Evidence map›Paper›PMID 26912792›Full record

ArticleMolecular biology of the cell2016

An improved smaller biotin ligase for BioID proximity labeling.

Dae In Kim, Samuel C Jensen, Kyle A Noble, Birendra Kc, Kenneth H Roux, Khatereh Motamedchaboki, Kyle J Roux

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 527 papers.

0numbers the graph read from it
0cells of the map it votes in
527citing papers in PubMed
–field-weighted citation impact
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

527 citing papers in PubMed.

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  17. Mass spectrometry proteomics for studying mitostasis.Protein science : a publication of the Protein Society · 2026
    Review
  18. Article
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467 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

7 authors.

Dae In KimSanford Children's Health Research Center, Sanford Research, Sioux Falls, SD 57104.
Samuel C JensenSanford Children's Health Research Center, Sanford Research, Sioux Falls, SD 57104.
Kyle A NobleDepartment of Biological Science, Florida State University, Tallahassee, FL 32306.
Birendra KcSanford Children's Health Research Center, Sanford Research, Sioux Falls, SD 57104.
Kenneth H RouxDepartment of Biological Science, Florida State University, Tallahassee, FL 32306.
Khatereh MotamedchabokiSanford-Burnham Proteomics Facility, Sanford-Burnham Medical Research Institute, La Jolla, CA 92037.
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.

Funding

Tumor Microenvironment and Cancer ImmunologyP30CA030199 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI Michael Jackson · 1985 to 2026
$107.2M
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
NCI NIH HHS P30 CA030199NIBIB NIH HHS R01 EB014869NIBIB NIH HHS R01EB014869NIGMS NIH HHS P20 GM103548NIGMS 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

The BioID method uses a promiscuous biotin ligase to detect protein-protein associations as well as proximate proteins in living cells. Here we report improvements to the BioID method centered on BioID2, a substantially smaller promiscuous biotin ligase. BioID2 enables more-selective targeting of fusion proteins, requires less biotin supplementation, and exhibits enhanced labeling of proximate proteins. Thus BioID2 improves the efficiency of screening for protein-protein associations. We also demonstrate that the biotinylation range of BioID2 can be considerably modulated using flexible linkers, thus enabling application-specific adjustment of the biotin-labeling radius.

Indexed as

AnimalsBiotinBiotinylationCarbon-Nitrogen LigasesEscherichia coli ProteinsHumansIntracellular Signaling Peptides and ProteinsMembrane ProteinsMiceMolecular BiologyNIH 3T3 CellsNuclear Pore Complex ProteinsNuclear ProteinsProtein EngineeringProtein Interaction MappingRecombinant Fusion ProteinsBiotinbirA protein, E coliCarbon-Nitrogen LigasesEscherichia coli ProteinsIntracellular Signaling Peptides and ProteinsMembrane ProteinsNuclear Pore Complex ProteinsNuclear ProteinsNUP107 protein, humanNUP160 protein, humanRecombinant Fusion ProteinsRepressor ProteinsSUN2 protein, human

Identifiers

PMID26912792
PMCPMC4831873

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LicenceCC BY-NC-SA
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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.