ArticleNature2012
The 2.8 Å crystal structure of the dynein motor domain.
Article in Nature, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 151 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.
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Who cites it
151 citing papers in PubMed, 1 synthesis or guideline pooled it, 276 citations in OpenAlex.
- Genetic spectrum and genotype-phenotype correlations in DNAH5-mutated primary ciliary dyskinesia: a systematic review.Orphanet journal of rare diseases · 2025Pooled it
- Modelling nano-particle-PEG-NLS complexes for nucleus-targeted drug delivery: revisiting the multi-dynein nano-cargo transport on microtubules.Drug delivery · 2026Article
- Structural and functional characterization of DNAH5 variants in a Portuguese family with primary ciliary dyskinesia.Journal of assisted reproduction and genetics · 2026Article
- Post-LECA Origin and Diversification of an Axonemal Outer Arm Dynein Motor.Cytoskeleton (Hoboken, N.J.) · 2026Review
- A nucleotide code governs Lis1's ability to relieve dynein autoinhibition.Nature chemical biology · 2026Article
- Biallelic TruncatingInternational journal of molecular sciences · 2026Review
- Structural and ensemble-based mechanistic insights into cytoplasmic dynein-1.Frontiers in molecular biosciences · 2026Review
- Cryo-ET and MD simulations reveal that dynein-2 is tuned for binding to the A-tubule of the ciliary doublet.The EMBO journal · 2025Article
- The mechanochemical cycle of reactive full-length human dynein 1.Nature structural & molecular biology · 2025Article
- Multiple steps of dynein activation by Lis1 visualized by cryo-EM.Nature structural & molecular biology · 2025Article
- Cryo-EM captures early intermediate steps in dynein activation by LIS1.Nature communications · 2025Article
- Phyloproteomics reveals conserved patterns of axonemal dynein methylation across the motile ciliated eukaryotes.Molecular biology of the cell · 2025Article
- Trypanosome doublet microtubule structures reveal flagellum assembly and motility mechanisms.Science (New York, N.Y.) · 2025Article
- Favorable response to ketogenic diet therapy in a patient withEpilepsy & behavior reports · 2025Article
- DNAHX: a novel, non-motile dynein heavy chain subfamily, identified by cryo-EM endogenously.bioRxiv : the preprint server for biology · 2025Article
- Application of temperature replica exchange molecular dynamics: Structure of mitotic spindle-associated protein SHE1 and its binding to dynein.Computational and structural biotechnology journal · 2025Article
- MINFLUX reveals dynein stepping in live neurons.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The mechanism and energetics of the dynein priming stroke.Structure (London, England : 1993) · 2024Article
- Lis1 slows force-induced detachment of cytoplasmic dynein from microtubules.Nature chemical biology · 2024Article
- Molecular mechanism of dynein-dynactin complex assembly by LIS1.Science (New York, N.Y.) · 2024Article
91 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
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dyneins are microtubule-based AAA(+) motor complexes that power ciliary beating, cell division, cell migration and intracellular transport. Here we report the most complete structure obtained so far, to our knowledge, of the 380-kDa motor domain of Dictyostelium discoideum cytoplasmic dynein at 2.8 Å resolution; the data are reliable enough to discuss the structure and mechanism at the level of individual amino acid residues. Features that can be clearly visualized at this resolution include the coordination of ADP in each of four distinct nucleotide-binding sites in the ring-shaped AAA(+) ATPase unit, a newly identified interaction interface between the ring and mechanical linker, and junctional structures between the ring and microtubule-binding stalk, all of which should be critical for the mechanism of dynein motility. We also identify a long-range allosteric communication pathway between the primary ATPase and the microtubule-binding sites. Our work provides a framework for understanding the mechanism of dynein-based motility.
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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.