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ProteomicsRat Kir4.1 interactome with the particular purpose to identify 10 kDa copurified proteins using LC-MSMS
The project aims to determine the interactome of full-length Kir4.1 overexpressed in HEK293 stable cells. The overexpressed proteins were purified, and the purified samples, along with three bands from a 1D SDS-PAGE gel, were analyzed by LC-MSMS after trypsin digestion. The primary goal was to ident...
ORGANISM(S): Homo sapiens (Human) 
2025-05-07 | PXD060340 | Pride
Lc-msms Hek293 stable cells Full length rat kir4.1 Lc8 copurification 
ProteomicsProteomic analysis of the human milieu of gamete /embryo maternal interaction
The improvement of the embryo culture media is of high relevance due to its influence on successful implantation rates, pregnancy, neonatal outcomes and potential effects in the adult life. The ideal conditions for embryo development are those naturally occurring in the female reproductive tract, i....
ORGANISM(S): Homo sapiens (Human) 
2019-10-29 | PXD015980 | Pride
Low abundance proteins  human reproductive fluids  salpingectomy 
UnknownWhich Low-Abundance Proteins are Present in the Human Milieu of Gamete/Embryo Maternal Interaction?
Not available
S-EPMC6861935 | biostudies-literature
OtherA Coordinated Proteomic Approach for Identifying Proteins that Interact with the E. coli Ribosomal Protein S12.
Data from PASSEL: [[https://db.systemsbiology.net/sbeams/cgi/PeptideAtlas/PASS_View?datasetPassword=IR4769n&identifier=PASS00136 PASS00136]]. Experiment: 1st exerimental NAc pQ MeS, data file: F571953.mgf. Data published as part of J Proteome Res. 2013 12:1289-99 . From the Abstract: {{i}} ... To f...
ORGANISM(S): Escherichia_coli_k_12_substr__dh10b, Escherichia_coli_k_12_substr__mg1655, Enterobacteria_phage_13a, Enterobacteria_phage_933w, Enterobacteria_phage_alpha3, Enterobacteria_phage_ba14, Enterobacteria_phage_bp_4795, Enterobacteria_phage_bz13, Enterobacteria_phage_cdti, Enterobacteria_phage_ecods1, Enterobacteria_phage_eps7, Enterobacteria_phage_epsilon15, Enterobacteria_phage_es18, Enterobacteria_phage_felix_01, Enterobacteria_phage_fels_2, Enterobacteria_phage_fi_sensu_lato, Enterobacteria_phage_g4_sensu_lato, Enterobacteria_phage_hk022, Enterobacteria_phage_hk620, Enterobacteria_phage_hk97, Enterobacteria_phage_i2_2, Enterobacteria_phage_id18_sensu_lato, Enterobacteria_phage_id2, Enterobacteria_phage_if1, Enterobacteria_phage_ike, Enterobacteria_phage_jk06, Enterobacteria_phage_js10, Enterobacteria_phage_js98, Enterobacteria_phage_jse, Enterobacteria_phage_k1e, Enterobacteria_phage_k1f, Enterobacteria_phage_k1_5, Enterobacteria_phage_lambda, Enterobacteria_phage_m13, Enterobacteria_phage_min27, Enterobacteria_phage_ms2, Enterobacteria_phage_mu, Enterobacteria_phage_n15, Enterobacteria_phage_n4, Enterobacteria_phage_p1, Enterobacteria_phage_p2, Enterobacteria_phage_p22, Enterobacteria_phage_p4, Enterobacteria_phage_phi1, Enterobacteria_phage_phieco32, Enterobacteria_phage_phiecom_gj1, Enterobacteria_phage_phip27, Enterobacteria_phage_phiv10, Enterobacteria_phage_phix174_sensu_lato, Enterobacteria_phage_prd1, Enterobacteria_phage_psp3, Enterobacteria_phage_rb14, Enterobacteria_phage_rb32, Enterobacteria_phage_rb43, Enterobacteria_phage_rb49, Enterobacteria_phage_rb51, Enterobacteria_phage_rb69, Enterobacteria_phage_rtp, Enterobacteria_phage_sf6, Enterobacteria_phage_sfv, Enterobacteria_phage_sp6, Enterobacteria_phage_ssl_2009a, Enterobacteria_phage_st104, Enterobacteria_phage_st64t, Enterobacteria_phage_st_1, Enterobacteria_phage_t1, Enterobacteria_phage_t3, Enterobacteria_phage_t4, Enterobacteria_phage_t5, Enterobacteria_phage_t7, Enterobacteria_phage_tls, Enterobacteria_phage_vt2_sakai, Enterobacteria_phage_wa13_sensu_lato, Enterobacteria_phage_wv8, Enterobacteria_phage_yyz_2008, Enterobacteriophage_qbeta 
