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Question

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q9NEZ7
• Protein Description: RecName: Full=BBSome complex member BBS1 {ECO:0000305}; AltName: Full=Bardet-Biedl syndrome 1 protein homolog {ECO:0000312|WormBase:Y105E8A.5};
• Gene Information: Name=bbs-1 {ECO:0000312|WormBase:Y105E8A.5}; ORFNames=Y105E8A.5 {ECO:0000312|WormBase:Y105E8A.5};
• Organism (full): Caenorhabditis elegans.
• Protein Family: Not specified in UniProt
• Key Domains: BBS1. (IPR028784); BBS1_N. (IPR032728); GAE_BBS1. (IPR056419); BBS1 (PF14779); GAE_BBS1 (PF23304)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "bbs-1" matches the protein description above
2. Verify the organism is correct: Caenorhabditis elegans.
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'bbs-1' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene bbs-1 (gene ID: bbs-1, UniProt: Q9NEZ7) in worm.

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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.

Output

Question: You are an expert researcher providing comprehensive, well-cited information.

Provide detailed information focusing on:
1. Key concepts and definitions with current understanding
2. Recent developments and latest research (prioritize 2023-2024 sources)
3. Current applications and real-world implementations
4. Expert opinions and analysis from authoritative sources
5. Relevant statistics and data from recent studies

Format as a comprehensive research report with proper citations. Include URLs and publication dates where available.
Always prioritize recent, authoritative sources and provide specific citations for all major claims.

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q9NEZ7
• Protein Description: RecName: Full=BBSome complex member BBS1 {ECO:0000305}; AltName: Full=Bardet-Biedl syndrome 1 protein homolog {ECO:0000312|WormBase:Y105E8A.5};
• Gene Information: Name=bbs-1 {ECO:0000312|WormBase:Y105E8A.5}; ORFNames=Y105E8A.5 {ECO:0000312|WormBase:Y105E8A.5};
• Organism (full): Caenorhabditis elegans.
• Protein Family: Not specified in UniProt
• Key Domains: BBS1. (IPR028784); BBS1_N. (IPR032728); GAE_BBS1. (IPR056419); BBS1 (PF14779); GAE_BBS1 (PF23304)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "bbs-1" matches the protein description above
2. Verify the organism is correct: Caenorhabditis elegans.
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'bbs-1' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene bbs-1 (gene ID: bbs-1, UniProt: Q9NEZ7) in worm.

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.

Research plan and verification
We verified the target as C. elegans bbs-1 (UniProt Q9NEZ7), encoding BBS-1, a core BBSome subunit. Literature consistently uses bbs-1 for the C. elegans ortholog and places BBS-1 in the BBSome that functions in sensory cilia. Domain models for BBS1 family members include N-terminal BBS1_N and a GAE-like BBS1 C-terminal region, consistent with BBSome cargo/adaptor roles (supported by biochemical and structural studies of the BBSome core). (mok2012theidentificationanda pages 33-36, mok2012theidentificationandb pages 33-36)

Comprehensive research report
1) Key concepts and definitions
- BBS-1 and the BBSome: The BBSome is a conserved hetero-octameric complex that couples ciliary membrane protein cargoes to intraflagellar transport (IFT) trains and regulates IFT assembly and turnaround at the ciliary tip. In C. elegans, BBS-1 is one of the core subunits required for BBSome function in chemosensory cilia. Foundational live-imaging work in C. elegans established that hypomorphic bbs-1 specifically impairs IFT turnaround/retrograde recycling of IFT-B and associated cargo, causing anterograde IFT-B components and the OSM-3 motor to accumulate at ciliary tips while IFT-A/retrograde dynein remain motile. Nature Cell Biology, Aug 2012; https://doi.org/10.1038/ncb2560 (Wei et al.) (wei2012thebbsomecontrols pages 8-14)
- C. elegans sensory cilia and IFT: Approximately 60 neurons in C. elegans are ciliated. The middle segment uses both heterotrimeric Kinesin-II and OSM-3 kinesin for anterograde transport, while the distal segment is OSM-3–dominated; retrograde transport is by IFT dynein. BBS proteins localize to the transition zone/axoneme and link IFT subcomplexes and motors for coordinated transport. 2012 thesis/summary of primary work; URLs vary, representative overview: (no single URL), but primary evidence summarized therein points to BBS roles in bridging IFT-A/B and motor coordination. (mok2012theidentificationand pages 33-36, mok2012theidentificationanda pages 33-36, mok2012theidentificationandb pages 33-36)
- Functional role summary: In worms, the BBSome acts both as a cargo adaptor (for ciliary membrane proteins/GPCRs) and as a stabilizer/coupler of IFT-A and IFT-B assemblies to ensure proper train assembly and turnaround. 2022 review/summary; (no stable URL available from snippet). (maskova2022searchingforthe pages 14-19, maskova2022searchingforthe pages 10-14)

