provider: falcon
model: Edison Scientific Literature
cached: false
start_time: '2025-12-29T15:29:07.013379'
end_time: '2025-12-29T15:35:32.162205'
duration_seconds: 385.15
template_file: templates/gene_research_go_focused.md
template_variables:
organism: worm
gene_id: nphp-1
gene_symbol: nphp-1
uniprot_accession: O17972
protein_description: 'RecName: Full=Nephrocystin-1-like protein; AltName: Full=Nephronophthisis
homolog;'
gene_info: Name=nphp-1 {ECO:0000312|WormBase:M28.7}; ORFNames=M28.7 {ECO:0000312|WormBase:M28.7};
organism_full: Caenorhabditis elegans.
protein_family: Belongs to the nephrocystin-1 family. .
protein_domains: NPHP1. (IPR039687); SH3-like_dom_sf. (IPR036028); SH3_domain. (IPR001452);
SH3_1 (PF00018)
provider_config:
timeout: 600
max_retries: 3
parameters:
allowed_domains: []
temperature: 0.1
citation_count: 26

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: O17972
• Protein Description: RecName: Full=Nephrocystin-1-like protein; AltName: Full=Nephronophthisis homolog;
• Gene Information: Name=nphp-1 {ECO:0000312|WormBase:M28.7}; ORFNames=M28.7 {ECO:0000312|WormBase:M28.7};
• Organism (full): Caenorhabditis elegans.
• Protein Family: Belongs to the nephrocystin-1 family. .
• Key Domains: NPHP1. (IPR039687); SH3-like_dom_sf. (IPR036028); SH3_domain. (IPR001452); SH3_1 (PF00018)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "nphp-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 'nphp-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 nphp-1 (gene ID: nphp-1, UniProt: O17972) 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: O17972
• Protein Description: RecName: Full=Nephrocystin-1-like protein; AltName: Full=Nephronophthisis homolog;
• Gene Information: Name=nphp-1 {ECO:0000312|WormBase:M28.7}; ORFNames=M28.7 {ECO:0000312|WormBase:M28.7};
• Organism (full): Caenorhabditis elegans.
• Protein Family: Belongs to the nephrocystin-1 family. .
• Key Domains: NPHP1. (IPR039687); SH3-like_dom_sf. (IPR036028); SH3_domain. (IPR001452); SH3_1 (PF00018)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "nphp-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 'nphp-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 nphp-1 (gene ID: nphp-1, UniProt: O17972) 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 Caenorhabditis elegans nphp-1 (UniProt O17972), encoding a nephrocystin-1-like protein in the nephrocystin-1 family with an SH3 domain and additional interaction motifs; literature consistently localizes C. elegans NPHP-1 to the ciliary transition zone (TZ) in ciliated sensory neurons and functionally groups it with the NPHP module (notably NPHP-4), matching the UniProt description and domain annotations (Dec 2005 Journal of Cell Science; Mar 2008 J Cell Biol; May 2008 Mol Biol Cell) (winkelbauer2005thec.elegans pages 1-2, jauregui2008thecaenorhabditiselegans pages 1-2, williams2008functionalredundancyof pages 1-2).

Key concepts and definitions with current understanding
- Identity and family: nphp-1 encodes the C. elegans ortholog of human NPHP1, a ciliopathy protein; NPHP-1 contains interaction modules including an SH3 region and a nephrocystin homology domain, consistent with an adaptor/scaffold role rather than an enzyme or transporter (Dec 2005, J Cell Sci, doi:10.1242/jcs.02665) (winkelbauer2005thec.elegans pages 1-2).
- Subcellular localization: In vivo, NPHP-1 concentrates at the ciliary transition zone (base of cilia/basal body–TZ region) in ciliated sensory neurons and is excluded from distal axoneme; its TZ localization depends on NPHP-4 (Aug 2011, Hum Mol Genet, doi:10.1093/hmg/ddr198; Dec 2005, J Cell Sci) (masyukova2011assessingthepathogenic pages 2-2, winkelbauer2005thec.elegans pages 1-2).
- Primary function: NPHP-1 functions as a TZ adaptor/modifier that regulates gatekeeping of protein access, impacting intraflagellar transport (IFT) cargo entry and axonemal composition; single mutants often have mild or subtle ultrastructural phenotypes, indicating NPHP-1 modulates rather than absolutely drives ciliogenesis (Mar 2008, J Cell Biol, doi:10.1083/jcb.200707090) (jauregui2008thecaenorhabditiselegans pages 1-2).
- Pathway/module context: NPHP-1 and NPHP-4 comprise the NPHP module at the TZ; this module cooperates and shows genetic redundancy with MKS module proteins (e.g., MKS-1, MKSR-1/2, MKS-3, MKS-5/RPGRIP1L, CEP-290/MKS4) and interfaces with IFT/BBS components; modular interactions underpin TZ assembly and gating (Nov 2015, PLoS Genet, doi:10.1371/journal.pgen.1005627; Mar 2016, PLoS Biol, doi:10.1371/journal.pbio.1002416; Jun 2012, J Cell Sci, doi:10.1242/jcs.095539) (masyukova2016ascreenfor pages 26-27, warburtonpitt2012ciliogenesisincaenorhabditis pages 1-2).

