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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 supplied UniProt record identifies Q9Y366 as human intraflagellar transport protein 52 homolog, encoded by IFT52; C20orf9, NGD5 and CGI-53 are supplied aliases. Independent studies explicitly investigate human IFT52, identify its product as an intraflagellar transport B (IFT-B) subunit, and describe the corresponding GIFT, central and C-terminal architecture. The reviewed literature therefore supports research on the specified protein, not a similarly named gene. The accession and aliases themselves are taken from the supplied UniProt record rather than independently established by the retrieved papers. (ishida2022molecularbasisunderlying pages 1-2, taschner2014crystalstructuresof pages 2-3)
Functional conclusion. IFT52 is principally a nonenzymatic structural organizer and coupling component of the IFT-B complex. It helps assemble the protein scaffold of intraflagellar transport trains, couples IFT-B subassemblies to one another and to the kinesin-II transport machinery, and thereby supports cilium formation and transport toward the ciliary tip. It is not itself the motor, a transporter with a defined small-molecule substrate, or an enzyme with an established catalytic reaction. Specific cargo associations demonstrated in IFT52-perturbed cells are discussed below; the evidence does not assign IFT52 an independently established, exclusive cargo specificity. (ishida2022molecularbasisunderlying pages 3-5, lacey2023themolecularstructure pages 4-5, ishida2022molecularbasisunderlying pages 1-2, ishida2022molecularbasisunderlying pages 7-10)
IFT-B supplies the backbone of polymeric trains moving along ciliary microtubules. Its IFT-B1 core and IFT-B2 peripheral modules meet at a composite interface containing IFT52 and IFT88 on the B1 side and IFT38 and IFT57 on the B2 side. Human-cell interaction assays identify this four-protein assembly as a binding site for heterotrimeric kinesin-II (KIF3A–KIF3B–KAP3). The IFT52–IFT88 pair also contributes to the interface with IFT-A proteins IFT122–IFT144; these are interactions within a larger transport apparatus, not evidence that IFT52 alone drives retrograde movement. (ishida2022molecularbasisunderlying pages 2-3, ishida2022molecularbasisunderlying pages 3-5, ishida2022molecularbasisunderlying pages 1-2)
The domain assignments supplied for Q9Y366—IFT52/GIFT, central and C-terminal regions—fit experimental structural work. An N-terminal GIFT region contributes to an intact B1–B2 assembly interface: the human disease-associated p.Ala199Thr substitution retains several tested B1 contacts but weakens association with IFT38/IFT57 and kinesin-II. A central, proline-rich region associates with IFT70; a conserved algal IFT52 peptide is enclosed by IFT70’s tetratricopeptide-repeat superhelix. Structural models additionally place the central IFT52 region alongside IFT88 at the B1–B2 junction. The C-terminal region forms an α-helical heterodimer with IFT46, facilitating incorporation of other IFT-B components. These conclusions combine human interaction assays with structures determined predominantly in Chlamydomonas and Tetrahymena: their published residue numbers must not be applied directly to human Q9Y366. The cropped published domain schematic and IFT70–IFT52 structure illustrate the assignments. (ishida2022molecularbasisunderlying pages 2-3, taschner2014crystalstructuresof pages 7-8, taschner2014crystalstructuresof pages 2-3, lacey2023themolecularstructure pages 4-5, taschner2014crystalstructuresof media 5b5ac48e)
The interaction map is supported by perturbation experiments rather than structure prediction alone. In human HEK293T interaction assays, the disease-associated C-terminal truncation p.Leu293Alafs (reported as L293Afs) failed to support tested IFT-B contacts, B1–B2 coupling, kinesin-II association and an IFT-A-associated interaction. In IFT52-knockout human retinal pigment epithelial cells it failed to rescue ciliogenesis, whereas wild-type IFT52 rescued it; p.Ala199Thr afforded incomplete rescue. Separately, structural modeling of IFT-B was checked against cross-linking mass spectrometry, scattering, crystallography, mutagenesis and binding assays. (ishida2022molecularbasisunderlying pages 2-3, ishida2022molecularbasisunderlying pages 3-5, petriman2022biochemicallyvalidatedstructural pages 4-6)