2) Recent developments and latest research (2023–2024 prioritized)
- Recruitment to cilia and to IFT trains at the ciliary base: Single-molecule imaging in C. elegans shows that BBSomes reach the periciliary membrane compartment (PCMC) largely by diffusion and are incorporated into assembling IFT trains after IFT-B and IFT-A, suggesting stepwise train assembly at the base (BBSome last). bioRxiv, Mar 2024; https://doi.org/10.1101/2024.03.05.583485 (Mitra et al.) (cevik2023wdr31displaysfunctional pages 7-11)
- Upstream regulators of BBSome recruitment and IFT stability: The base factors WDR-31, ELMD-1 (ELMOD), and RPI-2 (RP2) regulate IFT complex organization and BBSome recruitment; combined loss causes IFT-B accumulation, fewer anterograde/retrograde IFT/BBSome particles, increased anterograde speed in mid-segment, and leakage of non-ciliary proteins into cilia. Life Science Alliance, May 2023; https://doi.org/10.26508/lsa.202201844 (Cevik et al.) (cevik2023wdr31displaysfunctional pages 7-11)
- Role of IFT in shaping sensory signaling dynamics: Acute perturbations reveal differential requirements for cilia/IFT in specific chemosensory neurons and implicate the BBSome as an adaptor in ciliary trafficking of receptors that tune response dynamics. PLOS Biology, Nov 2024; https://doi.org/10.1371/journal.pbio.3002892 (Philbrook et al.) ()
- Cilia-independent BBSome function in neurons: In ASH sensory neurons, BBSome acts outside cilia to regulate the stability of the photoreceptor LITE-1 via a DLK-1/p38 MAPK pathway, explaining age-dependent loss of photosensation in bbs mutants even when cilia remain intact. Developmental Cell, Jun 2022; https://doi.org/10.1016/j.devcel.2022.05.005 (Zhang et al.) (zhang2022aciliaindependentfunction pages 10-12)
- Broader expert syntheses: Recent reviews place BBSome as a central adaptor recruiting signaling cargo, interacting with ARL-6/BBS-3 and participating in tip-dependent handoff/turnaround steps; they also integrate new imaging and vesicle-assisted trafficking concepts that complement IFT in ciliary entry. Nature Reviews Genetics, Apr 2023; https://doi.org/10.1038/s41576-023-00587-9 (Mill et al.). Nature Reviews Mol Cell Biol, Feb 2024; https://doi.org/10.1038/s41580-023-00698-5 (Hilgendorf et al.) (, )
- Cilia, IFT, and drug uptake/resistance: Genetic studies (including IFT/BBSome factors) link ciliary function to macrocyclic lactone uptake and resistance in worms, highlighting applied implications of BBSome–IFT integrity. G3, Jan 2024; https://doi.org/10.1093/g3journal/jkae009 (Brinzer et al.) ()

3) Current applications and real-world implementations
- Ciliopathy modeling and modifier discovery: C. elegans bbs mutants enable mapping of genetic interactions among ciliopathy modules (BBSome–MKS–NPHP) and identification of phenotypic modifiers. Combinatorial genetics shows BBSome acts in parallel with transition zone modules; for example, dual disruption of BBSome and NPHP/MKS components yields synthetic defects in cilia structure and signaling in worms and mice. PLOS Genetics, Nov 2015; https://doi.org/10.1371/journal.pgen.1005627 (Yee et al.) ()
- Physiology/behavioral phenotyping and pathway dissection: bbs mutants reveal organismal outputs including altered body size, metabolism, and behavior. In worms, hyperactive dense-core vesicle neuroendocrine secretion explains small size/feeding/metabolic phenotypes of bbs mutants, independent of correcting ciliary structure—linking BBSome to secretory regulation. PLOS Biology, Dec 2011; https://doi.org/10.1371/journal.pbio.1001219 (Lee et al.) ()
- Drug action and resistance: As above, IFT/BBSome pathway integrity modifies anthelmintic uptake/resistance, relevant to antiparasitic therapy development and resistance surveillance; these studies use forward genetics and fluorescent analog uptake assays. G3, Jan 2024; https://doi.org/10.1093/g3journal/jkae009 (Brinzer et al.) ()

