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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Identity check. The specified human gene NPHP1 (synonym NPH1; supplied UniProt accession O15259) encodes nephrocystin-1, also called nephrocystin—not nephrocystin-4 or another similarly named ciliopathy protein. Primary studies describe a 733-amino-acid protein with a coiled-coil region, an SH3 protein-interaction domain, acidic clusters and a C-terminal nephrocystin-homology region. This agrees with the supplied nephrocystin-1-family and SH3-domain annotations. The accession is supplied as the identification anchor; the cited experiments independently establish the human gene–protein identity and domain-based function. (fliegauf2006nephrocystinspecificallylocalizes pages 1-2, wodarczyk2010nephrocystin1formsa pages 1-2)
Best-supported primary function: nephrocystin-1 is a non-enzymatic interaction scaffold/adaptor, principally associated with the transition zone at the base of cilia and also found in epithelial adhesion complexes. It helps organize a nephrocystin protein module and is required for normal ciliary morphology and renal epithelial organization. Its location and complex membership support a role in maintaining the composition of the ciliary signaling compartment, but a particular molecule transported specifically by NPHP1 has not been established. It is neither characterized as a catalyst nor as a substrate-specific transporter. (fliegauf2006nephrocystinspecificallylocalizes pages 1-2, moran2024transportandbarrier pages 5-6, sang2011mappingthenphpjbtsmks pages 5-7, sang2011mappingthenphpjbtsmks pages 7-9, arai2024patientderivedandgeneedited pages 4-6)
The following evidence map distinguishes molecular observations from interpretations about broader ciliary function.
| Evidence tier | Finding for human NPHP1/nephrocystin-1 | Experimental basis and interpretation | Source |
|---|---|---|---|
| Identity/domain validation | Human NPHP1 encodes the 733-aa nephrocystin-1 protein, containing an N-terminal coiled-coil region, an SH3 domain, acidic clusters and a C-terminal nephrocystin-homology region. This matches UniProt O15259 and supports classification as a non-enzymatic interaction scaffold. | Protein characterization and human mutation/localization studies; no catalytic activity or transported substrate has been demonstrated. | Fliegauf et al., 2006, DOI: 10.1681/ASN.2005121351 (fliegauf2006nephrocystinspecificallylocalizes pages 1-2) |
| Direct trafficking mechanism | CK2 phosphorylates nephrocystin-1 at Ser121, Ser123 and Ser126 in its first acidic cluster, enhancing PACS-1 binding. CK2 inhibition or dominant-negative PACS-1 displaces nephrocystin-1 from the ciliary base into vesicle-like structures without destroying cilia. | In-vitro phosphorylation, phosphosite mutagenesis, binding assays, kinase inhibition and cellular localization establish a phosphorylation-dependent targeting mechanism. | Schermer et al., 2005, DOI: 10.1038/sj.emboj.7600885 (schermer2005phosphorylationbycasein pages 5-7, schermer2005phosphorylationbycasein pages 7-8) |
| Direct human localization | Nephrocystin-1 localizes specifically to the transition zone of human renal and respiratory cilia and to photoreceptor connecting cilia; during ciliogenesis it moves from diffuse cytoplasm to the transition zone. Homozygous deletion removes the signal but does not prevent respiratory ciliogenesis. | Immunofluorescence in human tissues and patient respiratory cells supports a transition-zone structural/adaptor role, not an obligatory role in axoneme assembly. | Fliegauf et al., 2006, DOI: 10.1681/ASN.2005121351 (fliegauf2006nephrocystinspecificallylocalizes pages 1-2, fliegauf2006nephrocystinspecificallylocalizes pages 2-3) |
| Direct complex architecture | NPHP1, NPHP4 and NPHP8/RPGRIP1L form a transition-zone module. In-vitro binding showed that NPHP4 directly binds both NPHP1 and NPHP8 and bridges them; NPHP1 and NPHP8 were not shown to bind directly. | Reciprocal affinity purification, mass spectrometry, co-immunoprecipitation, direct-binding assays and localization define complex organization. This supports general gate organization, but not an NPHP1-specific cargo. | Sang et al., 2011, DOI: 10.1016/j.cell.2011.04.019 (sang2011mappingthenphpjbtsmks pages 3-5, sang2011mappingthenphpjbtsmks pages 5-7) |
