Proteomics

Dataset Information

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Quantitative proteomics and phosphoproteomics reveal that PIM3 modulates cell migration via regulating Rho GTPase signaling


ABSTRACT: For the phosphoproteomic analysis, three biological replicates and two technical replicates were analyzed, resulting in twelve data for quantification. Statistical analysis was performed using student’s t-test as described in details in the “LC-MS/MS and data analysis” section

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Na Jiang  

LAB HEAD: ruibing chen

PROVIDER: PXD014044 | Pride | 2020-02-04

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
PCOH1_F1_R1.raw Raw
PCOH1_F1_R2.raw Raw
PCOH2_F1_R1.raw Raw
PCOH2_F1_R2.raw Raw
PCOH3_F1_R1.raw Raw
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Publications

Proto-Oncogene Serine/Threonine Kinase PIM3 Promotes Cell Migration via Modulating Rho GTPase Signaling.

Dang Yamei Y   Jiang Na N   Wang Hao H   Chen Xuechun X   Gao Yan Y   Zhang Xiangyang X   Qin Guoxuan G   Li Yongmei Y   Chen Ruibing R  

Journal of proteome research 20200207 3


The proto-oncogene serine/threonine-protein kinase PIM3 plays critical roles in cancer, and it has been extensively exploited as a drug target. Here, we investigated the quantitative changes in the cellular proteome and phosphoproteome in liver cancer cells overexpressing PIM3 to obtain a better understanding of the regulatory functions of PIM3 and the underlying molecular mechanisms. This work depicted the landscape of gene expression and protein phosphorylation potentially regulated by PIM3. A  ...[more]

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