Evidence map›Paper›PMID 28826505›Full record

ArticleeLife2017

A novel SH2 recognition mechanism recruits Spt6 to the doubly phosphorylated RNA polymerase II linker at sites of transcription.

Matthew A Sdano, James M Fulcher, Sowmiya Palani, Mahesh B Chandrasekharan, Timothy J Parnell, Frank G Whitby, Tim Formosa, Christopher P Hill

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

56 citing papers in PubMed, 79 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Genetic alterations in SUPT6H are associated with neurodevelopmental disorders.Biochimica et biophysica acta. Molecular basis of disease · 2026
    Article
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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

8 authors at 1 institution in 1 country.

Matthew A SdanoDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.ORCID http://orcid.org/0000-0001-6702-2755
James M FulcherDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.ORCID http://orcid.org/0000-0001-9033-3623
Sowmiya PalaniDepartment of Radiation Oncology, University of Utah School of Medicine, Salt Lake City, United States.
Mahesh B ChandrasekharanDepartment of Radiation Oncology, University of Utah School of Medicine, Salt Lake City, United States.
Timothy J ParnellDepartment of Radiation Oncology, University of Utah School of Medicine, Salt Lake City, United States.
Frank G WhitbyDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.
Tim FormosaDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.ORCID http://orcid.org/0000-0002-8477-2483
Christopher P HillDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.ORCID https://orcid.org/0000-0001-6796-7740
University of Utah · US

Funding

UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI KATHARINE S ULLMAN · 1986 to 2026
$72.6M
X-ray Cryst. CoreP50GM082545 · NIGMS · UNIVERSITY OF UTAH · PI SUNDQUIST, WESLEY I. · 2007 to 2018
$51.1M
Biochemical, Genetic, and Genomic Analysis of Nucleosome Reorganization by FACTR01GM064649 · NIGMS · UNIVERSITY OF UTAH · PI FORMOSA, TIMOTHY G · 2002 to 2022
$6.4M
Structure, mechanism, and function of the histone chaperones Spt6 and FACTR01GM116560 · NIGMS · UNIVERSITY OF UTAH · PI FORMOSA, TIMOTHY G, HILL, CHRISTOPHER P. · 2016 to 2019
$1.2M
LINEAR ION-TRAP /FOURIER TRANSFORM MASS SPECTROMETER: PROTEOMICS: DIABETESS10RR020883 · NCRR · UNIVERSITY OF UTAH · PI NELSON, CHAD P · 2005 to 2005
$500k
Maldi/ToF/ToF Mass Spectrometer for the University of UtahS10RR025532 · NCRR · UNIVERSITY OF UTAH · PI NELSON, CHAD C · 2010 to 2010
$490k
NCI NIH HHS P30 CA042014NCRR NIH HHS S10 RR020883NCRR NIH HHS S10 RR025532NIGMS NIH HHS P50 GM082545NIGMS NIH HHS R01 GM064649NIGMS NIH HHS R01 GM116560
6 · The paper itself

Abstract

We determined that the tandem SH2 domain of

Indexed as

Protein Processing, Post-TranslationalCrystallography, X-RayHistone ChaperonesModels, MolecularPhosphorylationProtein BindingProtein ConformationRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscriptional Elongation FactorsTranscription, GeneticHistone ChaperonesRNA Polymerase IIRPB1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSPT6 protein, S cerevisiaeTranscriptional Elongation Factorsbiophysicschromosomesgeneshistone chaperonephosphorylationRNA polymerase IIS. cerevisiaeSH2 domainSpt6structural biologytranscription

Identifiers

PMID28826505
PMCPMC5599234
OpenAlexW2748861120

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.