ReviewBiochemistry2011
The expanding horizons of asparagine-linked glycosylation.
Review in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 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.
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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
107 citing papers in PubMed, 222 citations in OpenAlex.
- Asparagine Synthetase Deficiency: Neuropathological Evidence of Disrupted Cortical Development.JIMD reports · 2026Article
- Asparagine-linked glycosylation protein 1 (ALG1) promotes aggressive phenotypes of lung adenocarcinoma cells, A549, via modulating N-linked glycosylation and ER-Stress.Glycoconjugate journal · 2025Article
- Targeting O-GlcNAcylation: Novel Therapeutic Strategies for Neurological Disease.Molecular neurobiology · 2025Review
- Improving recombinant protein secretion inMetabolic engineering communications · 2025Article
- Structural insights into polyisoprenyl-binding glycosyltransferases.Structure (London, England : 1993) · 2025Review
- Case Report of Friedreich's Ataxia and ALG1 -Related Biochemical Abnormalities in a Patient With Progressive Spastic Paraplegia.American journal of medical genetics. Part A · 2025Article
- Rft1 catalyzes lipid-linked oligosaccharide translocation across the ER membrane.Nature communications · 2024Article
- Evolutionary patterns of archaea predominant in acidic environment.Environmental microbiome · 2023Article
- The Mutual Relationship between Glycosylation and Non-Coding RNAs in Cancer and Other Physio-Pathological Conditions.International journal of molecular sciences · 2022Review
- Agl24 is an ancient archaeal homolog of the eukaryotic N-glycan chitobiose synthesis enzymes.eLife · 2022Article
- Topological and enzymatic analysis of human Alg2 mannosyltransferase reveals its role in lipid-linked oligosaccharide biosynthetic pathway.Communications biology · 2022Article
- Distinct Regions of the Haloferax volcanii Dolichol Phosphate-Mannose Synthase AglD Mediate the Assembly and Subsequent Processing of the Lipid-Linked Mannose.Journal of bacteriology · 2022Article
- Genetic defects are common in myopathies with tubular aggregates.Annals of clinical and translational neurology · 2022Article
- Detecting Glucose Fluctuations in theACS chemical biology · 2021Article
- Genetic and process engineering strategies for enhanced recombinant N-glycoprotein production in bacteria.Microbial cell factories · 2021Article
- The structure of an archaeal oligosaccharyltransferase provides insight into the strict exclusion of proline from the N-glycosylation sequon.Communications biology · 2021Article
- The possible association of clusterin fucosylation changes with male fertility disorders.Scientific reports · 2021Article
- Glycobiology of the Epithelial to Mesenchymal Transition.Biomedicines · 2021Review
- A Significant Change in Free Amino Acids of Soybean (Molecules (Basel, Switzerland) · 2021Article
- Subtle Influence of ACE2 Glycan Processing on SARS-CoV-2 Recognition.Journal of molecular biology · 2021Article
47 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Asparagine-linked glycosylation involves the sequential assembly of an oligosaccharide onto a polyisoprenyl donor, followed by the en bloc transfer of the glycan to particular asparagine residues within acceptor proteins. These N-linked glycans play a critical role in a wide variety of biological processes, such as protein folding, cellular targeting and motility, and the immune response. In the past decade, research in the field of N-linked glycosylation has achieved major advances, including the discovery of new carbohydrate modifications, the biochemical characterization of the enzymes involved in glycan assembly, and the determination of the biological impact of these glycans on target proteins. It is now firmly established that this enzyme-catalyzed modification occurs in all three domains of life. However, despite similarities in the overall logic of N-linked glycoprotein biosynthesis among the three kingdoms, the structures of the appended glycans are markedly different and thus influence the functions of elaborated proteins in various ways. Though nearly all eukaryotes produce the same nascent tetradecasaccharide (Glc(3)Man(9)GlcNAc(2)), heterogeneity is introduced into this glycan structure after it is transferred to the protein through a complex series of glycosyl trimming and addition steps. In contrast, bacteria and archaea display diversity within their N-linked glycan structures through the use of unique monosaccharide building blocks during the assembly process. In this review, recent progress toward gaining a deeper biochemical understanding of this modification across all three kingdoms will be summarized. In addition, a brief overview of the role of N-linked glycosylation in viruses will also be presented.
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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.