ArticleMolecular & cellular proteomics : MCP2018
Structures of N-Glycans of
Article in Molecular & cellular proteomics : MCP, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
7 citing papers in PubMed, 27 citations in OpenAlex.
- Unraveling the Glycosylation Machinery ofInternational journal of molecular sciences · 2026Article
- Animal Venoms Targeting Cellular Mechanisms: Advances and Implications for Drug Discovery and Disease Therapy.Toxins · 2026Review
- Article
- Molecular engineering of Komagataella phaffii for venom toxin production.Applied microbiology and biotechnology · 2026Review
- Article
- Insights into the Role of Proteolytic and Adhesive Domains of Snake Venom Metalloproteinases fromToxins · 2025Article
- Overview of protein posttranslational modifications in Arthropoda venoms.The journal of venomous animals and toxins including tropical diseases · 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
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The complexity of snake venoms has long been investigated to explore a myriad of biologically active proteins and peptides that are used for immobilizing or killing prey, and are responsible for the pathological effects observed on envenomation. Glycosylation is the main post-translational modification (PTM) of viperid venoms but currently there is little understanding of how protein glycosylation impacts the variation of venom proteomes. We have previously reported that
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What OpenQuestion holds
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.