ArticleProceedings of the National Academy of Sciences of the United States of America2008
Different assemblies of the DAM1 complex follow shortening microtubules by distinct mechanisms.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 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
65 citing papers in PubMed, 93 citations in OpenAlex.
- Ndc80 complex, a conserved coupler for kinetochore-microtubule motility, is a sliding molecular clutch.Science advances · 2025Article
- Micron-scale protein transport along microtubules by kinesin-driven shepherding.bioRxiv : the preprint server for biology · 2025Article
- Measuring and modeling forces generated by microtubules.Biophysical reviews · 2023Review
- The importance of microtubule-dependent tension in accurate chromosome segregation.Frontiers in cell and developmental biology · 2023Review
- Ultrafast Force-Clamp Spectroscopy of Microtubule-Binding Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Regulation of microtubule dynamics, mechanics and function through the growing tip.Nature reviews. Molecular cell biology · 2021Review
- Permitted and restricted steps of human kinetochore assembly in mitotic cell extracts.Molecular biology of the cell · 2021Article
- Cdk1 Phosphorylation of the Dam1 Complex Strengthens Kinetochore-Microtubule Attachments.Current biology : CB · 2020Article
- Structural view of the yeast Dam1 complex, a ring-shaped molecular coupler for the dynamic microtubule end.Essays in biochemistry · 2020Review
- Microtubule end conversion mediated by motors and diffusing proteins with no intrinsic microtubule end-binding activity.Nature communications · 2019Article
- Electron cryotomography analysis of Dam1C/DASH at the kinetochore-spindle interface in situ.The Journal of cell biology · 2019Article
- Probing Mitotic CENP-E Kinesin with the Tethered Cargo Motion Assay and Laser Tweezers.Biophysical journal · 2018Article
- In vitro reconstitution of lateral to end-on conversion of kinetochore-microtubule attachments.Methods in cell biology · 2018Article
- How Kinetochore Architecture Shapes the Mechanisms of Its Function.Current biology : CB · 2017Review
- Tension sensors reveal how the kinetochore shares its load.BioEssays : news and reviews in molecular, cellular and developmental biology · 2017Review
- Review
- Article
- A Molecular View of Kinetochore Assembly and Function.Biology · 2017Review
- Molecular architecture of the Dam1 complex-microtubule interaction.Open biology · 2016Article
- Multisite phosphorylation of the NDC80 complex gradually tunes its microtubule-binding affinity.Molecular biology of the cell · 2015Article
5 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
9 authors at 7 institutions in 3 countries.
Funding
Abstract
Mitotic chromosomes segregate at the ends of shortening spindle microtubules (MTs). In budding yeast, the Dam1 multiprotein complex supports this dynamic attachment, thereby contributing to accurate chromosome segregation. Purified Dam1 will track the end of a depolymerizing MT and can couple it to microbead transport in vitro. The processivity of such motions has been thought to depend on rings that the Dam1 complex can form around MTs, but the possibility that alternative coupling geometries contribute to these motilities has not been considered. Here, we demonstrate that both rings and nonencircling Dam1 oligomers can track MT ends and enable processive cargo movement in vitro. The coupling properties of these two assemblies are, however, quite different, so each may make a distinct contribution to chromosome motility.
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.