The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Comprehensive Research Report: BBS10 (Bardet-Biedl Syndrome 10 Protein)

Gene Identity and Classification

BBS10 (UniProt: Q8TAM1) encodes the Bardet-Biedl syndrome 10 protein in Homo sapiens (human) (gupta2022bardet–biedlsyndromethe pages 1-2). This protein is also known by its chromosomal designation C12orf58 and belongs to the TCP-1 chaperonin family, specifically classified within the group II chaperonins related to the CCT/TRiC (chaperonin containing TCP-1/T-complex protein-1 ring complex) family (gupta2022bardet–biedlsyndromethe pages 3-4, tian2023organizationfunctionsand pages 5-6, alvarezsatta2017bardetbiedlsyndromeas pages 2-3). The protein contains key InterPro domains including BBS10 (IPR042619), Cpn60/GroEL/TCP-1 (IPR002423), GroEL-like apical domain superfamily (IPR027409), GroEL-like equatorial superfamily (IPR027413), and TCP-1-like intermediate superfamily (IPR027410), confirming its chaperonin-like architecture (gupta2022bardet–biedlsyndromethe pages 1-2).

Molecular Function and Primary Role

BBSome Assembly Function

The primary molecular function of BBS10 is to mediate BBSome assembly through a chaperonin-like mechanism (zhang2012intrinsicproteinproteininteractionmediated pages 1-2, seo2010bbs6bbs10and pages 1-2). BBS10 is not itself a component of the mature BBSome—the octameric protein complex comprising BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9, and BBS18/BBIP1 that regulates ciliary membrane protein trafficking (tian2023organizationfunctionsand pages 1-2, tian2023organizationfunctionsand pages 5-6). Instead, BBS10 functions as part of a specialized BBS/CCT assembly machinery required for BBSome biogenesis (tian2023organizationfunctionsand pages 6-7, seo2010bbs6bbs10and pages 1-2).

BBS10 forms a higher-order complex with two other chaperonin-like BBS proteins, BBS6/MKKS and BBS12, together with six canonical CCT chaperonin subunits (CCT1, CCT2, CCT3, CCT4, CCT5, and CCT8) (seo2010bbs6bbs10and pages 2-3, seo2010bbs6bbs10and pages 1-2). This BBS/CCT complex functions as the assembly platform for the BBSome. Landmark studies by Seo et al. (2010) demonstrated through sequential affinity purification and size exclusion chromatography that BBS6, BBS10, and BBS12 associate with CCT/TRiC family chaperonins to form a complex essential for BBSome assembly (seo2010bbs6bbs10and pages 1-2). In Bbs6 null mouse tissues, BBSome subunits fail to properly associate with each other and show aberrant elution profiles, demonstrating that the chaperonin-like BBS proteins are required for BBSome formation (seo2010bbs6bbs10and pages 2-3).

Mechanism of Action in BBSome Assembly

The assembly mechanism operates through a stepwise process where BBS10 and its partners act as a substrate-binding unit that regulates BBS7 stability (tian2023organizationfunctionsand pages 6-7, zhang2012intrinsicproteinproteininteractionmediated pages 1-2). The BBS/CCT complex promotes BBS7 stabilization and facilitates its productive association with BBS2 to form the critical BBS2-BBS7-BBS9 core complex, which serves as the assembly intermediate upon which other BBSome subunits (BBS1, BBS4, BBS5, and BBS8) are subsequently recruited (tian2023organizationfunctionsand pages 6-7, zhang2012intrinsicproteinproteininteractionmediated pages 1-2). Zhang et al. (2012) demonstrated through characterization of BBSome assembly intermediates that the BBS-chaperonin complex plays a role in BBS7 stability, and that BBS7 interacts with BBS2 to become part of the BBSome core complex before additional subunits are incorporated (zhang2012intrinsicproteinproteininteractionmediated pages 1-2).

BBS10 is positioned functionally upstream in the assembly pathway, acting before or during the transition from the BBS-chaperonin complex to the BBS2-BBS7-BBS9 core intermediate (tian2023organizationfunctionsand pages 5-6, tian2023organizationfunctionsand pages 6-7). Recent work has also identified post-translational regulation of BBSome assembly, including ubiquitylation events that affect BBSome stability and function (tian2023organizationfunctionsand pages 2-3).