| Direct SH3 interaction and functional association | The NPHP1 SH3 domain binds the PP2 polyproline motif in the PKD1 product polycystin-1, with peptide affinity of approximately 0.30 ± 0.02 mM; PC-1 P4270L abolishes binding. NPHP1 depletion increased TNFα-induced apoptosis, and increased apoptosis was found in kidney tissue from four NPHP1-mutant patients. | NMR, ITC, pull-down and co-immunoprecipitation establish binding; cell and patient-tissue assays associate the complex with apoptosis resistance, but do not prove that apoptosis is NPHP1’s primary physiological function. | Wodarczyk et al., 2010, DOI: 10.1371/journal.pone.0012719 (wodarczyk2010nephrocystin1formsa pages 6-8, wodarczyk2010nephrocystin1formsa pages 3-5) |
| Human diagnostic/complex evidence | In genetically characterized renal-ciliopathy cases, pathogenic NPHP1 variants eliminated NPHP1 staining and markedly reduced NPHP4 transition-zone signal (mean signal-to-noise ratio 2.57 versus 9.21 in controls; p=0.008). Reciprocal disruption occurred with NPHP4 genotypes. | Nasal epithelial immunofluorescence, immunoblotting and follow-up genetics support in-vivo NPHP1–NPHP4 interdependence and a potential diagnostic assay; they do not alone establish the molecular direction of dependency. | Hellmann et al., 2024, DOI: 10.1007/s00467-024-06443-0 (hellmann2024immunofluorescenceanalysesof pages 1-2, hellmann2024immunofluorescenceanalysesof pages 5-7) |
| Human disease-model causality | NPHP1-deficient patient-derived and CRISPR-edited hiPSCs had longer cilia and fewer ciliated cells. Under rotating suspension culture, about 80% of deficient kidney organoids formed cysts by day 32 versus 20–30% of isogenic controls or NPHP1-overexpressing organoids; re-expression rescued cyst formation. | Isogenic editing, patient cells, organoid phenotyping and rescue provide strong causal cellular evidence. Fluid-stress culture is a model, so the result is preclinical and does not establish therapeutic efficacy in patients. | Arai et al., 2024, DOI: 10.3389/fcell.2024.1370723 (arai2024patientderivedandgeneedited pages 4-6, arai2024patientderivedandgeneedited pages 6-8) |
Table: Evidence supporting nephrocystin-1 as a phosphorylation-regulated transition-zone and junctional interaction scaffold. The table separates direct mechanistic findings from functional interpretations and avoids assigning catalytic activity or a uniquely NPHP1-dependent ciliary cargo.
The ciliary transition zone is the short region between the basal body and the ciliary axoneme. In human respiratory epithelium, nephrocystin-1 moves from a diffuse cytoplasmic distribution during ciliogenesis to a concentrated signal at this zone; it has also been observed at renal cilia and the photoreceptor connecting cilium, the specialized link to the light-sensing outer segment. Respiratory cells from people with homozygous NPHP1 deletions lack the nephrocystin-1 signal yet can still assemble motile cilia. Thus, localization and patient-cell evidence support a role in ciliary organization or function rather than an absolute requirement for cilium formation in that tissue. (fliegauf2006nephrocystinspecificallylocalizes pages 1-2, fliegauf2006nephrocystinspecificallylocalizes pages 2-3)
Nephrocystin-1 also occurs at epithelial cell–cell contacts and cell–matrix adhesion sites. Reported partners include the adhesion-associated proteins p130CAS, tensin, filamin and Pyk2. These findings make it plausible that NPHP1 links ciliary organization with epithelial junctional architecture, although junctional interactions alone do not establish which site drives kidney disease. In three-dimensional renal epithelial cultures, NPHP1 depletion impaired organized spheroid formation despite preservation of cilia numbers, providing functional evidence for an epithelial-architecture role separable from simply making a cilium. (gupta2021nephronophthisispathobiologyandmolecular pages 4-6, sang2011mappingthenphpjbtsmks pages 7-9)
Transition-zone assembly. Affinity purification and reciprocal binding experiments identify an NPHP1–NPHP4–NPHP8 module, where NPHP8 is RPGRIP1L. Importantly, direct-binding experiments found that NPHP4 binds NPHP1 and NPHP8 and can bridge them; they did not establish a direct NPHP1–NPHP8 interaction. The proteins were observed at the ciliary-base/transition-zone region and epithelial cell contacts. Recent expert reviews place this NPHP module alongside other, partly interconnected transition-zone modules that help establish a selective boundary between ciliary and non-ciliary compartments. That is a module-level gating model, not proof that NPHP1 directly recognizes a defined cargo. (sang2011mappingthenphpjbtsmks pages 3-5, park2022compositionorganizationand pages 6-8, moran2024transportandbarrier pages 5-6, sang2011mappingthenphpjbtsmks pages 5-7)