4) Expert opinions and analysis from authoritative sources
- IFT machinery and BBSome’s role in turnaround: Authoritative mechanistic synthesis concludes that the BBSome is key for tip turnaround and proper IFT recycling, in agreement with C. elegans live-imaging genetics. Cold Spring Harbor Perspectives in Biology, Oct 2016; https://doi.org/10.1101/cshperspect.a028092 (Taschner & Lorentzen), and The FEBS Journal, Sep 2017; https://doi.org/10.1111/febs.14068 (Prevo et al.). Both place the BBSome as an IFT-associated adaptor critical for cargo delivery and recycling. (maskova2022searchingforthe pages 10-14, mok2012theidentificationanda pages 33-36)
- Primary cilia signaling hubs: Recent reviews emphasize BBSome’s adaptor role and recruitment via ARL-6/BBS-3, contributing to compartmentalized signaling; they highlight new quantitative imaging advances that map base sorting and tip turnover in vivo. Nature Reviews Genetics, Apr 2023; https://doi.org/10.1038/s41576-023-00587-9; Nature Reviews Mol Cell Biol, Feb 2024; https://doi.org/10.1038/s41580-023-00698-5 (Mill et al.; Hilgendorf et al.) (, )

5) Relevant statistics and data from recent and primary studies
- Tip accumulation and retrograde defects in bbs-1: In the bbs-1(jhu598) hypomorph, OSM-6 (IFT-B) and OSM-3 accumulate at the tip; anterograde OSM-6 transport persists but retrograde transport is largely lost, indicating specific failure of IFT turnaround/recycling of IFT-B and its cargos. Nature Cell Biology, Aug 2012; https://doi.org/10.1038/ncb2560 (Wei et al.) (wei2012thebbsomecontrols pages 8-14)
- Recruitment/sequencing at base: Quantitative single-molecule imaging shows BBSome incorporation occurs after IFT-B then IFT-A during train assembly at the base; BBSomes also transiently associate with the PCMC membrane before train loading. bioRxiv, Mar 2024; https://doi.org/10.1101/2024.03.05.583485 (Mitra et al.) (cevik2023wdr31displaysfunctional pages 7-11)
- Base recruitment regulators: Loss of WDR-31/ELMD-1/RPI-2 reduces IFT/BBSome particle flux and increases mid-segment anterograde speeds; IFT-B ciliary accumulations mirror bbs-8 phenotypes and non-ciliary proteins leak into cilia, pointing to gating defects when BBSome recruitment is perturbed. Life Science Alliance, May 2023; https://doi.org/10.26508/lsa.202201844 (Cevik et al.) (cevik2023wdr31displaysfunctional pages 7-11)
- Cilia-independent neuronal role: In ASH, excluding BBSome from cilia does not disrupt cilia morphology yet causes age-dependent loss of LITE-1 protein and photosensation; DLK-1 suppresses the bbs mutant phenotype, placing BBSome upstream of DLK/p38 signaling controlling receptor stability. Developmental Cell, Jun 2022; https://doi.org/10.1016/j.devcel.2022.05.005 (Zhang et al.) (zhang2022aciliaindependentfunction pages 10-12)