Protein Structure and Domains

Chaperonin-Like Architecture

BBS10 possesses the canonical chaperonin domain architecture consisting of three functional domains: apical, intermediate, and equatorial (gupta2022bardet–biedlsyndromethe pages 5-6, alvarezsatta2017bardetbiedlsyndromeas pages 1-2). This structure is characteristic of group II chaperonins, where the apical domain typically mediates substrate interactions, the intermediate domain connects structural elements, and the equatorial domain in canonical chaperonins harbors ATP-binding and hydrolysis functions (gupta2022bardet–biedlsyndromethe pages 5-6). BBS10 protein contains ~694 amino acids in the human sequence.

Divergence from Classical Chaperonin Function

Despite structural homology to the CCT family of group II chaperonins, BBS10 has diverged functionally and does not exhibit validated classical chaperonin activity (gupta2022bardet–biedlsyndromethe pages 3-4, tian2023organizationfunctionsand pages 6-7, alvarezsatta2017bardetbiedlsyndromeas pages 1-2). Key differences include:

1. Lack of conserved ATP-binding motifs: While canonical CCT chaperonins mediate protein folding in an ATP-dependent manner through coordinated ATP binding and hydrolysis, BBS6 and BBS12 do not contain conserved ATP-binding motifs, and the ATPase activity of BBS10 has not been validated (gupta2022bardet–biedlsyndromethe pages 3-4, tian2023organizationfunctionsand pages 6-7, alvarezsatta2017bardetbiedlsyndromeas pages 1-2).

2. Specialized substrate specificity: Rather than functioning as a general protein-folding machine, BBS10 acts specifically as part of the substrate-binding unit for BBSome assembly, particularly targeting BBS7 stabilization (tian2023organizationfunctionsand pages 6-7).

3. No autonomous chaperonin activity: The protein folding activity of the BBS/CCT complex is accomplished through the incorporated canonical CCT chaperonins rather than through intrinsic enzymatic activity of BBS10 itself (tian2023organizationfunctionsand pages 6-7, alvarezsatta2017bardetbiedlsyndromeas pages 1-2).

This functional specialization positions BBS10 as a chaperonin-like assembly factor rather than a classical ATP-dependent molecular chaperone (alvarezsatta2017bardetbiedlsyndromeas pages 1-2, alvarezsatta2017bardetbiedlsyndromeas pages 2-3).

Subcellular Localization

BBS10 localizes primarily to the basal body and pericentriolar region of ciliated cells (gupta2022bardet–biedlsyndromethe pages 2-3, gupta2022bardet–biedlsyndromethe pages 5-6). Unlike core BBSome components that traffic along the cilium during intraflagellar transport (IFT), chaperonin-like BBS proteins including BBS10 are generally not detected along the primary cilium itself but are instead restricted to the ciliary base and cytoplasmic compartments where BBSome assembly is coordinated (gupta2022bardet–biedlsyndromethe pages 2-3). BBS10 protein has been detected at the basal body in ciliated inner medullary collecting duct (IMCD) cells, though low endogenous protein levels have made comprehensive subcellular localization studies challenging (gupta2022bardet–biedlsyndromethe pages 5-6).

The pericentriolar localization is consistent with BBS10's role in BBSome assembly, which occurs in the cytoplasm and at centriolar satellites before the mature BBSome is recruited to the ciliary base for subsequent ciliary targeting (tian2023organizationfunctionsand pages 6-7, tian2023organizationfunctionsand pages 7-9, seo2010bbs6bbs10and pages 1-2). The spatial separation between BBS10 function (assembly at the basal body/pericentriolar zone) and BBSome function (ciliary membrane trafficking) reflects the temporal sequence of BBSome biogenesis and deployment.

