ReviewSeminars in cell & developmental biology2014
The role of E3 ligases in the ubiquitin-dependent regulation of spermatogenesis.
Review in Seminars in cell & developmental biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
44 citing papers in PubMed, 1 synthesis or guideline pooled it, 89 citations in OpenAlex.
- The association between mutations in ubiquitin-specific protease 26 (Asian journal of andrologyPooled it
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- Metabolic hubs in reproduction: The regulatory network of lipid droplets in gamete and embryo physiology (Review).International journal of molecular medicine · 2026Review
- The Potential Role of Deubiquitinating Enzymes (DUBs) in Male Fertility.Biomolecules · 2026Review
- Seasonality affects key physiological pathways in Pontastacus leptodactylus during an Aphanomyces astaci epidemic outbreak.Scientific reports · 2025Article
- Single-cell RNA sequencing uncovers dynamic roadmap during chicken spermatogenesis.BMC genomics · 2025Article
- New strategy against sperm oxidative damage: supplementing NaHS to enhance the activity of the HAmerican journal of clinical and experimental immunology · 2025Article
- DCUN1D2 is insignificant for spermatogenesis and male fertility in mice.American journal of translational research · 2025Article
- Article
- A Comparison of White and Yellow Seminal Plasma Phosphoproteomes Obtained from Turkey (International journal of molecular sciences · 2024Article
- FBXO47 regulates centromere pairing as key component of centromeric SCF E3 ligase in mouse spermatocytes.Communications biology · 2024Article
- Article
- FBXO24 deletion causes abnormal accumulation of membraneless electron-dense granules in sperm flagella and male infertility.bioRxiv : the preprint server for biology · 2024Article
- The deubiquitinase cofactor UAF1 interacts with USP1 and plays an essential role in spermiogenesis.iScience · 2024Article
- Transcriptome analysis of reproductive tract tissues of male river prawn Macrobrachium americanum.Molecular biology reports · 2024Article
- Enhanced bovine genome annotation through integration of transcriptomics and epi-transcriptomics datasets facilitates genomic biology.GigaScience · 2024Article
- Article
- E3 ligase FBXO22 is not significant for spermatogenesis and male fertility in mice.American journal of translational research · 2024Article
- Integrated analysis of the ubiquitination mechanism reveals the specific signatures of tissue and cancer.BMC genomics · 2023Article
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 3 institutions in 1 country.
Funding
Abstract
The ubiquitination of proteins is a post-translational modification that was first described as a means to target misfolded or unwanted proteins for degradation by the proteasome. It is now appreciated that the ubiquitination of proteins also serves as a mechanism to modify protein function and cellular functions such as protein trafficking, cell signaling, DNA repair, chromatin modifications, cell-cycle progression and cell death. The ubiquitination of proteins occurs through the hierarchal transfer of ubiquitin from an E1 ubiquitin-activating enzyme to an E2 ubiquitin-conjugating enzyme and finally to an E3 ubiquitin ligase that transfers the ubiquitin to its target protein. It is the final E3 ubiquitin ligase that confers the substrate specificity for ubiquitination and is the focus of this review. Spermatogenesis is a complex and highly regulated process by which spermatogonial stem cells undergo mitotic proliferation and expansion of the diploid spermatogonial population, differentiate into spermatocytes and progress through two meiotic divisions to produce haploid spermatids that proceed through a final morphogenesis to generate mature spermatozoa. The ubiquitination of proteins in the cells of the testis occurs in many of the processes required for the progression of mature spermatozoa. Since it is the E3 ubiquitin ligase that recognizes the target protein and provides the specificity and selectivity for ubiquitination, this review highlights known examples of E3 ligases in the testis and the differing roles that they play in maintaining functional spermatogenesis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.