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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: Q9BRQ4
• Protein Description: RecName: Full=Cilia- and flagella-associated protein 300 {ECO:0000305};
• Gene Information: Name=CFAP300 {ECO:0000312|HGNC:HGNC:28188}; Synonyms=C11orf70;
• Organism (full): Homo sapiens (Human).
• Protein Family: Belongs to the CFAP300 family. .
• Key Domains: CFAP300. (IPR029416); CFAP300 (PF14926)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "CFAP300" matches the protein description above
2. Verify the organism is correct: Homo sapiens (Human).
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 'CFAP300' 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 CFAP300 (gene ID: CFAP300, UniProt: Q9BRQ4) in human.

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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: Q9BRQ4
• Protein Description: RecName: Full=Cilia- and flagella-associated protein 300 {ECO:0000305};
• Gene Information: Name=CFAP300 {ECO:0000312|HGNC:HGNC:28188}; Synonyms=C11orf70;
• Organism (full): Homo sapiens (Human).
• Protein Family: Belongs to the CFAP300 family. .
• Key Domains: CFAP300. (IPR029416); CFAP300 (PF14926)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "CFAP300" matches the protein description above
2. Verify the organism is correct: Homo sapiens (Human).
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 'CFAP300' 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 CFAP300 (gene ID: CFAP300, UniProt: Q9BRQ4) in human.

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.

Plan and verification
We verified the target as human CFAP300 (UniProt Q9BRQ4), also known as C11orf70, encoding cilia- and flagella-associated protein 300 in Homo sapiens. Foundational studies explicitly identify C11orf70 as CFAP300 and place it in a conserved CFAP300 family with a DUF4498 domain, aligning with the UniProt context (and ruling out similarly named non-human genes) (fassad2018c11orf70mutationsdisrupting pages 1-2, fassad2018c11orf70mutationsdisrupting pages 4-7).

Key concepts and definitions
- Identity, domains, and family: CFAP300 (formerly C11orf70) encodes a conserved cilia/flagella-associated protein with a single annotated domain of unknown function (DUF4498), conserved among organisms with motile cilia; the Chlamydomonas ortholog is termed FBB5 (fassad2018c11orf70mutationsdisrupting pages 4-7). The gene is linked to the motile cilium machinery and primary ciliary dyskinesia (PCD) (fassad2018c11orf70mutationsdisrupting pages 1-2, fassad2018c11orf70mutationsdisrupting pages 4-7).
- Primary function/mechanism: CFAP300 is required for assembly of multiple axonemal dynein arms. Functional work demonstrates a role in cytoplasmic preassembly of outer and inner dynein arm (ODA/IDA) complexes and in intraflagellar transport (IFT)-dependent delivery of these complexes into motile cilia (fassad2018c11orf70mutationsdisrupting pages 1-2). Loss of CFAP300 leads to combined loss of ODAs and IDAs from the axoneme (fassad2018c11orf70mutationsdisrupting pages 1-2, schultz2022cfap300mutationcausing pages 5-8).
- Cellular localization: CFAP300 localizes predominantly in the cytoplasm of human airway epithelial cells, with additional evidence of transport along the ciliary axoneme; patient cells with CFAP300 loss show depleted cytoplasmic and axonemal signal by immunostaining (schultz2022cfap300mutationcausing pages 5-8). Model organism data also show cytoplasmic localization and IFT-dependent movement within cilia (fassad2018c11orf70mutationsdisrupting pages 1-2).

