Evidence map›Paper›PMID 12163470›Full record

ArticleThe Journal of cell biology2002

Barrier-to-autointegration factor: major roles in chromatin decondensation and nuclear assembly.

Miriam Segura-Totten, Amy K Kowalski, Robert Craigie, Katherine L Wilson

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

90 citing papers in PubMed, 175 citations in OpenAlex.

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  12. BAF-L Modulates Histone-to-Protamine Transition during Spermiogenesis.International journal of molecular sciences · 2022
    Article
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  20. K6-linked SUMOylation of BAF regulates nuclear integrity and DNA replication in mammalian cells.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article

30 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

4 authors at 3 institutions in 1 country.

Miriam Segura-TottenDepartment of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Amy K Kowalski
Robert Craigie
Katherine L Wilson
Johns Hopkins University · USJohns Hopkins Medicine · USNational Institutes of Health · US

Funding

REGULATION OF NUCLEAR ENVELOPE ASSEMBLY AND DISASSEMBLYR01GM048646 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WILSON, KATHERINE L · 1994 to 2012
$4.9M
STUDIES ON THE MECHANISM OF RETROVIRAL DNA INTEGRATIONZ01DK036108 · NIDDK · DIABETES, DIGESTIVE, KIDNEY DISEASES · PI CRAIGIE, ROBERT · 1988 to 2006
–
NIGMS NIH HHS GM48646NIGMS NIH HHS R01 GM048646
6 · The paper itself

Abstract

Barrier-to-autointegration factor (BAF) is a DNA-bridging protein, highly conserved in metazoans. BAF binds directly to LEM (LAP2, emerin, MAN1) domain nuclear membrane proteins, including LAP2 and emerin. We used site-directed mutagenesis and biochemical analysis to map functionally important residues in human BAF, including those required for direct binding to DNA or emerin. We also tested wild-type BAF and 25 point mutants for their effects on nuclear assembly in Xenopus egg extracts, which contain approximately 12 microM endogenous BAF dimers. Exogenous BAF caused two distinct effects: at low added concentrations, wild-type BAF enhanced chromatin decondensation and nuclear growth; at higher added concentrations, wild-type BAF completely blocked chromatin decondensation and nuclear growth. Mutants fell into four classes, including one that defines a novel functional surface on the BAF dimer. Our results suggest that BAF, unregulated, potently compresses chromatin structure, and that BAF interactions with both DNA and LEM proteins are critical for membrane recruitment and chromatin decondensation during nuclear assembly.

Indexed as

Nuclear ProteinsAmino Acid SequenceAnimalsCells, CulturedChromatinCloning, MolecularDimerizationDNA-Binding ProteinsDNA, ComplementaryEukaryotic CellsFemaleMembrane ProteinsMicroscopy, ElectronMutagenesis, Site-DirectedNuclear EnvelopeOocytesBANF1 protein, humanChromatinDNA-Binding ProteinsDNA, Complementaryemerinlamina-associated polypeptide 2Membrane ProteinsNuclear ProteinsThymopoietins

Identifiers

PMID12163470
PMCPMC2173821
OpenAlexW1965965755

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.