Evidence map›Paper›PMID 33714893›Full record

ReviewCurrent opinion in chemical biology2021

Advancements in chemical biology targeting the kinases and phosphatases of RNA polymerase II-mediated transcription.

Wantae Kim, Blase LeBlanc, Wendy L Matthews, Zhong-Yin Zhang, Yan Zhang

Open access · greenAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Current opinion in chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 52% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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

5 authors at 2 institutions in 1 country.

Wantae KimMcKetta Department of Chemical Engineering, University of Texas at Austin, Austin, TX, 78712, USA.
Blase LeBlancDepartment of Molecular Biosciences, University of Texas at Austin, Austin, TX, 78712, USA.
Wendy L MatthewsDepartment of Molecular Biosciences, University of Texas at Austin, Austin, TX, 78712, USA.
Zhong-Yin ZhangDepartment of Medicinal Chemistry and Molecular Pharmacology, Department of Chemistry, and Institute for Drug Discovery, Purdue University, West Lafayette, IN, 47907, USA.
Yan ZhangDepartment of Molecular Biosciences, University of Texas at Austin, Austin, TX, 78712, USA; The Institute for Cellular and Molecular Biology. University of Texas at Austin, Austin, TX, 78712, USA. Electronic address: jeszhang@cm.utexas.edu.
The University of Texas at Austin · USPurdue University West Lafayette · US

Funding

Structure/Function of Protein Tyrosine PhosphatasesR01CA069202 · NCI · YESHIVA UNIVERSITY · PI Zhong-Yin Zhang · 1996 to 2026
$7.3M
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
Interpretation of the phosphorylation code of RNA polymerase II during eukaryotic transcriptionR01GM125882 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S., ZHANG, YAN JESSIE · 2018 to 2021
$1.4M
NCI NIH HHS R01 CA069202NIGMS NIH HHS R01 GM104896NIGMS NIH HHS R01 GM125882
6 · The paper itself

Abstract

Phosphorylation of RNA polymerase II (RNAP II) coordinates the temporal progression of eukaryotic transcription. The development and application of chemical genetic methods have enhanced our ability to investigate the intricate and intertwined pathways regulated by the kinases and phosphatases targeting RNAP II to ensure transcription accuracy and efficiency. Although identifying small molecules that modulate these enzymes has been challenging due to their highly conserved structures, powerful new chemical biology strategies such as targeted covalent inhibitors and small molecule degraders have significantly improved chemical probe specificity. The recent success in discovering phosphatase holoenzyme activators and inhibitors, which demonstrates the feasibility of selective targeting of individual phosphatase complexes, opens up new avenues into the study of transcription. Herein, we summarize how chemical biology is used to delineate kinases' identities involved in RNAP II regulation and new concepts in inhibitor/activator design implemented for kinases/phosphatases involved in modulating RNAP II-mediated transcription.

Indexed as

Enzyme InhibitorsModels, MolecularPhosphoric Monoester HydrolasesPhosphorylationPhosphotransferasesProtein BindingProtein ConformationRNA Polymerase IIStructure-Activity RelationshipSubstrate SpecificityTranscription, GeneticEnzyme InhibitorsPhosphoric Monoester HydrolasesPhosphotransferasesRNA Polymerase IIAnalog-sensitive kinaseCDKChemical biologyChemical geneticsPP1PP2ARNA polymerase IITargeted covalent inhibitorTranscription

Identifiers

PMID33714893
PMCPMC8384638
OpenAlexW3139231987

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.