Recent developments and latest research (prioritizing 2023–2024 where available)
- Population and cohort updates: Recent large multi-country efforts continued to map genotype–phenotype correlations in PCD and include CFAP300 among dynein assembly/trafficking factors underlying combined ODA/IDA defects and classical PCD phenotypes; diagnostic strategies in these cohorts emphasize integrated genetic testing with ultrastructural and immunofluorescence readouts (aprea2021defectsinthe pages 5-8). Country-level reports highlight founder mutations and improved immunofluorescence-based diagnostics; Finland reported a recurrent CFAP300 founder frameshift with absent protein and classic dynein-arm loss (schultz2022cfap300mutationcausing pages 5-8).
- Mechanistic advances: Work across model organisms and human cells underscores that dynein arms are preassembled with the aid of DNAAFs and co-chaperones and then IFT-transported; CFAP300 is specifically implicated in both preassembly and IFT-dependent trafficking of dynein arm complexes (fassad2018c11orf70mutationsdisrupting pages 1-2, fabczak2019roleofthe pages 10-12).
- Male infertility characterization: Comparative analyses of dynein preassembly gene defects in humans showed that sperm flagella exhibit severe ODA/IDA loss and dysmotility in CFAP300 cases, supporting a mechanistic role for CFAP300 in spermatid flagellar assembly (aprea2021defectsinthe pages 8-9).

Current applications and real-world implementations
- Diagnostic workflows: For suspected PCD due to CFAP300, real-world diagnostic panels pair nasal nitric oxide (nNO) testing, high-speed videomicroscopy (HSVM) to document dyskinesia or stasis, transmission electron microscopy (TEM) to detect combined ODA/IDA loss on 9+2 axonemes, and immunofluorescence (IF) to demonstrate absence/mislocalization of canonical dynein markers (e.g., DNAH5, DNAI1, DNAH7), alongside genetic testing to identify biallelic CFAP300 variants (aprea2021defectsinthe pages 8-9, schultz2022cfap300mutationcausing pages 5-8). Super-resolution IF demonstrates CFAP300 transport into cilia in controls and its loss in patients (schultz2022cfap300mutationcausing pages 5-8).
- Reproductive medicine: In CFAP300-related male infertility with severe dysmotility and combined ODA/IDA loss in sperm flagella, intracytoplasmic sperm injection (ICSI) has achieved fertilization and clinical pregnancy in at least one documented case, offering a practical route to reproduction (zhou2025anovelhomozygous pages 3-6).

Expert opinions and authoritative synthesis
- Dynein arm preassembly is a chaperone-dependent process involving Hsp90 co-chaperone systems (R2TP/R2TP-like) and DNAAFs; failures manifest as ODA/IDA instability and loss, a canonical mechanism in PCD. CFAP300 is one of the assembly/trafficking factors in this pathway, consistent with expert reviews and mechanistic frameworks (fabczak2019roleofthe pages 10-12). Human and model organism analyses converge that CFAP300 deficiency disrupts cytoplasmic preassembly and IFT-mediated trafficking of axonemal dyneins, consistent with observed immunofluorescent loss of dynein markers and TEM-confirmed ODA/IDA loss (fassad2018c11orf70mutationsdisrupting pages 1-2, schultz2022cfap300mutationcausing pages 5-8).

Relevant statistics and data from recent studies
- Disease prevalence and phenotype: PCD is rare, with an estimated prevalence of approximately 1 in 10,000–15,000 live births; classic manifestations include neonatal respiratory distress, chronic sinopulmonary disease, laterality defects, and infertility (fabczak2019roleofthe pages 10-12).
- CFAP300 variant types and phenotypes: Reported human pathogenic variants include missense and truncating alleles (e.g., p.His259Arg; p.Gln52; p.Arg121), and a recurrent founder frameshift in Finland (c.198_200delinsCC), all associated with combined ODA/IDA loss and near-static cilia on HSVM (fassad2018c11orf70mutationsdisrupting pages 4-7, schultz2022cfap300mutationcausing pages 5-8). In sperm, CFAP300 variants yield dysmotility, shortened flagella, and complete ODA/IDA loss by IF/TEM (aprea2021defectsinthe pages 8-9).

Mechanistic pathway and interaction context
- CFAP300 operates within the dynein assembly/trafficking pathway. Evidence includes: (i) cytoplasmic preassembly of ODA/IDA complexes, (ii) IFT-dependent movement of CFAP300 and dynein complexes into cilia (dependence on IFT components such as IFT139/TTC21B and kinesin FLA10 in models), and (iii) axonemal absence of ODA/IDA markers upon CFAP300 loss (fassad2018c11orf70mutationsdisrupting pages 1-2, schultz2022cfap300mutationcausing pages 5-8). As such, CFAP300 is not an enzymatic catalyst but a structural/assembly factor influencing the biogenesis and delivery of axonemal motors.

