Evidence map›Paper›PMID 19995907›Full record

ArticleMolecular and cellular biology2010

Structure-specific recognition protein 1 facilitates microtubule growth and bundling required for mitosis.

Shelya X Zeng, Yanping Li, Yetao Jin, Qi Zhang, David M Keller, Carolyn M McQuaw, Eric Barklis, Stacie Stone, Maureen Hoatlin, Yingming Zhao and 1 more

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

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  9. SSRP1 Contributes to the Malignancy of Hepatocellular Carcinoma and Is Negatively Regulated by miR-497.Molecular therapy : the journal of the American Society of Gene Therapy · 2016
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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 5 institutions in 1 country.

Shelya X ZengDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, MS-0051, 635 Barnhill Drive, Indianapolis, IN 46202, USA.
Yanping Li
Yetao Jin
Qi Zhang
David M Keller
Carolyn M McQuaw
Eric Barklis
Stacie Stone
Maureen Hoatlin
Yingming Zhao
Hua Lu
Indiana University Health · USIndiana University School of MedicineOregon Health & Science University · USVollum Institute · USUniversity of Chicago · US

Funding

The Role of Ribosomal Proteins in the P53-MDM2 PathwayR01CA095441 · NCI · TULANE UNIVERSITY OF LOUISIANA · PI LU, HUA · 2002 to 2021
$5.1M
MOLECULAR DISSECTION OF A NOVEL P53 LIKE PROTEINR01CA079721 · NCI · OREGON HEALTH & SCIENCE UNIVERSITY · PI LU, HUA · 1999 to 2006
$1.8M
Role of ribosomal proteins in regulating c-MycR01CA129828 · NCI · TULANE UNIVERSITY OF LOUISIANA · PI LU, HUA · 2008 to 2012
$1.5M
Study of a FACTp140-SSRP1-associated p53 KinaseR01CA093614 · NCI · OREGON HEALTH & SCIENCE UNIVERSITY · PI LU, HUA · 2002 to 2006
$1.5M
NCI NIH HHS CA079721NCI NIH HHS CA095441NCI NIH HHS CA129828NCI NIH HHS CA93614NCI NIH HHS R01 CA079721NCI NIH HHS R01 CA093614NCI NIH HHS R01 CA095441NCI NIH HHS R01 CA129828
6 · The paper itself

Abstract

Tight regulation of microtubule (MT) dynamics is essential for proper chromosome movement during mitosis. Here we show, using mammalian cells, that structure-specific recognition protein 1 (SSRP1) is a novel regulator of MT dynamics. SSRP1 colocalizes with the spindle and midbody MTs, and associates with MTs both in vitro and in vivo. Purified SSRP1 facilitates tubulin polymerization and MT bundling in vitro. Knockdown of SSRP1 inhibits the growth of MTs and leads to disorganized spindle structures, reduction of K-fibers and midbody fibers, disrupted chromosome movement, and attenuated cytokinesis in vivo. These results demonstrate that SSRP1 is crucial for MT growth and spindle assembly during mitosis.

Indexed as

MitosisCell LineChromosome SegregationDNA-Binding ProteinsHigh Mobility Group ProteinsHumansMicroscopy, Electron, TransmissionMicrotubulesProtein BindingSpindle ApparatusTranscriptional Elongation FactorsDNA-Binding ProteinsHigh Mobility Group ProteinsSSRP1 protein, humanTranscriptional Elongation Factors

Identifiers

PMID19995907
PMCPMC2815565
OpenAlexW2080890380

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.