Evidence map›Paper›PMID 11390638›Full record

ArticleMolecular and cellular biology2001

Phosphorylation of the RNA polymerase II carboxy-terminal domain by the Bur1 cyclin-dependent kinase.

S Murray, R Udupa, S Yao, G Hartzog, G Prelich

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
–field-weighted citation impact
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

54 citing papers in PubMed.

  1. Review
  2. Article
  3. Cyclin-dependent kinases: Masters of the eukaryotic universe.Wiley interdisciplinary reviews. RNA · 2023
    Review
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  5. Article
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  11. Review
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  15. Review
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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

5 authors.

S MurrayDepartment of Molecular Genetics, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
R Udupa
S Yao
G Hartzog
G Prelich

Funding

GENETIC ANALYSIS OF BASAL TRANSCRIPTION IN YEASTR01GM052486 · NIGMS · YESHIVA UNIVERSITY · PI PRELICH, GREGORY · 1996 to 2009
$3.4M
FUNCTIONS OF SPT4/SPT5 IN TRANSCRIPTIONR01GM060479 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI HARTZOG, GRANT A · 2000 to 2008
$2.2M
NIGMS NIH HHS GM52486NIGMS NIH HHS GM60479NIGMS NIH HHS R01 GM052486NIGMS NIH HHS R01 GM060479
6 · The paper itself

Abstract

BUR1, which was previously identified by a selection for mutations that have general effects on transcription in Saccharomyces cerevisiae, encodes a cyclin-dependent kinase that is essential for viability, but none of its substrates have been identified to date. Using an unbiased biochemical approach, we have identified the carboxy-terminal domain (CTD) of Rpb1, the largest subunit of RNA polymerase II, as a Bur1 substrate. Phosphorylation of Rpb1 by Bur1 is likely to be physiologically relevant, since bur1 mutations interact genetically with rpb1 CTD truncations and with mutations in other genes involved in CTD function. Several genetic interactions are presented, implying a role for Bur1 during transcriptional elongation. These results identify Bur1 as a fourth S. cerevisiae CTD kinase and provide striking functional similarities between Bur1 and metazoan P-TEFb.

Indexed as

Protein KinasesProtein Structure, TertiarySaccharomyces cerevisiae ProteinsAnimalsCyclin-Dependent KinasesGenes, ReporterHumansImmunoblottingPeptidesPhosphorylationPlasmidsPrecipitin TestsProtein SubunitsRecombinant Fusion ProteinsRNA Polymerase IISaccharomyces cerevisiaeCTDK-I protein complex, S cerevisiaeCyclin-Dependent KinasesPeptidesProtein KinasesProtein SubunitsRecombinant Fusion ProteinsRNA Polymerase IISaccharomyces cerevisiae ProteinsSGV1 protein, S cerevisiae

Identifiers

PMID11390638
PMCPMC87070

What OpenQuestion holds

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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.