ReviewJournal of cell science2025
Molecular models of the sperm head-tail coupling apparatus.
Review in Journal of cell science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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
6 citing papers in PubMed.
- Article
- Basal body docking failure triggers centriole clustering and elimination in mammalian spermatogenesis.EMBO reports · 2026Article
- The Nuclear Pore Complex Facilitates Centriole-Nuclear Attachment in Spermatids.bioRxiv : the preprint server for biology · 2026Article
- TENT5C extends Odf1 poly(A) tail to sustain sperm morphogenesis and fertility.Nature communications · 2026Article
- Togaram Ensures Axial Alignment of the Sperm Neck.bioRxiv : the preprint server for biology · 2026Article
- Loss of cilia drives centriole clustering and elimination during mammalian spermatogenesis.bioRxiv : the preprint server for biology · 2025Article
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.
Funding
Abstract
A stable connection between the sperm head (nucleus) and tail (flagellum) is crucial for proper fertility. This linkage is mediated by centrioles, or their remnants, at a structure known as the head-tail coupling apparatus (HTCA). Although many proteins have been implicated at the HTCA, the precise molecular linkage that connects the head and tail is poorly understood. This Review proposes three molecular models for the HTCA based on the presence of three key components: nuclear envelope proteins, cytoplasmic proteins and centriole proteins. As it relates to these models, we discuss the current literature that describes the linkage from nuclear envelope proteins to cytosolic and centriole proteins, including a LINC-complex-based linkage, a nuclear pore complex linkage and a direct linkage that bypasses the outer nuclear membrane. Finally, we discuss outstanding questions in the field and how future studies might delineate the complex molecular machinery at the HTCA.
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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.