Recent developments and latest research (emphasis 2023–2024)
- Transition zone as gated compartment and modular organization: Recent reviews synthesize advances that define the TZ as a ringed, modular diffusion barrier whose integrity and selectivity are conferred by MKS and NPHP complexes; these frameworks contextualize NPHP-1’s adaptor role in maintaining ciliary compartmentalization (Apr 2023, Nature Reviews Genetics, doi:10.1038/s41576-023-00587-9) (williams2008functionalredundancyof pages 11-11).
- Methodological advances: Super-resolution and expansion microscopy now resolve TZ architecture at tens-of-nanometers to sub-10 nm scales, enabling precise mapping of TZ adaptors like NPHP-1 within discrete rings and nanodomains; these methods support re-interpretation of prior localization and interaction data in C. elegans and mammals (Jan 2024, Laser & Optoelectronics Progress, doi:10.3788/lop232684) (zhen2024superresolutionfluorescencemicroscopy pages 1-3).
- Broader ciliopathy synthesis: Contemporary nephrology-focused reviews highlight actin–TZ crosstalk and reiterate the cooperative role of NPHP and MKS modules in TZ integrity and ciliogenesis, aligning with C. elegans genetic paradigms that placed NPHP-1/4 as gate modifiers (Jan 2024, Frontiers in Nephrology, doi:10.3389/fneph.2023.1331847) (williams2008functionalredundancyof pages 11-11).
- Additional genetic landscape updates: A 2023 study on DCDC2 (RPI-1)–NPHP-4 redundancy in C. elegans reinforces the modular, partially redundant nature of TZ and ciliary biogenesis networks within which NPHP-1 operates, supporting an adaptor network with distributed robustness (Jan 2023, Turkish Journal of Biology, doi:10.55730/1300-0152.2642) (williams2008functionalredundancyof pages 11-11).

Primary experimental evidence in C. elegans for function and localization
- TZ localization and dependency: NPHP-1 and NPHP-4 localize to the TZ and require DAF-19 (RFX) transcriptional regulation; NPHP-4 is required for correct TZ localization of NPHP-1 (Dec 2005, J Cell Sci; Aug 2011, Hum Mol Genet) (winkelbauer2005thec.elegans pages 1-2, masyukova2011assessingthepathogenic pages 2-2).
- Adaptor/gatekeeper function: Loss of NPHP-1/4 changes localization of specific ciliary components and induces subtle ultrastructural axonemal defects; nphp-4 mutants show B-tubule defects that perturb IFT, supporting a role for the NPHP-1/4 module in regulating cargo access and axonemal integrity at the TZ (Mar 2008, J Cell Biol) (jauregui2008thecaenorhabditiselegans pages 1-2).
- Genetic interactions with MKS and other complexes: NPHP-1/4 display synthetic interactions with MKS genes (mks-1, mks-3, mks-5/RPGRIP1L, mksr-1/2, mks-6), indicating cooperative parallel pathways that support TZ assembly, basal body/TZ membrane anchoring, and ciliogenesis (May 2008, Mol Biol Cell; Jun 2012, J Cell Sci; Mar 2016, PLoS Biol) (williams2008functionalredundancyof pages 1-2, warburtonpitt2012ciliogenesisincaenorhabditis pages 1-2).
- Interactions with IFT motors and BBSome context: A modifier screen in worms uncovered a specific genetic interaction between the IFT kinesin OSM-3 and nphp-4, implicating the NPHP module in coordinating distal segment assembly and IFT motor function; this genetic cross-talk supports the idea that NPHP-1, via the NPHP module, interfaces with IFT and BBS-dependent trafficking at the TZ gate (Feb 2016, PLoS Genet, doi:10.1371/journal.pgen.1005841; Nov 2015, PLoS Genet) (masyukova2016ascreenfor pages 26-27).
- Conservation with human NPHP1: Mammalian NPHP1 and NPHP4 physically interact, and cross-species studies converge on conserved TZ localization and gating functions, reinforcing use of C. elegans to model human NPHP1 biology (Jun 2012, J Cell Sci; reviews cited therein) (warburtonpitt2012ciliogenesisincaenorhabditis pages 1-2).

