ArticleActa crystallographica. Section F, Structural biology communications2020
Structure of the AAVhu.37 capsid by cryoelectron microscopy.
Article in Acta crystallographica. Section F, Structural biology communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed.
- Directed evolution of liver-detargeted AAV vectors for systemic gene delivery to skeletal muscle and heart.Molecular therapy. Methods & clinical development · 2025Article
- The amazing AAV capsids: Into the structure-verse.Molecular therapy. Methods & clinical development · 2025Review
- Artificial Intelligence-Based Approaches for AAV Vector Engineering.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Characterization and biodistribution of under-employed gene therapy vector AAV7.Journal of virology · 2023Article
- Structural and antigenic characterization of the avian adeno-associated virus capsid.Journal of virology · 2023Article
- Article
- Cryo-electron Microscopy of Adeno-associated Virus.Chemical reviews · 2022Review
- Characterization of the Serpentine Adeno-Associated Virus (SAAV) Capsid Structure: Receptor Interactions and Antigenicity.Journal of virology · 2022Article
- Structural Study of Aavrh.10 Receptor and Antibody Interactions.Journal of virology · 2021Article
- Adeno-associated virus capsid assembly is divergent and stochastic.Nature communications · 2021Article
- Completion of the AAV Structural Atlas: Serotype Capsid Structures Reveals Clade-Specific Features.Viruses · 2021Article
- Characterization of AAV-Specific Affinity Ligands: Consequences for Vector Purification and Development Strategies.Molecular therapy. Methods & clinical development · 2020Article
- Structural characterization of a bat Adeno-associated virus capsid.Journal of structural biology · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Adeno-associated viruses (AAVs) are used as in vivo gene-delivery vectors in gene-therapy products and have been heavily investigated for numerous indications. Over 100 naturally occurring AAV serotypes and variants have been isolated from primate samples. Many reports have described unique properties of these variants (for instance, differences in potency, target cell or evasion of the immune response), despite high amino-acid sequence conservation. AAVhu.37 is of interest for clinical applications owing to its proficient transduction of the liver and central nervous system. The sequence identity of the AAVhu.37 VP1 to the well characterized AAVrh.10 serotype, for which no structure is available, is greater than 98%. Here, the structure of the AAVhu.37 capsid at 2.56 Å resolution obtained via single-particle cryo-electron microscopy is presented.
Indexed as
Identifiers
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.