Evidence map›Paper›PMID 11553702›Full record

ArticleMolecular biology of the cell2001

Dad1p, third component of the Duo1p/Dam1p complex involved in kinetochore function and mitotic spindle integrity.

M Enquist-Newman, I M Cheeseman, D Van Goor, D G Drubin, P B Meluh, G Barnes

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

45 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Phosphoregulation promotes release of kinetochores from dynamic microtubules via multiple mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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 · 2011
    Review
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 2 institutions in 1 country.

M Enquist-NewmanDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA.
I M Cheeseman
D Van Goor
D G Drubin
P B Meluh
G Barnes
University of California, Berkeley · USMemorial Sloan Kettering Cancer Center · US

Funding

SACCHAROMYCES CEREVISIAE MICROTUBULE CYTOSKELETONR01GM047842 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BARNES, GEORJANA · 1993 to 2022
$7.5M
CENTROMERE STRUCTURE, ASSEMBLY AND FUNCTION IN YEASTR01GM060464 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI MELUH, PAMELA B · 2000 to 2004
$1.2M
SACCHAROMYCES CEREVISIAE MICROTUBULE CYTOSKELETONR55GM047842 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BARNES, GEORJANA · 1992 to 1992
–
NIGMS NIH HHS GM-47842NIGMS NIH HHS R01 GM047842NIGMS NIH HHS R01 GM060464NIGMS NIH HHS R01 GM-60464-02
6 · The paper itself

Abstract

We showed recently that a complex between Duo1p and Dam1p is required for both spindle integrity and kinetochore function in the budding yeast Saccharomyces cerevisiae. To extend our understanding of the functions and interactions of the Duo1p/Dam1p complex, we analyzed the novel gene product Dad1p (for Duo1 and Dam1 interacting). Dad1p physically associates with Duo1p by two-hybrid analysis, coimmunoprecipitates with Duo1p and Dam1p out of yeast protein extracts, and shows interdependent localization with Duo1p and Dam1p to the mitotic spindle. These results indicate that Dad1p functions as a component of the Duo1p/Dam1p complex. Like Duo1p and Dam1p, Dad1p also localizes to kinetochore regions in chromosomes spreads. Here, we also demonstrate by chromatin immunoprecipitation that Duo1p, Dam1p, and Dad1p associate specifically with centromeric DNA in a manner that is dependent upon Ndc10 and partially dependent upon the presence of microtubules. To explore the functions of Dad1p in vivo, we generated a temperature-sensitive allele, dad1-1. This allele shows spindle defects and a mitotic arrest phenotype that is dependent upon the spindle assembly checkpoint. In addition, dad1-1 mutants undergo chromosome mis-segregation at the restrictive temperature, resulting in a dramatic decrease in viability.

Indexed as

Saccharomyces cerevisiae ProteinsAllelesAmino Acid SequenceCell Cycle ProteinsChromatinChromosome SegregationCytoskeletal ProteinsEpistasis, GeneticGene Expression Regulation, FungalKinetochoresMicroscopy, FluorescenceMicrotubule-Associated ProteinsMolecular Sequence DataMutationNocodazolePrecipitin TestsCell Cycle ProteinsChromatinCytoskeletal ProteinsDad1 protein, S cerevisiaeDAM1 protein, S cerevisiaeDUO1 protein, S cerevisiaeMicrotubule-Associated ProteinsNocodazoleSaccharomyces cerevisiae Proteins

Identifiers

PMID11553702
PMCPMC59698
OpenAlexW2125483939

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.