ReviewAnnual review of biophysics and biomolecular structure2003
Nucleic acid recognition by OB-fold proteins.
Review in Annual review of biophysics and biomolecular structure, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 276 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
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
276 citing papers in PubMed, 494 citations in OpenAlex.
- A direct protein bridge connects the ds and ds-ss junction telomeric DNA segments inScience advances · 2026Article
- Hemizygous loss-of-function variants of EIF1AX are associated with a syndromic neurodevelopmental disorder.European journal of human genetics : EJHG · 2026Article
- Snapshots of Motion: A Novel Structural Intermediate Reveals Conserved Dynamics in Archaeal DNA Ligases.Proteins · 2026Article
- KREPA6 functions in RNA editing catalytic complex structural organization and gRNA utilization in Trypanosoma brucei.Nucleic acids research · 2026Article
- An integrative structural biology approach reveals the dynamic organization of the R2SP quaternary chaperone complex.Nature communications · 2026Article
- caRBP-Pred: Leveraging Protein Language Models for the Prediction of Chromatin-Associated RNA-Binding Proteins.Computational and structural biotechnology journal · 2026Article
- RNA-Binding Proteins in Dinoflagellates.International journal of molecular sciences · 2026Review
- Two OB-fold proteins from a Gram-positive conjugative element engage in relaxosome assembly and DNA processing.Nucleic acids research · 2025Article
- Staphylococcal nuclease and tudor domain-containing protein 1: An emerging therapeutic target in cancer (Review).Molecular and clinical oncology · 2025Review
- AIM2 and IFI16 as nucleic acid sensors in Periodontitis-Driven systemic inflammation: emerging evidence and therapeutic implications.Clinical oral investigations · 2025Review
- Bacterial Hachiman complex executes DNA cleavage for antiphage defense.Nature communications · 2025Article
- Structural basis for cooperative ssDNA binding by bacteriophage protein filament P12.Nucleic acids research · 2025Article
- RNA methyltransferase SPOUT1/CENP-32 links mitotic spindle organization with the neurodevelopmental disorder SpADMiSS.Nature communications · 2025Article
- Impact of ions, pH and the nature of substrate on the structure and activity of a robust single-stranded DNA binding (SSB)-like protein from Phi11.Archives of microbiology · 2025Article
- Diverse single-stranded nucleic acid binding proteins enable both stable protection and rapid exchange required for biological function.QRB discovery · 2025Article
- Structural and functional insights into the interaction between the bacteriophage T4 DNA processing proteins gp32 and Dda.Nucleic acids research · 2024Article
- The Last Universal Common Ancestor of Ribosome-Encoding Organisms: Portrait of LUCA.Journal of molecular evolution · 2024Review
- Protein Fold Usages in Ribosomes: Another Glance to the Past.International journal of molecular sciences · 2024Article
- PrgE: an OB-fold protein from plasmid pCF10 with striking differences to prototypical bacterial SSBs.Life science alliance · 2024Article
- Structural basis of tRNA recognition by the widespread OB fold.Nature communications · 2024Article
216 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
3 authors at 1 institution in 1 country.
Funding
Abstract
The OB-fold domain is a compact structural motif frequently used for nucleic acid recognition. Structural comparison of all OB-fold/nucleic acid complexes solved to date confirms the low degree of sequence similarity among members of this family while highlighting several structural sequence determinants common to most of these OB-folds. Loops connecting the secondary structural elements in the OB-fold core are extremely variable in length and in functional detail. However, certain features of ligand binding are conserved among OB-fold complexes, including the location of the binding surface, the polarity of the nucleic acid with respect to the OB-fold, and particular nucleic acid-protein interactions commonly used for recognition of single-stranded and unusually structured nucleic acids. Intriguingly, the observation of shared nucleic acid polarity may shed light on the longstanding question concerning OB-fold origins, indicating that it is unlikely that members of this family arose via convergent evolution.
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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.