Evidence map›Paper›PMID 39062573›Full record

ReviewBiomolecules2024

Comprehensive Review on Bimolecular Fluorescence Complementation and Its Application in Deciphering Protein-Protein Interactions in Cell Signaling Pathways.

Houming Ren, Qingshan Ou, Qian Pu, Yuqi Lou, Xiaolin Yang, Yujiao Han, Shiping Liu

Abstract readReview
In one paragraph

Review in Biomolecules, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Deciphering Protein Interaction Dynamics Using the Yeast Three-Hybrid System.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  5. Review
  6. Review
  7. Review
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.

Houming RenState Key Laboratory of Resource Insects, Southwest University, Chongqing 400716, China.
Qingshan OuState Key Laboratory of Resource Insects, Southwest University, Chongqing 400716, China.
Qian PuState Key Laboratory of Resource Insects, Southwest University, Chongqing 400716, China.
Yuqi LouState Key Laboratory of Resource Insects, Southwest University, Chongqing 400716, China.
Xiaolin YangState Key Laboratory of Resource Insects, Southwest University, Chongqing 400716, China.
Yujiao HanState Key Laboratory of Resource Insects, Southwest University, Chongqing 400716, China.
Shiping LiuState Key Laboratory of Resource Insects, Southwest University, Chongqing 400716, China.ORCID 0000-0002-2917-0172

Funding

Chongqing Graduate Student Research Innovation Project CYB21132; CYB240144Chongqing Science and Technology Plan Project CSTB2022NSCQ-MSX0491Fundamental Research Funds for the Central Universities SWU-XJPY202309National Natural Science Foundation of China 32172797
6 · The paper itself

Abstract

Signaling pathways are responsible for transmitting information between cells and regulating cell growth, differentiation, and death. Proteins in cells form complexes by interacting with each other through specific structural domains, playing a crucial role in various biological functions and cell signaling pathways. Protein-protein interactions (PPIs) within cell signaling pathways are essential for signal transmission and regulation. The spatiotemporal features of PPIs in signaling pathways are crucial for comprehending the regulatory mechanisms of signal transduction. Bimolecular fluorescence complementation (BiFC) is one kind of imaging tool for the direct visualization of PPIs in living cells and has been widely utilized to uncover novel PPIs in various organisms. BiFC demonstrates significant potential for application in various areas of biological research, drug development, disease diagnosis and treatment, and other related fields. This review systematically summarizes and analyzes the technical advancement of BiFC and its utilization in elucidating PPIs within established cell signaling pathways, including TOR, PI3K/Akt, Wnt/β-catenin, NF-κB, and MAPK. Additionally, it explores the application of this technology in revealing PPIs within the plant hormone signaling pathways of ethylene, auxin, Gibberellin, and abscisic acid. Using BiFC in conjunction with CRISPR-Cas9, live-cell imaging, and ultra-high-resolution microscopy will enhance our comprehension of PPIs in cell signaling pathways.

Indexed as

Signal TransductionAnimalsFluorescenceHumansProtein Interaction Mappingbimolecular fluorescence complementation (BiFC)cell signaling pathwayprotein–protein interactions (PPIs)

Identifiers

PMID39062573
PMCPMC11274695

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.