Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Phospho-proteomic and proteomic analysis of WT and xip

ABSTRACT: We extracted proteins from WT and xip for phospho-peptide enrichment and employed a quantitative phospho-proteomics approach to systematically survey the relevant modification changes.

ORGANISM(S): Arabidopsis Thaliana

SUBMITTER: Yan Zhu

PROVIDER: PXD034766 | iProX | Wed Jul 13 00:00:00 BST 2022

REPOSITORIES: iProX

ACCESS DATA

Json Xml

Similar Datasets

Arabidopsis γ-H2A.X-INTERACTING PROTEIN participates in DNA damage response and safeguards chromatin stability

Project description:We extracted proteins from WT and xip for phospho-peptide enrichment and employed a quantitative phospho-proteomics approach to systematically survey the relevant modification changes.

2022-09-28 | PXD037072 |

iCLIP Analysis of WT, phospho-defective, and phospho-mimicking mutants of mouse Nucleolin in iKras PDAC cells

Project description:This experiment aimed to identify Nucleolin (Ncl) binding sites on a transcriptome-wide scale, by performing iCLIP in mouse iKras PDAC cells (Ying et al., 2012) transiently transfected with a mammalian expression construct encoding a wild-type (WT) myc-Ncl, a phospho-defective mutant in which S28, S34, S40, and S41 residues were mutated to A, or a phospho-mimicking mutant with these residues mutated to D. Cells transfected with an empty vector (myc-pRK5-DEST) were used as controls in the experiment.

2023-03-01 | E-MTAB-12481 | biostudies-arrayexpress

iCLIP Analysis of WT, phospho-defective, and phospho-mimicking mutants of mouse Nucleolin in iKras PDAC cells

Project description:iCLIP Analysis of WT, phospho-defective, and phospho-mimicking mutants of mouse Nucleolin in iKras PDAC cells

| PRJEB58806 | ENA

RNA-seq analysis of mRNAs immunoprecipitated by wild-type (WT), phospho-mimetic (S200D), or phospho-null (S200A) FLAG-LIN28A

Project description:RNA-seq analysis of mRNAs immunoprecipitated by wild-type (WT), phospho-mimetic (S200D), or phospho-null (S200A) FLAG-LIN28A

| PRJNA327369 | ENA

RNA-seq analysis of mRNAs immunoprecipitated by wild-type (WT) or phospho-mimetic (S200D) FLAG-LIN28A in PA1 cells

Project description:To explore the effect of LIN28 (S200) phosphorylation on LIN28's association with mRNAs on a transcriptome-wide scale, we performed mRNA-seq on RNAs immunoprecipitated (RIP-seq) by wild-type (WT) or phospho-mimetic (S200D) LIN28 in PA1 cells.

2016-10-28 | GSE83905 | GEO

RNA-seq analysis of mRNAs immunoprecipitated by wild-type (WT) or phospho-null (S200A) FLAG-LIN28A in HeLa cells

2016-10-28 | GSE83904 | GEO

The profiling of phospho-ribosomal protein S6 associated RNAs from mouse vomeronasal organ whole cell extract

Project description:Phospho-ribosome associated RNAs were immunopurified using the antibodies against phospho-S6. The purified RNAs were converted to cDNAs, which were sequenced in Illumina HiSeq platform. Vomeronasal organs were extracted from male CD-1 animals exposed to either pup cues or fresh bedding.

2018-12-13 | GSE122138 | GEO

Linking Phospho-Gonadotropin Regulated Testicular RNA Helicase (GRTH/DDX25) to Histone Ubiquitination and Acetylation Essential for Spermatid Development During Spermiogenesis

Project description:In this study, we examined genome-wide transcriptome profiles of germ cells isolated from GRTH Knock-In and WT mice testis using RNA-Seq. We used homozygous KI mice with R242H mutation in GRTH gene resulting loss of phospho-GRTH to further understand its role in spermatid development during spermiogenesis by analyzing the DEGs from RNA-Seq. The analysis of RNA-Seq data allowed us to find the relevant DEGs related to ubiquitination pathway that are essential for spermatid development. This study using KI mice model demonstrated that loss of phospho-GRTH impairs UBE2J1 and RNF8 dependent histone modifications hampering initial stages of spermatid elongation process.

2020-03-04 | GSE145047 | GEO

PI3K/mTOR specific phospho-antibody microarray to study the effect of rapamycin to the innate immune respsonse

Project description:To comprehensively analyze the effects of mTORC1 inhibition on GSK3, we employed the use of a PI3K/mTOR-specific phospho-antibody microarray that analyzed the site-specific phosphorylation of over 130 kinases within the PI3K/mTOR pathway. The phosphorylation levels of different kinases in monocytes were measured when stimulated with LPS in the presence or absence of a kind of mTORC1 inhibitor, rapamycin More than 130 highly specific and characterized phospho-antibodies for the human mTOR signaling pathway were immobilized and replicated six times on glass slides. The same non-phosphorylated target antibodies were included to allow the determination of the relative level of phosphorylatioin

2010-11-25 | E-GEOD-25520 | biostudies-arrayexpress

Phlpp1 regulates endochondral ossification via the chondrocyte phospho-proteome

Project description:Appendicular growth and bone mass acquisition are controlled by a variety of growth factors, hormones, and mechanical forces in a dynamic process called endochondral ossification. Chondrocytes in the growth plate must proliferate and undergo hypertrophy to drive growth plate expansion and lay the template for bone. Pleckstrin homology (PH) domain and leucine rich repeat phosphatase 1 and 2 (Phlpp1 and Phlpp2) are protein phosphatases that regulate intracellular signaling cascades through posttranslational modification of AKT, PKC, and S6K, among others. Phlpp1 controls chondrocyte proliferation and survival and germline deletion of Phlpp1 suppresses bone lengthening. Here, we demonstrate that Phlpp2 does not regulate endochondral ossification. Phlpp2-/- mice are phenotypically indistinguishable from their wildtype (WT) littermates, with similar bone length, bone mass, and growth plate dynamics. By contrast, Phlpp1/2-/- mice are phenotypically indistinguishable from Phlpp1-/- mice. Deletion of Phlpp1 or Phlpp2 had moderate effects on the chondrocyte transcriptome and proteome compared to WT control cells. By contrast, Phlpp1-/- and Phlpp1/2-/- chondrocytes had significantly altered phospho-proteomes compared to WT and Phlpp2-/- chondrocytes. Data integration via multiomics analysis revealed that RAF-MEK-ERK signaling was altered in cells lacking Phlpp1. In conclusion, these data demonstrate that Phlpp1, but not Phlpp2, regulates endochondral ossification via the chondrocyte phospho-proteome.

2024-09-30 | GSE265773 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data