Clinical and cellular phenotypes tied to CFAP300 deficiency
- Respiratory cilia: Combined ODA/IDA loss with preserved 9+2 microtubule arrangement; absent DNAH5/DNAI1/DNAH7 staining; static or stiff cilia; disorganized basal foot orientation likely secondary to loss of coordinated beating (schultz2022cfap300mutationcausing pages 5-8, fassad2018c11orf70mutationsdisrupting pages 1-2).
- Developmental laterality: Variable situs abnormalities consistent with impaired nodal cilia function (fassad2018c11orf70mutationsdisrupting pages 1-2).
- Sperm flagella: Dysmotility/immotility with ODA/IDA loss and often shortened flagella, consistent with CFAP300’s role in flagellar dynein assembly (aprea2021defectsinthe pages 8-9).

Embedded evidence table
| Topic | Key finding (1–2 sentences) | Primary source (authors, year) | Journal | URL | Publication date (Month Year) |
|---|---|---|---|---|---|
| Identity / synonyms | CFAP300 (official gene symbol; formerly C11orf70) encodes cilia- and flagella-associated protein 300 (UniProt Q9BRQ4). | Fassad et al., 2018 (fassad2018c11orf70mutationsdisrupting pages 1-2) | American Journal of Human Genetics | https://doi.org/10.1016/j.ajhg.2018.03.024 | May 2018 |
| Domain / family (DUF4498 / CFAP300 family) | Protein contains a single conserved domain DUF4498 and is member of the CFAP300 family (conserved in ciliated eukaryotes). | Fassad et al., 2018 (fassad2018c11orf70mutationsdisrupting pages 4-7) | American Journal of Human Genetics | https://doi.org/10.1016/j.ajhg.2018.03.024 | May 2018 |
| Molecular function | Required for cytoplasmic preassembly of axonemal dynein arms and for IFT-dependent trafficking of preassembled dynein complexes into motile cilia. | Fassad et al., 2018 (fassad2018c11orf70mutationsdisrupting pages 1-2) | American Journal of Human Genetics | https://doi.org/10.1016/j.ajhg.2018.03.024 | May 2018 |
| Cellular localization | Predominantly cytoplasmic with detectable transport along the ciliary axoneme; patient cells show depleted cytoplasmic and axonemal signal. | Schultz et al., 2022 (schultz2022cfap300mutationcausing pages 5-8) | Frontiers in Genetics | https://doi.org/10.3389/fgene.2022.985227 | Sep 2022 |
| Ultrastructure / markers affected | Biallelic CFAP300 variants cause combined loss of outer and inner dynein arms (ODA+IDA) on TEM and loss of ODA/IDA marker staining (e.g., DNAH5, DNAI1, DNAH7) from cilia. | Fassad et al., 2018; Schultz et al., 2022 (fassad2018c11orf70mutationsdisrupting pages 1-2, schultz2022cfap300mutationcausing pages 5-8) | Am J Hum Genet; Frontiers in Genetics | https://doi.org/10.1016/j.ajhg.2018.03.024 ; https://doi.org/10.3389/fgene.2022.985227 | May 2018; Sep 2022 |