IFT52 acts inside the cell at the mother centriole/basal body and within the cilium, rather than as a secreted protein. IFT-B subunits accumulate at the ciliary base, where the transport apparatus is recruited and assembled; IFT-B-containing trains subsequently traverse the ciliary shaft toward the tip. In human hTERT-RPE1 cells, IFT52 knockout eliminates detectable mother-centriole IFT88 and IFT38 and prevents ciliogenesis. A 2025 knockout comparison found that IFT38 can still be recruited to a centriole in non-ciliated KIF3B-knockout cells: IFT-B recruitment therefore does not simply follow cilium formation. Another 2025 study found mother-centriole recruitment of IFT-A and IFT-B can occur independently, refining—but not making IFT52 dispensable for—the model of pre-train assembly. (ishida2022molecularbasisunderlying pages 3-5, tasaki2025mutuallyindependentand pages 2-4, tasaki2025assemblyandmother pages 5-10)
The most detailed in situ train architecture currently cited here comes from 2023 cryo-electron tomography and structure-guided modeling of Chlamydomonas reinhardtii flagella, not human cilia. It places IFT52 centrally in the repeating anterograde IFT-B architecture and links its configuration to IFT88 and the B1–B2 interface. This is strong evidence for a conserved structural mechanism, although individual human-train contacts remain an extrapolation. Earlier experiments in Chlamydomonas found that IFT52 associates with IFT46 in the cytoplasm and recruits it to basal bodies and flagella, supporting preassembly and targeting as well as transport roles. (lacey2023themolecularstructure pages 4-5, lacey2023themolecularstructure pages 1-2, lv2017intraflagellartransportprotein pages 1-4)
An additional, less-established extraciliary centrosomal role has been proposed. A 2019 study reported distal-centriole association of IFT52 with centrin and, particularly in Ift52-null mouse IMCD3 kidney cells, abnormal centrin distribution, microtubule anchorage/dynamics and centrosome cohesion; wild-type but not certain patient-derived variant constructs corrected centriole splitting. These observations merit consideration when interpreting renal phenotypes, but evidence that this mechanism independently causes human disease is weaker than the convergent human-cell evidence for IFT-B assembly and ciliogenesis. (dupont2019humanift52mutations pages 16-21, dupont2019humanift52mutations pages 13-16)
The following evidence summary separates human experiments from conserved-organism inference.
| Evidence setting | Finding relevant to IFT52 | Interpretation or limitation |
|---|---|---|
| 2014 — algal and protist structural studies | Crystal structures of IFT70–IFT52 and IFT52–IFT46 supported an architecture comprising an N-terminal GIFT domain, central region and small C-terminal region. The conserved central region binds IFT70, whereas the C-terminal region forms an α-helical interface with IFT46 and helps connect IFT-B assemblies. (taschner2014crystalstructuresof pages 7-8, taschner2014crystalstructuresof pages 8-10, taschner2014crystalstructuresof pages 2-3) | Strong structural evidence for a scaffold function. Residue indices and structures came principally from Chlamydomonas and Tetrahymena proteins; conservation supports, but does not prove, identical residue-level contacts in human Q9Y366. |
| 2016 — human SRPS fibroblasts and chondrocytes | Biallelic IFT52 variants markedly reduced IFT52 and destabilized other IFT-B components, including IFT74, IFT81 and IFT88. Patient cells showed an approximately 60% reduction in ciliation, abnormal ciliary-length regulation and loss of detectable ciliary IFT88 above background. (zhang2016ift52mutationsdestabilize pages 5-6, zhang2016ift52mutationsdestabilize pages 3-4, zhang2016ift52mutationsdestabilize pages 4-5, zhang2016ift52mutationsdestabilize pages 1-1) | Direct patient-cell evidence that IFT52 is required for IFT-B stability and ciliogenesis; the compound-allelic state does not isolate the effect of each allele. |
| 2019 — human genetics and mouse IMCD3 cells | Human biallelic variants were associated with short-rib thoracic dysplasia, Sensenbrenner syndrome or CAKUT, with residual-function alleles helping explain phenotypic severity. In Ift52-null mouse IMCD3 cells, IFT52 loss altered centrin organization, centrosomal microtubule anchorage and dynamics, and centriole cohesion; wild-type rescue was more effective than N98S or D259H rescue. (dupont2019humanift52mutations pages 13-16, dupont2019humanift52mutations pages 6-9, dupont2019humanift52mutations pages 16-21) | Human genetics supports disease relevance, but the detailed centrin and centrosome mechanism was established mainly in a murine kidney-cell model and is less independently replicated than the canonical IFT-B function. |
