Evidence map›Paper›PMID 7479833›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

The nuclear matrix protein NMP-1 is the transcription factor YY1.

B Guo, P R Odgren, A J van Wijnen, T J Last, J Nickerson, S Penman, J B Lian, J L Stein, G S Stein

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

51 citing papers in PubMed, 174 citations in OpenAlex.

  1. Review
  2. Yin Yang 1: Function, Mechanisms, and Glia.Neurochemical research · 2025
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Transcription factor YY1 is essential for regulation of the Th2 cytokine locus and for Th2 cell differentiation.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  8. The abbreviated pluripotent cell cycle.Journal of cellular physiology · 2013
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. An architectural genetic and epigenetic perspective.Integrative biology : quantitative biosciences from nano to macro · 2011
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

9 authors at 2 institutions in 1 country.

B GuoDepartment of Cell Biology, University of Masachusetts Medical Center, Worcester 01655, USA.
P R Odgren
A J van Wijnen
T J Last
J Nickerson
S Penman
J B Lian
J L Stein
G S Stein
Massachusetts Institute of Technology · USOrthopedic One · US

Funding

IDENTIFICATION OF HUMAN HISTONE GENE REGULATORY SEQUENCER01GM032010 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI STEIN, GARY S. · 1985 to 2006
$3.4M
NUCLEAR MATRIX MEDIATED TRANSCRIPTIONAL CONTROL OF OSTEOBLAST GENE EXPRESSIONP01AR042262 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI STEIN, GARY S. · 1994 to 1997
–
NIAMS NIH HHS AR42262NIGMS NIH HHS GM32010
6 · The paper itself

Abstract

NMP-1 was initially identified as a nuclear matrix-associated DNA-binding factor that exhibits sequence-specific recognition for the site IV regulatory element of a histone H4 gene. This distal promoter domain is a nuclear matrix interaction site. In the present study, we show that NMP-1 is the multifunctional transcription factor YY1. Gel-shift and Western blot analyses demonstrate that NMP-1 is immunoreactive with YY1 antibody. Furthermore, purified YY1 protein specifically recognizes site IV and reconstitutes the NMP-1 complex. Western blot and gel-shift analyses indicate that YY1 is present within the nuclear matrix. In situ immunofluorescence studies show that a significant fraction of YY1 is localized in the nuclear matrix, principally but not exclusively associated with residual nucleoli. Our results confirm that NMP-1/YY1 is a ubiquitous protein that is present in both human cells and in rat osteosarcoma ROS 17/2.8 cells. The finding that NMP-1 is identical to YY1 suggests that this transcriptional regulator may mediate gene-matrix interactions. Our results are consistent with the concept that the nuclear matrix may functionally compartmentalize the eukaryotic nucleus to support regulation of gene expression.

Indexed as

AnimalsAntibody SpecificityBase SequenceBinding SitesBlotting, WesternCell CompartmentationCell NucleolusCell NucleusCross ReactionsDNADNA-Binding ProteinsErythroid-Specific DNA-Binding FactorsHeLa CellsHumansMolecular Sequence DataNuclear MatrixDNADNA-Binding ProteinsErythroid-Specific DNA-Binding FactorsOligodeoxyribonucleotidesRecombinant ProteinsTranscription FactorsYY1 protein, humanYy1 protein, ratYY1 Transcription Factor

Identifiers

PMID7479833
PMCPMC40644
OpenAlexW2077150554

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.