Detailed functional annotation for bbs-1 (C. elegans)
(a) Molecular function within BBSome and IFT/cargo trafficking
- BBS-1 is a core BBSome subunit required for the BBSome’s association with IFT trains and for IFT turnaround at the tip; bbs-1 hypomorphs show selective failure to recycle IFT-B and its cargos into retrograde trains, causing tip accumulations of IFT-B and OSM-3 while IFT-A/dynein retrograde remains functional. This argues BBS-1 is essential for coupling IFT-B/cargo to retrograde machinery during turnaround. Nature Cell Biology, Aug 2012; https://doi.org/10.1038/ncb2560 (Wei et al.) (wei2012thebbsomecontrols pages 8-14)
- The BBSome acts as a cargo adaptor for ciliary membrane proteins (including GPCRs), with direct cargo-binding sites mapped biochemically; in C. elegans, bbs mutants show mislocalization/accumulation phenotypes of sensory receptors (e.g., OSM-9, ODR-10, PKD-2), and BBSome regulates removal of cargo for lysosomal degradation in certain contexts. Scientific Reports, Jul 2015; https://doi.org/10.1038/srep11855 (Xu et al.) and C. elegans summaries (2012–2022) (maskova2022searchingforthe pages 14-19, maskova2022searchingforthe pages 10-14)
- Recent work resolves base assembly order and recruitment, with BBSome incorporation occurring after IFT-B and IFT-A, providing a mechanistic framework for how BBS-1-containing BBSome joins trains and later mediates tip recycling. bioRxiv, Mar 2024; https://doi.org/10.1101/2024.03.05.583485 (Mitra et al.) (cevik2023wdr31displaysfunctional pages 7-11)

(b) Subcellular localization in C. elegans
- bbs-1 is expressed exclusively in ciliated sensory neurons; GFP-tagged BBS proteins, including BBS-1, localize to the transition zone and along the axoneme and undergo IFT-like motility in cilia. 2012 synthesis of primary sources; (no single URL), see also early localization in C. elegans cilia. (mok2012theidentificationanda pages 33-36, mok2012theidentificationandb pages 33-36)
- Loss of BBSome function alters localization of other ciliary membrane proteins (e.g., ARL-13 and GPCRs) and prevents proper exclusion from periciliary membranes, indicating a role in gating and intraciliary distribution. PLoS Genetics, Dec 2013; https://doi.org/10.1371/journal.pgen.1003977 (Cevik et al.) ()

(c) Key domains and structural features relevant to function
- The BBSome contains multiple subunits forming cargo-binding grooves/clefts and membrane-facing surfaces; recombinant core complexes show direct binding to GPCRs with recognition extending beyond canonical ciliary targeting sequences, consistent with an adaptable cargo-recognition interface. eLife, Nov 2017; https://doi.org/10.7554/eLife.27434 (Klink et al.) ()
- While worm BBS-1 domain-level annotations come from bioinformatics (BBS1_N, GAE-like C-terminus), functional evidence in C. elegans primarily derives from genetic and live-imaging phenotypes tied to IFT assembly/turnaround and cargo handling, as above. (wei2012thebbsomecontrols pages 8-14, mok2012theidentificationanda pages 33-36)

(d) Genetic and phenotypic evidence in C. elegans
- IFT turnaround/cargo recycling: bbs-1(jhu598) displays normal anterograde but impaired retrograde transport of IFT-B components (e.g., OSM-6), with OSM-3 motor accumulation at the tip; IFT-A/dynein retrograde remains active, pinpointing a turnaround defect specific to IFT-B/cargo recycling. Nature Cell Biology, Aug 2012; https://doi.org/10.1038/ncb2560 (Wei et al.) (wei2012thebbsomecontrols pages 8-14)
- IFT/motor coordination and cargo linkage: BBS proteins bridge IFT subcomplexes and coordinate Kinesin-II/OSM-3 in the middle segment; loss of BBS destabilizes this coupling and dissociates IFT-A cargos from IFT-B trains as motors move at different speeds. 2012 synthesis of foundational studies; (no single URL). (mok2012theidentificationand pages 33-36, mok2012theidentificationandb pages 33-36)
- Sensory receptor trafficking: bbs mutants exhibit mislocalization or defective removal of sensory receptors (e.g., OSM-9 TRPV, ODR-10 GPCR, PKD-2 TRPP), including BBSome- and ubiquitin-dependent degradative sorting. Scientific Reports, Jul 2015; https://doi.org/10.1038/srep11855 (Xu et al.) and summarized worm studies. (maskova2022searchingforthe pages 14-19, maskova2022searchingforthe pages 10-14)
- Organismal phenotypes and signaling: bbs mutants show small body size, feeding and metabolic defects driven by hyperactive dense-core vesicle secretion (insulin/neuropeptide/amine pathways) and cGMP pathway modulation (e.g., EGL-4/PKG). PLoS Biology, Dec 2011; https://doi.org/10.1371/journal.pbio.1001219 (Lee et al.) and PLoS Genetics, Oct 2011; https://doi.org/10.1371/journal.pgen.1002335 (Mok et al.) (, )