| 2022 — human hTERT-RPE1 knockout and rescue | IFT52 knockout abolished ciliogenesis and basal-body IFT88 localization. Wild-type IFT52 rescued these defects; A199T produced partial rescue with reduced IFT-B–kinesin-II coupling, whereas L293Afs* failed to restore cilia and behaved as a functional null. A199T and Δ139–162 did not visibly alter agonist-induced SMO entry or GPR161 exit, although KIF17 and ICK/CILK1 tip localization was impaired. (ishida2022molecularbasisunderlying pages 3-5, ishida2022molecularbasisunderlying pages 7-10, ishida2022molecularbasisunderlying pages 5-7) | Direct human-cell evidence for IFT52 as an IFT-B assembly and motor-coupling hub. The receptor-trafficking assay does not exclude defects in downstream GLI processing, transcription or other signaling contexts. |
| 2023 — in situ cryo-electron tomography in Chlamydomonas | Molecular modeling of anterograde trains placed IFT52 centrally within the repeating IFT-B1 architecture. Its central region associates with IFT88 and contributes with IFT57 and IFT38 to the IFT-B1–IFT-B2 interface; IFT-B repeats occur at approximately 6-nm spacing. (lacey2023themolecularstructure pages 4-5, conde2024shippoproteinfunction pages 36-39, lacey2023themolecularstructure pages 1-2) | High-resolution native-context evidence for a structural train-organizing role rather than catalytic activity. The structure is from algal flagella and is not a human IFT-train structure. |
| 2025 — human hTERT-RPE1 knockout studies | IFT52 knockout eliminated detectable mother-centriole recruitment of IFT38 and IFT88. IFT-B recruitment persisted in non-ciliated KIF3B-knockout cells, showing that recruitment to the mother centriole can precede and occur independently of ciliogenesis. (tasaki2025mutuallyindependentand pages 2-4, tasaki2025assemblyandmother pages 5-10) | Direct human-cell evidence that the IFT52-containing IFT-B1b module is required for IFT-B assembly or recruitment at the ciliary base; it does not distinguish defective preassembly from defective centriole docking. |
Table: Evidence progresses from conserved model-organism structures to human patient cells and targeted human-cell knockouts. The table distinguishes direct human findings from conclusions based on non-human systems.
IFT52 is best placed upstream of cilium-dependent signaling, by sustaining the organelle and the transport machinery that position signaling proteins. In a zebrafish ift52 knockout, reduced expression of the Hedgehog target genes ptc2 and gli1 accompanied ciliary and craniofacial defects, supporting a connection to Hedgehog-dependent development. This is a model-organism phenotype, not proof that IFT52 directly binds Hedgehog components or regulates GLI transcription in human cells. (dupont2019humanift52mutations pages 9-13)
Human-cell results make the distinction more precise. In IFT52-knockout RPE1 cells complemented with the partially functional Δ139–162 or p.Ala199Thr variant, Smoothened agonist still produced broadly normal ciliary SMO entry and GPR161 exit among the cilia assessed. Nevertheless, p.Ala199Thr diminished ciliary IFT-B abundance, and variant-expressing cells showed impaired tip localization of KIF17 and ICK/CILK1. Thus the observed defect is in IFT-B assembly/motor coupling and selected tip trafficking; it would be incorrect to claim that these variants demonstrably block every Hedgehog receptor-trafficking step. Downstream GLI processing or transcription was not established by that human-cell receptor assay. Nor do the cited IFT52-specific experiments establish a direct Wnt-signaling, kinase or enzymatic activity for IFT52. (ishida2022molecularbasisunderlying pages 3-5, ishida2022molecularbasisunderlying pages 7-10, ishida2022molecularbasisunderlying pages 5-7)
