Evidence map›Paper›PMID 18573091›Full record

ReviewAnnual review of biophysics2008

Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells.

Tom K Kerppola

Abstract readReview
In one paragraph

Review in Annual review of biophysics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 355 papers.

0numbers the graph read from it
0cells of the map it votes in
355citing 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

355 citing papers in PubMed.

  1. Protein-Ratio Rheostats: Integrating Stoichiometry, Abundance, and Binding Affinity in Cellular Function.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
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  17. Targeting G3BP1 Condensate Topology Promotes Stress Granule Assembly via mAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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295 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

1 author.

Tom K KerppolaHoward Hughes Medical Institute and Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109-0650, USA. kerppola@umich.edu

Funding

Optimization of Bimolecular Fluorescence Complementation Probes for New Imaging FR01GM086213 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KERPPOLA, TOM KLAUS, REDDY, KAREN LYNN · 2008 to 2011
$2.8M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM086213
6 · The paper itself

Abstract

Protein interactions are a fundamental mechanism for the generation of biological regulatory specificity. The study of protein interactions in living cells is of particular significance because the interactions that occur in a particular cell depend on the full complement of proteins present in the cell and the external stimuli that influence the cell. Bimolecular fluorescence complementation (BiFC) analysis enables direct visualization of protein interactions in living cells. The BiFC assay is based on the association between two nonfluorescent fragments of a fluorescent protein when they are brought in proximity to each other by an interaction between proteins fused to the fragments. Numerous protein interactions have been visualized using the BiFC assay in many different cell types and organisms. The BiFC assay is technically straightforward and can be performed using standard molecular biology and cell culture reagents and a regular fluorescence microscope or flow cytometer.

Indexed as

Cell Physiological PhenomenaMolecular Probe TechniquesMicroscopy, FluorescenceProtein Interaction MappingProteomeSignal TransductionProteome

Identifiers

PMID18573091
PMCPMC2829326

What OpenQuestion holds

Textmetadata
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.