Evidence map›Paper›PMID 23446052›Full record

ReviewJournal of the Royal Society, Interface2013

The role of the nucleosome acidic patch in modulating higher order chromatin structure.

Anna A Kalashnikova, Mary E Porter-Goff, Uma M Muthurajan, Karolin Luger, Jeffrey C Hansen

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of the Royal Society, Interface, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 156 papers.

0numbers the graph read from it
0cells of the map it votes in
156citing papers in PubMed
8.7field-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

156 citing papers in PubMed, 270 citations in OpenAlex.

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  8. SMARCD1 and Its Functional Relevance in SWI/SNF and Cancer.International journal of molecular sciences · 2026
    Review
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  20. Structure and nucleic acid interactions of the SProceedings of the National Academy of Sciences of the United States of America · 2025
    Article

96 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Anna A KalashnikovaDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523-1870, USA.
Mary E Porter-Goff
Uma M Muthurajan
Karolin Luger
Jeffrey C Hansen
Colorado State University · US

Funding

project 3P01GM088409 · NIGMS · COLORADO STATE UNIVERSITY · PI NYBORG, JENNIFER K. · 2010 to 2014
$7.3M
CHROMATIN STRUCTURE AND STABILITY IN THE SOLUTION STATER01GM045916 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI HANSEN, JEFFREY C · 1996 to 2012
$3.3M
MeCP2 Structure and FunctionR01GM066834 · NIGMS · COLORADO STATE UNIVERSITY-FORT COLLINS · PI HANSEN, JEFFREY C · 2003 to 2011
$2.4M
CHROMATIN STRUCTURE AND STABILITY IN THE SOLUTION STATER29GM045916 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI HANSEN, JEFFREY C · 1991 to 1995
–
Howard Hughes Medical InstituteNIGMS NIH HHS GM045916NIGMS NIH HHS GM066834NIGMS NIH HHS GM088409NIGMS NIH HHS P01 GM088409NIGMS NIH HHS R01 GM045916NIGMS NIH HHS R01 GM066834
6 · The paper itself

Abstract

Higher order folding of chromatin fibre is mediated by interactions of the histone H4 N-terminal tail domains with neighbouring nucleosomes. Mechanistically, the H4 tails of one nucleosome bind to the acidic patch region on the surface of adjacent nucleosomes, causing fibre compaction. The functionality of the chromatin fibre can be modified by proteins that interact with the nucleosome. The co-structures of five different proteins with the nucleosome (LANA, IL-33, RCC1, Sir3 and HMGN2) recently have been examined by experimental and computational studies. Interestingly, each of these proteins displays steric, ionic and hydrogen bond complementarity with the acidic patch, and therefore will compete with each other for binding to the nucleosome. We first review the molecular details of each interface, focusing on the key non-covalent interactions that stabilize the protein-acidic patch interactions. We then propose a model in which binding of proteins to the nucleosome disrupts interaction of the H4 tail domains with the acidic patch, preventing the intrinsic chromatin folding pathway and leading to assembly of alternative higher order chromatin structures with unique biological functions.

Indexed as

Chromosomal Proteins, Non-HistoneModels, MolecularNucleosomesAnimalsChromatin Assembly and DisassemblyHumansChromosomal Proteins, Non-HistoneNucleosomes

Identifiers

PMID23446052
PMCPMC3627075
OpenAlexW1965200310

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.