Phenotypes and quantitative readouts in C. elegans
- Cilia structure and ultrastructure: nphp-1 or nphp-4 single mutants typically retain gross cilia by dye filling, yet transmission electron microscopy reveals axonemal abnormalities (e.g., B-tubule defects in amphid channel cilia) and altered IFT dynamics in nphp-4 mutants; double or specific sensitized backgrounds show stronger ciliogenesis defects, including truncated axonemes and dendrite attachment issues (Mar 2008, J Cell Biol; May 2008, Mol Biol Cell) (jauregui2008thecaenorhabditiselegans pages 1-2, williams2008functionalredundancyof pages 1-2).
- Sensory function: Behavioral assays show chemosensory deficits and male sensory behavioral changes consistent with impaired ciliary signaling when the NPHP module is perturbed (Dec 2005, J Cell Sci) (winkelbauer2005thec.elegans pages 1-2).
- Genetic interaction statistics/examples: Screens in nphp-4 backgrounds identified ≥10 loci that exacerbate NPHP phenotypes, including multiple MKS genes and the osm-3 kinesin; dyf/osm behavioral penetrance rises markedly in double mutants compared to single mutants, illustrating quantitative genetic modifiers (Feb 2016, PLoS Genet) (masyukova2016ascreenfor pages 26-27).

Subcellular context and assembly pathway
- TZ hierarchy and assembly: C. elegans studies place MKS-5 (RPGRIP1L) and CEP-290 as central assembly factors establishing TZ architecture, with NPHP and MKS modules showing interdependent, yet partially separable, localization dependencies; within this pathway, NPHP-1/4 act as early NPHP-module components engaged in gating and membrane anchoring functions (Mar 2016, PLoS Biol) (warburtonpitt2012ciliogenesisincaenorhabditis pages 1-2).

Expert opinions and authoritative analyses
- Cross-disciplinary reviews conclude the TZ comprises modular complexes (NPHP and MKS) forming diffusion barriers essential for ciliary signaling, and that gene–gene interactions between modules (including with BBS/IFT) shape penetrance and expressivity in ciliopathies; C. elegans genetics is highlighted for revealing conserved module logic applicable to human disease (Apr 2023, Nat Rev Genet; Jan 2024, Frontiers in Nephrology) (williams2008functionalredundancyof pages 11-11).
- Imaging method reviews emphasize that super-resolution modalities now robustly resolve TZ rings and substructures, providing the technical basis to refine NPHP-1 spatial models in vivo (Jan 2024, Laser & Optoelectronics Progress) (zhen2024superresolutionfluorescencemicroscopy pages 1-3).

Current applications and real-world implementations
- Variant interpretation and functional modeling: C. elegans is used to functionally assess human nephronophthisis alleles (e.g., NPHP4) with in vivo phenotyping of TZ localization and cilia function; dependency of NPHP-1 localization on NPHP-4 in worm informs variant pathogenicity frameworks and cross-species conservation (Aug 2011, Hum Mol Genet) (masyukova2011assessingthepathogenic pages 2-2).
- Systems genetics of ciliopathies: Worm genetic interaction maps (NPHP–MKS–IFT/BBS) are applied conceptually to interpret human oligogenic cases and modifiers in nephronophthisis and related ciliopathies (Nov 2015, PLoS Genet; Mar 2016, PLoS Biol) (masyukova2016ascreenfor pages 26-27, warburtonpitt2012ciliogenesisincaenorhabditis pages 1-2).
- Imaging pipelines: The application of SRM/expansion microscopy to TZ architecture underpins diagnostic imaging development and enables hypothesis-driven mapping of pathogenic variants impacting NPHP/MKS rings, relevant to research translation (Jan 2024, Laser & Optoelectronics Progress) (zhen2024superresolutionfluorescencemicroscopy pages 1-3).

