ReviewSe pu = Chinese journal of chromatography2021
[Recent advances in glycopeptide enrichment and mass spectrometry data interpretation approaches for glycoproteomics analyses].
Review in Se pu = Chinese journal of chromatography, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
4 citing papers in PubMed, 19 citations in OpenAlex.
- Glycosylation: mechanisms, biological functions and clinical implications.Signal transduction and targeted therapy · 2024Review
- Identification and characterization of intact glycopeptides in human urine.Scientific reports · 2024Article
- Article
- [Application of smart responsive materials in phosphopeptide and glycopeptide enrichment].Se pu = Chinese journal of chromatography · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein glycosylation is one of the most important post-translational modifications (PTMs). The glycosylation is crucial in a variety of physiological and pathological processes that include protein stability, intracellular and intercellular signal transduction, hormone activation or inactivation, and immune regulation. Protein glycosylation is generated by complex biosynthetic pathways comprising hundreds of glycosyltransferases, glycosidases, transcriptional factors, transporters, and protein backbones. Abnormal protein glycosylation is closely associated with the occurrence and development of diseases. Many disease biomarkers in clinical screening are glycoproteins (alfa fetoprotein for liver cancer, carbohydrate antigen 125 for ovarian cancer, carcinoembryonic antigen for colon cancer, prostate-specific antigen for prostate cancer, etc.), and glycan antigens (carbohydrate antigen 19-9 for gastrointestinal cancer and pancreatic cancer, etc.). Glycoproteomics research and technological developments are important to elucidate the mechanism of protein glycosylation in vivo. Mass spectrometry (MS)-based proteomics provides an excellent approach for the comprehensive analysis of proteins and their modifications. In bottom-up proteomics, glycoproteomic analysis is more difficult than other PTMs because intact glycopeptides have diverse peptide backbones and glycan chains, relatively low abundance and ionization efficiency, and pronounced heterogeneity. In recent years, glycoproteomic methodologies such as intact glycopeptide enrichment methods, MS fragmentation and acquisition approaches, MS data interpretation tools and software, and quantification strategies have been appreciably improved. These methodologies have driven in-depth glycoproteomics research. This review focuses on the recent advances in MS-based glycoproteomics. New enrichment methods and spectral interpretation approaches of intact
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.