Biallelic human IFT52 variants have been reported in skeletal ciliopathies, including short-rib polydactyly/short-rib thoracic dysplasia and cranioectodermal dysplasia (Sensenbrenner syndrome). A 2019 investigation additionally described an individual with congenital kidney/urinary-tract abnormalities and homozygous p.Asp259His. Clinical presentations and variant effects are not interchangeable: p.Arg142* was initially described as a nonsense variant, but subsequent analysis detected exon skipping and a residual, partially functional protein; p.Asp259His retained substantial ciliary-complex behavior in tested cells, despite effects in additional assays. The authors cautioned that modifiers or oligogenic factors could contribute to the renal presentation. (dupont2019humanift52mutations pages 13-16, dupont2019humanift52mutations pages 6-9, dupont2019humanift52mutations pages 16-21, girisha2016ahomozygousnonsense pages 1-2)
Patient-cell findings connect genotype to mechanism. In the original short-rib polydactyly report, affected fibroblasts had an approximately 60% reduction in ciliation; IFT52 and other IFT-B components were reduced, and detectable ciliary IFT88 was lost. In the 2022 human-cell knockout/rescue experiments, wild-type IFT52 restored cilia, p.Ala199Thr produced milder defects, and L293Afs did not restore cilium formation. These are informative quantitative and functional observations, not* population estimates of disease frequency or evidence of a treatment. (zhang2016ift52mutationsdestabilize pages 4-5, ishida2022molecularbasisunderlying pages 3-5, zhang2016ift52mutationsdestabilize pages 1-1)
The principal current application is research and variant interpretation: sequencing identifies candidate biallelic variants; patient fibroblasts or engineered RPE1 cells permit testing of IFT-B stability, basal-body recruitment, ciliation, ciliary IFT88 and variant-specific rescue. Structural interfaces help interpret why a variant disrupts the scaffold. Phenotypes should be interpreted alongside the precise allele and experimental system, because a partially functional variant can preserve one trafficking readout while impairing another. The sources reviewed do not establish an IFT52-directed clinical therapy. (zhang2016ift52mutationsdestabilize pages 5-6, ishida2022molecularbasisunderlying pages 3-5, dupont2019humanift52mutations pages 13-16, ishida2022molecularbasisunderlying pages 5-7)
Overall assessment: Direct human genetics and knockout/rescue experiments strongly establish IFT52 as an IFT-B scaffold required for ciliary assembly and anterograde transport. The 2023 structural advance explains that function largely in a conserved algal system; subsequent human-cell experiments refine where the complex assembles. Cargo-specific signaling effects and an independent centrosome-to-disease mechanism remain more conditional conclusions. (ishida2022molecularbasisunderlying pages 3-5, lacey2023themolecularstructure pages 4-5, tasaki2025assemblyandmother pages 5-10, dupont2019humanift52mutations pages 16-21)
References
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(taschner2014crystalstructuresof pages 2-3): Michael Taschner, Fruzsina Kotsis, Philipp Braeuer, E. Wolfgang Kuehn, and Esben Lorentzen. Crystal structures of ift70/52 and ift52/46 provide insight into intraflagellar transport b core complex assembly. The Journal of Cell Biology, 207:269-282, Oct 2014. URL: https://doi.org/10.1083/jcb.201408002, doi:10.1083/jcb.201408002. This article has 139 citations.
(ishida2022molecularbasisunderlying pages 3-5): Yamato Ishida, Koshi Tasaki, Yohei Katoh, and Kazuhisa Nakayama. Molecular basis underlying the ciliary defects caused by ift52 variations found in skeletal ciliopathies. Molecular Biology of the Cell, Aug 2022. URL: https://doi.org/10.1091/mbc.e22-05-0188, doi:10.1091/mbc.e22-05-0188. This article has 13 citations and is from a domain leading peer-reviewed journal.
(lacey2023themolecularstructure pages 4-5): Samuel E. Lacey, Helen E. Foster, and Gaia Pigino. The molecular structure of ift-a and ift-b in anterograde intraflagellar transport trains. Nature Structural & Molecular Biology, 30:584-593, Jan 2023. URL: https://doi.org/10.1038/s41594-022-00905-5, doi:10.1038/s41594-022-00905-5. This article has 124 citations and is from a highest quality peer-reviewed journal.
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(ishida2022molecularbasisunderlying pages 2-3): Yamato Ishida, Koshi Tasaki, Yohei Katoh, and Kazuhisa Nakayama. Molecular basis underlying the ciliary defects caused by ift52 variations found in skeletal ciliopathies. Molecular Biology of the Cell, Aug 2022. URL: https://doi.org/10.1091/mbc.e22-05-0188, doi:10.1091/mbc.e22-05-0188. This article has 13 citations and is from a domain leading peer-reviewed journal.
