Evidence map›Paper›PMID 28103682›Full record

ArticleACS chemical biology2017

Mapping the Phosphorylation Pattern of Drosophila melanogaster RNA Polymerase II Carboxyl-Terminal Domain Using Ultraviolet Photodissociation Mass Spectrometry.

Joshua E Mayfield, Michelle R Robinson, Victoria C Cotham, Seema Irani, Wendy L Matthews, Anjana Ram, David S Gilmour, Joe R Cannon, Yan Jessie Zhang, Jennifer S Brodbelt

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

23 citing papers in PubMed, 30 citations in OpenAlex.

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  18. Top-Down Proteomics: Ready for Prime Time?Analytical chemistry · 2018
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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

10 authors at 3 institutions in 1 country.

Joshua E Mayfield
Michelle R Robinson
Victoria C Cotham
Seema Irani
Wendy L Matthews
Anjana Ram
David S GilmourDepartment of Biochemistry and Molecular Biology, Penn State University , University Park, Pennsylvania 16802, United States.
Joe R Cannon
Jennifer S Brodbelt
The University of Texas at Austin · USHarvard University · USPennsylvania State University · US

Funding

POTENTIATED STATE OF THE HSP70 HEAT SHOCK GENER01GM047477 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI GILMOUR, DAVID SCOTT · 1992 to 2022
$6.7M
Gene-specific transcriptional silencing directed by dephosphorylation of RNAP IIR01GM104896 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI ZHANG, YAN JESSIE · 2013 to 2022
$2.4M
Mapping the C Terminal Domain of RNA Polymerase II by UVPD Mass SpectrometryR21EB018391 · NIBIB · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2014 to 2015
$405k
NIBIB NIH HHS R21 EB018391NIGMS NIH HHS R01 GM047477NIGMS NIH HHS R01 GM104896
6 · The paper itself

Abstract

Phosphorylation of the C-terminal domain of RNA polymerase II (CTD) plays an essential role in eukaryotic transcription by recruiting transcriptional regulatory factors to the active polymerase. However, the scarcity of basic residues and repetitive nature of the CTD sequence impose a huge challenge for site-specific characterization of phosphorylation, hindering our understanding of this crucial biological process. Herein, we apply LC-UVPD-MS methods to analyze post-translational modification along native sequence CTDs. Application of our method to the Drosophila melanogaster CTD reveals the phosphorylation pattern of this model organism for the first time. The divergent nature of fly CTD allows us to derive rules defining how flanking residues affect phosphorylation choice by CTD kinases. Our data support the use of LC-UVPD-MS to decipher the CTD code and determine rules that program its function.

Indexed as

Amino Acid SequenceAnimalsDrosophila melanogasterMass SpectrometryMitogen-Activated Protein Kinase 1PhosphorylationProtein DomainsProtein Processing, Post-TranslationalRNA Polymerase IISaccharomyces cerevisiaeUltraviolet RaysMitogen-Activated Protein Kinase 1RNA Polymerase II

Identifiers

PMID28103682
PMCPMC5376213
OpenAlexW2554756234

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.