ArticleThe Journal of biological chemistry2015
Structural Characterization of Bardet-Biedl Syndrome 9 Protein (BBS9).
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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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
14 citing papers in PubMed, 22 citations in OpenAlex.
- Identifying Significant SNPs of the Total Number of Piglets Born and Their Relationship with Leg Bumps in Pigs.Biology · 2024Article
- Organization, functions, and mechanisms of the BBSome in development, ciliopathies, and beyond.eLife · 2023Review
- Next-Generation Sequencing of a Large Gene Panel for Outcome Prediction of Bariatric Surgery in Patients with Severe Obesity.Journal of clinical medicine · 2022Article
- A Novel BBS9 Mutation Identified via Whole-Exome Sequencing in a Chinese Family with Bardet-Biedl Syndrome.BioMed research international · 2021Article
- The BBSome assembly is spatially controlled by BBS1 and BBS4 in human cells.The Journal of biological chemistry · 2020Article
- Structure of the yeast Swi/Snf complex in a nucleosome free state.Nature communications · 2020Article
- Structure of the human BBSome core complex.eLife · 2020Article
- Article
- Molecular architecture of the Bardet-Biedl syndrome protein 2-7-9 subcomplex.The Journal of biological chemistry · 2019Article
- The Molecular Architecture of Native BBSome Obtained by an Integrated Structural Approach.Structure (London, England : 1993) · 2019Article
- Trafficking of ciliary membrane proteins by the intraflagellar transport/BBSome machinery.Essays in biochemistry · 2018Review
- Article
- BBS1 is involved in retrograde trafficking of ciliary GPCRs in the context of the BBSome complex.PloS one · 2018Article
- Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The Bardet-Biedl syndrome protein complex (BBSome) is an octameric complex that transports membrane proteins into the primary cilium signaling organelle in eukaryotes and is implicated in human disease. Here we have analyzed the 99-kDa human BBS9 protein, one of the eight BBSome components. The protein is composed of four structured domains, including a β-stranded N-terminal domain. The 1.8 Å crystal structure of the 46-kDa N-terminal domain reveals a seven-bladed β-propeller. A structure-based homology search suggests that it functions in protein-protein interactions. We show that the Bardet-Biedl syndrome-causing G141R mutation in BBS9 likely results in misfolding of the β-propeller. Although the C-terminal half of BBS9 dimerizes in solution, the N-terminal domain only does so in the crystal lattice. This C-terminal dimerization interface might be important for the assembly of the BBSome.
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