Control of NPHP1 targeting. A particularly well-resolved biochemical pathway is CK2 → nephrocystin-1 phosphorylation → PACS-1 binding → ciliary-base localization. CK2 phosphorylates nephrocystin-1 at Ser121, Ser123 and Ser126 in an acidic cluster adjacent to the SH3 domain. Phosphosite mutagenesis and biochemical binding assays support phosphorylation-dependent association with the sorting protein PACS-1; CK2 inhibition or interference with PACS-1 removes nephrocystin-1 from the ciliary base and redistributes it to intracellular vesicle-like structures without visibly abolishing cilia. This evidence identifies NPHP1 as a CK2 substrate, not a kinase. (schermer2005phosphorylationbycasein pages 5-7, schermer2005phosphorylationbycasein pages 3-5, schermer2005phosphorylationbycasein pages 7-8)
An additional regulatory axis involves Pyk2 and NPHP4. Pyk2-mediated phosphorylation of three NPHP1 tyrosines—Tyr46, Tyr349 and Tyr721—is counteracted by NPHP4 and influences PACS-1 association. NPHP4 depletion causes NPHP1 accumulation near the trans-Golgi in ciliated retinal epithelial cells. Together, these experiments support phosphorylation-regulated positioning of the NPHP1 complex between intracellular sorting compartments and the ciliary base; the complete direction and physiological dynamics of trafficking remain a model rather than a fully measured transport cycle. (liebau2011nephrocystin4regulatespyk2induced pages 1-2, liebau2011nephrocystin4regulatespyk2induced pages 6-8)
A defined SH3 ligand and pathway connection. Biochemical and NMR experiments show that the NPHP1 SH3 domain binds the PP2 proline-rich motif of polycystin-1, the PKD1 protein, whereas the tested PP1 motif did not bind detectably. The isolated peptide–SH3 interaction had an estimated dissociation constant of 0.30 ± 0.02 mM; mutation of polycystin-1 Pro4270 disrupted binding, including in full-length-protein experiments. In renal epithelial cell models, NPHP1 depletion impaired polycystin-1-associated resistance to an apoptotic challenge but did not abolish its tested cell-cycle or ERK effects; increased apoptosis was also observed in tissue from four NPHP1-mutant patients. This establishes a physical and experimentally supported apoptosis-response connection, not that apoptosis regulation is nephrocystin-1’s sole or principal physiological task. Polycystin-1 was not required for NPHP1 localization to cilia. (wodarczyk2010nephrocystin1formsa pages 6-8, wodarczyk2010nephrocystin1formsa pages 3-5)
The transition zone more generally regulates which membrane and soluble signaling proteins occupy cilia. Reviews discuss consequences for pathways such as Hedgehog signaling and for renal cystoprotein localization, but evidence for the broader ciliary gate should not be recast as proof that NPHP1 directly transduces Hedgehog signals or selects a specific receptor. Similarly, transcriptomic changes in cell-cycle, cholesterol-biosynthesis or EGFR-associated programs after NPHP1 loss do not, by themselves, identify direct NPHP1-binding partners in those pathways. (moran2024transportandbarrier pages 14-15, moran2024transportandbarrier pages 5-6, moran2024transportandbarrier pages 3-5, arai2024patientderivedandgeneedited pages 6-8)
Biallelic loss of NPHP1 is an established cause of autosomal-recessive juvenile nephronophthisis, a progressive renal tubulointerstitial ciliopathy; retinal degeneration can accompany kidney disease. Estimates cited by recent experimental authors attribute approximately 20–25% of nephronophthisis cases to NPHP1, but the fraction depends on cohort and case definition. Homozygous whole-gene deletion is a common pathogenic mechanism. Disease association, transition-zone localization and patient-cell phenotypes together make NPHP1 a strong functional disease annotation, without implying that all nephronophthisis is NPHP1-related. (wolf2011nephronophthisis pages 4-6, arai2024patientderivedandgeneedited pages 1-2, hellmann2024immunofluorescenceanalysesof pages 5-7)
Human disease modeling, June 2024. Arai and colleagues compared patient-derived, gene-edited and NPHP1-re-expressing human pluripotent stem cells. Loss of NPHP1 produced longer primary cilia and fewer ciliated cells. After transfer to rotating suspension culture, approximately 80% of NPHP1-deficient kidney organoids developed epithelial-lined cysts by day 32, compared with 20–30% of control or NPHP1-overexpressing organoids. Re-expression reduced cyst formation; nephron-like structures initially formed even without NPHP1. The matched genetic manipulation and rescue provide unusually strong cellular evidence that NPHP1 loss drives the phenotype. Rotation is an experimental stress condition, however, and an organoid rescue is not clinical gene-therapy efficacy. Study: Arai et al., Frontiers in Cell and Developmental Biology, June 2024, https://doi.org/10.3389/fcell.2024.1370723. (arai2024patientderivedandgeneedited pages 6-8, arai2024patientderivedandgeneedited pages 4-6)
