Revealing Griffithsin Recognition of Diverse Virus-Associated N-glycans using Atomistic Simulations: Glycan Composition and Branching Pattern are Key Determinants

For peer review purposes only. The dataset contains the supplementary information (SI) data files associated with the study, including the initial and final atomic coordinates of all simulated systems (high-mannose, hybrid, and complex type N-glycans). The archive also includes the molecular dynamics parameter (.mdp) file used to generate the trajectories.

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Publication Details

Journal
Zenodo (CERN European Organization for Nuclear Research)
Published
2025-12-04
DOI
https://doi.org/10.5281/zenodo.17806788
Primary Topic
Glycosylation and Glycoproteins Research
Type
article
Field-Weighted Citation Impact
0.00
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article

Revealing Griffithsin Recognition of Diverse Virus-Associated N-glycans using Atomistic Simulations: Glycan Composition and Branching Pattern are Key Determinants

Zenodo (CERN European Organization for Nuclear Research)
Glycosylation and Glycoproteins Research
article

Revealing Griffithsin Recognition of Diverse Virus-Associated N-glycans using Atomistic Simulations: Glycan Composition and Branching Pattern are Key Determinants

article en

Abstract

For peer review purposes only. The dataset contains the supplementary information (SI) data files associated with the study, including the initial and final atomic coordinates of all simulated systems (high-mannose, hybrid, and complex type N-glycans). The archive also includes the molecular dynamics parameter (.mdp) file used to generate the trajectories.

Zenodo (CERN European Organization for Nuclear Research)
Central Salt and Marine Chemicals Research Institute (IN)
Openalex Percentile: Top 42%
Glycosylation and Glycoproteins Research
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Revealing Griffithsin Recognition of Diverse Virus-Associated N-glycans using Atomistic Simulations: Glycan Composition and Branching Pattern are Key Determinants · Zenodo (CERN European Organization for Nuclear Research) (2025) | TGRS Research Map | TGRS