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ProteomicsLC-MS peptide analysis of cytotoxin digested with multiple-proteolytic enzyme
In this study, multiple enzyme digestion method was used to enhance the peptide sequence coverage of cytotoxin to characterize its epitope properties. This epitope excision method exhibits no preference for either consecutive or assembled epitopes, based on the specific binding between an antibody a...
ORGANISM(S): Serpentes 
2023-08-01 | PXD040420 | Pride
Lc-ms Cytotoxin Multiple enzyme digestion 
MetabolomicsAcute response to a high-saturated, high-refined carbohydrate meal in healthy young men shows novel perturbation of multiple metabolic and defense pathways

Regular consumption of fat and refined carbohydrates induces metabolic stress, increasing chronic metabolic disease risk. In healthy volunteers, we characterised the response to a high-fat/high-carbohydrate meal (HFHCM), typical of an ultra-processed food, by proteomic and metabolomics analyses, ...

2026-04-02 | MTBLS10972 | MetaboLights
GenomicsMNase digestion-sensitive nucleosomes in Saccharomyces cerevisiae
The structural complexity of nucleosomes underlies their functional versatility. Here we report a new type of complexity – nucleosome fragility, manifested as high sensitivity to micrococcal nuclease, in contrast to the common presumption that nucleosomes are similar in resistance to MNase digestio...
ORGANISM(S): Saccharomyces cerevisiae 
2011-01-24 | E-GEOD-26412 | biostudies-arrayexpress
ProteomicsExosome-transmitted HSPA9 facilitates bortezomib signaling in multiple myeloma
LC-MS was conducted to screen potential proteins that interacting with HSPA9 in multiple myeloma
ORGANISM(S): Homo Sapiens 
2025-03-13 | PXD061782 |
ProteomicsMultiple protease based human phosphopeptide atlas
Site-specific phospho-antibodies are commonly used to study these changes, however only a limited number of good antibodies is available, covering just a few signaling nodes in important pathways. It is highly unlikely that specific antibodies, covering the more than hundred thousands of estimated p...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2016-10-04 | MSV000080223 | MassIVE
TranscriptomicsIdentifying multi-locus chromatin contacts in human cells using tethered multiple 3C
Background: DNA in the nucleus of a living cell carries out its functions in the context of a complex, three-dimensional chromatin architecture. Several recently developed methods, each an extension of the chromatin conformation capture (3C) assay, have enabled the genome-wide profiling of chroma...
ORGANISM(S): Homo sapiens 
2015-04-29 | E-GEOD-60623 | biostudies-arrayexpress
ProteomicsCombination of multi-enzyme digestions and C-TAILS approach for deep screening of C-terminome
Protein C-termini study is still a challenging task and far behind its counterpart N-termini study. The identification of C-termini is often hampered by low ionization response in MS and fewer efficient enrichment methods existing. We previously optimized the C-TAILS (C-terminal amine-based isotope ...
ORGANISM(S): Escherichia coli 
2017-11-24 | PXD004275 | Pride
Protein c-termini C-tails Multi-enzyme Scii 
ProteomicsInfluence of digestion protocol in Protein Quantitation
Quantitative determination of absolute and relative protein amounts is an essential requirement for most current bottom-up proteomics applications, but protein quantitation estimates are affected by several sources of variability such as sample preparation, mass spectrometric acquisition, and data a...
ORGANISM(S): Escherichia coli 
2014-07-30 | PXD001187 | Pride
Protein quantitation Digestion protocols Fasp 
TranscriptomicsExpression profiles of PBMC from multiple sclerosis patients
Affymetrix GeneChip Human Gene 1.0 ST Array was applied to compare the expression profiles in peripheral blood mononuclear cells(PBMC) between healthy controls and multiple sclerosis patients(MS pt). It suggested that certain genes involved in apoptosis pathway have been changed regulated in PBMC ...
ORGANISM(S): Homo sapiens 
2011-03-01 | E-GEOD-23832 | biostudies-arrayexpress
ProteomicsMulti-Enzymatic Limited Digestion - the Next-Generation Sequencing for Proteomics
An innovative approach merging both the bottom-up and middle-down ideologies to provide fast, robust and comprehensive solutions for proteomics studies. The methodology, referred to as MELD for Multiple-Enzymatic Limited Digestion, capitalizes on a single two-hour long proteolytic step involving the...
ORGANISM(S): Homo sapiens (Human) 
2019-05-08 | PXD009800 | Pride
Ptms Digestibility profile Limited digestion Mass spectrometry Proteolytic method Protein characterization De novo sequencing  mabs 
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