Evidence map›Paper›PMID 30373818›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Fork pausing allows centromere DNA loop formation and kinetochore assembly.

Diana M Cook, Maggie Bennett, Brandon Friedman, Josh Lawrimore, Elaine Yeh, Kerry Bloom

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.1field-weighted citation impact, top 25% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Point centromere activity requires an optimal level of centromeric noncoding RNA.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Diana M CookDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280.
Maggie BennettDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280.
Brandon FriedmanDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280.
Josh LawrimoreDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280.
Elaine YehDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280.
Kerry BloomDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280 kerry_bloom@unc.edu.
University of North Carolina at Chapel Hill · US

Funding

Structure and Function of a Eukaryotic CentromereR37GM032238 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BLOOM, KERRY S, YEH, ELAINE YING · 2011 to 2020
$5.2M
Big Data to Knowledge Training ProgramT32CA201159 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI FOREST, MARK GREGORY, KOSOROK, MICHAEL R · 2015 to 2015
$316k
NCI NIH HHS T32 CA201159NIGMS NIH HHS R37 GM032238
6 · The paper itself

Abstract

De novo kinetochore assembly, but not template-directed assembly, is dependent on COMA, the kinetochore complex engaged in cohesin recruitment. The slowing of replication fork progression by treatment with phleomycin (PHL), hydroxyurea, or deletion of the replication fork protection protein Csm3 can activate de novo kinetochore assembly in COMA mutants. Centromere DNA looping at the site of de novo kinetochore assembly can be detected shortly after exposure to PHL. Using simulations to explore the thermodynamics of DNA loops, we propose that loop formation is disfavored during bidirectional replication fork migration. One function of replication fork stalling upon encounters with DNA damage or other blockades may be to allow time for thermal fluctuations of the DNA chain to explore numerous configurations. Biasing thermodynamics provides a mechanism to facilitate macromolecular assembly, DNA repair, and other nucleic acid transactions at the replication fork. These loop configurations are essential for sister centromere separation and kinetochore assembly in the absence of the COMA complex.

Indexed as

Cell Cycle ProteinsCentromereChromatinChromosomal Proteins, Non-HistoneCohesinsDNADNA DamageDNA RepairDNA ReplicationKinetochoresPhleomycinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpindle ApparatusThermodynamicsCell Cycle ProteinsChromatinChromosomal Proteins, Non-HistoneCohesinsDNAPhleomycinsSaccharomyces cerevisiae ProteinscentromereCOMAkinetochore

Identifiers

PMID30373818
PMCPMC6243264
OpenAlexW2898765127

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.