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ProteomicsHuman, ovarian epithelial cancer cell line, LC-MSMS
We investigated the functions of ECM1 subtypes ECM1a (inlcuding wild type and mutant) and ECM1b in ovarian cancer cell line HEYA8. While ECM1a is oncogenic, ECM1b is a tumor suppressor. To identify the molecules binding to ECM1a or ECM1b within cells, protein samples were generated by co-IP using HA...
ORGANISM(S): Homo sapiens (Human) 
2021-05-27 | PXD025239 | Pride
Human Ecm1 subtypes Ecm1a wild type (wt) Ecm1b Ecm1a mutant (mt) Ovarian epithelial cell line 
ProteomicsKnown ratios of SILAC labels in E. Coli
3 raw datasets corresponding to known mixtures of lysine and arginine in E. Coli.
ORGANISM(S): Escherichia coli 
2016-03-01 | PXD003327 | Pride
Silac Ls-msms 
ProteomicsLabel-Free Quantification of Nuclear Proteins in Six Plant Species
Label-Free Quantification of Nuclear Proteins in Six Plant Species
ORGANISM(S): Glycine max Arabidopsis thaliana (Mouse-ear cress) Zea mays (Maize) Capsicum annuum Solanum lycopersicum Oryza sativa (Rice) 
2026-06-11 | PXD074734 | Pride
Plant Lfq Ls-msms 
ProteomicsProteomics of the Milk Fat Globule Membrane from Camelus dromedarius
Camel milk is widely characterized with regard to caseins and whey proteins. However, in camelids, close to nothing is known about the Milk Fat Globule Membrane (MFGM), the membrane surrounding fat globules in milk. The purpose of this study was thus to identify MFGM proteins from Camelus dromedariu...
ORGANISM(S): Camelus dromedarius (Dromedary) (Arabian camel) 
2013-02-05 | PXD000059 | Pride
Dromedarius Mfgm Ls-msms 
ProteomicsUnderstanding the role of yeast Yme1 in mitochondrial finction using biochemical and proteomics analysis
Mitochondrial proteome comparison between S. cerevisiae BY4741 WT and Yme1 deletion mutant. Mitochondria were isolated by fractionation as described by Titorenko et al. (2009). Briefly, cells were grown in YPGal and harvested at later exponential phases of OD ~1.5. After pre- treatment with DTT buff...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-11-11 | PXD036367 | Pride
Mitochondria Yeast Ls/msms 
ProteomicsIdentification of proteins that interacted with DPYSL2
Dihydropyrimidinase like 2 promotes bladder cancer progression via pyruvate kinase M2-induced aerobic glycolysis and epithelial–mesenchymal transition. DPYSL2 promotes bladder cancer progression via PKM2.
ORGANISM(S): Homo sapiens (Human) 
2021-09-09 | PXD023279 | Pride
Human Ls-msms Dpysl2 
ProteomicsRUNX1 aberrations in blast-phase CML induce the RBP SPATS2L which promotes growth, survival and stress granule assembly
The RUNX1 transcription factor is a critical regulator of hematopoiesis and frequently mutated in myeloid malignancies. In the myeloproliferative neoplasm, chronic myeloid leukemia (CML), secondary somatic RUNX1 mutations and RUNX1::MECOM/EVI1, are associated with tyrosine kinase inhibitor (TKI) res...
ORGANISM(S): Homo sapiens (Human) 
2026-09-30 | PXD076395 | Pride
Runx1  bp-cml  oops  rbp  spats2l  homoharringtonine  stress granules 
ProteomicsProteogenomics of adenosine-to-inosine RNA editing in fruit fly
This dataset is a part of a bigger work on RNA editing in D. melanogaster brain. We present Orbitrap spectra searched against a customized database of Drosophila proteome with introduction of variants provided by RNA editing. Tree files reflect 3 technical replicates.
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2019-03-13 | PXD004949 | Pride
Proteomics Ls-msms Rna editing Drosophila melanogaster 
ProteomicsProteomic investigation on Anopheles gambiae in Burkina Faso related to insecticide pressures from different climatic regions
In Sub-Saharan Africa, Anopheles gambiae Giles (Diptera: Culicidae) largely contributes to malaria transmission, in direct relation to environmental conditions influencing the vector ecology. Therefore, our study aimed to compare the proteomes of An. gambiae according to varying insecticide pressure...
ORGANISM(S): Anopheles gambiae (African malaria mosquito) 
2020-03-09 | PXD016300 | Pride
Burkina faso Insecticide pressures Proteomic Anopheles gambiae 
ProteomicsDeciphering changes to human platelet proteome and degradome during storage before transfusion
Proteases, and specifically metalloproteinases, have been linked to the loss of platelet function during storage before transfusion, albeit the mechanism remains unknown. We used a dedicated N-terminomics technique, multiplex iTRAQ-TAILS (Terminal Amine Isotope Labeling of Substrates), to characteri...
ORGANISM(S): Homo sapiens (Human) 
2014-10-24 | PXD000906 | Pride
Platelets Metalloproteinases Degradome Proteases Tails Human Ls-msms 
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