(taschner2014crystalstructuresof pages 7-8): Michael Taschner, Fruzsina Kotsis, Philipp Braeuer, E. Wolfgang Kuehn, and Esben Lorentzen. Crystal structures of ift70/52 and ift52/46 provide insight into intraflagellar transport b core complex assembly. The Journal of Cell Biology, 207:269-282, Oct 2014. URL: https://doi.org/10.1083/jcb.201408002, doi:10.1083/jcb.201408002. This article has 139 citations.
(taschner2014crystalstructuresof media 5b5ac48e): Michael Taschner, Fruzsina Kotsis, Philipp Braeuer, E. Wolfgang Kuehn, and Esben Lorentzen. Crystal structures of ift70/52 and ift52/46 provide insight into intraflagellar transport b core complex assembly. The Journal of Cell Biology, 207:269-282, Oct 2014. URL: https://doi.org/10.1083/jcb.201408002, doi:10.1083/jcb.201408002. This article has 139 citations.
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(dupont2019humanift52mutations pages 16-21): Marie Alice Dupont, Camille Humbert, Céline Huber, Quentin Siour, Ida Chiara Guerrera, Vincent Jung, Anni Christensen, Aurore Pouliet, Meriem Garfa-Traoré, Patrick Nitschké, Marie Injeyan, Kathryn Millar, David Chitayat, Patrick Shannon, Katta Mohan Girisha, Anju Shukla, Charlotte Mechler, Esben Lorentzen, Alexandre Benmerah, Valérie Cormier-Daire, Cécile Jeanpierre, Sophie Saunier, and Marion Delous. Human ift52 mutations uncover a novel role for the protein in microtubule dynamics and centrosome cohesion. Human molecular genetics, 28:2720-2737, May 2019. URL: https://doi.org/10.1093/hmg/ddz091, doi:10.1093/hmg/ddz091. This article has 39 citations and is from a domain leading peer-reviewed journal.
(dupont2019humanift52mutations pages 13-16): Marie Alice Dupont, Camille Humbert, Céline Huber, Quentin Siour, Ida Chiara Guerrera, Vincent Jung, Anni Christensen, Aurore Pouliet, Meriem Garfa-Traoré, Patrick Nitschké, Marie Injeyan, Kathryn Millar, David Chitayat, Patrick Shannon, Katta Mohan Girisha, Anju Shukla, Charlotte Mechler, Esben Lorentzen, Alexandre Benmerah, Valérie Cormier-Daire, Cécile Jeanpierre, Sophie Saunier, and Marion Delous. Human ift52 mutations uncover a novel role for the protein in microtubule dynamics and centrosome cohesion. Human molecular genetics, 28:2720-2737, May 2019. URL: https://doi.org/10.1093/hmg/ddz091, doi:10.1093/hmg/ddz091. This article has 39 citations and is from a domain leading peer-reviewed journal.
(taschner2014crystalstructuresof pages 8-10): Michael Taschner, Fruzsina Kotsis, Philipp Braeuer, E. Wolfgang Kuehn, and Esben Lorentzen. Crystal structures of ift70/52 and ift52/46 provide insight into intraflagellar transport b core complex assembly. The Journal of Cell Biology, 207:269-282, Oct 2014. URL: https://doi.org/10.1083/jcb.201408002, doi:10.1083/jcb.201408002. This article has 139 citations.
(zhang2016ift52mutationsdestabilize pages 5-6): Wenjuan Zhang, S. Paige Taylor, Lisette Nevarez, Ralph S. Lachman, Deborah A. Nickerson, Michael Bamshad, Deborah Krakow, and Daniel H. Cohn. Ift52 mutations destabilize anterograde complex assembly, disrupt ciliogenesis and result in short rib polydactyly syndrome. Human molecular genetics, 25 18:4012-4020, Sep 2016. URL: https://doi.org/10.1093/hmg/ddw241, doi:10.1093/hmg/ddw241. This article has 58 citations and is from a domain leading peer-reviewed journal.
(zhang2016ift52mutationsdestabilize pages 3-4): Wenjuan Zhang, S. Paige Taylor, Lisette Nevarez, Ralph S. Lachman, Deborah A. Nickerson, Michael Bamshad, Deborah Krakow, and Daniel H. Cohn. Ift52 mutations destabilize anterograde complex assembly, disrupt ciliogenesis and result in short rib polydactyly syndrome. Human molecular genetics, 25 18:4012-4020, Sep 2016. URL: https://doi.org/10.1093/hmg/ddw241, doi:10.1093/hmg/ddw241. This article has 58 citations and is from a domain leading peer-reviewed journal.
