ArticleBiology direct2017
Cellular origin of the viral capsid-like bacterial microcompartments.
Article in Biology direct, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
The trial behind it
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Microcompartments in archaeal ancestors of eukaryotes: a bioenergetic engine that could have fuelled eukaryogenesis.bioRxiv : the preprint server for biology · 2025Article
- An invariant C-terminal tryptophan in McdB mediates its interaction and positioning function with carboxysomes.Molecular biology of the cell · 2024Article
- Modeling bacterial microcompartment architectures for enhanced cyanobacterial carbon fixation.Frontiers in plant science · 2024Review
- Trajectories for the evolution of bacterial COProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Variety of size and form of GRM2 bacterial microcompartment particles.Protein science : a publication of the Protein Society · 2021Article
- A Place for Viruses on the Tree of Life.Frontiers in microbiology · 2020Review
- Origin of viruses: primordial replicators recruiting capsids from hosts.Nature reviews. Microbiology · 2019Review
- Ancestrality and Mosaicism of Giant Viruses Supporting the Definition of the Fourth TRUC of Microbes.Frontiers in microbiology · 2018Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
ᅟ: Bacterial microcompartments (BMC) are proteinaceous organelles that structurally resemble viral capsids, but encapsulate enzymes that perform various specialized biochemical reactions in the cell cytoplasm. The BMC are constructed from two major shell proteins, BMC-H and BMC-P, which form the facets and vertices of the icosahedral assembly, and are functionally equivalent to the major and minor capsid proteins of viruses, respectively. This equivalence notwithstanding, neither of the BMC proteins displays structural similarity to known capsid proteins, rendering the origins of the BMC enigmatic. Here, using structural and sequence comparisons, we show that both BMC-H and BMC-P, most likely, were exapted from bona fide cellular proteins, namely, PII signaling protein and OB-fold domain-containing protein, respectively. This finding is in line with the hypothesis that many major viral structural proteins have been recruited from cellular proteomes. REVIEWERS: This article was reviewed by Igor Zhulin, Jeremy Selengut and Narayanaswamy Srinivasan. For complete reviews, see the Reviewers' reports section.
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.