ArticleMolecular biology of the cell2007
Protein arms in the kinetochore-microtubule interface of the yeast DASH complex.
Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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
35 citing papers in PubMed, 59 citations in OpenAlex.
- A communication hub for phosphoregulation of kinetochore-microtubule attachment.Current biology : CB · 2024Article
- Evidence for an interaction of paracingulin with microtubules.microPublication biology · 2024Article
- Functional plasticity in chromosome-microtubule coupling on the evolutionary time scale.Life science alliance · 2023Article
- Structure of the Ndc80 complex and its interactions at the yeast kinetochore-microtubule interface.Open biology · 2023Article
- Structural view of the yeast Dam1 complex, a ring-shaped molecular coupler for the dynamic microtubule end.Essays in biochemistry · 2020Review
- Electron cryotomography analysis of Dam1C/DASH at the kinetochore-spindle interface in situ.The Journal of cell biology · 2019Article
- Structure of the DASH/Dam1 complex shows its role at the yeast kinetochore-microtubule interface.Science (New York, N.Y.) · 2018Article
- Structural plasticity of the living kinetochore.The Journal of cell biology · 2017Article
- Review
- Molecular architecture of the Dam1 complex-microtubule interaction.Open biology · 2016Article
- The molecular architecture of the Dam1 kinetochore complex is defined by cross-linking based structural modelling.Nature communications · 2015Article
- Kinetochores require oligomerization of Dam1 complex to maintain microtubule attachments against tension and promote biorientation.Nature communications · 2014Article
- A mathematical model of force generation by flexible kinetochore-microtubule attachments.Biophysical journal · 2014Article
- Phosphoregulation promotes release of kinetochores from dynamic microtubules via multiple mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Suppressors of ipl1-2 in components of a Glc7 phosphatase complex, Cdc48 AAA ATPase, TORC1, and the kinetochore.G3 (Bethesda, Md.) · 2012Article
- Subunit organization in the Dam1 kinetochore complex and its ring around microtubules.Molecular biology of the cell · 2011Article
- Visualizing kinetochore architecture.Current opinion in structural biology · 2011Review
- The Dam1 ring binds to the E-hook of tubulin and diffuses along the microtubule.Molecular biology of the cell · 2011Article
- Kinetochores' gripping feat: conformational wave or biased diffusion?Trends in cell biology · 2011Review
- Tubulin depolymerization may be an ancient biological motor.Journal of cell science · 2010Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The yeast DASH complex is a heterodecameric component of the kinetochore necessary for accurate chromosome segregation. DASH forms closed rings around microtubules with a large gap between the DASH ring and the microtubule cylinder. We characterized the microtubule-binding properties of limited proteolysis products and subcomplexes of DASH, thus identifying candidate polypeptide extensions involved in establishing the DASH-microtubule interface. The acidic C-terminal extensions of tubulin subunits are not essential for DASH binding. We also measured the molecular mass of DASH rings on microtubules with scanning transmission electron microscopy and found that approximately 25 DASH heterodecamers assemble to form each ring. Dynamic association and relocation of multiple flexible appendages of DASH may allow the kinetochore to translate along the microtubule surface.
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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.