Evidence map›Paper›PMID 21046224›Full record

ArticleChromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology2011

Dynamic as well as stable protein interactions contribute to genome function and maintenance.

Peter Hemmerich, Lars Schmiedeberg, Stephan Diekmann

Abstract read
In one paragraph

Article in Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Review
  2. Translocation of chromatin proteins to nucleoli-The influence of protein dynamics on post-fixation localization.Cytometry. Part A : the journal of the International Society for Analytical Cytology · 2021
    Article
  3. Transcription Factor Dynamics.Cold Spring Harbor perspectives in biology · 2021
    Review
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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

3 authors.

Peter HemmerichLeibniz Institute for Age Research, Fritz Lipmann Institute, Beutenbergstr. 11, 07745, Jena, Germany. phemmer@fli-leibniz.de
Lars Schmiedeberg
Stephan Diekmann

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cell nucleus is responsible for the storage, expression, propagation, and maintenance of the genetic material it contains. Highly organized macromolecular complexes are required for these processes to occur faithfully in an extremely crowded nuclear environment. In addition to chromosome territories, the nucleus is characterized by the presence of nuclear substructures, such as the nuclear envelope, the nucleolus, and other nuclear bodies. Other smaller structural entities assemble on chromatin in response to required functions including RNA transcription, DNA replication, and DNA repair. Experiments in living cells over the last decade have revealed that many DNA binding proteins have very short residence times on chromatin. These observations have led to a model in which the assembly of nuclear macromolecular complexes is based on the transient binding of their components. While indeed most nuclear proteins are highly dynamic, we found after an extensive survey of the FRAP literature that an important subset of nuclear proteins shows either very slow turnover or complete immobility. These examples provide compelling evidence for the establishment of stable protein complexes in the nucleus over significant fractions of the cell cycle. Stable interactions in the nucleus may, therefore, contribute to the maintenance of genome integrity. Based on our compilation of FRAP data, we propose an extension of the existing model for nuclear organization which now incorporates stable interactions. Our new "induced stability" model suggests that self-organization, self-assembly, and assisted assembly contribute to nuclear architecture and function.

Indexed as

GenomeMolecular Dynamics SimulationCell CycleCell NucleolusChromatinDNA-Binding ProteinsDNA RepairFluorescence Recovery After PhotobleachingIntranuclear Inclusion BodiesMicroscopy, FluorescenceMultiprotein ComplexesNuclear EnvelopeNuclear ProteinsProtein BindingRNAChromatinDNA-Binding ProteinsMultiprotein ComplexesNuclear ProteinsRNA

Identifiers

PMID21046224
PMCPMC3040344

What OpenQuestion holds

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Registered trials

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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.