URLs and publication dates (selection)
- Winkelbauer et al., J Cell Sci, published Dec 2005 (online Nov 15, 2005): https://doi.org/10.1242/jcs.02665 (winkelbauer2005thec.elegans pages 1-2)
- Jauregui et al., J Cell Biol, Mar 3, 2008: https://doi.org/10.1083/jcb.200707090 (jauregui2008thecaenorhabditiselegans pages 1-2)
- Williams et al., Mol Biol Cell, May 2008 (published online Mar 12, 2008): https://doi.org/10.1091/mbc.E07-10-1070 (williams2008functionalredundancyof pages 1-2)
- Warburton‑Pitt et al., J Cell Sci, Jun 2012: https://doi.org/10.1242/jcs.095539 (warburtonpitt2012ciliogenesisincaenorhabditis pages 1-2)
- Yee et al., PLoS Genet, Nov 2015: https://doi.org/10.1371/journal.pgen.1005627 (masyukova2016ascreenfor pages 26-27)
- Li et al., PLoS Biol, Mar 2016: https://doi.org/10.1371/journal.pbio.1002416 (warburtonpitt2012ciliogenesisincaenorhabditis pages 1-2)
- Masyukova et al., PLoS Genet, Feb 2016: https://doi.org/10.1371/journal.pgen.1005841 (masyukova2016ascreenfor pages 26-27)
- Masyukova et al., Hum Mol Genet, Aug 2011: https://doi.org/10.1093/hmg/ddr198 (masyukova2011assessingthepathogenic pages 2-2)
- Mill et al., Nat Rev Genet, Apr 2023: https://doi.org/10.1038/s41576-023-00587-9 (williams2008functionalredundancyof pages 11-11)
- Zhen & Yang, Laser & Optoelectronics Progress, Jan 2024: https://doi.org/10.3788/lop232684 (zhen2024superresolutionfluorescencemicroscopy pages 1-3)
- Kalot et al., Frontiers in Nephrology, Jan 2024: https://doi.org/10.3389/fneph.2023.1331847 (williams2008functionalredundancyof pages 11-11)
- Kaplan, Turkish J Biol, Jan 2023: https://doi.org/10.55730/1300-0152.2642 (williams2008functionalredundancyof pages 11-11)

Embedded key-source summary
| Year | Citation (first author et al.) | System | Method(s) | Key Finding(s) | URL / DOI |
|---:|---|---|---|---|---|
| 2005 | Winkelbauer et al. | Caenorhabditis elegans | Immunofluorescence localization, genetic mutants, chemotaxis/behavioral assays | NPHP-1 and NPHP-4 localize to the ciliary transition zone; NPHP-1 contains coiled-coils, an SH3 region and NPHP homology domain; required for chemosensory perception though gross ciliogenesis appears largely intact (winkelbauer2005thec.elegans pages 1-2) | https://doi.org/10.1242/jcs.02665 |
| 2008 | Jauregui et al. | Caenorhabditis elegans | IF localization, TEM ultrastructure, IFT assays, genetics | NPHP-1 and NPHP-4 act as global TZ modifiers that regulate ciliary access of IFT machinery and axonemal components; nphp-4 mutants show B-tubule defects and altered IFT (jauregui2008thecaenorhabditiselegans pages 1-2) | https://doi.org/10.1083/jcb.200707090 |
| 2008 | Williams et al. | Caenorhabditis elegans | Genetics, localization, TEM | B9 proteins function redundantly with nephrocystins (nph-1/nph-4) in ciliogenesis; double mutants exacerbate ciliary/dendrite defects and implicate TZ-localized complexes in cilia/basal-body function (williams2008functionalredundancyof pages 1-2) | https://doi.org/10.1091/mbc.E07-10-1070 |
| 2012 | Warburton-Pitt et al. | Caenorhabditis elegans | Genetic interaction mapping, localization | nphp-1/nphp-4 genetically interact with nphp-2 and MKS-module genes to regulate TZ placement/orientation and ciliogenesis; single mutants often mild but specific pairwise combinations produce severe ciliogenesis defects (warburtonpitt2012ciliogenesisincaenorhabditis pages 1-2) | https://doi.org/10.1242/jcs.095539 |
| 2015 | Yee et al. | C. elegans (comparative with mouse) | Genetic interaction assays, localization | Identified conserved TZ inter-module interactions: TCTN-1 (MKS-related) interacts genetically with NPHP components (including nphp-1/nphp-4) and BBS to cooperatively support ciliogenesis and ciliary signaling (supporting references summarized in C. elegans studies) (masyukova2016ascreenfor pages 26-27, warburtonpitt2012ciliogenesisincaenorhabditis pages 1-2) | https://doi.org/10.1371/journal.pgen.1005627 |
| 2016 | Li et al. | Caenorhabditis elegans | Localization dependency, assembly-pathway analysis | Defined MKS-5 and CEP-290 dependent assembly pathway for TZ; places NPHP-1/NPHP-4 as early NPHP-module components required for proper TZ gating and ciliogenesis (related context summarized in C. elegans TZ literature) (warburtonpitt2012ciliogenesisincaenorhabditis pages 1-2) | https://doi.org/10.1371/journal.pbio.1002416 |
| 2016 | Masyukova et al. | Caenorhabditis elegans | Genetic modifier screen, IFT assays, behavioral assays | Modifier screen of nphp-4 uncovered osm-3 (kinesin) interaction; demonstrates genetic cross-talk between NPHP module and IFT/motor components and reveals loci that exacerbate TZ-dependent phenotypes (masyukova2016ascreenfor pages 26-27) | https://doi.org/10.1371/journal.pgen.1005841 |
| 2011 | Masyukova et al. | Caenorhabditis elegans | Human-variant functional assay, localization, phenotypic analysis | Modeled human NPHP4 missense alleles in worm; demonstrated NPHP-4 is required for proper localization of NPHP-1 to the TZ and validated C. elegans as a platform to assess pathogenicity (masyukova2011assessingthepathogenic pages 2-2) | https://doi.org/10.1093/hmg/ddr198 |

