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ProteomicsProteomic Profiling of Serum Exosomes from Patients with Metastatic Gastric Cancer
Clinical management of metastatic gastric cancer (mGC) remains a major challenge due to a lack of specific biomarkers and effective therapeutic targets. Recently, accumulating evidence has suggested that exosomes play an essential role in cancer metastasis and can be an excellent reservoir of novel ...
ORGANISM(S): Homo sapiens (Human) 
2020-06-29 | PXD019387 | Pride
Metastatic gastric cancer  serum exosomes  lc-ms/ms 
ProteomicsImmobilization of Ce(IV)-substituted polyoxometalate on ethylenediamine-functionalized graphene oxide for the isolation of intact phosphoproteins
Phosphorylation of protein plays a key role in the regulation of many biological processes. Herein, a simple approach is developed by immobilization of Ce(IV)-substituted polyoxometalate on ethylenediamine-functionalized graphene oxide (CeEGO) as adsorbent for selective isolation of intact phosphop...
ORGANISM(S): Homo Sapiens 
2018-07-20 | PXD010524 |
ProteomicsKLF16 enhances stress tolerance of colorectal carcinomas by modulating nucleolar homeostasis and translational reprogramming
Translational reprogramming is part of the unfolded protein response (UPR) during endoplasmic reticulum (ER) stress, which acts to the advantage of cancer growth and development in different stress conditions. But the mechanism of ER stress-related translational reprogramming in colorectal carcinoma...
ORGANISM(S): Homo Sapiens 
2022-05-16 | PXD033930 |
ProteomicsCharacterization of progressive denaturation and unfolding intermediates of proteins by fast cross-linking using di-ortho-phthalaldehyde
Chemical cross-linking of proteins coupled with mass spectrometry (CXMS) is widely used in protein structural analysis. In this study we develop a new class of non-hydrolyzable amine-selective di-ortho-phthalaldehyde (DOPA) cross-linkers, one of which is DOPA2. Cross-linking of proteins with DOPA2 i...
ORGANISM(S): Staphylococcus Aureus Bos Taurus 
2021-12-20 | PXD030552 |
ProteomicsImproving Mass Spectrometry Analysis of Protein Structures with Arginine-Selective Chemical Cross-linkers
we develop a series of arginine selective bifunctional aromatic glyoxal cross-linkers (ArGOs) and demonstrate their ability to cross-link model proteins and a protein complex. We also introduce the first arginine-lysine heterobifunctional cross-linker (KArGO), which provides significantly greater su...
ORGANISM(S): Escherichia Coli 
2019-01-14 | PXD012341 |
ProteomicsMeasurement of site-specific H2O2-sensitivity and identification of sulfenic acid modification of CLOCK cysteines
In vitro H2O2-sensitivity of CLOCK cysteines was measured with a quantitative chemoproteomic approach termed as QTRP (Quantitative Thiol Reactivity Profiling) as previously reported. In brief, 5 μg of recombinant CLOCK proteins were reduced with 1 mM DTT for 30 min at room temperature. After reactio...
ORGANISM(S): Homo Sapiens Mus Musculus 
2019-08-31 | PXD015266 |
Proteomicsmouse liver concatenated tandem array of consensus TF response elements (catTFRE) with H2O2
a pull-down assay using a concatenated tandem array of consensus TF response elements (catTFRE) to trap the TFs expressed in mouse livers following treatment with or without H2O2
ORGANISM(S): Mus Musculus 
2019-08-31 | PXD015265 |
ProteomicsA Pandas complex adapted for piRNA-guided transposon silencing and heterochromatin formation
dNxf2 directly interacts with dNxf1 to compete with its binding to NPC
ORGANISM(S): Drosophila Melanogaster 
2019-08-01 | PXD014884 |
ProteomicsA Pandas complex adapted for piRNA-guided transposon silencing and heterochromatin formation, Panx-IP-MS
The repression of transposons by the Piwi-interacting RNA (piRNA) pathway is essential to protect animal germ cells. In Drosophila ovaries, Panoramix (Panx) enforces transcriptional silencing by binding to the target-engaged Piwi-piRNA complex, although the precise mechanisms by which this occurs re...
ORGANISM(S): Drosophila Melanogaster 
2019-08-06 | PXD014926 |
ProteomicsUtilization of cross-linking mass spectrometry (XL-MS) for structural analysis of the ApoD-CD36 protein interaction
Structural analysis of the ApoD-CD36 complex by XL-MS.
ORGANISM(S): Homo Sapiens 
2025-11-20 | PXD070975 |
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