Cellular Pathways and Biological Processes

Ciliary Trafficking Pathway

BBS10 participates in the ciliary trafficking pathway indirectly by enabling assembly of the BBSome, which acts as a cargo adapter for ciliary membrane protein transport (tian2023organizationfunctionsand pages 1-2, singh2020structureandactivation pages 1-2, wingfield2018traffickingofciliary pages 1-2). The mature BBSome functions as an adaptor complex that recognizes ciliary targeting sequences on membrane proteins, particularly G-protein-coupled receptors (GPCRs), and links them to the intraflagellar transport (IFT) machinery for regulated entry into and exit from cilia (singh2020structureandactivation pages 1-2, wingfield2018traffickingofciliary pages 1-2, chou2019themoleculararchitecture pages 1-3).

The BBSome cycles through cilia via association with IFT trains, which are propelled by molecular motors (kinesin-2 for anterograde transport to the ciliary tip, dynein-2 for retrograde transport back to the cell body) along the ciliary microtubule axoneme (wingfield2018traffickingofciliary pages 1-2). Recent evidence indicates the BBSome primarily functions in the removal of specific transmembrane and peripheral membrane proteins from cilia, acting as a cargo adapter for ciliary export (wingfield2018traffickingofciliary pages 1-2). By ensuring proper BBSome formation, BBS10 indirectly enables these ciliary trafficking functions.

Signaling Pathways Regulated Through BBSome Function

Through its role in BBSome assembly, BBS10 impacts multiple ciliary signaling pathways:

1. Hedgehog signaling: The BBSome regulates ciliary localization of Hedgehog pathway components including GPR161 and Smoothened (SMO). Loss of BBS proteins leads to ciliary dislocation of hedgehog signaling components, accounting for developmental defects and polydactyly phenotypes in BBS (tian2023organizationfunctionsand pages 2-3, tian2023organizationfunctionsand pages 1-2).

2. GPCR signaling: The BBSome controls ciliary trafficking of multiple GPCRs including neuropeptide Y receptor 2 (NPY2R), serotonin receptor 5-HT2CR, and leptin receptor. Mislocalization of these receptors in hypothalamic neurons may contribute to hyperphagia and obesity in BBS (tian2023organizationfunctionsand pages 2-3).

3. Photoreceptor homeostasis: In retinal photoreceptors, the BBSome is essential for maintaining proper protein and lipid composition of the outer segment, which is a specialized ciliary structure. BBS defects lead to rhodopsin mislocalization and photoreceptor apoptosis, causing retinal degeneration (tian2023organizationfunctionsand pages 2-3).

Emerging Non-Ciliary Roles

Recent studies suggest BBS10 may have additional pleiotropic roles beyond BBSome assembly (gupta2022bardet–biedlsyndromethe pages 7-8, gupta2022bardet–biedlsyndromethe pages 6-7):

1. Insulin signaling: BBS10 has been shown to participate in insulin signaling through direct interaction with the insulin receptor. Human mutant fibroblasts with BBS10 deficiency show impaired insulin signaling, with more severe defects than BBS1 mutations (gupta2022bardet–biedlsyndromethe pages 6-7). BBS10 co-immunoprecipitates with the insulin receptor, and BBS10 mutations decrease insulin receptor autophosphorylation (gupta2022bardet–biedlsyndromethe pages 6-7).

2. Leptin signaling: Leptin signaling is deregulated in BBS10-deficient hypothalamic-derived neurons, though whether this reflects impaired leptin receptor trafficking via BBSome abnormalities or direct regulation of leptin receptor stability by BBS10 remains unclear (gupta2022bardet–biedlsyndromethe pages 6-7).

3. Adipogenesis: BBS10 has been implicated in regulation of adipogenesis and metabolic processes, contributing to the obesity phenotype in BBS (tian2023organizationfunctionsand pages 2-3, gupta2022bardet–biedlsyndromethe pages 7-8).

These emerging non-ciliary functions require further validation but suggest BBS10 may have evolved additional roles beyond its primary BBSome assembly function.

