Evidence map›Paper›PMID 16207353›Full record

ArticleGenome biology2005

Sequence and structural analysis of BTB domain proteins.

Peter J Stogios, Gregory S Downs, Jimmy J S Jauhal, Sukhjeen K Nandra, Gilbert G Privé

Open access · goldAbstract read
In one paragraph

Article in Genome biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 360 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
360citing papers in PubMed, 1 pooled it
9.8field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

360 citing papers in PubMed, 1 synthesis or guideline pooled it, 692 citations in OpenAlex.

  1. Putative Animal Models of Restless Legs Syndrome: A Systematic Review and Evaluation of Their Face and Construct Validity.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2023
    Pooled it
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  16. International journal of molecular sciences · 2025
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300 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Peter J StogiosDepartment of Medical Biophysics, University of Toronto, Toronto, Ontario, M5G 2M9, Canada. pstogios@uhnres.utoronto.ca
Gregory S Downs
Jimmy J S Jauhal
Sukhjeen K Nandra
Gilbert G Privé
University of Toronto · CAOntario Institute for Cancer Research · CASeneca Polytechnic · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe BTB domain (also known as the POZ domain) is a versatile protein-protein interaction motif that participates in a wide range of cellular functions, including transcriptional regulation, cytoskeleton dynamics, ion channel assembly and gating, and targeting proteins for ubiquitination. Several BTB domain structures have been experimentally determined, revealing a highly conserved core structure.

resultsWe surveyed the protein architecture, genomic distribution and sequence conservation of BTB domain proteins in 17 fully sequenced eukaryotes. The BTB domain is typically found as a single copy in proteins that contain only one or two other types of domain, and this defines the BTB-zinc finger (BTB-ZF), BTB-BACK-kelch (BBK), voltage-gated potassium channel T1 (T1-Kv), MATH-BTB, BTB-NPH3 and BTB-BACK-PHR (BBP) families of proteins, among others. In contrast, the Skp1 and ElonginC proteins consist almost exclusively of the core BTB fold. There are numerous lineage-specific expansions of BTB proteins, as seen by the relatively large number of BTB-ZF and BBK proteins in vertebrates, MATH-BTB proteins in Caenorhabditis elegans, and BTB-NPH3 proteins in Arabidopsis thaliana. Using the structural homology between Skp1 and the PLZF BTB homodimer, we present a model of a BTB-Cul3 SCF-like E3 ubiquitin ligase complex that shows that the BTB dimer or the T1 tetramer is compatible in this complex.

conclusionDespite widely divergent sequences, the BTB fold is structurally well conserved. The fold has adapted to several different modes of self-association and interactions with non-BTB proteins.

Indexed as

Sequence Analysis, ProteinAmino Acid SequenceAnimalsDNA-Binding ProteinsGenomeModels, MolecularMolecular Sequence DataPhylogenyProtein BindingProtein FoldingProtein Structure, TertiarySequence Analysis, DNAZinc FingersDNA-Binding Proteins

Identifiers

PMID16207353
PMCPMC1257465
OpenAlexW2159956236

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.