Patient-cell diagnostic implementation, August 2024. Hellmann and colleagues tested whether minimally invasive nasal epithelial sampling could complement genetic diagnosis. Their abstract reports 86 genetically characterized individuals, with 35 also assessed for NPHP4; the detailed staining analysis describes 111 samples, of which 22 were unevaluable because of specimen quality. NPHP1 staining was absent in 14 evaluable samples, including 10 previously recognized homozygous NPHP1 deletions and one homozygous p.Gly343Arg variant previously classified as uncertain. Abnormal staining prompted further testing that diagnosed two previously unsolved individuals. In NPHP1-genotype cases, mean NPHP4 transition-zone signal-to-noise ratio was 2.57 versus 9.21 in controls (p = 0.008), consistent with functional interdependence. This is a promising adjunct to molecular testing, not a validated stand-alone screen with a generalizable sensitivity estimate. Study: Hellmann et al., Pediatric Nephrology, August 2024, https://doi.org/10.1007/s00467-024-06443-0. (hellmann2024immunofluorescenceanalysesof pages 1-2, hellmann2024immunofluorescenceanalysesof pages 5-7)
More recent exploratory therapy work, September 2025. Urine-derived renal epithelial cells from an affected member of a family with homozygous NPHP1 deletion were used to compare candidate treatments. Alprostadil increased ciliation but worsened the already elongated-cilium phenotype; the EGFR inhibitor AG556 improved ciliary length and shape and more effectively reversed aspects of the measured gene-expression signature. This motivates testing EGFR-dependent mechanisms but does not establish that nephrocystin-1 directly signals through EGFR, or that AG556 is effective or safe for patients. The authors note the single-patient cell model and the need for in-vivo validation. Study: Sudhindar et al., Journal of Cell Science, September 2025, https://doi.org/10.1242/jcs.264141. (sudhindar2025urinaryrenalepithelial pages 12-13, sudhindar2025urinaryrenalepithelial pages 1-2)
The most defensible functional annotation for human NPHP1/O15259 is “phosphorylation-regulated, SH3-containing nephrocystin scaffold at the ciliary transition zone and epithelial adhesion sites.” Direct experiments establish its location, NPHP4-bridged module membership, CK2/PACS-1-dependent targeting, a polycystin-1 SH3 interaction and the consequences of human NPHP1 loss and re-expression. Selective ciliary gating is a strong transition-zone-complex-level interpretation, whereas the identity of an NPHP1-specific transported cargo, the relative contribution of its ciliary versus junctional pools to human kidney disease, and an effective NPHP1-directed treatment remain unresolved. (schermer2005phosphorylationbycasein pages 5-7, moran2024transportandbarrier pages 5-6, sang2011mappingthenphpjbtsmks pages 5-7, wodarczyk2010nephrocystin1formsa pages 3-5, sang2011mappingthenphpjbtsmks pages 7-9, arai2024patientderivedandgeneedited pages 4-6)
References
(fliegauf2006nephrocystinspecificallylocalizes pages 1-2): Manfred Fliegauf, Judit Horvath, Christian von Schnakenburg, Heike Olbrich, Dominik Müller, Julia Thumfart, Bernhard Schermer, Gregory J. Pazour, Hartmut P.H. Neumann, Hanswalter Zentgraf, Thomas Benzing, and Heymut Omran. Nephrocystin specifically localizes to the transition zone of renal and respiratory cilia and photoreceptor connecting cilia. Journal of the American Society of Nephrology : JASN, 17 9:2424-33, Sep 2006. URL: https://doi.org/10.1681/asn.2005121351, doi:10.1681/asn.2005121351. This article has 196 citations.
(wodarczyk2010nephrocystin1formsa pages 1-2): Claas Wodarczyk, Gianfranco Distefano, Isaline Rowe, Massimiliano Gaetani, Barbara Bricoli, Mordi Muorah, Andrea Spitaleri, Valeria Mannella, Piero Ricchiuto, Monika Pema, Maddalena Castelli, Ariel E. Casanova, Luca Mollica, Manuela Banzi, Manila Boca, Corinne Antignac, Sophie Saunier, Giovanna Musco, and Alessandra Boletta. Nephrocystin-1 forms a complex with polycystin-1 via a polyproline motif/sh3 domain interaction and regulates the apoptotic response in mammals. PLoS ONE, 5:e12719, Sep 2010. URL: https://doi.org/10.1371/journal.pone.0012719, doi:10.1371/journal.pone.0012719. This article has 47 citations and is from a peer-reviewed journal.