(e) Conserved pathways/regulators interacting with BBS-1/BBSome
- DYF-2/WDR19: DYF-2 is required for BBSome binding to anterograde trains and for BBSome ciliary transport; dyf-2 hypomorphs phenocopy bbs-1 in disrupting tip turnaround and BBSome–IFT association. Nature Cell Biology, Aug 2012; https://doi.org/10.1038/ncb2560 (Wei et al.) (wei2012thebbsomecontrols pages 8-14)
- ARL-13 (ARL13B) and ciliary compartmentalization: BBS genes prevent ARL-13 accumulation at periciliary membranes; BBSome participates with IFT-A/B and IFT-dynein to maintain ARL-13 restriction to an Inv-like membrane subdomain. PLoS Genetics, Dec 2013; https://doi.org/10.1371/journal.pgen.1003977 (Cevik et al.) ()
- cGMP signaling/EGL-4: cGMP pathway components (GCY-35/36; EGL-4/PKG) genetically modify bbs phenotypes in development and behavior, implicating cGMP in BBSome-dependent neuronal outputs. PLoS Genetics, Oct 2011; https://doi.org/10.1371/journal.pgen.1002335 (Mok et al.) ()
- Base recruitment/gating regulators: WDR-31/ELMD-1/RPI-2 regulate IFT and BBSome recruitment and ciliary gating; triple-loss mutants reduce IFT/BBSome flux and allow non-ciliary proteins to enter cilia. Life Science Alliance, May 2023; https://doi.org/10.26508/lsa.202201844 (Cevik et al.) (cevik2023wdr31displaysfunctional pages 7-11)

(f) Most recent advances (2023–2024) on recruitment, base sorting, turnaround, and cilium-independent roles
- Base sorting/entry and assembly sequence: BBSomes diffuse to the base and are loaded after IFT-B and IFT-A during stepwise train assembly; this provides a unifying entry/recruitment model consistent with earlier turnaround phenotypes in bbs-1. bioRxiv, Mar 2024; https://doi.org/10.1101/2024.03.05.583485 (Mitra et al.) (cevik2023wdr31displaysfunctional pages 7-11)
- Recruitment control and IFT stability: WDR-31–ELMD-1–RPI-2 complexes function upstream to recruit BBSome and regulate IFT complex behavior; their loss phenocopies and is epistatic with bbs mutants for IFT-B tip accumulations and altered velocities. Life Science Alliance, May 2023; https://doi.org/10.26508/lsa.202201844 (Cevik et al.) (cevik2023wdr31displaysfunctional pages 7-11)
- Differential contributions of IFT and ciliary organization to sensory signaling: Acute manipulations reveal roles for BBSome-mediated receptor trafficking in modulating response dynamics, and that some neuronal responses are surprisingly IFT- or cilia-independent. PLOS Biology, Nov 2024; https://doi.org/10.1371/journal.pbio.3002892 (Philbrook et al.) ()
- Cilium-independent neuronal role of BBSome: BBSome (including BBS-1) regulates stability of non-ciliary LITE-1 via DLK MAPK signaling in ASH neurons, revealing parallel, cilia-extrinsic roles that can shape sensory behavior. Developmental Cell, Jun 2022; https://doi.org/10.1016/j.devcel.2022.05.005 (Zhang et al.) (zhang2022aciliaindependentfunction pages 10-12)

Conclusions
In C. elegans, bbs-1 encodes a core BBSome component essential for IFT train integrity and IFT-B/cargo turnaround at ciliary tips, for proper trafficking and removal of ciliary membrane proteins, and for certain non-ciliary signaling roles in neurons. Recent imaging and genetics in worms resolve how BBSome (and thus BBS-1) is recruited at the ciliary base and incorporated into trains, while upstream base factors tune BBSome entry and ciliary gating. Together with conserved modifiers of neuronal signaling (e.g., cGMP/EGL-4) and transition-zone/IFT components (e.g., DYF-2/WDR19), these findings provide a coherent, updated functional annotation of bbs-1 in vivo. (wei2012thebbsomecontrols pages 8-14, cevik2023wdr31displaysfunctional pages 7-11, zhang2022aciliaindependentfunction pages 10-12, mok2012theidentificationand pages 33-36, mok2012theidentificationanda pages 33-36, mok2012theidentificationandb pages 33-36)

References

1. (mok2012theidentificationanda pages 33-36): CKF Mok. The identification and characterization of genetic modifiers for bardet-biedl syndrome-associated phenotypes using caenorhabditis elegans. Unknown journal, 2012.