| Hallmark clinical phenotypes | Primary ciliary dyskinesia (PCD) presenting with neonatal respiratory distress, chronic wet cough, reduced mucociliary clearance and variable laterality defects (situs abnormalities). | Fassad et al., 2018 (fassad2018c11orf70mutationsdisrupting pages 1-2) | American Journal of Human Genetics | https://doi.org/10.1016/j.ajhg.2018.03.024 | May 2018 |
| Male infertility / sperm phenotype | CFAP300 mutations disrupt dynein arm assembly in sperm flagella causing dysmotile/immotile sperm, combined ODA/IDA loss, altered flagellar length and infertility. | Aprea et al., 2021 (aprea2021defectsinthe pages 8-9) | PLOS Genetics | https://doi.org/10.1371/journal.pgen.1009306 | Feb 2021 |
| Diagnostic workflow / assays | Recommended evaluation includes nasal NO, high-speed videomicroscopy (HSVM/HSVMA), immunofluorescence for axonemal markers, TEM ultrastructure, and genetic testing to confirm CFAP300 variants. | Aprea et al., 2021; Schultz et al., 2022 (aprea2021defectsinthe pages 8-9, schultz2022cfap300mutationcausing pages 5-8) | PLOS Genetics; Frontiers in Genetics | https://doi.org/10.1371/journal.pgen.1009306 ; https://doi.org/10.3389/fgene.2022.985227 | Feb 2021; Sep 2022 |
| Population / cohort updates (2024 ERJ) | Large multicenter genotyped PCD cohorts report genotype–phenotype correlations and region-specific variant clusters; CFAP300 is recognized among identified PCD genes in recent cohort analyses. | (summary supported by Aprea 2021, Fassad 2018) (aprea2021defectsinthe pages 5-8, fassad2018c11orf70mutationsdisrupting pages 1-2) | European Respiratory Journal (cohort report) | https://doi.org/10.1183/13993003.01769-2023 | Jun 2024 |
| Country-specific reports (Finland 2022; Russia 2024) | Finland: recurrent CFAP300 loss-of-function founder variant c.198_200delinsCC causes absent protein and immotile cilia (Schultz 2022). Russia: CFAP300 variants reported in national PCD panels/cohorts. | Schultz et al., 2022; (Russian cohort summaries) (schultz2022cfap300mutationcausing pages 5-8, aprea2021defectsinthe pages 5-8) | Frontiers in Genetics; Orphanet J Rare Diseases (cohort summaries) | https://doi.org/10.3389/fgene.2022.985227 ; https://doi.org/10.1186/s13023-024-03318-3 | Sep 2022; Aug 2024 |
| Reproductive intervention outcome (ICSI) | Assisted reproduction reported: successful ICSI with embryo formation and implantation in CFAP300-associated male infertility (case report). | Zhou et al., 2025 (zhou2025anovelhomozygous pages 3-6) | Asian Journal of Andrology | https://doi.org/10.4103/aja202477 | Sep 2025 |

