Evidence map›Paper›PMID 21278158›Full record

ArticleNucleic acids research2011

Effects of HMGN variants on the cellular transcription profile.

Mark Rochman, Leila Taher, Toshihiro Kurahashi, Srujana Cherukuri, Vladimir N Uversky, David Landsman, Ivan Ovcharenko, Michael Bustin

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

30 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Structural and functional analysis of "non-smelly" proteins.Cellular and molecular life sciences : CMLS · 2020
    Article
  11. Article
  12. Article
  13. Article
  14. Research advances in HMGN5 and cancer.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Review
  15. Article
  16. Article
  17. Article
  18. HMGB1 in health and disease.Molecular aspects of medicine · 2014
    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

8 authors at 4 institutions in 1 country.

Mark RochmanProtein Section, Laboratory of Metabolism, Center for Cancer Research, National Cancer Institute, Computational Biology Branch, National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, 9000 Rockville Pike, Bethesda, MD 20894, USA.
Leila Taher
Toshihiro Kurahashi
Srujana Cherukuri
Vladimir N Uversky
David Landsman
Ivan Ovcharenko
Michael Bustin
National Cancer Center · USNational Center for Biotechnology Information · USIndiana University Bloomington · USNational Institutes of Health · US

Funding

Regulatory landscape of the human genome: comparative and evolutionary analysis.ZIALM200881 · NLM · NATIONAL LIBRARY OF MEDICINE · PI OVCHARENKO, IVAN · 2009 to 2025
$20.1M
Chromosomal Proteins and Chromosomal FunctionsZIABC004496 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BUSTIN, MICHAEL · 2009 to 2023
$12.9M
Biological Functions of Chromosomal ProteinsZIABC011154 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BUSTIN, MICHAEL · 2009 to 2023
$11.0M
Gene Regulatory Sequences And Protein Binding in Genome SequencesZIALM000084 · NLM · NATIONAL LIBRARY OF MEDICINE · PI LANDSMAN, DAVID · 2009 to 2025
$7.7M
Structural And Functional Analysis Of Protein Sequence FamiliesZIALM000071 · NLM · NATIONAL LIBRARY OF MEDICINE · PI LANDSMAN, DAVID · 2009 to 2025
$3.7M
Intramural NIH HHS
6 · The paper itself

Abstract

High mobility group N (HMGN) is a family of intrinsically disordered nuclear proteins that bind to nucleosomes, alters the structure of chromatin and affects transcription. A major unresolved question is the extent of functional specificity, or redundancy, between the various members of the HMGN protein family. Here, we analyze the transcriptional profile of cells in which the expression of various HMGN proteins has been either deleted or doubled. We find that both up- and downregulation of HMGN expression altered the cellular transcription profile. Most, but not all of the changes were variant specific, suggesting limited redundancy in transcriptional regulation. Analysis of point and swap HMGN mutants revealed that the transcriptional specificity is determined by a unique combination of a functional nucleosome-binding domain and C-terminal domain. Doubling the amount of HMGN had a significantly larger effect on the transcription profile than total deletion, suggesting that the intrinsically disordered structure of HMGN proteins plays an important role in their function. The results reveal an HMGN-variant-specific effect on the fidelity of the cellular transcription profile, indicating that functionally the various HMGN subtypes are not fully redundant.

Indexed as

Transcription, GeneticAmino Acid SequenceAnimalsHMGN ProteinsMiceMice, KnockoutMolecular Sequence DataMutationSequence Homology, Amino AcidHMGN Proteins

Identifiers

PMID21278158
PMCPMC3105402
OpenAlexW2036487868

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.