Evidence map›Paper›PMID 10094402›Full record

ArticleMolecular and cellular biochemistry1999

Role of protein kinase CK2 in phosphorylation nucleosomal proteins in relation to transcriptional activity.

C Guo, A T Davis, S Yu, S Tawfic, K Ahmed

Abstract read
PubMed
In one paragraph

Article in Molecular and cellular biochemistry, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.7field-weighted citation impact, top 9% 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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Protein kinase CK2--a key suppressor of apoptosis.Advances in enzyme regulation · 2008
    Review
  9. Protein kinase CK2 in gene control at cell cycle entry.Molecular and cellular biochemistry · 2005
    Article
  10. Article
  11. Consequences of CK2 signaling to the nuclear matrix.Molecular and cellular biochemistry · 2001
    Article
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.

C GuoDepartment of Laboratory Medicine and Pathology, University of Minnesota and the Department of Veterans Affairs Medical Center, Minneapolis 55417, USA.
A T Davis
S Yu
S Tawfic
K Ahmed
University of Minnesota Medical Center · USMinneapolis VA Medical Center · US

Funding

Studies of Normal and Neoplastic ProstateU01CA015062 · NCI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI AHMED, KHALIL · 2004 to 2008
$1.1M
STUDIES OF NORMAL AND NEOPLASTIC PROSTATER01CA015062 · NCI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI AHMED, KHALIL · 1985 to 2002
$578k
STUDIES OF NORMAL AND NEOPLASTIC PROSTATER37CA015062 · NCI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI AHMED, KHALIL · 1986 to 1993
–
NCI NIH HHS CA-15062
6 · The paper itself

Abstract

Protein kinase CK2 undergoes rapid translocation to nuclear matrix and nucleosomes on androgenic stimulation of growth in prostatic epithelial cells. Further, CK2 appears to be regulated differentially in the transcriptionally active and inactive nucleosomes. We have investigated the role of CK2 in phosphorylation of nucleosome-associated proteins in the transcriptionally active and inactive nucleosomes that were isolated from ventral prostate subjected to different androgenic status in vivo. Proteins associated with these nucleosomes were phosphorylated via the intrinsic protein kinase activity, using [gamma-32P]ATP in the absence and presence of GTP. Several proteins appear to be potential substrates for CK2 associated with the nucleosomes. Among them are proteins that are differentially associated with the transcriptionally active and inactive nucleosomes. Phosphorylation of several of these proteins is modulated depending not only on their sites of association (i.e., active vs. inactive nucleosomes) but also on the state of transcriptional activity. Differential phosphorylation of specific proteins by CK2 associated with the active and inactive nucleosomes may be pertinent to the process of transcription regulation.

Indexed as

Transcription, GeneticAnimalsCasein Kinase IIMaleNucleosomesPhosphorylationProtein Serine-Threonine KinasesRatsRats, Sprague-DawleyCasein Kinase IINucleosomesProtein Serine-Threonine Kinases

Identifiers

PMID10094402
OpenAlexW1540025446

What OpenQuestion holds

Texttitle and abstract
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.