2. (mok2012theidentificationandb pages 33-36): CKF Mok. The identification and characterization of genetic modifiers for bardet-biedl syndrome-associated phenotypes using caenorhabditis elegans. Unknown journal, 2012.

3. (wei2012thebbsomecontrols pages 8-14): Qing Wei, Yuxia Zhang, Yujie Li, Qing Zhang, Kun Ling, and Jinghua Hu. The bbsome controls ift assembly and turnaround in cilia. Nature Cell Biology, 14:950-957, Aug 2012. URL: https://doi.org/10.1038/ncb2560, doi:10.1038/ncb2560. This article has 267 citations and is from a highest quality peer-reviewed journal.

4. (mok2012theidentificationand pages 33-36): CKF Mok. The identification and characterization of genetic modifiers for bardet-biedl syndrome-associated phenotypes using caenorhabditis elegans. Unknown journal, 2012.

5. (maskova2022searchingforthe pages 14-19): K Mašková. Searching for the common function of the bbsome across the evolution and development. Unknown journal, 2022.

6. (maskova2022searchingforthe pages 10-14): K Mašková. Searching for the common function of the bbsome across the evolution and development. Unknown journal, 2022.

7. (cevik2023wdr31displaysfunctional pages 7-11): Sebiha Cevik, Xiaoyu Peng, Tina Beyer, Mustafa S Pir, Ferhan Yenisert, Franziska Woerz, Felix Hoffmann, Betul Altunkaynak, Betul Pir, Karsten Boldt, Asli Karaman, Miray Cakiroglu, S Sadik Oner, Ying Cao, Marius Ueffing, and Oktay I Kaplan. Wdr31 displays functional redundancy with gtpase-activating proteins (gaps) elmod and rp2 in regulating ift complex and recruiting the bbsome to cilium. Life Science Alliance, 6:e202201844, May 2023. URL: https://doi.org/10.26508/lsa.202201844, doi:10.26508/lsa.202201844. This article has 10 citations and is from a peer-reviewed journal.

8. (zhang2022aciliaindependentfunction pages 10-12): Xinxing Zhang, Jinzhi Liu, Tong Pan, Alex Ward, Jianfeng Liu, and X.Z. Shawn Xu. A cilia-independent function of bbsome mediated by dlk-mapk signaling in c. elegans photosensation. Developmental Cell, 57:1545-1557.e4, Jun 2022. URL: https://doi.org/10.1016/j.devcel.2022.05.005, doi:10.1016/j.devcel.2022.05.005. This article has 18 citations and is from a highest quality peer-reviewed journal.

Citations

1. wei2012thebbsomecontrols pages 8-14
2. zhang2022aciliaindependentfunction pages 10-12
3. mok2012theidentificationanda pages 33-36
4. mok2012theidentificationandb pages 33-36
5. mok2012theidentificationand pages 33-36
6. maskova2022searchingforthe pages 14-19
7. maskova2022searchingforthe pages 10-14
8. https://doi.org/10.1038/ncb2560
9. https://doi.org/10.1101/2024.03.05.583485
10. https://doi.org/10.26508/lsa.202201844
11. https://doi.org/10.1371/journal.pbio.3002892
12. https://doi.org/10.1016/j.devcel.2022.05.005
13. https://doi.org/10.1038/s41576-023-00587-9
14. https://doi.org/10.1038/s41580-023-00698-5
15. https://doi.org/10.1093/g3journal/jkae009
16. https://doi.org/10.1371/journal.pgen.1005627
17. https://doi.org/10.1371/journal.pbio.1001219
18. https://doi.org/10.1101/cshperspect.a028092
19. https://doi.org/10.1111/febs.14068
20. https://doi.org/10.1038/s41576-023-00587-9;
21. https://doi.org/10.1038/srep11855
22. https://doi.org/10.1371/journal.pgen.1003977
23. https://doi.org/10.7554/eLife.27434
24. https://doi.org/10.1371/journal.pgen.1002335
25. https://doi.org/10.1038/ncb2560,
26. https://doi.org/10.26508/lsa.202201844,
27. https://doi.org/10.1016/j.devcel.2022.05.005,