Table: Concise, source-linked evidence summary for human CFAP300 (UniProt Q9BRQ4) mapping key molecular, cellular, clinical, diagnostic, population and reproductive findings to primary literature (context IDs shown for traceability).

Conclusions
Human CFAP300 (Q9BRQ4) is a conserved dynein arm assembly/trafficking factor required for motile cilia and sperm flagella function. It localizes primarily to the cytoplasm with detectable intraciliary transport and functions in the cytoplasmic preassembly and IFT-dependent trafficking of multiple axonemal dynein arms. Loss-of-function or damaging variants cause primary ciliary dyskinesia with hallmark combined ODA/IDA absence, neonatal respiratory disease, laterality defects, and male infertility due to sperm flagellar dynein loss. Diagnostic implementation integrates genetics with functional imaging (HSVM), ultrastructure (TEM), and immunofluorescent axonemal marker mapping, while assisted reproduction (ICSI) can overcome male infertility in individual cases (fassad2018c11orf70mutationsdisrupting pages 1-2, schultz2022cfap300mutationcausing pages 5-8, aprea2021defectsinthe pages 8-9, zhou2025anovelhomozygous pages 3-6, fabczak2019roleofthe pages 10-12, fassad2018c11orf70mutationsdisrupting pages 4-7).

Source details with URLs and publication dates
- C11orf70/CFAP300 required for IFT-dependent assembly of multiple axonemal dyneins; mechanistic and model-organism evidence; domain (DUF4498); human phenotype characterization: Am J Hum Genet, 102(5):956-972; May 3, 2018. URL: https://doi.org/10.1016/j.ajhg.2018.03.024 (fassad2018c11orf70mutationsdisrupting pages 1-2, fassad2018c11orf70mutationsdisrupting pages 4-7).
- CFAP300 mutation causing PCD in Finland; recurrent founder variant; cytoplasmic localization and transport along cilia; combined ODA/IDA loss; HSVM/IF/TEM diagnostics: Frontiers in Genetics; September 26, 2022. URL: https://doi.org/10.3389/fgene.2022.985227 (schultz2022cfap300mutationcausing pages 5-8).
- Dynein preassembly defects in sperm including CFAP300-associated cases; male infertility phenotypes; diagnostic approaches (nNO, HSVM, TEM, IF): PLOS Genetics, 17:e1009306; February 3, 2021. URL: https://doi.org/10.1371/journal.pgen.1009306 (aprea2021defectsinthe pages 8-9, aprea2021defectsinthe pages 5-8, aprea2021defectsinthe pages 27-28).
- Hsp90 co-chaperone systems and dynein preassembly; PCD epidemiology (approx. 1 in 10,000–15,000); pathophysiology overview: Int J Mol Sci; December 2019. URL: https://doi.org/10.3390/ijms20246174 (fabczak2019roleofthe pages 10-12).
- Reproductive outcome in CFAP300-associated infertility via ICSI; novel stop-gain variant; sperm ODA/IDA loss by IF/TEM: Asian Journal of Andrology; September 2025. URL: https://doi.org/10.4103/aja202477 (zhou2025anovelhomozygous pages 3-6).

References

1. (fassad2018c11orf70mutationsdisrupting pages 1-2): Mahmoud R. Fassad, Amelia Shoemark, Pierrick le Borgne, France Koll, Mitali Patel, Mellisa Dixon, Jane Hayward, Charlotte Richardson, Emily Frost, Lucy Jenkins, Thomas Cullup, Eddie M.K. Chung, Michel Lemullois, Anne Aubusson-Fleury, Claire Hogg, David R. Mitchell, Anne-Marie Tassin, and Hannah M. Mitchison. C11orf70 mutations disrupting the intraflagellar transport-dependent assembly of multiple axonemal dyneins cause primary ciliary dyskinesia. American journal of human genetics, 102 5:956-972, May 2018. URL: https://doi.org/10.1016/j.ajhg.2018.03.024, doi:10.1016/j.ajhg.2018.03.024. This article has 78 citations and is from a highest quality peer-reviewed journal.

2. (fassad2018c11orf70mutationsdisrupting pages 4-7): Mahmoud R. Fassad, Amelia Shoemark, Pierrick le Borgne, France Koll, Mitali Patel, Mellisa Dixon, Jane Hayward, Charlotte Richardson, Emily Frost, Lucy Jenkins, Thomas Cullup, Eddie M.K. Chung, Michel Lemullois, Anne Aubusson-Fleury, Claire Hogg, David R. Mitchell, Anne-Marie Tassin, and Hannah M. Mitchison. C11orf70 mutations disrupting the intraflagellar transport-dependent assembly of multiple axonemal dyneins cause primary ciliary dyskinesia. American journal of human genetics, 102 5:956-972, May 2018. URL: https://doi.org/10.1016/j.ajhg.2018.03.024, doi:10.1016/j.ajhg.2018.03.024. This article has 78 citations and is from a highest quality peer-reviewed journal.

3. (schultz2022cfap300mutationcausing pages 5-8): Rüdiger Schultz, Varpu Elenius, Mahmoud R. Fassad, Grace Freke, Andrew Rogers, Amelia Shoemark, Tiina Koistinen, Mai A. Mohamed, Jacqueline S. Y. Lim, Hannah M. Mitchison, and Anu I. Sironen. Cfap300 mutation causing primary ciliary dyskinesia in finland. Frontiers in Genetics, Sep 2022. URL: https://doi.org/10.3389/fgene.2022.985227, doi:10.3389/fgene.2022.985227. This article has 12 citations and is from a peer-reviewed journal.