GPM11210013346 | GPMDB
ProteomicsBienertia s. chloroplast compartments replica 2 CCCP band1to10
Bienertia sinuspersici performs C4 photosynthesis without Kranz anatomy through subcellular compartmentalization of carbon fixation within individual cells. In this species, central compartment chloroplasts (C) and peripheral chloroplasts (P) collaborate with cytosolic and mitochondrial components i...
ORGANISM(S): Bienertia sinuspersici 
2019-05-14 | PXD001814 | Pride
Development Chloroplast compartment Shorgun proteomics Bienertia sinuspersicis 
ProteomicsA proteomics approach to study the role of lipid droplets in plant defense
Lipid Droplets (LDs), classically viewed as lipid storage particles, are recently emerging as dynamic organelles associated with stress responses and development; however, their involvement in plant immunity has been little investigated. Here we studied LDs in Arabidopsis thaliana leaves that respon...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2022-02-23 | PXD011499 | Pride
Lipid droplets/pseudomonas/hr-induced defense/senescence/arabidopsis 
ProteomicsExosomes and cells protein content from human subpopulations of pancreatic ductal adenocarcinoma (PDAC)
Characterization of the protein composition of exosomes and subpopulations of cells from four human PDAC cell lines (BxPC-3, PANC-1, T3M4, and MIA PaCa-2), via liquid chromatography electrospray ionization tandem mass spectrometry (LC/ESI–MS/MS).
ORGANISM(S): Homo sapiens (Human) 
2022-01-25 | PXD023529 | Pride
Cancer Exosomes Pancreas Pdac 
ProteomicsLC-MS/MS data of Tinospora cordifolia
Tinospora cordifolia has been used for thousands of years to treat various health conditions, including neurodegenerative diseases. The study aimed to elucidate the mechanism of action and protein targets of T. cordifolia in the context of Alzheimers disease through untargeted metabolomics and netwo...
ORGANISM(S): Tinospora Cordifolia (ncbitaxon:285590) 
2024-11-04 | MSV000096283 | MassIVE
ProteomicsBiofilm formation displays intrinsic offensive and defensive features of Bacillus cereus
Biofilm formation is a strategy of many bacterial species to adapt to a variety of stresses and has become a part of infections, contaminations or beneficial interactions. In this study, we demonstrate that profound physiological changes permit Bacillus cereus to switch from a floating to a sessile ...
ORGANISM(S): Bacillus cereus (strain ATCC 14579 / DSM 31) 
2020-05-26 | PXD010211 | Pride
Attack defence Planktonics Bacillus Cereus Toxins Biofilm Antimicrobials 
ProteomicsProfiling of fasting-feeding dynamics in mouse liver
Daily biological rhythms are orchestrated by a combination of the intrinsic circadian clock and external food/feeding-related signals which influence metabolism in health and disease. Understanding how and to which extent both circadian and fasting/feeding rhythms contribute to regulating daily phys...
ORGANISM(S): Mus musculus (Mouse) 
2021-01-22 | PXD008944 | Pride
Metabolism Mouse Fasting Liver 1d-lc-msms Online 2d-lc-msms Feeding 
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