ArticleThe EMBO journal2001
Atomic structure of the major capsid protein of rotavirus: implications for the architecture of the virion.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 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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Who cites it
91 citing papers in PubMed, 201 citations in OpenAlex.
- Development and Validation of an Antigen-Capture ELISA for Quantitative Detection of Donkey-Origin Rotavirus: Application in Vaccine Manufacturing Process Monitoring.Microorganisms · 2026Article
- Partial nucleotide sequence analysis of the VP6 gene from rotavirus species A, D, and F identified in diarrheic broiler chickens.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026Article
- Development of MoSLife (Basel, Switzerland) · 2026Article
- Evaluating the Structural Stability of Recombinant Rotavirus Capsid Protein VP6 in Altered Physicochemical States Using Fluorescence and CD Spectroscopy.The protein journal · 2026Article
- Structural diversity and conservation among CRESS-DNA bacilladnaviruses revealed through cryo-EM and computational modelling.Virology journal · 2025Article
- TREM-1 Interacts with Rotavirus Proteins and Drives Inflammatory Responses: A Combined Experimental and Computational Approach.Pathogens (Basel, Switzerland) · 2025Article
- Structural determinants of rotavirus proteolytic activation.PLoS pathogens · 2025Article
- Generation of single-round infectious rotavirus with a mutation in the intermediate capsid protein VP6.Journal of virology · 2024Article
- Spectroscopic analysis of the bacterially expressed head domain of rotavirus VP6.Bioscience reports · 2024Article
- MAXIMUM LIKELIHOOD FOR HIGH-NOISE GROUP ORBIT ESTIMATION AND SINGLE-PARTICLE CRYO-EM.Annals of statistics · 2024Article
- Review
- The structure of a 12-segmented dsRNA reovirus: New insights into capsid stabilization and organization.PLoS pathogens · 2023Article
- Strain-Specific Interactions between the Viral Capsid Proteins VP4, VP7 and VP6 Influence Rescue of Rotavirus Reassortants by Reverse Genetics.International journal of molecular sciences · 2023Article
- Article
- Reverse genetic engineering of simian rotaviruses with temperature-sensitive lesions in VP1, VP2, and VP6.Virus research · 2021Article
- Review
- Article
- Expression of influenza A virus-derived peptides on a rotavirus VP6-based delivery platform.Archives of virology · 2021Article
- Reverse Genetics Approach for Developing Rotavirus Vaccine Candidates Carrying VP4 and VP7 Genes Cloned from Clinical Isolates of Human Rotavirus.Journal of virology · 2020Article
- Understanding the penetrance of intrinsic protein disorder in rotavirus proteome.International journal of biological macromolecules · 2020Article
31 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The structural protein VP6 of rotavirus, an important pathogen responsible for severe gastroenteritis in children, forms the middle layer in the triple-layered viral capsid. Here we present the crystal structure of VP6 determined to 2 A resolution and describe its interactions with other capsid proteins by fitting the atomic model into electron cryomicroscopic reconstructions of viral particles. VP6, which forms a tight trimer, has two distinct domains: a distal beta-barrel domain and a proximal alpha-helical domain, which interact with the outer and inner layer of the virion, respectively. The overall fold is similar to that of protein VP7 from bluetongue virus, with the subunits wrapping about a central 3-fold axis. A distinguishing feature of the VP6 trimer is a central Zn(2+) ion located on the 3-fold molecular axis. The crude atomic model of the middle layer derived from the fit shows that quasi-equivalence is only partially obeyed by VP6 in the T = 13 middle layer and suggests a model for the assembly of the 260 VP6 trimers onto the T = 1 viral inner layer.
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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.