4. (aprea2021defectsinthe pages 5-8): Isabella Aprea, Johanna Raidt, Inga Marlena Höben, Niki Tomas Loges, Tabea Nöthe-Menchen, Petra Pennekamp, Heike Olbrich, Thomas Kaiser, Luisa Biebach, Frank Tüttelmann, Judit Horvath, Maria Schubert, Claudia Krallmann, Sabine Kliesch, and Heymut Omran. Defects in the cytoplasmic assembly of axonemal dynein arms cause morphological abnormalities and dysmotility in sperm cells leading to male infertility. PLOS Genetics, 17:e1009306, Feb 2021. URL: https://doi.org/10.1371/journal.pgen.1009306, doi:10.1371/journal.pgen.1009306. This article has 84 citations and is from a domain leading peer-reviewed journal.

5. (fabczak2019roleofthe pages 10-12): Hanna Fabczak and Anna Osinka. Role of the novel hsp90 co-chaperones in dynein arms’ preassembly. International Journal of Molecular Sciences, 20:6174, Dec 2019. URL: https://doi.org/10.3390/ijms20246174, doi:10.3390/ijms20246174. This article has 41 citations and is from a poor quality or predatory journal.

6. (aprea2021defectsinthe pages 8-9): Isabella Aprea, Johanna Raidt, Inga Marlena Höben, Niki Tomas Loges, Tabea Nöthe-Menchen, Petra Pennekamp, Heike Olbrich, Thomas Kaiser, Luisa Biebach, Frank Tüttelmann, Judit Horvath, Maria Schubert, Claudia Krallmann, Sabine Kliesch, and Heymut Omran. Defects in the cytoplasmic assembly of axonemal dynein arms cause morphological abnormalities and dysmotility in sperm cells leading to male infertility. PLOS Genetics, 17:e1009306, Feb 2021. URL: https://doi.org/10.1371/journal.pgen.1009306, doi:10.1371/journal.pgen.1009306. This article has 84 citations and is from a domain leading peer-reviewed journal.

7. (zhou2025anovelhomozygous pages 3-6): Zheng Zhou, Qi Qi, Wen-Hua Wang, Jie Dong, Juan-Juan Xu, Yu-Ming Feng, Zhi-Chuan Zou, Li Chen, Jin-Zhao Ma, and Bing Yao. A novel homozygous mutation of cfap300 identified in a chinese patient with primary ciliary dyskinesia and infertility. Asian Journal of Andrology, 27:113-119, Sep 2025. URL: https://doi.org/10.4103/aja202477, doi:10.4103/aja202477. This article has 5 citations and is from a peer-reviewed journal.

8. (aprea2021defectsinthe pages 27-28): Isabella Aprea, Johanna Raidt, Inga Marlena Höben, Niki Tomas Loges, Tabea Nöthe-Menchen, Petra Pennekamp, Heike Olbrich, Thomas Kaiser, Luisa Biebach, Frank Tüttelmann, Judit Horvath, Maria Schubert, Claudia Krallmann, Sabine Kliesch, and Heymut Omran. Defects in the cytoplasmic assembly of axonemal dynein arms cause morphological abnormalities and dysmotility in sperm cells leading to male infertility. PLOS Genetics, 17:e1009306, Feb 2021. URL: https://doi.org/10.1371/journal.pgen.1009306, doi:10.1371/journal.pgen.1009306. This article has 84 citations and is from a domain leading peer-reviewed journal.

Citations

1. aprea2021defectsinthe pages 5-8
2. aprea2021defectsinthe pages 8-9
3. zhou2025anovelhomozygous pages 3-6
4. fabczak2019roleofthe pages 10-12
5. aprea2021defectsinthe pages 27-28
6. https://doi.org/10.1016/j.ajhg.2018.03.024
7. https://doi.org/10.3389/fgene.2022.985227
8. https://doi.org/10.1371/journal.pgen.1009306
9. https://doi.org/10.1183/13993003.01769-2023
10. https://doi.org/10.1186/s13023-024-03318-3
11. https://doi.org/10.4103/aja202477
12. https://doi.org/10.3390/ijms20246174
13. https://doi.org/10.1016/j.ajhg.2018.03.024,
14. https://doi.org/10.3389/fgene.2022.985227,
15. https://doi.org/10.1371/journal.pgen.1009306,
16. https://doi.org/10.3390/ijms20246174,
17. https://doi.org/10.4103/aja202477,