Proteomics

Dataset Information

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PRM-based quantitative proteomic analysis of mouse tissues, testicular cells and cell lines


ABSTRACT: PRM analysis of RPL39L, RPL10L and RPL3L in 9 mouse tissues, including testis, fat, brain, liver, kidney, lung, skeletal muscle, heart and spleen; PRM analysis of RPL39 and RPL39L, RPL10 and RPL10L, and RPL22 and RPL22L1 in testicular cells; PRM analysis of RPL39L and RPL39 in RibosomeRPL39L-/- and wild type mouse spermatocytes and spermatids; PRM analysis of 17 down-regulated proteins and 1 unchanged protein (DYNC1LI2) in RibosomeRPL39L-/- testes; PRM analysis of RPL39 and RPL39L in GC-1 ribosomes, and RibosomeRPL39L-/- and wild type N2a ribosomes, Consistency between the observed and expected signal ratios of the light and heavy peptides by PRM in serial dilution experiments. Bovine serum albumin (BSA) as a negative control.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Spleen, Heart, Testis, Brain, Lung, Liver, Kidney

SUBMITTER: Yao liping  

LAB HEAD: Xuejiang Guo

PROVIDER: PXD020922 | Pride | 2022-09-30

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
PRM-9mousetissues.zip Other
PRM-Linearityanalysis-1.zip Other
PRM-Linearityanalysis-2.zip Other
PRM-N2a_GC1-ribosome.zip Other
PRM-RPL39Lknockout-spermatids-17proteins.zip Other
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Publications


Ribosomes are highly sophisticated translation machines that have been demonstrated to be heterogeneous in the regulation of protein synthesis<sup>1,2</sup>. Male germ cell development involves complex translational regulation during sperm formation<sup>3</sup>. However, it remains unclear whether translation during sperm formation is performed by a specific ribosome. Here we report a ribosome with a specialized nascent polypeptide exit tunnel, Ribosome<sup>ST</sup>, that is assembled with the m  ...[more]

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