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ProteomicsProteogenomic Integration Reveals Therapeutic Targets in Breast Cancer Xenografts
Huang K, Li S, Mertins P, Cao S, Gunawardena HP, Ruggles KV, et al., (2017) Nature Communications | 8:14864 | DOI: 10.1038/ncomms14864 | http://www.nature.com/articles/ncomms14864

Recent advances in mass spectrometry (MS) hav...

ORGANISM(S): Homo Sapiens (ncbitaxon:9606) Mus Musculus (ncbitaxon:10090) 
2019-08-28 | MSV000084249 | MassIVE
MetabolomicsSIN-3 transcriptional coregulator maintains mitochondrial homeostasis and polyamine flux
Mitochondrial function relies on the coordinated transcription of mitochondrial and nuclear genomes to assemble respiratory chain complexes. Across species, the SIN3 coregulator influences mitochondrial functions, but how its loss impacts mitochondrial homeostasis and metabolism in the context of a ...
2024-04-01 | MTBLS8439 | MetaboLights
ProteomicsSuper-SILAC analysis of human lung primary tumor-derived xenografts LC-MS/MS
Non-small cell lung cancer (NSCLC) accounts for 85% of lung cancers, and is subdived into 2 major histological subtypes: adenocacinoma (ADC) and squamous cell carcinoma (SCC). Super-SILAC methodology was used to facilitate the quantitative comparisons of human primary tumor-derived xenograft proteom...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2016-07-02 | MSV000079881 | MassIVE
ProteomicsChlamydomonas reinhardtii Mannosidase 1A and Xylosyltransferase1A N-glycosylation LC/MS-MS
We have identified insertional mutants of mannosidase 1A and xylosyltransferase 1A in Chlamydomonas reinhardtii. Mass spectrometric analyses of intact N-glycopeptides revealed that disruption of the genes altered the N-glycan composition of the alga (in single as well as double mutant). In contrast ...
ORGANISM(S): Chlamydomonas reinhardtii 
2018-02-27 | PXD005254 | Pride
Chlamydomonas reinhardtii N-gylcoproteomics Lc-ms/ms 
ProteomicsSurface and global proteome profiling of osteosarcoma patient derived xenografts
This study analyzed 22 unique OS patient-derived xenografts (PDXs) using proteomics to identify surface proteins for potential immunotherapeutic targeting. Plasma membranes were enriched using density gradient ultracentrifugation and compared to a reference standard of 12 immortalized non-OS cell li...
ORGANISM(S): Homo sapiens (Human) 
2026-07-28 | PXD075484 | Pride
Osteosarcoma 
ProteomicsIn-cell isotope-coded labeling and LC-MS/MS analysis probe warfarin inhibition mechanism
Warfarin targets human vitamin K epoxide reductase (hVKOR), a redox enzyme in the membrane of endoplasmic reticulum (ER), to prevent the formation of blood clots. Although warfarin has been a popular medication since 1954, its mechanism of action is still unclear. A fundamental issue is the controve...
ORGANISM(S): Homo sapiens (Human) 
2017-03-30 | PXD003774 | Pride
Human vitamin k epoxide reuctase N-ethylmeleimide Isotope Bottom-up proteomics Warfarin 
UnknownAn integrated multi-omic approach for discovery and dereplication of bioactive microbial natural products.
Not available
S-EPMC12560952 | biostudies-literature
ProteomicsMag-Net: Rapid enrichment of membrane-bound particles enables high coverage quantitative analysis of the plasma proteome
Membrane-bound particles in plasma are composed of exosomes, microvesicles, and apoptotic bodies and represent ~1-2% of the total protein composition. Proteomic interrogation of this subset of plasma proteins augments the representation of tissue-specific proteins, representing a “liquid biopsy,” wh...
ORGANISM(S): Homo Sapiens 
PXD042947 | panorama
ProteomicsMass spectrometry-based proteomics reveals potential roles of NEK9 and MAP2K4 in resistance to PI3K inhibitors in triple negative breast cancer

Filip Mundt, Sandeep Rajput, Shunqiang Li, Kelly Ruggles, Arshag D. Mooradian, Philipp Mertins, Michael A. Gillette, Karsten Krug, et al., Cancer Res. 2018 May 15;78(10):2732-2746. doi: 10.1158/0008-5472.CAN-17-1990.

Activation of phosphoinositide 3-kinase (PI3K) signaling is frequently obs...

ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2018-10-19 | MSV000083050 | MassIVE
UnknownSelf-Assembly, Rearrangement, and Disassembly of {Cr<sub>6</sub>} Horseshoe Oligomers.
Not available
S-EPMC12668306 | biostudies-literature
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