Evidence map›Paper›PMID 10454562›Full record

ArticleMolecular and cellular biology1999

MCM proteins are associated with RNA polymerase II holoenzyme.

K Yankulov, I Todorov, P Romanowski, D Licatalosi, K Cilli, S McCracken, R Laskey, D L Bentley

Abstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

43 citing papers in PubMed.

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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.

K YankulovDepartment of Molecular Biology and Genetics, University of Guelph, Guelph, Ontario N1G 2W1, Canada. yankulov@uoguelph.ca
I Todorov
P Romanowski
D Licatalosi
K Cilli
S McCracken
R Laskey
D L Bentley

Funding

Coupling of Transcription with Pre-mRNA MetabolismR01GM058613 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI BENTLEY, DAVID L · 1999 to 2014
$5.5M
NIGMS NIH HHS GM-58613NIGMS NIH HHS R01 GM058613Wellcome Trust
6 · The paper itself

Abstract

MCMs are a family of proteins related to ATP-dependent helicases that bind to origin recognition complexes and are required for initiation of DNA replication. We report that antibodies against MCM2(BM28) specifically inhibited transcription by RNA polymerase II (Pol II) in microinjected Xenopus oocytes. Consistent with this observation, MCM2 and other MCMs copurified with Pol II and general transcription factors (GTFs) in high-molecular-weight holoenzyme complexes isolated from Xenopus oocytes and HeLa cells. Pol II and GTFs also copurified with MCMs isolated by anti-MCM3 immunoaffinity chromatography. MCMs were specifically displaced from the holoenzyme complex by antibody against the C-terminal domain (CTD) of Pol II. In addition, MCMs bound to a CTD affinity column, suggesting that their association with holoenzyme depends in part on this domain of Pol II. These results suggest a new function for MCM proteins as components of the Pol II transcriptional apparatus.

Indexed as

AnimalsAntibodiesBinding SitesCell Cycle ProteinsChromatography, AffinityDNA Polymerase IIDogsFemaleHeLa CellsHoloenzymesHumansMacromolecular SubstancesMinichromosome Maintenance Complex Component 2Nuclear ProteinsOocytesRNA HelicasesAntibodiesCell Cycle ProteinsDNA Polymerase IIHoloenzymesMacromolecular SubstancesMCM2 protein, humanMinichromosome Maintenance Complex Component 2Nuclear ProteinsRNA HelicasesTranscription Factors

Identifiers

PMID10454562
PMCPMC84545

What OpenQuestion holds

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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.