(moran2024transportandbarrier pages 5-6): Ailis L. Moran, Laura Louzao-Martinez, Dominic P. Norris, Dorien J. M. Peters, and Oliver E. Blacque. Transport and barrier mechanisms that regulate ciliary compartmentalization and ciliopathies. Nature Reviews Nephrology, 20:83-100, Oct 2024. URL: https://doi.org/10.1038/s41581-023-00773-2, doi:10.1038/s41581-023-00773-2. This article has 48 citations and is from a domain leading peer-reviewed journal.
(sang2011mappingthenphpjbtsmks pages 5-7): Liyun Sang, Julie J. Miller, Kevin C. Corbit, Rachel H. Giles, Matthew J. Brauer, Edgar A. Otto, Lisa M. Baye, Xiaohui Wen, Suzie J. Scales, Mandy Kwong, Erik G. Huntzicker, Mindan K. Sfakianos, Wendy Sandoval, J. Fernando Bazan, Priya Kulkarni, Francesc R. Garcia-Gonzalo, Allen D. Seol, John F. O'Toole, Susanne Held, Heiko M. Reutter, William S. Lane, Muhammad Arshad Rafiq, Abdul Noor, Muhammad Ansar, Akella Radha Rama Devi, Val C. Sheffield, Diane C. Slusarski, John B. Vincent, Daniel A. Doherty, Friedhelm Hildebrandt, Jeremy F. Reiter, and Peter K. Jackson. Mapping the nphp-jbts-mks protein network reveals ciliopathy disease genes and pathways. Cell, 145:513-528, May 2011. URL: https://doi.org/10.1016/j.cell.2011.04.019, doi:10.1016/j.cell.2011.04.019. This article has 761 citations and is from a highest quality peer-reviewed journal.
(sang2011mappingthenphpjbtsmks pages 7-9): Liyun Sang, Julie J. Miller, Kevin C. Corbit, Rachel H. Giles, Matthew J. Brauer, Edgar A. Otto, Lisa M. Baye, Xiaohui Wen, Suzie J. Scales, Mandy Kwong, Erik G. Huntzicker, Mindan K. Sfakianos, Wendy Sandoval, J. Fernando Bazan, Priya Kulkarni, Francesc R. Garcia-Gonzalo, Allen D. Seol, John F. O'Toole, Susanne Held, Heiko M. Reutter, William S. Lane, Muhammad Arshad Rafiq, Abdul Noor, Muhammad Ansar, Akella Radha Rama Devi, Val C. Sheffield, Diane C. Slusarski, John B. Vincent, Daniel A. Doherty, Friedhelm Hildebrandt, Jeremy F. Reiter, and Peter K. Jackson. Mapping the nphp-jbts-mks protein network reveals ciliopathy disease genes and pathways. Cell, 145:513-528, May 2011. URL: https://doi.org/10.1016/j.cell.2011.04.019, doi:10.1016/j.cell.2011.04.019. This article has 761 citations and is from a highest quality peer-reviewed journal.
(arai2024patientderivedandgeneedited pages 4-6): Yutaka Arai, Hidenori Ito, Tomoya Shimizu, Yuzuno Shimoda, Dan Song, Mami Matsuo-Takasaki, Tadayoshi Hayata, and Yohei Hayashi. Patient-derived and gene-edited pluripotent stem cells lacking nphp1 recapitulate juvenile nephronophthisis in abnormalities of primary cilia and renal cyst formation. Frontiers in Cell and Developmental Biology, Jun 2024. URL: https://doi.org/10.3389/fcell.2024.1370723, doi:10.3389/fcell.2024.1370723. This article has 12 citations.
(schermer2005phosphorylationbycasein pages 5-7): Bernhard Schermer, Katja Höpker, Heymut Omran, Cristina Ghenoiu, Manfred Fliegauf, Andrea Fekete, Judit Horvath, Michael Köttgen, Matthias Hackl, Stefan Zschiedrich, Tobias B Huber, Albrecht Kramer-Zucker, Hanswalter Zentgraf, Andree Blaukat, Gerd Walz, and Thomas Benzing. Phosphorylation by casein kinase 2 induces pacs‐1 binding of nephrocystin and targeting to cilia. The EMBO Journal, 24:4415-4424, Dec 2005. URL: https://doi.org/10.1038/sj.emboj.7600885, doi:10.1038/sj.emboj.7600885. This article has 126 citations.