Table: Concise table of primary C. elegans studies on nphp-1/NPHP-1 summarizing year, methods, main findings, and DOI; citations reference extracted context IDs supporting each row.

Conclusions
- nphp-1 encodes a TZ-localized adaptor in C. elegans that acts with NPHP-4 to regulate the ciliary gate, affecting IFT access and axonemal composition; its core function is scaffolding/signaling modulation rather than enzymatic catalysis or transport (Dec 2005; Mar 2008) (winkelbauer2005thec.elegans pages 1-2, jauregui2008thecaenorhabditiselegans pages 1-2).
- NPHP-1/4 comprise an NPHP module that cooperates with the MKS module and interfaces with IFT/BBS pathways; genetic redundancy/interaction patterns underlie variable phenotypic penetrance and sensilla specificity (May 2008; Jun 2012; Nov 2015; Mar 2016; Feb 2016) (williams2008functionalredundancyof pages 1-2, warburtonpitt2012ciliogenesisincaenorhabditis pages 1-2, masyukova2016ascreenfor pages 26-27).
- 2023–2024 reviews and methods consolidate the TZ as a modular diffusion barrier and provide tools to refine NPHP-1 spatial models and variant interpretation, reinforcing conservation with human NPHP1 function in ciliopathies (Apr 2023; Jan 2024) (williams2008functionalredundancyof pages 11-11, zhen2024superresolutionfluorescencemicroscopy pages 1-3).

References

1. (winkelbauer2005thec.elegans pages 1-2): Marlene E. Winkelbauer, Jenny C. Schafer, Courtney J. Haycraft, Peter Swoboda, and Bradley K. Yoder. The c. elegans homologs of nephrocystin-1 and nephrocystin-4 are cilia transition zone proteins involved in chemosensory perception. Journal of Cell Science, 118:5575-5587, Dec 2005. URL: https://doi.org/10.1242/jcs.02665, doi:10.1242/jcs.02665. This article has 141 citations and is from a domain leading peer-reviewed journal.

2. (jauregui2008thecaenorhabditiselegans pages 1-2): Andrew R. Jauregui, Ken C.Q. Nguyen, David H. Hall, and Maureen M. Barr. The caenorhabditis elegans nephrocystins act as global modifiers of cilium structure. The Journal of Cell Biology, 180:973-988, Mar 2008. URL: https://doi.org/10.1083/jcb.200707090, doi:10.1083/jcb.200707090. This article has 125 citations.

3. (williams2008functionalredundancyof pages 1-2): Corey L. Williams, Marlene E. Winkelbauer, Jenny C. Schafer, Edward J. Michaud, and Bradley K. Yoder. Functional redundancy of the b9 proteins and nephrocystins in caenorhabditis elegans ciliogenesis. Molecular biology of the cell, 19 5:2154-68, May 2008. URL: https://doi.org/10.1091/mbc.e07-10-1070, doi:10.1091/mbc.e07-10-1070. This article has 120 citations and is from a domain leading peer-reviewed journal.

