ReviewThe Biochemical journal2003
Deglycosylation of glycoproteins with trifluoromethanesulphonic acid: elucidation of molecular structure and function.
Review in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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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.
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Who cites it
35 citing papers in PubMed, 121 citations in OpenAlex.
- Assessment of Peanut Allergen Cross-Contact Risk from Reused Roasting Oil Using a Targeted Proteomics Method.Journal of agricultural and food chemistry · 2026Article
- Molecular-level architecture of Chlamydomonas reinhardtii's glycoprotein-rich cell wall.Nature communications · 2024Article
- Fungal chitin-binding glycoprotein induces Dectin-2-mediated allergic airway inflammation synergistically with chitin.PLoS pathogens · 2024Article
- Glucose Oxidase, an Enzyme "Ferrari": Its Structure, Function, Production and Properties in the Light of Various Industrial and Biotechnological Applications.Biomolecules · 2022Review
- Glycosyltransferase Jhp0106 (PseE) contributes to flagellin maturation in Helicobacter pylori.Helicobacter · 2021Article
- Article
- Triflic Acid Treatment Enables LC-MS/MS Analysis of Insoluble Bacterial Biomass.Journal of proteome research · 2018Article
- Chemical Glycoproteomics.Chemical reviews · 2016Review
- Identification of Novel N-Glycosylation Sites at Noncanonical Protein Consensus Motifs.Journal of proteome research · 2016Article
- Label-free in vivo molecular imaging of underglycosylated mucin-1 expression in tumour cells.Nature communications · 2015Article
- Kexin-like endoprotease KexB is required for N-glycan processing, morphogenesis and virulence in Aspergillus fumigatus.Fungal genetics and biology : FG & B · 2015Article
- Protein-centric N-glycoproteomics analysis of membrane and plasma membrane proteins.Journal of proteome research · 2014Review
- Refolding of β-stranded class I chitinases of Hippophae rhamnoides enhances the antifreeze activity during cold acclimation.PloS one · 2014Article
- Analytical tools for the study of cellular glycosylation in the immune system.Frontiers in immunology · 2013Review
- Binding Specificity of Philyra pisum Lectin to Pathogen-Associated Molecular Patterns, and Its Secondary Structure.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2013Article
- Opticin, a small leucine-rich proteoglycan, is uniquely expressed and translocated to the nucleus of chronic lymphocytic leukemia cells.Experimental hematology & oncology · 2013Article
- One single basic amino acid at the ω-1 or ω-2 site is a signal that retains glycosylphosphatidylinositol-anchored protein in the plasma membrane of Aspergillus fumigatus.Eukaryotic cell · 2013Article
- A proline/arginine-rich end leucine-rich repeat protein (PRELP) variant is uniquely expressed in chronic lymphocytic leukemia cells.PloS one · 2013Article
- Article
- Extracellular proteins from Lactobacillus plantarum BMCM12 prevent adhesion of enteropathogens to mucin.Current microbiology · 2012Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The alteration of proteins by post-translational modifications, including phosphorylation, sulphation, processing by proteolysis, lipid attachment and glycosylation, gives rise to a broad range of molecules that can have an identical underlying protein core. An understanding of glycosylation of proteins is important in clarifying the nature of the numerous variants observed and in determining the biological roles of these modifications. Deglycosylation with TFMS (trifluoromethanesulphonic acid) [Edge, Faltynek, Hof, Reichert, and Weber, (1981) Anal. Biochem. 118, 131-137] has been used extensively to remove carbohydrate from glycoproteins, while leaving the protein backbone intact. Glycosylated proteins from animals, plants, fungi and bacteria have been deglycosylated with TFMS, and the most extensively studied types of carbohydrate chains in mammals, the N-linked, O-linked and glycosaminoglycan chains, are all removed by this procedure. The method is based on the finding that linkages between sugars are sensitive to cleavage by TFMS, whereas the peptide bond is stable and is not broken, even with prolonged deglycosylation. The relative susceptibility of individual sugars in glycosidic linkage varies with the substituents at C-2 and the occurrence of amido and acetyl groups, but even the most stable sugars are removed under conditions that are sufficiently mild to prevent scission of peptide bonds. The post-translational modifications of proteins have been shown to be required for diverse biological functions, and selective procedures to remove these modifications play an important role in the elucidation of protein structure and function.
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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.