Evidence map›Paper›PMID 25772494›Full record

ReviewJournal of molecular biology2015

Bimolecular Fluorescence Complementation (BiFC) Analysis: Advances and Recent Applications for Genome-Wide Interaction Studies.

Kristi E Miller, Yeonsoo Kim, Won-Ki Huh, Hay-Oak Park

Abstract readReview
In one paragraph

Review in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.

0numbers the graph read from it
0cells of the map it votes in
134citing papers in PubMed
26.5field-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

134 citing papers in PubMed, 251 citations in OpenAlex.

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  12. A Prion-Like Domain in EBV EBNA1 Promotes Phase Separation and Enables SRRM1 Splicing.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  13. Review
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74 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

4 authors at 2 institutions in 2 countries.

Kristi E Miller *Molecular Cellular Developmental Biology Program, Ohio State University, OH, USA.
Yeonsoo Kim *Department of Biological Sciences, Seoul National University, Seoul 151-747, Korea.
Won-Ki HuhDepartment of Biological Sciences, Seoul National University, Seoul 151-747, Korea.
Hay-Oak ParkMolecular Cellular Developmental Biology Program, Ohio State University, OH, USA.
Seoul National University · KRThe Ohio State University · US

Funding

Spatial and temporal regulation of polarity establishment in budding yeastR01GM114582 · NIGMS · OHIO STATE UNIVERSITY · PI PARK, HAY-OAK · 2015 to 2018
$1.4M
Regulation of polarized cell growth by GTPasesR01GM076375 · NIGMS · OHIO STATE UNIVERSITY · PI PARK, HAY-OAK · 2006 to 2009
$1.3M
NIGMS NIH HHS R01 GM076375NIGMS NIH HHS R01 GM114582NIGMS NIH HHS R01 GM76375
6 · The paper itself

Abstract

Complex protein networks are involved in nearly all cellular processes. To uncover these vast networks of protein interactions, various high-throughput screening technologies have been developed. Over the last decade, bimolecular fluorescence complementation (BiFC) assay has been widely used to detect protein-protein interactions (PPIs) in living cells. This technique is based on the reconstitution of a fluorescent protein in vivo. Easy quantification of the BiFC signals allows effective cell-based high-throughput screenings for protein binding partners and drugs that modulate PPIs. Recently, with the development of large screening libraries, BiFC has been effectively applied for genome-wide PPI studies and has uncovered novel protein interactions, providing new insight into protein functions. In this review, we describe the development of reagents and methods used for BiFC-based screens in yeast, plants, and mammalian cells. We also discuss the advantages and drawbacks of these methods and highlight the application of BiFC in large-scale studies.

Indexed as

Molecular Probe TechniquesAnimalsArabidopsis ProteinsFluorescent DyesGenome-Wide Association StudyGreen Fluorescent ProteinsHigh-Throughput Screening AssaysHumansMammalsProtein Interaction MappingProteomicsTelomereYeastsArabidopsis ProteinsCyan Fluorescent ProteinFluorescent DyesGreen Fluorescent Proteinsbimolecular fluorescence complementation (BiFC) analysisfluorescent proteinsgenomicsproteomics

Identifiers

PMID25772494
PMCPMC4417415
OpenAlexW2058687710

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.