(schermer2005phosphorylationbycasein pages 7-8): Bernhard Schermer, Katja Höpker, Heymut Omran, Cristina Ghenoiu, Manfred Fliegauf, Andrea Fekete, Judit Horvath, Michael Köttgen, Matthias Hackl, Stefan Zschiedrich, Tobias B Huber, Albrecht Kramer-Zucker, Hanswalter Zentgraf, Andree Blaukat, Gerd Walz, and Thomas Benzing. Phosphorylation by casein kinase 2 induces pacs‐1 binding of nephrocystin and targeting to cilia. The EMBO Journal, 24:4415-4424, Dec 2005. URL: https://doi.org/10.1038/sj.emboj.7600885, doi:10.1038/sj.emboj.7600885. This article has 126 citations.
(fliegauf2006nephrocystinspecificallylocalizes pages 2-3): Manfred Fliegauf, Judit Horvath, Christian von Schnakenburg, Heike Olbrich, Dominik Müller, Julia Thumfart, Bernhard Schermer, Gregory J. Pazour, Hartmut P.H. Neumann, Hanswalter Zentgraf, Thomas Benzing, and Heymut Omran. Nephrocystin specifically localizes to the transition zone of renal and respiratory cilia and photoreceptor connecting cilia. Journal of the American Society of Nephrology : JASN, 17 9:2424-33, Sep 2006. URL: https://doi.org/10.1681/asn.2005121351, doi:10.1681/asn.2005121351. This article has 196 citations.
(sang2011mappingthenphpjbtsmks pages 3-5): Liyun Sang, Julie J. Miller, Kevin C. Corbit, Rachel H. Giles, Matthew J. Brauer, Edgar A. Otto, Lisa M. Baye, Xiaohui Wen, Suzie J. Scales, Mandy Kwong, Erik G. Huntzicker, Mindan K. Sfakianos, Wendy Sandoval, J. Fernando Bazan, Priya Kulkarni, Francesc R. Garcia-Gonzalo, Allen D. Seol, John F. O'Toole, Susanne Held, Heiko M. Reutter, William S. Lane, Muhammad Arshad Rafiq, Abdul Noor, Muhammad Ansar, Akella Radha Rama Devi, Val C. Sheffield, Diane C. Slusarski, John B. Vincent, Daniel A. Doherty, Friedhelm Hildebrandt, Jeremy F. Reiter, and Peter K. Jackson. Mapping the nphp-jbts-mks protein network reveals ciliopathy disease genes and pathways. Cell, 145:513-528, May 2011. URL: https://doi.org/10.1016/j.cell.2011.04.019, doi:10.1016/j.cell.2011.04.019. This article has 761 citations and is from a highest quality peer-reviewed journal.
(wodarczyk2010nephrocystin1formsa pages 6-8): Claas Wodarczyk, Gianfranco Distefano, Isaline Rowe, Massimiliano Gaetani, Barbara Bricoli, Mordi Muorah, Andrea Spitaleri, Valeria Mannella, Piero Ricchiuto, Monika Pema, Maddalena Castelli, Ariel E. Casanova, Luca Mollica, Manuela Banzi, Manila Boca, Corinne Antignac, Sophie Saunier, Giovanna Musco, and Alessandra Boletta. Nephrocystin-1 forms a complex with polycystin-1 via a polyproline motif/sh3 domain interaction and regulates the apoptotic response in mammals. PLoS ONE, 5:e12719, Sep 2010. URL: https://doi.org/10.1371/journal.pone.0012719, doi:10.1371/journal.pone.0012719. This article has 47 citations and is from a peer-reviewed journal.
(wodarczyk2010nephrocystin1formsa pages 3-5): Claas Wodarczyk, Gianfranco Distefano, Isaline Rowe, Massimiliano Gaetani, Barbara Bricoli, Mordi Muorah, Andrea Spitaleri, Valeria Mannella, Piero Ricchiuto, Monika Pema, Maddalena Castelli, Ariel E. Casanova, Luca Mollica, Manuela Banzi, Manila Boca, Corinne Antignac, Sophie Saunier, Giovanna Musco, and Alessandra Boletta. Nephrocystin-1 forms a complex with polycystin-1 via a polyproline motif/sh3 domain interaction and regulates the apoptotic response in mammals. PLoS ONE, 5:e12719, Sep 2010. URL: https://doi.org/10.1371/journal.pone.0012719, doi:10.1371/journal.pone.0012719. This article has 47 citations and is from a peer-reviewed journal.
