ReviewVirology2015
Nature's favorite building block: Deciphering folding and capsid assembly of proteins with the HK97-fold.
Review in Virology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 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
84 citing papers in PubMed, 135 citations in OpenAlex.
- Small viruses reveal bidirectional evolution between HK97-fold viruses and encapsulins via procapsids.Nature communications · 2026Article
- Cryo-EM structure of bacteriophage Nocturne116: insights into the architecture of c2-likeJournal of virology · 2026Article
- Many paths, similar destinations: viruses and bacterial microcompartments form polyhedra inside cells.Journal of virology · 2026Review
- Diverse bacterial pattern recognition receptors sense the conserved phage proteome.bioRxiv : the preprint server for biology · 2026Article
- Genomic, Evolutionary and Phenotypic Insights intoViruses · 2025Article
- Insights into the structure and initial host attachment of the flagellotropic bacteriophage 7-7-1.Communications biology · 2025Article
- Cryo-EM resolves the structure of the archaeal dsDNA virus HFTV1 from head to tail.Science advances · 2025Article
- Review
- A Two-Component Pseudo-Icosahedral Protein Nanocompartment with Variable Shell Composition and Irregular Tiling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Highly stable bacteriophages PIN1 and PIN2 have hallmarks of flagellotropic phages but infect immotile bacteria.Npj viruses · 2025Article
- High-Fidelity In Vitro Packaging of Diverse Synthetic Cargo into Encapsulin Protein Cages.Angewandte Chemie (International ed. in English) · 2025Article
- Stabilization mechanism accommodating genome length variation in evolutionarily related viral capsids.Nature communications · 2025Article
- Mystique, a broad host range Acinetobacter phage, reveals the impact of culturing conditions on phage isolation and infectivity.PLoS pathogens · 2025Article
- Phi29 assembly intermediates reveal how scaffold interactions with capsid protein drive capsid construction and maturation.Science advances · 2025Article
- The nucleocapsid architecture and structural atlas of the prototype baculovirus define the hallmarks of a new viral realm.Science advances · 2024Article
- The Structural Diversity of Encapsulin Protein Shells.Chembiochem : a European journal of chemical biology · 2024Review
- Structure and replication of Pseudomonas aeruginosa phage JBD30.The EMBO journal · 2024Article
- Point mutation in a virus-like capsid drives symmetry reduction to form tetrahedral cages.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structural basis for peroxidase encapsulation inside the encapsulin from the Gram-negative pathogen Klebsiella pneumoniae.Nature communications · 2024Article
- A widespread bacterial protein compartment sequesters and stores elemental sulfur.Science advances · 2024Article
24 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
For many (if not all) bacterial and archaeal tailed viruses and eukaryotic Herpesvirdae the HK97-fold serves as the major architectural element in icosahedral capsid formation while still enabling the conformational flexibility required during assembly and maturation. Auxiliary proteins or Δ-domains strictly control assembly of multiple, identical, HK97-like subunits into procapsids with specific icosahedral symmetries, rather than aberrant non-icosahedral structures. Procapsids are precursor structures that mature into capsids in a process involving release of auxiliary proteins (or cleavage of Δ-domains), dsDNA packaging, and conformational rearrangement of the HK97-like subunits. Some coat proteins built on the ubiquitous HK97-fold also have accessory domains or loops that impart specific functions, such as increased monomer, procapsid, or capsid stability. In this review, we analyze the numerous HK97-like coat protein structures that are emerging in the literature (over 40 at time of writing) by comparing their topology, additional domains, and their assembly and misassembly reactions.
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.