ReviewJournal of cell science2009
Structure-function insights into the yeast Dam1 kinetochore complex.
Review in Journal of cell science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed.
- SET1/MLL family of proteins: functions beyond histone methylation.Epigenetics · 2021Review
- The Opposing Functions of Protein Kinases and Phosphatases in Chromosome Bipolar Attachment.International journal of molecular sciences · 2019Review
- AMPK-mediated activation of MCU stimulates mitochondrial CaNature cell biology · 2019Article
- Electron cryotomography analysis of Dam1C/DASH at the kinetochore-spindle interface in situ.The Journal of cell biology · 2019Article
- The kinetochore module Okp1The EMBO journal · 2019Article
- A Kinesin-5, Cin8, Recruits Protein Phosphatase 1 to Kinetochores and Regulates Chromosome Segregation.Current biology : CB · 2018Article
- Article
- How the kinetochore couples microtubule force and centromere stretch to move chromosomes.Nature cell biology · 2016Article
- Directed and persistent movement arises from mechanochemistry of the ParA/ParB system.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Kinetochore-microtubule error correction is driven by differentially regulated interaction modes.Nature cell biology · 2015Article
- Amphitelic orientation of centromeres at metaphase I is an important feature for univalent-dependent meiotic nonreduction.Journal of genetics · 2014Article
- Centromeric heterochromatin: the primordial segregation machine.Annual review of genetics · 2014Review
- Subunit organization in the Dam1 kinetochore complex and its ring around microtubules.Molecular biology of the cell · 2011Article
- The essentiality of the fungus-specific Dam1 complex is correlated with a one-kinetochore-one-microtubule interaction present throughout the cell cycle, independent of the nature of a centromere.Eukaryotic cell · 2011Article
- Ringing the changes: emerging roles for DASH at the kinetochore-microtubule Interface.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2011Review
- The Ndc80 loop region facilitates formation of kinetochore attachment to the dynamic microtubule plus end.Current biology : CB · 2011Article
- Kinetochore-microtubule interactions: steps towards bi-orientation.The EMBO journal · 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
2 authors.
Funding
Abstract
Faithful segregation of genetic material during cell division requires the dynamic but robust attachment of chromosomes to spindle microtubules during all stages of mitosis. This regulated attachment occurs at kinetochores, which are complex protein organelles that are essential for cell survival and genome integrity. In budding yeast, in which a single microtubule attaches per kinetochore, a heterodecamer known as the Dam1 complex (or DASH complex) is required for proper chromosome segregation. Recent years have seen a burst of structural and biophysical data concerning this interesting complex, which has caught the attention of the mitosis research field. In vitro, the Dam1 complex interacts directly with tubulin and self-assembles into ring structures around the microtubule surface. The ring is capable of tracking with depolymerizing ends, and a model has been proposed whereby the circular geometry of the oligomeric Dam1 complex allows it to couple the depolymerization of microtubules to processive chromosome movement in the absence of any additional energy source. Although it is attractive and simple, several important aspects of this model remain controversial. Additionally, the generality of the Dam1 mechanism has been questioned owing to the fact that there are no obvious Dam1 homologs beyond fungi. In this Commentary, we discuss recent structure-function studies of this intriguing complex.
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.