Disease Relevance: Bardet-Biedl Syndrome

Genetic Contribution and Clinical Significance

BBS10 is one of the most important genes mutated in Bardet-Biedl syndrome (BBS; OMIM #209900), a rare autosomal recessive ciliopathy (alvarezsatta2017bardetbiedlsyndromeas pages 2-3). BBS10 alone accounts for approximately 20% of molecularly diagnosed BBS cases, making it second only to BBS1 (~28% of cases) in mutational frequency (tian2023organizationfunctionsand pages 5-6, alvarezsatta2017bardetbiedlsyndromeas pages 2-3). Together with BBS6/MKKS and BBS12, the three chaperonin-like BBS genes account for over 30% of the total BBS mutational burden, highlighting the critical importance of the BBSome assembly machinery in disease pathogenesis (gupta2022bardet–biedlsyndromethe pages 2-3, alvarezsatta2017bardetbiedlsyndromeas pages 2-3).

This high mutational burden is particularly striking given the extensive genetic heterogeneity of BBS, with 21-26 genes now identified (tian2023organizationfunctionsand pages 1-2, alvarezsatta2017bardetbiedlsyndromeas pages 2-3). The mutational frequency varies by population; for example, BBS10 accounts for 43% of cases in Danish cohorts but only 8.3% in Spanish cohorts, while showing the typical ~20% frequency in multiethnic cohorts (alvarezsatta2017bardetbiedlsyndromeas pages 2-3).

Pathogenic Variants

Approximately 100 different disease-causing variants in BBS10 have been reported, including nonsense, frameshift, missense, and splice site mutations distributed throughout the gene (gupta2022bardet–biedlsyndromethe pages 5-6, alvarezsatta2017bardetbiedlsyndromeas pages 2-3). A recurrent pathogenic allele in populations of European descent is p.Cys91Leufs*5, reaching 26-48% frequency among BBS10 mutations in these populations (alvarezsatta2017bardetbiedlsyndromeas pages 2-3). Truncating mutations affecting the intermediate and equatorial domains are predicted to disrupt regions classically responsible for ATP binding and protein interaction in canonical chaperonins, likely ablating BBS10's assembly function (gupta2022bardet–biedlsyndromethe pages 5-6).

Genotype-Phenotype Correlations

BBS families with pathogenic variants in chaperonin-like BBS genes (BBS6, BBS10, or BBS12) generally display more severe phenotypes than families with mutations in core BBSome component genes (tian2023organizationfunctionsand pages 5-6, alvarezsatta2017bardetbiedlsyndromeas pages 1-2, alvarezsatta2017bardetbiedlsyndromeas pages 2-3). Key features include:

1. Earlier disease onset: BBS10 patients particularly show earlier presentation of symptoms (alvarezsatta2017bardetbiedlsyndromeas pages 2-3).

2. Greater prevalence of primary features: Higher frequency of all six primary diagnostic features of BBS: retinal dystrophy, obesity, polydactyly, cognitive impairment, hypogonadism, and renal anomalies (alvarezsatta2017bardetbiedlsyndromeas pages 2-3).

3. Severe renal involvement: Chaperonin-like BBS gene mutations correlate with more severe kidney impairment (gupta2022bardet–biedlsyndromethe pages 3-4).

4. Overlapping ciliopathy features: Higher frequency of features overlapping with other ciliopathies, particularly McKusick-Kaufman syndrome (MKKS) and Alström syndrome (alvarezsatta2017bardetbiedlsyndromeas pages 2-3).

The mechanistic basis for increased severity likely relates to the fact that mutations in chaperonin-like BBS proteins completely block BBSome assembly, preventing formation of any functional complexes, whereas mutations in individual BBSome subunits may allow accumulation of partially functional assembly intermediates that retain residual activity (alvarezsatta2017bardetbiedlsyndromeas pages 2-3).

Clinical Features of Bardet-Biedl Syndrome

BBS is characterized by the following primary features (tian2023organizationfunctionsand pages 1-2):

• Retinal degeneration (94% prevalence): Rod-cone dystrophy leading to progressive vision loss and blindness
• Obesity (89%): Truncal obesity typically developing in early childhood
• Postaxial polydactyly (79%): Extra digits on hands and/or feet
• Renal anomalies (52%): Structural kidney defects and progressive renal dysfunction
• Cognitive impairment (66%): Learning disabilities and developmental delays
• Hypogonadism: Particularly in males

Secondary features include diabetes mellitus, hypertension, dental anomalies, congenital heart disease, and hepatic fibrosis (tian2023organizationfunctionsand pages 1-2). Diagnosis requires either four primary features or three primary plus two secondary features (tian2023organizationfunctionsand pages 1-2).