(zhang2016ift52mutationsdestabilize pages 4-5): Wenjuan Zhang, S. Paige Taylor, Lisette Nevarez, Ralph S. Lachman, Deborah A. Nickerson, Michael Bamshad, Deborah Krakow, and Daniel H. Cohn. Ift52 mutations destabilize anterograde complex assembly, disrupt ciliogenesis and result in short rib polydactyly syndrome. Human molecular genetics, 25 18:4012-4020, Sep 2016. URL: https://doi.org/10.1093/hmg/ddw241, doi:10.1093/hmg/ddw241. This article has 58 citations and is from a domain leading peer-reviewed journal.
(zhang2016ift52mutationsdestabilize pages 1-1): Wenjuan Zhang, S. Paige Taylor, Lisette Nevarez, Ralph S. Lachman, Deborah A. Nickerson, Michael Bamshad, Deborah Krakow, and Daniel H. Cohn. Ift52 mutations destabilize anterograde complex assembly, disrupt ciliogenesis and result in short rib polydactyly syndrome. Human molecular genetics, 25 18:4012-4020, Sep 2016. URL: https://doi.org/10.1093/hmg/ddw241, doi:10.1093/hmg/ddw241. This article has 58 citations and is from a domain leading peer-reviewed journal.
(dupont2019humanift52mutations pages 6-9): Marie Alice Dupont, Camille Humbert, Céline Huber, Quentin Siour, Ida Chiara Guerrera, Vincent Jung, Anni Christensen, Aurore Pouliet, Meriem Garfa-Traoré, Patrick Nitschké, Marie Injeyan, Kathryn Millar, David Chitayat, Patrick Shannon, Katta Mohan Girisha, Anju Shukla, Charlotte Mechler, Esben Lorentzen, Alexandre Benmerah, Valérie Cormier-Daire, Cécile Jeanpierre, Sophie Saunier, and Marion Delous. Human ift52 mutations uncover a novel role for the protein in microtubule dynamics and centrosome cohesion. Human molecular genetics, 28:2720-2737, May 2019. URL: https://doi.org/10.1093/hmg/ddz091, doi:10.1093/hmg/ddz091. This article has 39 citations and is from a domain leading peer-reviewed journal.
(ishida2022molecularbasisunderlying pages 5-7): Yamato Ishida, Koshi Tasaki, Yohei Katoh, and Kazuhisa Nakayama. Molecular basis underlying the ciliary defects caused by ift52 variations found in skeletal ciliopathies. Molecular Biology of the Cell, Aug 2022. URL: https://doi.org/10.1091/mbc.e22-05-0188, doi:10.1091/mbc.e22-05-0188. This article has 13 citations and is from a domain leading peer-reviewed journal.
(conde2024shippoproteinfunction pages 36-39): J Sáez Conde. Shippo protein function in a protozoan and animal model system. Unknown journal, 2024.
(dupont2019humanift52mutations pages 9-13): Marie Alice Dupont, Camille Humbert, Céline Huber, Quentin Siour, Ida Chiara Guerrera, Vincent Jung, Anni Christensen, Aurore Pouliet, Meriem Garfa-Traoré, Patrick Nitschké, Marie Injeyan, Kathryn Millar, David Chitayat, Patrick Shannon, Katta Mohan Girisha, Anju Shukla, Charlotte Mechler, Esben Lorentzen, Alexandre Benmerah, Valérie Cormier-Daire, Cécile Jeanpierre, Sophie Saunier, and Marion Delous. Human ift52 mutations uncover a novel role for the protein in microtubule dynamics and centrosome cohesion. Human molecular genetics, 28:2720-2737, May 2019. URL: https://doi.org/10.1093/hmg/ddz091, doi:10.1093/hmg/ddz091. This article has 39 citations and is from a domain leading peer-reviewed journal.
(girisha2016ahomozygousnonsense pages 1-2): K. M. Girisha, A. Shukla, D. Trujillano, G. S. Bhavani, M. Hebbar, R. Kadavigere, and A. Rolfs. A homozygous nonsense variant in ift52 is associated with a human skeletal ciliopathy. Clinical Genetics, 90:536-539, Dec 2016. URL: https://doi.org/10.1111/cge.12762, doi:10.1111/cge.12762. This article has 90 citations and is from a peer-reviewed journal.