Evidence map›Paper›PMID 28241138›Full record

ArticleNature2017

The molecular architecture of lamins in somatic cells.

Yagmur Turgay, Matthias Eibauer, Anne E Goldman, Takeshi Shimi, Maayan Khayat, Kfir Ben-Harush, Anna Dubrovsky-Gaupp, K Tanuj Sapra, Robert D Goldman, Ohad Medalia

Open access · greenAbstract read
In one paragraph

Article in Nature, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 255 papers.

0numbers the graph read from it
0cells of the map it votes in
255citing papers in PubMed
21.9field-weighted citation impact, top 1% 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

255 citing papers in PubMed, 438 citations in OpenAlex.

  1. Review
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  10. Prelamin A in anArteriosclerosis, thrombosis, and vascular biology · 2026
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195 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

10 authors at 4 institutions in 3 countries.

Yagmur TurgayDepartment of Biochemistry, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.
Matthias EibauerDepartment of Biochemistry, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.
Anne E GoldmanDepartment of Cell and Molecular Biology, Northwestern University Feinberg School of Medicine, 303 E Chicago Avenue, Chicago, Illinois 60611, USA.
Takeshi ShimiDepartment of Cell and Molecular Biology, Northwestern University Feinberg School of Medicine, 303 E Chicago Avenue, Chicago, Illinois 60611, USA.
Maayan KhayatDepartment of Life Sciences and the National Institute for Biotechnology in the Negev, Ben-Gurion University, 84105 Beer-Sheva, Israel.
Kfir Ben-HarushDepartment of Chemical Engineering, Shamoon College of Engineering, Jabotinsky 84, 77245 Ashdod, Israel.
Anna Dubrovsky-GauppDepartment of Biochemistry, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.
K Tanuj SapraDepartment of Biochemistry, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.
Robert D GoldmanDepartment of Cell and Molecular Biology, Northwestern University Feinberg School of Medicine, 303 E Chicago Avenue, Chicago, Illinois 60611, USA.
Ohad MedaliaDepartment of Biochemistry, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.
University of Zurich · CHNorthwestern University · USBen-Gurion University of the Negev · ILSami Shamoon College of Engineering · IL

Funding

Super-resolution microscopy of nuclear lamin and spindle envelope/matrix functionR01GM106023 · NIGMS · CARNEGIE INSTITUTION OF WASHINGTON, D.C. · PI GOLDMAN, ROBERT D, ZHENG, YIXIAN · 2013 to 2020
$3.5M
NIGMS NIH HHS R01 GM106023
6 · The paper itself

Abstract

The nuclear lamina is a fundamental constituent of metazoan nuclei. It is composed mainly of lamins, which are intermediate filament proteins that assemble into a filamentous meshwork, bridging the nuclear envelope and chromatin. Besides providing structural stability to the nucleus, the lamina is involved in many nuclear activities, including chromatin organization, transcription and replication. However, the structural organization of the nuclear lamina is poorly understood. Here we use cryo-electron tomography to obtain a detailed view of the organization of the lamin meshwork within the lamina. Data analysis of individual lamin filaments resolves a globular-decorated fibre appearance and shows that A- and B-type lamins assemble into tetrameric filaments of 3.5 nm thickness. Thus, lamins exhibit a structure that is remarkably different from the other canonical cytoskeletal elements. Our findings define the architecture of the nuclear lamin meshworks at molecular resolution, providing insights into their role in scaffolding the nuclear lamina.

Indexed as

AnimalsChromatinCryoelectron MicroscopyCytoskeletonHumansIntermediate Filament ProteinsLaminsMiceNuclear LaminaTomographyChromatinIntermediate Filament ProteinsLamins

Identifiers

PMID28241138
PMCPMC5616216
OpenAlexW2593053801

What OpenQuestion holds

Textmetadata
LicenceTDM
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.