ReviewGenes to cells : devoted to molecular & cellular mechanisms2022
The structure-function analysis of Obg-like GTPase proteins along the evolutionary tree from bacteria to humans.
Review in Genes to cells : devoted to molecular & cellular mechanisms, 2022. 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.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Intracellular microbial shifts during COVID-19 infection and longitudinal recovery revealed by single-cell RNA sequencing.iScience · 2026Article
- Ribosomal allostery as a potential regulator of bacterial dormancy.Nature communications · 2026Article
- Enterococcus faecalis Extracellular Vesicles Deliver the Bacterial GTPase Obg to Hijack mTOR Signalling in Hepatocellular Carcinoma.Journal of extracellular vesicles · 2026Article
- Regulation of RNA-binding proteins by small biomolecules.Nature reviews. Molecular cell biology · 2026Review
- Ectopic overexpression and CRISPRi-based knockdown ofJournal of bacteriology · 2025Article
- Recent Advances in Bacterial Persistence Mechanisms.International journal of molecular sciences · 2023Review
- YbiB: a novel interactor of the GTPase ObgE.Nucleic acids research · 2023Article
- The structure-function analysis of Obg-like GTPase proteins along the evolutionary tree from bacteria to humans.Genes to cells : devoted to molecular & cellular mechanisms · 2022Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Obg proteins belong to P-loop guanine triphosphatase (GTPase) that are conserved from bacteria to humans. Like other GTPases, Obg cycles between guanine triphosphate (GTP) bound "on" state and guanine diphosphate (GDP)-bound "off" state, thereby controlling various cellular processes. Different members of this group have unique structural characteristics; a conserved glycine-rich N-terminal domain known as obg fold, a central conserved nucleotide binding domain, and a less conserved C-terminal domain of other functions. Obg is a ribosome dependent GTPase helps in ribosome maturation by interacting with several proteins of the 50S subunit of the ribosome. Obg proteins have been widely considered as a regulator of cellular functions, helping in DNA replication, cell division. Apart from that, this protein also takes part in various stress adaptation pathways like a stringent response, sporulation, and general stress response. In this particular review, the structural features of ObgE have been highlighted and how the structure plays important role in interacting with regulators like GTP, ppGpp that are crucial for executing biological function has been orchestrated. In particular, we believe that Obg-like proteins can provide a link between different global pathways that are necessary for fine-tuning cellular processes to maintain the cellular energy status.
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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.