Evidence map›Paper›PMID 33396475›Full record

ArticleCells2020

Separation of Coiled-Coil Structures in Lamin A/C Is Required for the Elongation of the Filament.

Jinsook Ahn, Soyeon Jeong, So-Mi Kang, Inseong Jo, Bum-Joon Park, Nam-Chul Ha

Open access · goldAbstract read
In one paragraph

Article in Cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed, 1 pooled it
1.1field-weighted citation impact, top 23% 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

18 citing papers in PubMed, 1 synthesis or guideline pooled it, 24 citations in OpenAlex.

  1. Pooled it
  2. Review
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  7. Article
  8. Resveratrol Activates SIRT1 to Inhibit Trophoblast Pyroptosis in Preeclampsia.Reproductive sciences (Thousand Oaks, Calif.) · 2025
    Article
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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

6 authors at 2 institutions in 1 country.

Jinsook AhnDepartment of Agricultural Biotechnology, Centre for Food and Bioconvergence, and Research Institute for Agriculture and Life Sciences, CALS, Seoul National University, Seoul 08826, Korea.
Soyeon JeongDepartment of Agricultural Biotechnology, Centre for Food and Bioconvergence, and Research Institute for Agriculture and Life Sciences, CALS, Seoul National University, Seoul 08826, Korea.
So-Mi KangDepartment of Molecular Biology, College of Natural Science, Pusan National University, Busan 46241, Korea.ORCID 0000-0001-5717-7841
Inseong JoDepartment of Agricultural Biotechnology, Centre for Food and Bioconvergence, and Research Institute for Agriculture and Life Sciences, CALS, Seoul National University, Seoul 08826, Korea.
Bum-Joon ParkDepartment of Molecular Biology, College of Natural Science, Pusan National University, Busan 46241, Korea.
Nam-Chul HaDepartment of Agricultural Biotechnology, Centre for Food and Bioconvergence, and Research Institute for Agriculture and Life Sciences, CALS, Seoul National University, Seoul 08826, Korea.ORCID 0000-0003-4813-748X
Seoul National University · KRPusan National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intermediate filaments (IFs) commonly have structural elements of a central α-helical coiled-coil domain consisting of coil 1a, coil 1b, coil 2, and their flanking linkers. Recently, the crystal structure of a long lamin A/C fragment was determined and showed detailed features of a tetrameric unit. The structure further suggested a new binding mode between tetramers, designated eA22, where a parallel overlap of coil 1a and coil 2 is the critical interaction. This study investigated the biochemical effects of genetic mutations causing human diseases, focusing on the eA22 interaction. The mutant proteins exhibited either weakened or augmented interactions between coil 1a and coil 2. The ensuing biochemical results indicated that the interaction requires the separation of the coiled-coils in the N-terminal of coil 1a and the C-terminal of coil 2, coupled with the structural transition in the central α-helical rod domain. This study provides insight into the role of coil 1a as a molecular regulator in the elongation of IF proteins.

Indexed as

Amino Acid SequenceCell Line, TumorCircular DichroismFluorescent Antibody TechniqueGene ExpressionHumansIntermediate FilamentsLaminsLamin Type AMutationProtein BindingProtein ConformationProtein Conformation, alpha-HelicalProtein DomainsProtein MultimerizationRecombinant Proteinslamin C protein, humanLaminsLamin Type ARecombinant Proteinsassembly mechanismeA22 interactionEDMDfilament assemblyintermediate filamentlaminopathiesmolecular regulatornuclear lamin A/Cstructural transition

Identifiers

PMID33396475
PMCPMC7824274
OpenAlexW3115778781

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.