Evolutionary and Structural Insights

Chaperonin Family Membership

BBS10 belongs to the evolutionarily ancient group II chaperonin superfamily, which includes the eukaryotic CCT/TRiC complex (gupta2022bardet–biedlsyndromethe pages 3-4, tian2023organizationfunctionsand pages 5-6, alvarezsatta2017bardetbiedlsyndromeas pages 2-3). Canonical CCT chaperonins form hetero-oligomeric complexes consisting of two stacked rings, each composed of eight radially arranged subunits (CCT1-8), that mediate ATP-dependent protein folding (tian2023organizationfunctionsand pages 5-6). BBS10 has retained the characteristic three-domain chaperonin architecture (apical, intermediate, equatorial) but has undergone neofunctionalization to serve a specialized role in BBSome assembly rather than general protein folding (alvarezsatta2017bardetbiedlsyndromeas pages 1-2, alvarezsatta2017bardetbiedlsyndromeas pages 2-3).

Conservation and Evolution

BBS10 and other chaperonin-like BBS proteins are conserved in organisms with cilia, including vertebrates, but are absent in some ciliated organisms such as Drosophila melanogaster that lack BBS2 and BBS7 and have simplified BBSome complexes (tian2023organizationfunctionsand pages 6-7). This phylogenetic distribution suggests that the BBS/CCT assembly machinery may be most important in organisms with complex, full BBSomes requiring elaborate assembly regulation (tian2023organizationfunctionsand pages 6-7). Alternative BBSome assembly mechanisms must exist in organisms lacking BBS10 homologs (tian2023organizationfunctionsand pages 6-7).

The evolutionary relationship to canonical chaperonins but functional specialization for BBSome assembly represents an interesting example of protein evolution where structural modules are maintained but catalytic functions are lost or modified for new regulatory roles (alvarezsatta2017bardetbiedlsyndromeas pages 2-3).

Current Research Directions and Future Perspectives

Recent Developments (2023-2024)

Recent comprehensive reviews have synthesized current understanding of BBSome organization, functions, and mechanisms (tian2023organizationfunctionsand pages 1-2). Work on ubiquitylation of BBSome subunits has revealed additional layers of post-translational regulation affecting BBSome stability, ciliary assembly, and signaling (tian2023organizationfunctionsand pages 2-3). Clinical perspectives have been updated to reflect growing knowledge of genotype-phenotype correlations and management strategies for BBS patients (Melluso et al. 2023).

Outstanding Questions

Key areas requiring further investigation include:

1. Precise molecular mechanism: The exact biochemical mechanism by which BBS10 and the BBS/CCT complex stabilize BBS7 and promote its association with BBS2 remains incompletely understood at the atomic level.

2. Non-ciliary functions: The emerging roles of BBS10 in insulin/leptin signaling and metabolic regulation require validation and mechanistic characterization to determine if these represent direct functions or downstream consequences of ciliary dysfunction.

3. Therapeutic targeting: Understanding BBS10 function could inform development of chaperonotherapy approaches to stabilize mutant proteins or enhance residual BBSome assembly in patients with hypomorphic alleles.

4. Structural biology: High-resolution structural determination of BBS10 and the BBS/CCT complex would provide atomic-level insights into the assembly mechanism and disease-causing mutations.

Summary

BBS10 (Q8TAM1) is a chaperonin-like protein belonging to the TCP-1/CCT family that serves as a critical component of the BBSome assembly machinery in humans. Its primary molecular function is to mediate BBSome biogenesis through formation of a higher-order complex with BBS6, BBS12, and CCT/TRiC chaperonins that stabilizes BBS7 and promotes formation of the BBS2-BBS7-BBS9 core complex. BBS10 localizes to the basal body and pericentriolar region where BBSome assembly occurs, distinct from the ciliary localization of mature BBSome. By enabling BBSome formation, BBS10 indirectly regulates ciliary membrane protein trafficking, GPCR signaling, hedgehog pathway activity, and photoreceptor homeostasis. Mutations in BBS10 account for ~20% of Bardet-Biedl syndrome cases and are associated with severe, early-onset ciliopathy phenotypes. The protein exemplifies evolutionary adaptation of ancient chaperonin architecture for specialized cellular regulatory functions in ciliary biology.

