ArticleJournal of virology2018
Functional Role of N-Linked Glycosylation in Pseudorabies Virus Glycoprotein gH.
Article in Journal of virology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT07069010 (Evaluation of Burnout Syndrome Among Healthcare Professionals in Intensive Care Units Within the EPIC), which is not on this map. Cited by 7 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.
Evaluation of Burnout Syndrome Among Healthcare Professionals in Intensive Care Units Within the EPIC (Enhancing Palliative Care in ICU) Research
Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- N-glycosylation of the PEDV spike protein modulates viral replication and pathogenicity.Veterinary research · 2025Article
- An easy method to generate recombinant pseudorabies virus expressing the capsid protein of Porcine circovirus type 2d.Frontiers in microbiology · 2023Article
- The role of N-linked glycosylation in proteolytic processing and cell surface transport of the Cedar virus fusion protein.Virology journal · 2022Article
- Review
- N-glycosylation of somatostatin receptor type 2 protects rats from acute pancreatitis.Annals of translational medicine · 2021Article
- Influence of N-glycosylation on Expression and Function of Pseudorabies Virus Glycoprotein gB.Pathogens (Basel, Switzerland) · 2021Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Many viral envelope proteins are modified by asparagine (N)-linked glycosylation, which can influence their structure, physicochemical properties, intracellular transport, and function. Here, we systematically analyzed the functional relevance of N-linked glycans in the alphaherpesvirus pseudorabies virus (PrV) glycoprotein H (gH), which is an essential component of the conserved core herpesvirus fusion machinery. Upon gD-mediated receptor binding, the heterodimeric complex of gH and gL activates gB to mediate fusion of the viral envelope with the host cell membrane for viral entry. gH contains five potential N-linked glycosylation sites at positions 77, 162, 542, 604, and 627, which were inactivated by conservative mutations (asparagine to glutamine) singly or in combination. The mutated proteins were tested for correct expression and fusion activity. Additionally, the mutated gH genes were inserted into the PrV genome for analysis of function during virus infection. Our results demonstrate that all five sites are glycosylated. Inactivation of the PrV-specific N77 or the conserved N627 resulted in significantly reduced
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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.