Evidence map›Paper›PMID 26030138›Full record

ArticlePloS one2015

Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin Dynamics.

Serena Nicolai, Silvia Filippi, Manuela Caputo, Lubos Cipak, Juraj Gregan, Gustav Ammerer, Mattia Frontini, Daniela Willems, Giorgio Prantera, Adayabalam S Balajee and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

10 citing papers in PubMed, 11 citations in OpenAlex.

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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 6 institutions in 5 countries.

Serena NicolaiUnit of Molecular Genetics of Aging, Department of Ecology and Biology, University of Tuscia, 01100, Viterbo, Italy.
Silvia FilippiUnit of Molecular Genetics of Aging, Department of Ecology and Biology, University of Tuscia, 01100, Viterbo, Italy.
Manuela CaputoUnit of Molecular Genetics of Aging, Department of Ecology and Biology, University of Tuscia, 01100, Viterbo, Italy.
Lubos CipakCancer Research Institute, Slovak Academy of Sciences, Bratislava, Slovak Republic.
Juraj GreganDepartment of Genetics, Comenius University in Bratislava, Slovakia.
Gustav AmmererDepartment of Biochemistry, Mass Spectrometry Facility, Max F. Perutz Laboratories, University of Vienna, Vienna, Austria.
Mattia FrontiniDepartment of Haematology, University of Cambridge, CB2 0PT, Cambridge, United Kingdom.
Daniela WillemsUnit of Molecular Genetics of Aging, Department of Ecology and Biology, University of Tuscia, 01100, Viterbo, Italy.
Giorgio PranteraUnit of Molecular Genetics of Aging, Department of Ecology and Biology, University of Tuscia, 01100, Viterbo, Italy.
Adayabalam S BalajeeCenter for Radiological Research, Department of Radiation Oncology, Columbia University Medical Center, New York, New York, 10032, United States of America.
Luca Proietti-De-SantisUnit of Molecular Genetics of Aging, Department of Ecology and Biology, University of Tuscia, 01100, Viterbo, Italy.
Università degli Studi della Tuscia · ITColumbia University Irving Medical Center · USComenius University Bratislava · SKMax Perutz Labs · ATSlovak Academy of Sciences · SKUniversity of Cambridge · GB

Funding

Austrian Science Fund FWF P 23609Telethon GGP11176
6 · The paper itself

Abstract

The CSB protein, a member of the SWI/SNF ATP dependent chromatin remodeling family of proteins, plays a role in a sub-pathway of nucleotide excision repair (NER) known as transcription coupled repair (TCR). CSB is frequently mutated in Cockayne syndrome group B, a segmental progeroid human autosomal recessive disease characterized by growth failure and degeneration of multiple organs. Though initially classified as a DNA repair protein, recent studies have demonstrated that the loss of CSB results in pleiotropic effects. Identification of novel proteins belonging to the CSB interactome may be useful not only for predicting the molecular basis for diverse pathological symptoms of CS-B patients but also for unraveling the functions of CSB in addition to its authentic role in DNA repair. In this study, we performed tandem affinity purification (TAP) technology coupled with mass spectrometry and co-immunoprecipitation studies to identify and characterize the proteins that potentially interact with CSB-TAP. Our approach revealed 33 proteins that were not previously known to interact with CSB. These newly identified proteins indicate potential roles for CSB in RNA metabolism involving repression and activation of transcription process and in the maintenance of chromatin dynamics and integrity.

Indexed as

Cell LineChromatinCockayne SyndromeDNA HelicasesDNA RepairDNA Repair EnzymesHumansImmunoprecipitationPoly-ADP-Ribose Binding ProteinsRNATranscription, GeneticChromatinDNA HelicasesDNA Repair EnzymesERCC6 protein, humanPoly-ADP-Ribose Binding ProteinsRNA

Identifiers

PMID26030138
PMCPMC4451243
OpenAlexW1546502595

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Registered trials

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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.