Table: This table summarizes the main functional, structural, localization, interaction, and disease-related features of human BBS10. It is useful as a compact evidence map linking BBS10’s chaperonin-like TCP-1/CCT ancestry to its experimentally supported role in early BBSome assembly.

References

1. (gupta2022bardet–biedlsyndromethe pages 1-2): Neha Gupta, Mariavittoria D'Acierno, Enrica Zona, Giovambattista Capasso, and Miriam Zacchia. Bardet–biedl syndrome: the pleiotropic role of the chaperonin‐like bbs6, 10, and 12 proteins. American Journal of Medical Genetics. Part C, Seminars in Medical Genetics, 190:9-19, Mar 2022. URL: https://doi.org/10.1002/ajmg.c.31970, doi:10.1002/ajmg.c.31970. This article has 27 citations.

2. (gupta2022bardet–biedlsyndromethe pages 3-4): Neha Gupta, Mariavittoria D'Acierno, Enrica Zona, Giovambattista Capasso, and Miriam Zacchia. Bardet–biedl syndrome: the pleiotropic role of the chaperonin‐like bbs6, 10, and 12 proteins. American Journal of Medical Genetics. Part C, Seminars in Medical Genetics, 190:9-19, Mar 2022. URL: https://doi.org/10.1002/ajmg.c.31970, doi:10.1002/ajmg.c.31970. This article has 27 citations.

3. (tian2023organizationfunctionsand pages 5-6): Xiaoyu Tian, Huijie Zhao, and Jun Zhou. Organization, functions, and mechanisms of the bbsome in development, ciliopathies, and beyond. eLife, Jul 2023. URL: https://doi.org/10.7554/elife.87623, doi:10.7554/elife.87623. This article has 84 citations and is from a domain leading peer-reviewed journal.

4. (alvarezsatta2017bardetbiedlsyndromeas pages 2-3): María Álvarez-Satta, Sheila Castro-Sánchez, and Diana Valverde. Bardet-biedl syndrome as a chaperonopathy: dissecting the major role of chaperonin-like bbs proteins (bbs6-bbs10-bbs12). Frontiers in Molecular Biosciences, Jul 2017. URL: https://doi.org/10.3389/fmolb.2017.00055, doi:10.3389/fmolb.2017.00055. This article has 89 citations.

5. (zhang2012intrinsicproteinproteininteractionmediated pages 1-2): Qihong Zhang, Dahai Yu, Seongjin Seo, Edwin M. Stone, and Val C. Sheffield. Intrinsic protein-protein interaction-mediated and chaperonin-assisted sequential assembly of stable bardet-biedl syndrome protein complex, the bbsome. Journal of Biological Chemistry, 287:20625-20635, Jun 2012. URL: https://doi.org/10.1074/jbc.m112.341487, doi:10.1074/jbc.m112.341487. This article has 204 citations and is from a domain leading peer-reviewed journal.

6. (seo2010bbs6bbs10and pages 1-2): Seongjin Seo, Lisa M. Baye, Nathan P. Schulz, John S. Beck, Qihong Zhang, Diane C. Slusarski, and Val C. Sheffield. Bbs6, bbs10, and bbs12 form a complex with cct/tric family chaperonins and mediate bbsome assembly. Proceedings of the National Academy of Sciences, 107:1488-1493, Jan 2010. URL: https://doi.org/10.1073/pnas.0910268107, doi:10.1073/pnas.0910268107. This article has 412 citations and is from a highest quality peer-reviewed journal.

