Evidence map›Paper›PMID 30274285›Full record

ArticleInternational journal of molecular sciences2018

Visualization of Tau⁻Tubulin Interaction in a Living Cell Using Bifluorescence Complementation Technique.

Seulgi Shin, Sungsu Lim, Hyeanjeong Jeong, Li Ting Kwan, Yun Kyung Kim

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Dynamic interactions and CaNature communications · 2021
    Article
  2. Review
  3. Article
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

5 authors at 3 institutions in 2 countries.

Seulgi ShinKorea Institute of Science and Technology (KIST), Brain Science Institute, Convergence Research Center for Diagnosis, Treatment and Care System of Dementia, Seoul 02792, Korea. seulgishin@kist.re.kr.
Sungsu LimKorea Institute of Science and Technology (KIST), Brain Science Institute, Convergence Research Center for Diagnosis, Treatment and Care System of Dementia, Seoul 02792, Korea. sungsulim@kist.re.kr.
Hyeanjeong JeongKorea Institute of Science and Technology (KIST), Brain Science Institute, Convergence Research Center for Diagnosis, Treatment and Care System of Dementia, Seoul 02792, Korea. guswjd7979@kist.re.kr.
Li Ting KwanKorea Institute of Science and Technology (KIST), Brain Science Institute, Convergence Research Center for Diagnosis, Treatment and Care System of Dementia, Seoul 02792, Korea. lkwan@wellesley.edu.
Yun Kyung KimKorea Institute of Science and Technology (KIST), Brain Science Institute, Convergence Research Center for Diagnosis, Treatment and Care System of Dementia, Seoul 02792, Korea. yunkyungkim@kist.re.kr.ORCID 0000-0002-8682-120X
Convergence Research Center for Diagnosis Treatment and Care System of Dementia · KRKorea University · KRWellesley College · US

Funding

Korea Institute Science and Technology Institutional Program 2V06480National Research Council of Science and Technology CRC-15-04-KISTNational Research Foundation of Korea 2016M3C7A1913844National Research Foundation of Korea 2017R1A6A3A04012384
6 · The paper itself

Abstract

Tau is a neuron-specific microtubule-binding protein that stabilizes microtubules. It is generally thought that highly phosphorylated tau dissociates from microtubules and becomes insoluble aggregates, leading to neuronal degeneration. Due to the implication of tau aggregation in neurodegenerative disorders, including Alzheimer's disease, great efforts have been made to identify the tau aggregation process. However, tau interaction with tubulin during the aggregation process remains largely unknown. To scrutinize the tau-tubulin interaction, we generated a cell model that enables visualization of the tau-tubulin interaction in a living cell using the Bifluorescence Complementation (BiFC) Technique. Upon diverse chemical stimulation that induced tau pathology, tau-tubulin BiFC cells showed significantly increased levels of BiFC fluorescence, indicating that tau aggregates together with tubulin. Our results suggest that tubulin should be considered as a key component in the tau aggregation process.

Indexed as

HEK293 CellsHumansMicrotubulesNeurodegenerative Diseasestau ProteinsTubulintau ProteinsTubulinBifluorescence Complementationmicrotubuleneurodegenerationtau aggregationtubulin

Identifiers

PMID30274285
PMCPMC6213793
OpenAlexW2893465320

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.