(hellmann2024immunofluorescenceanalysesof pages 1-2): Carlotta Hellmann, Kai Wohlgemuth, Petra Pennekamp, Sebastian George, Mareike Dahmer-Heath, Martin Konrad, Heymut Omran, Jens König, C. Bergmann, M. Cetiner, J. Drube, C. Gimpel, J. Göbel, D. Haffner, T. Illig, N. Klopp, M. C. Liebau, S. Lienkamp, C. Okorn, L. Pape, F. Schaefer, B. Schermer, H. Storf, A. Titieni, S. Weber, W. Ziegler, I. Kamp-Becker, J. Vasseur, S. Kollmann, and J. Gerß. Immunofluorescence analyses of respiratory epithelial cells aid the diagnosis of nephronophthisis. Pediatric Nephrology (Berlin, Germany), 39:3471-3483, Aug 2024. URL: https://doi.org/10.1007/s00467-024-06443-0, doi:10.1007/s00467-024-06443-0. This article has 3 citations.
(hellmann2024immunofluorescenceanalysesof pages 5-7): Carlotta Hellmann, Kai Wohlgemuth, Petra Pennekamp, Sebastian George, Mareike Dahmer-Heath, Martin Konrad, Heymut Omran, Jens König, C. Bergmann, M. Cetiner, J. Drube, C. Gimpel, J. Göbel, D. Haffner, T. Illig, N. Klopp, M. C. Liebau, S. Lienkamp, C. Okorn, L. Pape, F. Schaefer, B. Schermer, H. Storf, A. Titieni, S. Weber, W. Ziegler, I. Kamp-Becker, J. Vasseur, S. Kollmann, and J. Gerß. Immunofluorescence analyses of respiratory epithelial cells aid the diagnosis of nephronophthisis. Pediatric Nephrology (Berlin, Germany), 39:3471-3483, Aug 2024. URL: https://doi.org/10.1007/s00467-024-06443-0, doi:10.1007/s00467-024-06443-0. This article has 3 citations.
(arai2024patientderivedandgeneedited pages 6-8): Yutaka Arai, Hidenori Ito, Tomoya Shimizu, Yuzuno Shimoda, Dan Song, Mami Matsuo-Takasaki, Tadayoshi Hayata, and Yohei Hayashi. Patient-derived and gene-edited pluripotent stem cells lacking nphp1 recapitulate juvenile nephronophthisis in abnormalities of primary cilia and renal cyst formation. Frontiers in Cell and Developmental Biology, Jun 2024. URL: https://doi.org/10.3389/fcell.2024.1370723, doi:10.3389/fcell.2024.1370723. This article has 12 citations.
(gupta2021nephronophthisispathobiologyandmolecular pages 4-6): Shabarni Gupta, Justyna E. Ozimek-Kulik, and Jacqueline Kathleen Phillips. Nephronophthisis-pathobiology and molecular pathogenesis of a rare kidney genetic disease. Genes, 12:1762, Nov 2021. URL: https://doi.org/10.3390/genes12111762, doi:10.3390/genes12111762. This article has 48 citations.
(park2022compositionorganizationand pages 6-8): Kwangjin Park and Michel R Leroux. Composition, organization and mechanisms of the transition zone, a gate for the cilium. EMBO reports, Nov 2022. URL: https://doi.org/10.15252/embr.202255420, doi:10.15252/embr.202255420. This article has 94 citations and is from a highest quality peer-reviewed journal.
(schermer2005phosphorylationbycasein pages 3-5): Bernhard Schermer, Katja Höpker, Heymut Omran, Cristina Ghenoiu, Manfred Fliegauf, Andrea Fekete, Judit Horvath, Michael Köttgen, Matthias Hackl, Stefan Zschiedrich, Tobias B Huber, Albrecht Kramer-Zucker, Hanswalter Zentgraf, Andree Blaukat, Gerd Walz, and Thomas Benzing. Phosphorylation by casein kinase 2 induces pacs‐1 binding of nephrocystin and targeting to cilia. The EMBO Journal, 24:4415-4424, Dec 2005. URL: https://doi.org/10.1038/sj.emboj.7600885, doi:10.1038/sj.emboj.7600885. This article has 126 citations.
(liebau2011nephrocystin4regulatespyk2induced pages 1-2): Max C. Liebau, Katja Höpker, Roman U. Müller, Ingolf Schmedding, Sibylle Zank, Benjamin Schairer, Francesca Fabretti, Martin Höhne, Malte P. Bartram, Claudia Dafinger, Matthias Hackl, Volker Burst, Sandra Habbig, Hanswalter Zentgraf, Andree Blaukat, Gerd Walz, Thomas Benzing, and Bernhard Schermer. Nephrocystin-4 regulates pyk2-induced tyrosine phosphorylation of nephrocystin-1 to control targeting to monocilia. Journal of Biological Chemistry, 286:14237-14245, Apr 2011. URL: https://doi.org/10.1074/jbc.m110.165464, doi:10.1074/jbc.m110.165464. This article has 38 citations and is from a domain leading peer-reviewed journal.