7. (tian2023organizationfunctionsand pages 1-2): Xiaoyu Tian, Huijie Zhao, and Jun Zhou. Organization, functions, and mechanisms of the bbsome in development, ciliopathies, and beyond. eLife, Jul 2023. URL: https://doi.org/10.7554/elife.87623, doi:10.7554/elife.87623. This article has 84 citations and is from a domain leading peer-reviewed journal.

8. (tian2023organizationfunctionsand pages 6-7): Xiaoyu Tian, Huijie Zhao, and Jun Zhou. Organization, functions, and mechanisms of the bbsome in development, ciliopathies, and beyond. eLife, Jul 2023. URL: https://doi.org/10.7554/elife.87623, doi:10.7554/elife.87623. This article has 84 citations and is from a domain leading peer-reviewed journal.

9. (seo2010bbs6bbs10and pages 2-3): Seongjin Seo, Lisa M. Baye, Nathan P. Schulz, John S. Beck, Qihong Zhang, Diane C. Slusarski, and Val C. Sheffield. Bbs6, bbs10, and bbs12 form a complex with cct/tric family chaperonins and mediate bbsome assembly. Proceedings of the National Academy of Sciences, 107:1488-1493, Jan 2010. URL: https://doi.org/10.1073/pnas.0910268107, doi:10.1073/pnas.0910268107. This article has 412 citations and is from a highest quality peer-reviewed journal.

10. (tian2023organizationfunctionsand pages 2-3): Xiaoyu Tian, Huijie Zhao, and Jun Zhou. Organization, functions, and mechanisms of the bbsome in development, ciliopathies, and beyond. eLife, Jul 2023. URL: https://doi.org/10.7554/elife.87623, doi:10.7554/elife.87623. This article has 84 citations and is from a domain leading peer-reviewed journal.

11. (gupta2022bardet–biedlsyndromethe pages 5-6): Neha Gupta, Mariavittoria D'Acierno, Enrica Zona, Giovambattista Capasso, and Miriam Zacchia. Bardet–biedl syndrome: the pleiotropic role of the chaperonin‐like bbs6, 10, and 12 proteins. American Journal of Medical Genetics. Part C, Seminars in Medical Genetics, 190:9-19, Mar 2022. URL: https://doi.org/10.1002/ajmg.c.31970, doi:10.1002/ajmg.c.31970. This article has 27 citations.

12. (alvarezsatta2017bardetbiedlsyndromeas pages 1-2): María Álvarez-Satta, Sheila Castro-Sánchez, and Diana Valverde. Bardet-biedl syndrome as a chaperonopathy: dissecting the major role of chaperonin-like bbs proteins (bbs6-bbs10-bbs12). Frontiers in Molecular Biosciences, Jul 2017. URL: https://doi.org/10.3389/fmolb.2017.00055, doi:10.3389/fmolb.2017.00055. This article has 89 citations.

13. (gupta2022bardet–biedlsyndromethe pages 2-3): Neha Gupta, Mariavittoria D'Acierno, Enrica Zona, Giovambattista Capasso, and Miriam Zacchia. Bardet–biedl syndrome: the pleiotropic role of the chaperonin‐like bbs6, 10, and 12 proteins. American Journal of Medical Genetics. Part C, Seminars in Medical Genetics, 190:9-19, Mar 2022. URL: https://doi.org/10.1002/ajmg.c.31970, doi:10.1002/ajmg.c.31970. This article has 27 citations.

14. (tian2023organizationfunctionsand pages 7-9): Xiaoyu Tian, Huijie Zhao, and Jun Zhou. Organization, functions, and mechanisms of the bbsome in development, ciliopathies, and beyond. eLife, Jul 2023. URL: https://doi.org/10.7554/elife.87623, doi:10.7554/elife.87623. This article has 84 citations and is from a domain leading peer-reviewed journal.

15. (singh2020structureandactivation pages 1-2): Sandeep K Singh, Miao Gui, Fujiet Koh, Matthew CJ Yip, and Alan Brown. Structure and activation mechanism of the bbsome membrane protein trafficking complex. Jan 2020. URL: https://doi.org/10.7554/elife.53322, doi:10.7554/elife.53322. This article has 105 citations and is from a domain leading peer-reviewed journal.

