Evidence map›Paper›PMID 29350911›Full record

ArticleACS nano2018

A Programmable DNA Origami Platform for Organizing Intrinsically Disordered Nucleoporins within Nanopore Confinement.

Patrick D Ellis Fisher, Qi Shen, Bernice Akpinar, Luke K Davis, Kenny Kwok Hin Chung, David Baddeley, Anđela Šarić, Thomas J Melia, Bart W Hoogenboom, Chenxiang Lin and 1 more

Open access · greenAbstract read
In one paragraph

Article in ACS nano, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
5.3field-weighted citation impact, top 3% 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

49 citing papers in PubMed, 111 citations in OpenAlex.

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  19. The capsid lattice engages a bipartite NUP153 motif to mediate nuclear entry of HIV-1 cores.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

11 authors at 2 institutions in 2 countries.

Patrick D Ellis FisherDepartment of Cell Biology, Yale School of Medicine , New Haven, Connecticut 06520, United States.ORCID 0000-0002-4248-108X
Qi ShenDepartment of Cell Biology, Yale School of Medicine , New Haven, Connecticut 06520, United States.
Bernice AkpinarDepartment of Chemistry, Imperial College London , London SW7 2AZ, U.K.
Luke K DavisLondon Centre for Nanotechnology, University College London , 17-19 Gordon Street, London WC1H 0AH, U.K.
Kenny Kwok Hin ChungDepartment of Cell Biology, Yale School of Medicine , New Haven, Connecticut 06520, United States.
David BaddeleyDepartment of Cell Biology, Yale School of Medicine , New Haven, Connecticut 06520, United States.
Anđela Šarić
Thomas J MeliaDepartment of Cell Biology, Yale School of Medicine , New Haven, Connecticut 06520, United States.
Bart W HoogenboomLondon Centre for Nanotechnology, University College London , 17-19 Gordon Street, London WC1H 0AH, U.K.
Chenxiang LinDepartment of Cell Biology, Yale School of Medicine , New Haven, Connecticut 06520, United States.ORCID 0000-0001-7041-1946
C Patrick LuskDepartment of Cell Biology, Yale School of Medicine , New Haven, Connecticut 06520, United States.ORCID 0000-0003-4703-0533
Yale University · USLondon Centre for Nanotechnology · GB

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
The mechanism of ESCRT-mediated surveillance of the nuclear envelope barrierR01GM105672 · NIGMS · YALE UNIVERSITY · PI LUSK, CHARLES PATRICK · 2013 to 2025
$4.6M
Cell-free membrane remodeling guided by DNA nano-templatesDP2GM114830 · NIGMS · YALE UNIVERSITY · PI LIN, CHENXIANG · 2014 to 2014
$2.5M
Generating nuclear pore complex mimics with DNA origamiR21GM109466 · NIGMS · YALE UNIVERSITY · PI LIN, CHENXIANG, LUSK, CHARLES PATRICK · 2014 to 2015
$458k
NIGMS NIH HHS DP2 GM114830NIGMS NIH HHS R01 GM105672NIGMS NIH HHS R21 GM109466NIGMS NIH HHS T32 GM007223
6 · The paper itself

Abstract

Nuclear pore complexes (NPCs) form gateways that control molecular exchange between the nucleus and the cytoplasm. They impose a diffusion barrier to macromolecules and enable the selective transport of nuclear transport receptors with bound cargo. The underlying mechanisms that establish these permeability properties remain to be fully elucidated but require unstructured nuclear pore proteins rich in Phe-Gly (FG)-repeat domains of different types, such as FxFG and GLFG. While physical modeling and in vitro approaches have provided a framework for explaining how the FG network contributes to the barrier and transport properties of the NPC, it remains unknown whether the number and/or the spatial positioning of different FG-domains along a cylindrical, ∼40 nm diameter transport channel contributes to their collective properties and function. To begin to answer these questions, we have used DNA origami to build a cylinder that mimics the dimensions of the central transport channel and can house a specified number of FG-domains at specific positions with easily tunable design parameters, such as grafting density and topology. We find the overall morphology of the FG-domain assemblies to be dependent on their chemical composition, determined by the type and density of FG-repeat, and on their architectural confinement provided by the DNA cylinder, largely consistent with here presented molecular dynamics simulations based on a coarse-grained polymer model. In addition, high-speed atomic force microscopy reveals local and reversible FG-domain condensation that transiently occludes the lumen of the DNA central channel mimics, suggestive of how the NPC might establish its permeability properties.

Indexed as

AnimalsDiffusionDNAIntrinsically Disordered ProteinsMicroscopy, Atomic ForceMolecular Dynamics SimulationNanoporesNanotechnologyNuclear Pore Complex ProteinsPermeabilityProtein DomainsDNAIntrinsically Disordered ProteinsNuclear Pore Complex ProteinsDNA-directed self-assemblyDNA nanotechnologyDNA origamiintrinsically disordered proteinsnuclear pore complexnuclear transportnucleoporins

Identifiers

PMID29350911
PMCPMC5834394
OpenAlexW2782941528

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.