ArticleThe Journal of cell biology1992
Structural and functional reconstitution of inner dynein arms in Chlamydomonas flagellar axonemes.
Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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.
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Who cites it
28 citing papers in PubMed, 77 citations in OpenAlex.
- The many modes of flagellar and ciliary beating: Insights from a physical analysis.Cytoskeleton (Hoboken, N.J.) · 2021Review
- Ciliary Motility: Regulation of Axonemal Dynein Motors.Cold Spring Harbor perspectives in biology · 2017Review
- The nexin link and B-tubule glutamylation maintain the alignment of outer doublets in the ciliary axoneme.Cytoskeleton (Hoboken, N.J.) · 2016Article
- ATP Consumption of Eukaryotic Flagella Measured at a Single-Cell Level.Biophysical journal · 2015Article
- The ciliary inner dynein arm, I1 dynein, is assembled in the cytoplasm and transported by IFT before axonemal docking.Cytoskeleton (Hoboken, N.J.) · 2014Article
- Cryoelectron tomography reveals doublet-specific structures and unique interactions in the I1 dynein.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Distinct roles of 1alpha and 1beta heavy chains of the inner arm dynein I1 of Chlamydomonas flagella.Molecular biology of the cell · 2011Article
- Regulation of dynein-driven microtubule sliding by the axonemal protein kinase CK1 in Chlamydomonas flagella.The Journal of cell biology · 2009Article
- Dyneins across eukaryotes: a comparative genomic analysis.Traffic (Copenhagen, Denmark) · 2007Article
- IC138 is a WD-repeat dynein intermediate chain required for light chain assembly and regulation of flagellar bending.Molecular biology of the cell · 2004Article
- Localization of calmodulin and dynein light chain LC8 in flagellar radial spokes.The Journal of cell biology · 2001Article
- The Chlamydomonas PF6 locus encodes a large alanine/proline-rich polypeptide that is required for assembly of a central pair projection and regulates flagellar motility.Molecular biology of the cell · 2001Article
- The 9 + 2 axoneme anchors multiple inner arm dyneins and a network of kinases and phosphatases that control motility.The Journal of cell biology · 2000Review
- Insights into the structural organization of the I1 inner arm dynein from a domain analysis of the 1beta dynein heavy chain.Molecular biology of the cell · 2000Article
- The Rib43a protein is associated with forming the specialized protofilament ribbons of flagellar microtubules in Chlamydomonas.Molecular biology of the cell · 2000Article
- The Chlamydomonas IDA7 locus encodes a 140-kDa dynein intermediate chain required to assemble the I1 inner arm complex.Molecular biology of the cell · 1998Article
- The Mr 140,000 intermediate chain of Chlamydomonas flagellar inner arm dynein is a WD-repeat protein implicated in dynein arm anchoring.Molecular biology of the cell · 1998Article
- Evidence for four cytoplasmic dynein heavy chain isoforms in rat testis.Molecular biology of the cell · 1998Article
- The Chlamydomonas reinhardtii ODA3 gene encodes a protein of the outer dynein arm docking complex.The Journal of cell biology · 1997Article
- Regulation of flagellar dynein by phosphorylation of a 138-kD inner arm dynein intermediate chain.The Journal of cell biology · 1997Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The inner row of dynein arms contains three dynein subforms. Each is distinct in composition and location in flagellar axonemes. To begin investigating the specificity of inner dynein arm assembly, we assessed the capability of isolated inner arm dynein subforms to rebind to their appropriate positions on axonemal doublet microtubules by recombining them with either mutant or extracted axonemes missing some or all dyneins. Densitometry of Coomassie blue-stained polyacrylamide gels revealed that for each inner dynein arm subform, binding to axonemes was saturable and stoichiometric. Using structural markers of position and polarity, electron microscopy confirmed that subforms bound to the correct inner arm position. Inner arms did not bind to outer arm or inappropriate inner arm positions despite the availability of sites. These and previous observations implicate specialized tubulin isoforms or nontubulin proteins in designation of specific inner dynein arm binding sites. Further, microtubule sliding velocities were restored to dynein-depleted axonemes upon rebinding of the missing inner arm subtypes as evaluated by an ATP-induced microtubule sliding disintegration assay. Therefore, not only were the inner arm dynein subforms able to identify and bind to the correct location on doublet microtubules but they bound in a functionally active conformation.
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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.