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TranscriptomicsGenomic features and regulatory roles of intermediate-size non-coding RNAs in Arabidopsis
Recent advances in genome-wide techniques allowed the identification of thousands of non-coding RNAs with various sizes in eukaryotes, some of which have further been shown to serve important functions in many biological processes. However, in model plant Arabidopsis, novel intermediate-sized ncRNAs...
ORGANISM(S): Arabidopsis thaliana 
2014-01-20 | E-GEOD-44235 | biostudies-arrayexpress
TranscriptomicsRNA Sequencing analysis of Wild Type and HID1 mutant Transcriptomes
Seedling photomorphogenesis is a sophisticated developmental process that is controlled by both the transcriptional and posttranscriptional regulation of gene expression. Here, we identify an Arabidopsis noncoding RNA, designated HIDDEN TREASURE 1 (HID1), as a new factor promoting photomorphogenesis...
ORGANISM(S): Arabidopsis thaliana 
2014-07-01 | E-GEOD-57806 | biostudies-arrayexpress
ProteomicsA “Two birds One Stone” Strategy for Site-specific Analysis of the Core Fucosylation and O-GlcNAcylation
Core fucosylation and O-GlcNAcylation are two most famous protein glycosylations and regulate diverse physiological and pathological processes in living organism. Core fucosylation is a protein glycosylation in which a L-fucose residue attaches to the innermost N-acetylglucosamine (GlcNAc) of N-glyc...
ORGANISM(S): Homo Sapiens 
2023-12-04 | PXD047486 |
ProteomicsA Sensitive and Reversible Labeling Strategy Enables Global Mapping of the Core-Fucosylated Glycoproteome on Cell Surfaces
Core fucosylation, the attachment of α1,6-fucose to the innermost GlcNAc residue of N-glycans, is a unique protein glycosylation in living organisms. It plays significant roles in diverse physiological and pathological processes, and its upregulation has been observed in many cancers. Core fucosylat...
ORGANISM(S): Homo Sapiens 
2022-08-13 | PXD036051 |
ProteomicsConjugation site characterization of antibody–drug conjugates using electron-transfer/higher-energy collision dissociation (EThcD)
Antibody–drug conjugates (ADCs) are formed by binding of cytotoxic drugs to monoclonal antibodies (mAbs) through chemical linkers. A comprehensive evaluation of the critical quality attributes (CQAs) of ADCs is vital for drug development but remains challenging owing to ADC structural heterogeneity ...
ORGANISM(S): Homo Sapiens 
2023-02-14 | PXD040111 |
ProteomicsA “One-step” Strategy for the Global Characterization of Core-Fucosylated Glycoproteome
Core fucosylation, a special type of N-linked glycosylation, is important in tumor proliferation, invasion, metastatic potential, and therapy resistance. However, the core-fucosylated glycoproteome has not been extensively profiled due to the low abundance and poor ionization efficiency of glycosyla...
ORGANISM(S): Homo Sapiens 
2024-04-02 | PXD051139 |
ProteomicsIntegrated proteome and phosphoproteome analysis of interscapular brown adipose and subcutaneous white adipose tissues upon high fat diet feeding in mouse
Thermogenesis is a promising approach to limit weight gain in response to excess nutrition. In contrast to cold-induced thermogenesis, the molecular and cellular mechanisms of diet-induced thermogenesis (DIT) have not been fully characterized. Here, we explored the response of brown adipose tissue (...
ORGANISM(S): Mus Musculus 
2022-04-01 | PXD032888 |
ProteomicsOnline alkaline-pH reverse phase nanoelectrospray-tandem mass spectrometry complements conventional low-pH method for global proteomic analysis
The global proteome analysis was limited by the identification of peptides with low abundance or specific physiochemical properties. Here, a one-dimensional online alkaline-pH reverse phase nanoelectrospray-tandem mass spectrometry (AlkalinepH-MS/MS) method was developed and optimized for global pro...
ORGANISM(S): Homo Sapiens 
2023-01-15 | PXD039453 |
ProteomicsEndoglycosidases- treated N-glycosylation site identification
Glycoproteins, representing over 50% of human proteins and most biopharmaceuticals, are crucial for regulating various biological processes. The complexity of multiple glycosylation sites often leads to incomplete sequence coverage and ambiguous glycan modification profiles. Here, we developed an in...
ORGANISM(S): Homo Sapiens 
2024-12-30 | PXD059329 |
ProteomicsDecoding protein glycosylation by an integrative mass spectrometry-based de novo sequencing strategy
Glycoprotein is one of the most complex biomacromolecule，accounting for over 50% of total human proteins and the majority of biopharmaceuticals, exerting profound influences on various essential biological processes. With multiple N-glycosylation sites and O- glycosylation sites on the protein backb...
ORGANISM(S): Homo Sapiens Bos Taurus 
2024-08-24 | PXD055221 |
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