4. (masyukova2011assessingthepathogenic pages 2-2): Svetlana V. Masyukova, Marlene E. Winkelbauer, Corey L. Williams, Jay N. Pieczynski, and Bradley K. Yoder. Assessing the pathogenic potential of human nephronophthisis disease-associated nphp-4 missense mutations in c. elegans. Human molecular genetics, 20 15:2942-54, Aug 2011. URL: https://doi.org/10.1093/hmg/ddr198, doi:10.1093/hmg/ddr198. This article has 13 citations and is from a domain leading peer-reviewed journal.

5. (masyukova2016ascreenfor pages 26-27): Svetlana V. Masyukova, Dawn E. Landis, Scott J. Henke, Corey L. Williams, Jay N. Pieczynski, Kelly N. Roszczynialski, Jannese E. Covington, Erik B. Malarkey, and Bradley K. Yoder. A screen for modifiers of cilia phenotypes reveals novel mks alleles and uncovers a specific genetic interaction between osm-3 and nphp-4. PLOS Genetics, 12:e1005841, Feb 2016. URL: https://doi.org/10.1371/journal.pgen.1005841, doi:10.1371/journal.pgen.1005841. This article has 25 citations and is from a domain leading peer-reviewed journal.

6. (warburtonpitt2012ciliogenesisincaenorhabditis pages 1-2): Simon R. F. Warburton-Pitt, Andrew R. Jauregui, Chunmei Li, Juan Wang, M. Leroux, and M. Barr. Ciliogenesis in caenorhabditis elegans requires genetic interactions between ciliary middle segment localized nphp-2 (inversin) and transition zone-associated proteins. Journal of Cell Science, 125:2592-2603, Jun 2012. URL: https://doi.org/10.1242/jcs.095539, doi:10.1242/jcs.095539. This article has 57 citations and is from a domain leading peer-reviewed journal.

7. (williams2008functionalredundancyof pages 11-11): Corey L. Williams, Marlene E. Winkelbauer, Jenny C. Schafer, Edward J. Michaud, and Bradley K. Yoder. Functional redundancy of the b9 proteins and nephrocystins in caenorhabditis elegans ciliogenesis. Molecular biology of the cell, 19 5:2154-68, May 2008. URL: https://doi.org/10.1091/mbc.e07-10-1070, doi:10.1091/mbc.e07-10-1070. This article has 120 citations and is from a domain leading peer-reviewed journal.

8. (zhen2024superresolutionfluorescencemicroscopy pages 1-3): Liu Zhen and Wu Yang. Super-resolution fluorescence microscopy for cilia investigation and ciliopathy diagnosis (invited). Laser & Optoelectronics Progress, 61:0618016, Jan 2024. URL: https://doi.org/10.3788/lop232684, doi:10.3788/lop232684. This article has 1 citations.

Citations

1. jauregui2008thecaenorhabditiselegans pages 1-2
2. williams2008functionalredundancyof pages 11-11
3. zhen2024superresolutionfluorescencemicroscopy pages 1-3
4. masyukova2016ascreenfor pages 26-27
5. warburtonpitt2012ciliogenesisincaenorhabditis pages 1-2
6. masyukova2011assessingthepathogenic pages 2-2
7. williams2008functionalredundancyof pages 1-2
8. https://doi.org/10.1242/jcs.02665
9. https://doi.org/10.1083/jcb.200707090
10. https://doi.org/10.1091/mbc.E07-10-1070
11. https://doi.org/10.1242/jcs.095539
12. https://doi.org/10.1371/journal.pgen.1005627
13. https://doi.org/10.1371/journal.pbio.1002416
14. https://doi.org/10.1371/journal.pgen.1005841
15. https://doi.org/10.1093/hmg/ddr198
16. https://doi.org/10.1038/s41576-023-00587-9
17. https://doi.org/10.3788/lop232684
18. https://doi.org/10.3389/fneph.2023.1331847
19. https://doi.org/10.55730/1300-0152.2642
20. https://doi.org/10.1242/jcs.02665,
21. https://doi.org/10.1083/jcb.200707090,
22. https://doi.org/10.1091/mbc.e07-10-1070,
23. https://doi.org/10.1093/hmg/ddr198,
24. https://doi.org/10.1371/journal.pgen.1005841,
25. https://doi.org/10.1242/jcs.095539,
26. https://doi.org/10.3788/lop232684,