Evidence map›Paper›PMID 10958697›Full record

ArticleMolecular and cellular biology2000

MyoD-dependent induction during myoblast differentiation of p204, a protein also inducible by interferon.

C j Liu, H Wang, Z Zhao, S Yu, Y B Lu, J Meyer, G Chatterjee, S Deschamps, B A Roe, P Lengyel

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

22 citing papers in PubMed, 69 citations in OpenAlex.

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  11. Wanderings in biochemistry.The Journal of biological chemistry · 2014
    Article
  12. Review
  13. Article
  14. Acetylation modulates cellular distribution and DNA sensing ability of interferon-inducible protein IFI16.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  15. Article
  16. Review
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  18. ADAMTS-7: a metalloproteinase that directly binds to and degrades cartilage oligomeric matrix protein.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2006
    Article
  19. Article
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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 2 institutions in 1 country.

C j LiuDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, USA.
H Wang
Z Zhao
S Yu
Y B Lu
J Meyer
G Chatterjee
S Deschamps
B A Roe
P Lengyel
Yale University · USUniversity of Oklahoma · US

Funding

OKLAHOMA UNIVERSITY GENOME CENTER - ADVANCED CENTER FORU54HG002153 · NHGRI · UNIVERSITY OF OKLAHOMA NORMAN · PI ROE, BRUCE A · 1999 to 2003
$10.4M
INTERFERON, ANIMAL VIRUSES, AND PROTEIN SYNTHESISR37AI012320 · NIAID · YALE UNIVERSITY · PI LENGYEL, PETER · 1990 to 1999
–
NHGRI NIH HHS HG02153NHGRI NIH HHS U54 HG002153NIAID NIH HHS R37 AI012320NIAID NIH HHS R37AI12320
6 · The paper itself

Abstract

p204, an interferon-inducible p200 family protein, inhibits rRNA synthesis in fibroblasts by blocking the binding of the upstream binding factor transcription factor to DNA. Here we report that among 10 adult mouse tissues tested, the level of p204 was highest in heart and skeletal muscles. In cultured C2C12 skeletal muscle myoblasts, p204 was nucleoplasmic and its level was low. During myoblast fusion this level strongly increased, p204 became phosphorylated, and the bulk of p204 appeared in the cytoplasm of the myotubes. Leptomycin B, an inhibitor of nuclear export that blocked myoblast fusion, inhibited the nuclear export signal-dependent translocation of p204 to the cytoplasm. The increase in the p204 level during myoblast fusion was a consequence of MyoD transcription factor binding to several MyoD-specific sequences in the gene encoding p204, followed by transcription. Overexpression of p204 (in C2C12 myoblasts carrying an inducible p204 expression plasmid) accelerated the fusion of myoblasts to myotubes in differentiation medium and induced the fusion even in growth medium. The level of p204 in mouse heart muscle strongly increased during differentiation; it was barely detectable in 10. 5-day-old embryos, reached the peak level in 16.5-day-old embryos, and remained high thereafter. p204 is the second p200 family protein (after p202a) found to be involved in muscle differentiation. (p202a was formerly designated p202. The new designation is due to the identification of a highly similar protein-p202b [H. Wang, G. Chatterjee, J. J. Meyer, C. J. Liu, N. A. Manjunath, P. Bray-Ward, and P. Lengyel, Genomics 60:281-294, 1999].) These results reveal that p204 and p202a function in both muscle differentiation and interferon action.

Indexed as

ActininAnimalsBase SequenceBiological TransportCell DifferentiationCell FusionCells, CulturedCytoplasmDNA, ComplementaryFatty Acids, UnsaturatedGene ExpressionGenes, ReporterInterferonsMiceMice, Inbred C57BLMolecular Sequence DataActininDNA, ComplementaryFatty Acids, UnsaturatedIfi16 protein, mouseInterferonsleptomycin BMyoD ProteinNuclear ProteinsPhosphoproteins

Identifiers

PMID10958697
PMCPMC88777
OpenAlexW2131738138

What OpenQuestion holds

Textmetadata
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.