Evidence map›Paper›PMID 21467141›Full record

ArticleCold Spring Harbor symposia on quantitative biology2010

Molecular structures and interactions in the yeast kinetochore.

U-S Cho, K D Corbett, J Al-Bassam, J J Bellizzi, P De Wulf, C W Espelin, J J Miranda, K Simons, R R Wei, P K Sorger and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Cold Spring Harbor symposia on quantitative biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Structure, assembly and reading of centromeric chromatin.Current opinion in genetics & development · 2012
    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

11 authors at 7 institutions in 2 countries.

U-S ChoJack and Eileen Connors Structural Biology Laboratory, Harvard Medical School, Boston, Massachusetts 02115, USA.
K D Corbett
J Al-Bassam
J J Bellizzi
P De Wulf
C W Espelin
J J Miranda
K Simons
R R Wei
P K Sorger
S C Harrison
Harvard University Press · USCenter for Systems Biology · USEuropean Institute of Oncology · ITHarvard University · USHoward Hughes Medical Institute · USPfizer (United States) · USUniversity of Toledo · US

Funding

BIOCHEMICAL AND GENETIC ANALYSIS OF YEAST KINETOCHORESR01GM051464 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SORGER, PETER KARL · 1994 to 2010
$3.9M
Microtubule Polymerization and Depolymerization Mechanisms by Conserved ProteinsR00GM084292 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI AL-BASSAM, JAWDAT MH · 2011 to 2013
$715k
Microtubule Polymerization and Depolymerization Mechanisms by Conserved ProteinsK99GM084292 · NIGMS · HARVARD MEDICAL SCHOOL · PI AL-BASSAM, JAWDAT MH · 2008 to 2010
$217k
Howard Hughes Medical InstituteNIGMS NIH HHS K99 GM084292NIGMS NIH HHS K99-GM84292NIGMS NIH HHS R00 GM084292NIGMS NIH HHS R01 GM051464NIGMS NIH HHS R01-GM51464
6 · The paper itself

Abstract

Kinetochores are the elaborate protein assemblies that attach chromosomes to spindle microtubules in mitosis and meiosis. The kinetochores of point-centromere yeast appear to represent an elementary module, which repeats a number of times in kinetochores assembled on regional centromeres. Structural analyses of the discrete protein subcomplexes that make up the budding-yeast kinetochore have begun to reveal principles of kinetochore architecture and to uncover molecular mechanisms underlying functions such as transmission of tension and establishment and maintenance of bipolar attachment. The centromeric DNA is probably wrapped into a compact organization, not only by a conserved, centromeric nucleosome, but also by interactions among various other DNA-bound kinetochore components. The rod-like, heterotetrameric Ndc80 complex, roughly 600 Å long, appears to extend from the DNA-proximal assembly to the plus end of a microtubule, to which one end of the complex is known to bind. Ongoing structural studies will clarify the roles of a number of other well-defined complexes.

Indexed as

KinetochoresMicrotubulesModels, BiologicalMultiprotein ComplexesProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMultiprotein ComplexesSaccharomyces cerevisiae Proteins

Identifiers

PMID21467141
PMCPMC3207249
OpenAlexW2109222541

What OpenQuestion holds

Textmetadata
LicenceTDM
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.