16. (wingfield2018traffickingofciliary pages 1-2): Jenna L. Wingfield, Karl-Ferdinand Lechtreck, and Esben Lorentzen. Trafficking of ciliary membrane proteins by the intraflagellar transport/bbsome machinery. Essays in biochemistry, 62 6:753-763, Oct 2018. URL: https://doi.org/10.1042/ebc20180030, doi:10.1042/ebc20180030. This article has 183 citations and is from a peer-reviewed journal.

17. (chou2019themoleculararchitecture pages 1-3): Hui-Ting Chou, Luise Apelt, Daniel P. Farrell, Susan Roehl White, Jonathan Woodsmith, Vladimir Svetlov, Jaclyn S. Goldstein, Andrew R. Nager, Zixuan Li, Jean Muller, Hélène Dollfus, Evgeny Nudler, Ulrich Stelzl, Frank DiMaio, Maxence V. Nachury, and Thomas Walz. The molecular architecture of native bbsome obtained by an integrated structural approach. Structure, 27:1384-1394.e4, Sep 2019. URL: https://doi.org/10.1016/j.str.2019.06.006, doi:10.1016/j.str.2019.06.006. This article has 73 citations and is from a domain leading peer-reviewed journal.

18. (gupta2022bardet–biedlsyndromethe pages 7-8): Neha Gupta, Mariavittoria D'Acierno, Enrica Zona, Giovambattista Capasso, and Miriam Zacchia. Bardet–biedl syndrome: the pleiotropic role of the chaperonin‐like bbs6, 10, and 12 proteins. American Journal of Medical Genetics. Part C, Seminars in Medical Genetics, 190:9-19, Mar 2022. URL: https://doi.org/10.1002/ajmg.c.31970, doi:10.1002/ajmg.c.31970. This article has 27 citations.

19. (gupta2022bardet–biedlsyndromethe pages 6-7): Neha Gupta, Mariavittoria D'Acierno, Enrica Zona, Giovambattista Capasso, and Miriam Zacchia. Bardet–biedl syndrome: the pleiotropic role of the chaperonin‐like bbs6, 10, and 12 proteins. American Journal of Medical Genetics. Part C, Seminars in Medical Genetics, 190:9-19, Mar 2022. URL: https://doi.org/10.1002/ajmg.c.31970, doi:10.1002/ajmg.c.31970. This article has 27 citations.

20. (gupta2022bardet–biedlsyndromethe pages 4-5): Neha Gupta, Mariavittoria D'Acierno, Enrica Zona, Giovambattista Capasso, and Miriam Zacchia. Bardet–biedl syndrome: the pleiotropic role of the chaperonin‐like bbs6, 10, and 12 proteins. American Journal of Medical Genetics. Part C, Seminars in Medical Genetics, 190:9-19, Mar 2022. URL: https://doi.org/10.1002/ajmg.c.31970, doi:10.1002/ajmg.c.31970. This article has 27 citations.

Artifacts

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Citations

1. zhang2012intrinsicproteinproteininteractionmediated pages 1-2
2. tian2023organizationfunctionsand pages 2-3
3. tian2023organizationfunctionsand pages 6-7
4. wingfield2018traffickingofciliary pages 1-2
5. alvarezsatta2017bardetbiedlsyndromeas pages 2-3
6. tian2023organizationfunctionsand pages 1-2
7. tian2023organizationfunctionsand pages 5-6
8. alvarezsatta2017bardetbiedlsyndromeas pages 1-2
9. tian2023organizationfunctionsand pages 7-9
10. singh2020structureandactivation pages 1-2
11. chou2019themoleculararchitecture pages 1-3
12. https://doi.org/10.1002/ajmg.c.31970,
13. https://doi.org/10.7554/elife.87623,
14. https://doi.org/10.3389/fmolb.2017.00055,
15. https://doi.org/10.1074/jbc.m112.341487,
16. https://doi.org/10.1073/pnas.0910268107,
17. https://doi.org/10.7554/elife.53322,
18. https://doi.org/10.1042/ebc20180030,
19. https://doi.org/10.1016/j.str.2019.06.006,