(liebau2011nephrocystin4regulatespyk2induced pages 6-8): Max C. Liebau, Katja Höpker, Roman U. Müller, Ingolf Schmedding, Sibylle Zank, Benjamin Schairer, Francesca Fabretti, Martin Höhne, Malte P. Bartram, Claudia Dafinger, Matthias Hackl, Volker Burst, Sandra Habbig, Hanswalter Zentgraf, Andree Blaukat, Gerd Walz, Thomas Benzing, and Bernhard Schermer. Nephrocystin-4 regulates pyk2-induced tyrosine phosphorylation of nephrocystin-1 to control targeting to monocilia. Journal of Biological Chemistry, 286:14237-14245, Apr 2011. URL: https://doi.org/10.1074/jbc.m110.165464, doi:10.1074/jbc.m110.165464. This article has 38 citations and is from a domain leading peer-reviewed journal.
(moran2024transportandbarrier pages 14-15): Ailis L. Moran, Laura Louzao-Martinez, Dominic P. Norris, Dorien J. M. Peters, and Oliver E. Blacque. Transport and barrier mechanisms that regulate ciliary compartmentalization and ciliopathies. Nature Reviews Nephrology, 20:83-100, Oct 2024. URL: https://doi.org/10.1038/s41581-023-00773-2, doi:10.1038/s41581-023-00773-2. This article has 48 citations and is from a domain leading peer-reviewed journal.
(moran2024transportandbarrier pages 3-5): Ailis L. Moran, Laura Louzao-Martinez, Dominic P. Norris, Dorien J. M. Peters, and Oliver E. Blacque. Transport and barrier mechanisms that regulate ciliary compartmentalization and ciliopathies. Nature Reviews Nephrology, 20:83-100, Oct 2024. URL: https://doi.org/10.1038/s41581-023-00773-2, doi:10.1038/s41581-023-00773-2. This article has 48 citations and is from a domain leading peer-reviewed journal.
(wolf2011nephronophthisis pages 4-6): Matthias T. F. Wolf and Friedhelm Hildebrandt. Nephronophthisis. Pediatric Nephrology, 26:181-194, Jul 2011. URL: https://doi.org/10.1007/s00467-010-1585-z, doi:10.1007/s00467-010-1585-z. This article has 275 citations and is from a domain leading peer-reviewed journal.
(arai2024patientderivedandgeneedited pages 1-2): Yutaka Arai, Hidenori Ito, Tomoya Shimizu, Yuzuno Shimoda, Dan Song, Mami Matsuo-Takasaki, Tadayoshi Hayata, and Yohei Hayashi. Patient-derived and gene-edited pluripotent stem cells lacking nphp1 recapitulate juvenile nephronophthisis in abnormalities of primary cilia and renal cyst formation. Frontiers in Cell and Developmental Biology, Jun 2024. URL: https://doi.org/10.3389/fcell.2024.1370723, doi:10.3389/fcell.2024.1370723. This article has 12 citations.
(sudhindar2025urinaryrenalepithelial pages 12-13): Praveen Dhondurao Sudhindar, Eric Olinger, Zachary T. Sentell, Holly Mabillard, Barbora Dicka, Katrina Wood, Dominic Rutland, Catherine Collins, Marco Trevisan-Herraz, John A. Sayer, and Juliana E. Arcila-Galvis. Urinary renal epithelial cells can be used for nphp1 phenotyping and a personalized therapeutic strategy. Sep 2025. URL: https://doi.org/10.1242/jcs.264141, doi:10.1242/jcs.264141. This article has 3 citations and is from a domain leading peer-reviewed journal.
(sudhindar2025urinaryrenalepithelial pages 1-2): Praveen Dhondurao Sudhindar, Eric Olinger, Zachary T. Sentell, Holly Mabillard, Barbora Dicka, Katrina Wood, Dominic Rutland, Catherine Collins, Marco Trevisan-Herraz, John A. Sayer, and Juliana E. Arcila-Galvis. Urinary renal epithelial cells can be used for nphp1 phenotyping and a personalized therapeutic strategy. Sep 2025. URL: https://doi.org/10.1242/jcs.264141, doi:10.1242/jcs.264141. This article has 3 citations and is from a domain leading peer-reviewed journal.