ReviewGenome biology2008
The tektin family of microtubule-stabilizing proteins.
Review in Genome biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
63 citing papers in PubMed, 111 citations in OpenAlex.
- Tumor evolution: signaling pathways, molecular mechanisms and therapeutic targets.Signal transduction and targeted therapy · 2026Review
- Doublet microtubule-associated tektins and enzymes differentially regulate sperm flagellar integrity and motility.Nature communications · 2026Article
- Tekt2 regulates hair cell development and function by maintaining normal kinocilium morphology in zebrafish.Frontiers in cell and developmental biology · 2026Article
- Brief biology and pathophysiology of Tekt bundles.Cell adhesion & migration · 2025Review
- De Novo Assembly, Characterization and Comparative Transcriptome Analysis of the Mature Male and Female Gonads inAnimals : an open access journal from MDPI · 2025Article
- Single-cell profiling of the amphioxus digestive tract reveals conservation of endocrine cells in chordates.Science advances · 2024Article
- Single cell atlas of Xenoturbella bocki highlights limited cell-type complexity.Nature communications · 2024Article
- Tektin bundle interacting protein, TEKTIP1, functions to stabilize the tektin bundle and axoneme in mouse sperm flagella.Cellular and molecular life sciences : CMLS · 2024Article
- In-cell structural insight into the stability of sperm microtubule doublet.Cell discovery · 2023Article
- Identification of hub genes associated with spermatogenesis by bioinformatics analysis.Scientific reports · 2023Article
- Article
- Glucocorticoid exposure modifies the miRNA profile of sperm in the guinea pig: Implications for intergenerational transmission.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023Article
- Review
- Molecular Logic of Synaptic Diversity BetweenbioRxiv : the preprint server for biology · 2023Article
- Loss-of-function mutations inScience advances · 2022Article
- miR-199-5p regulates spermiogenesis at the posttranscriptional level via targeting Tekt1 in allotriploid crucian carp.Journal of animal science and biotechnology · 2022Article
- Article
- Article
- Motile cilia genetics and cell biology: big results from little mice.Cellular and molecular life sciences : CMLS · 2021Review
- Transcriptome analysis of turkey (Meleagris gallopavo) reproductive tract revealed key pathways regulating spermatogenesis and post-testicular sperm maturation.Poultry science · 2020Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Tektins are insoluble alpha-helical proteins essential for the construction of cilia and flagella and are found throughout the eukaryotes apart from higher plants. Being almost universal but still fairly free to mutate, their coding sequences have proved useful for estimating the evolutionary relationships between closely related species. Their protein molecular structure, typically consisting of four coiled-coil rod segments connected by linkers, resembles that of intermediate filament (IF) proteins and lamins. Tektins assemble into continuous rods 2 nm in diameter that are probably equivalent to subfilaments of the 10 nm diameter IFs. Tektin and IF rod sequences both have a repeating pattern of charged amino acids superimposed on the seven-amino-acid hydrophobic pattern of coiled-coil proteins. The length of the repeat segment matches that of tubulin subunits, suggesting that tektins and tubulins may have coevolved, and that lamins and IFs may have emerged later as modified forms of tektin. Unlike IFs, tektin sequences include one copy of a conserved peptide of nine amino acids that may bind tubulin. The 2 nm filaments associate closely with tubulin in doublet and triplet microtubules of axonemes and centrioles, respectively, and help to stabilize these structures. Their supply restricts the assembled lengths of cilia and flagella. In doublet microtubules, the 2 nm filaments may also help to organize the longitudinal spacing of accessory structures, such as groups of inner dynein arms and radial spokes.
Indexed as
Identifiers
What OpenQuestion holds
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.