ArticleProceedings of the National Academy of Sciences of the United States of America1992
Primary structure of tektin A1: comparison with intermediate-filament proteins and a model for its association with tubulin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 43 citations in OpenAlex.
- Article
- Taxon-specific expansion and loss of tektins inform metazoan ciliary diversity.BMC evolutionary biology · 2019Article
- Production of recombinant human tektin 1, 2, and 4 and in vitro assembly of human tektin 1.Cytoskeleton (Hoboken, N.J.) · 2018Article
- Association of polymorphisms in tektin-t gene with idiopathic asthenozoospermia in Sichuan, China.Journal of assisted reproduction and genetics · 2016Article
- Insights into the structure and function of ciliary and flagellar doublet microtubules: tektins, Ca2+-binding proteins, and stable protofilaments.The Journal of biological chemistry · 2014Article
- The tektin family of microtubule-stabilizing proteins.Genome biology · 2008Review
- Interchromosomal segmental duplications of the pericentromeric region on the human Y chromosome.Genome research · 2005Article
- A tektin homologue is decreased in chlamydomonas mutants lacking an axonemal inner-arm dynein.Molecular biology of the cell · 2004Article
- The Rib43a protein is associated with forming the specialized protofilament ribbons of flagellar microtubules in Chlamydomonas.Molecular biology of the cell · 2000Article
- Expression of ciliary tektins in brain and sensory development.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998Article
- SF-assemblin, the structural protein of the 2-nm filaments from striated microtubule associated fibers of algal flagellar roots, forms a segmented coiled coil.The Journal of cell biology · 1993Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Tektins are proteins that form filamentous polymers in the walls of ciliary and flagellar microtubules and that have biochemical and immunological properties similar to those of intermediate-filament proteins. We report here the sequence of a cDNA for tektin A1, one of the main tektins from Strongylocentrotus purpuratus sea urchin embryos. By hybridization analysis, tektin A mRNA appears maximally at ciliogenesis. The predicted structure of tektin A1 (M(r) 52,955) is a series of alpha-helical rod segments separated by nonhelical linkers. The two halves of the rod appear homologous and are probably related by gene duplication. Comparison of tektin A1 with intermediate-filament proteins, including nuclear lamins, reveals a low amino acid homology but similar molecular motif, i.e., pattern of helical and nonhelical domains. This study indicates that tektins are unique proteins but may be evolutionarily related to intermediate-filament proteins, and suggests a structural basis for the interaction of tektins and tubulin in microtubules.
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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.