquitinatio ...[more]

PMID: 34321666

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