Results 11 to 20 of about 3,095 (176)
The Hitchhiker's guide to glycoproteomics [PDF]
Biochemical Society Transactions, 2021 Protein glycosylation is one of the most common post-translational modifications that are essential for cell function across all domains of life. Changes in glycosylation are considered a hallmark of many diseases, thus making glycoproteins important diagnostic and prognostic biomarker candidates and therapeutic targets.
Tiago Oliveira +3 more
openaire +3 more sources
Targeting the glycoproteome [PDF]
Glycoconjugate Journal, 2012 Despite numerous original publications describing the structural complexity of N- and O-linked glycans on glycoproteins, only very few answer the basic question of which particular glycans are linked to which amino acid residues along the polypeptide chain.
Nilsson, Jonas +3 more
openaire +2 more sources
Chemical Glycoproteomics [PDF]
Chemical Reviews, 2016 Chemical tools have accelerated progress in glycoscience, reducing experimental barriers to studying protein glycosylation, the most widespread and complex form of posttranslational modification. For example, chemical glycoproteomics technologies have enabled the identification of specific glycosylation sites and glycan structures that modulate protein
Krishnan K, Palaniappan +1 more
openaire +2 more sources
Nanotechnologies in Glycoproteomics [PDF]
Clinical Proteomics, 2014 Protein glycosylation, as an important post-translational modification, is implicated in a number of ailments. Applying proteomic approaches, including mass spectrometry (MS) analyses that have played a significant role in biomarker detection and early diagnosis of diseases, to the study of glycoproteins or glycopeptides will facilitate a deeper ...
Zhao, Hu, Li, Yaojun, Hu, Ye
openaire +2 more sources
Glycan shield of the ebolavirus envelope glycoprotein GP
Communications Biology, 2022 Site-specific N-, O-, and C-linked glycans are characterized in the ebolavirus envelope glycoprotein GP using mass spectrometry-based glycoproteomics.
Weiwei Peng +9 more
doaj +1 more source
Frontiers in Molecular Biosciences, 2023 N-glycosylation is a key process for various biological functions like protein folding, maturation and sorting for the conventional secretory compartment, cell-cell communication and immune response.
Cristian V. A. Munteanu +3 more
doaj +1 more source
Beta-1,4-galactosyltransferase-3 deficiency suppresses the growth of immunogenic tumors in mice
Frontiers in Immunology, 2023 BackgroundBeta-1,4-galactosyltransferase-3 (B4GALT3) belongs to the family of beta-1,4-galactosyltransferases (B4GALTs) and is responsible for the transfer of UDP-galactose to terminal N-acetylglucosamine.
Heng Wei +7 more
doaj +1 more source
The glycoproteomics of hawk and caiman tears [PDF]
BMC Veterinary Research, 2021 Abstract Background Glycoproteins are important tear components that participate in the stability of the ocular surface. However, the glycopeptides that are present in the tears of wild animals have not yet been described. This work aimed to describe the glycoproteomic profile of roadside hawk (Rupornis magnirostris) and
Raposo, Ana Cláudia +4 more
openaire +5 more sources
BMC Plant Biology, 2021 Background C. sinensis is an important economic crop with fluoride over-accumulation in its leaves, which poses a serious threat to human health due to its leaf consumption as tea. Recently, our study has indicated that cell wall proteins (CWPs) probably
Yanli Liu +6 more
doaj +1 more source
Frontiers in Oncology, 2023 BackgroundThere is a need for new serum biomarkers for early detection of hepatocellular carcinoma (HCC). Haptoglobin (Hp) N-glycosylation is altered in HCC, but the diagnostic value of site-specific Hp glycobiomarkers is rarely reported.
Mahdokht Kohansal-Nodehi +14 more
doaj +1 more source