Evidence map›Paper›PMID 24927568›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Probing nuclear pore complex architecture with proximity-dependent biotinylation.

Dae In Kim, K C Birendra, Wenhong Zhu, Khatereh Motamedchaboki, Valérie Doye, Kyle J Roux

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 348 papers.

0numbers the graph read from it
0cells of the map it votes in
348citing papers in PubMed
13.5field-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

348 citing papers in PubMed, 585 citations in OpenAlex.

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288 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

6 authors at 4 institutions in 2 countries.

Dae In KimSanford Children's Health Research Center, Sanford Research, Sioux Falls, SD 57104;
K C BirendraSanford Children's Health Research Center, Sanford Research, Sioux Falls, SD 57104;
Wenhong ZhuSanford-Burnham Proteomics Facility, Sanford-Burnham Medical Research Institute, La Jolla, CA 92037;
Khatereh MotamedchabokiSanford-Burnham Proteomics Facility, Sanford-Burnham Medical Research Institute, La Jolla, CA 92037;
Valérie DoyeInstitut Jacques Monod, Unité Mixte de Recherche 7592, Centre National de la Recherche Scientifique, Université Paris Diderot, Sorbonne Paris Cité, F-75205 Paris, France; and.
Kyle J RouxSanford Children's Health Research Center, Sanford Research, Sioux Falls, SD 57104;Department of Pediatrics, Sanford School of Medicine, University of South Dakota, Sioux Falls, SD 57105 kyle.roux@sanfordhealth.org.
Sanford Burnham Prebys Medical Discovery Institute · USSanford Research · USSorbonne Paris Cité · FRUniversity of South Dakota · US

Funding

Yeast 2 HybridP20GM103620 · NIGMS · SANFORD RESEARCH/USD · PI ROUX, KYLE J · 2013 to 2023
$24.2M
The Impact of PD-1 Inhibition on Immune-Response to ChemoradiotherapyP20GM103548 · NIGMS · SANFORD RESEARCH/USD · PI MISKIMINS, W KEITH · 2012 to 2020
$20.8M
SUBSTRATE RIGIDITY AND GENE EXPRESSION: Role of Nuclear TensionR01EB014869 · NIBIB · UNIVERSITY OF FLORIDA · PI LELE, TANMAY P. · 2012 to 2019
$3.4M
Developing methods for proximity-dependent protein labelingR01GM102203 · NIGMS · SANFORD RESEARCH/USD · PI ROUX, KYLE J · 2013 to 2017
$1.5M
Cytoskeletal force generation on the nucleusR01GM102486 · NIGMS · UNIVERSITY OF FLORIDA · PI LELE, TANMAY P. · 2012 to 2015
$1.2M
NIBIB NIH HHS R01 EB014869NIBIB NIH HHS R01EB014869NIGMS NIH HHS P20 GM103548NIGMS NIH HHS P20GM103548NIGMS NIH HHS P20 GM103620NIGMS NIH HHS P20GM103620NIGMS NIH HHS R01 GM102203NIGMS NIH HHS R01GM102203NIGMS NIH HHS R01 GM102486NIGMS NIH HHS R01GM102486
6 · The paper itself

Abstract

Proximity-dependent biotin identification (BioID) is a method for identifying protein associations that occur in vivo. By fusing a promiscuous biotin ligase to a protein of interest expressed in living cells, BioID permits the labeling of proximate proteins during a defined labeling period. In this study we used BioID to study the human nuclear pore complex (NPC), one of the largest macromolecular assemblies in eukaryotes. Anchored within the nuclear envelope, NPCs mediate the nucleocytoplasmic trafficking of numerous cellular components. We applied BioID to constituents of the Nup107-160 complex and the Nup93 complex, two conserved NPC subcomplexes. A strikingly different set of NPC constituents was detected depending on the position of these BioID-fusion proteins within the NPC. By applying BioID to several constituents located throughout the extremely stable Nup107-160 subcomplex, we refined our understanding of this highly conserved subcomplex, in part by demonstrating a direct interaction of Nup43 with Nup85. Furthermore, by using the extremely stable Nup107-160 structure as a molecular ruler, we defined the practical labeling radius of BioID. These studies further our understanding of human NPC organization and demonstrate that BioID is a valuable tool for exploring the constituency and organization of large protein assemblies in living cells.

Indexed as

BiotinylationAlgorithmsBiotinCarbon-Nitrogen LigasesCell NucleusChromatography, LiquidCytoplasmGreen Fluorescent ProteinsHEK293 CellsHumansLigasesMembrane GlycoproteinsNuclear EnvelopeNuclear PoreNuclear Pore Complex ProteinsProtein BindingBiotinCarbon-Nitrogen LigasesGreen Fluorescent ProteinsLigasesMembrane GlycoproteinsNuclear Pore Complex Proteinsnuclear pore protein p62Nup93 protein, humanStreptavidin

Identifiers

PMID24927568
PMCPMC4066523
OpenAlexW2035671523

What OpenQuestion holds

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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.