Evidence map›Paper›PMID 35813206›Full record

ArticleFrontiers in cell and developmental biology2022

Tunable Cellular Localization and Extensive Cytoskeleton-Interplay of Reflectins.

Junyi Song, Chuanyang Liu, Baoshan Li, Liangcheng Liu, Ling Zeng, Zonghuang Ye, Ting Mao, Wenjian Wu, Biru Hu

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Frontiers in cell and developmental biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. 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

9 authors at 1 institution in 1 country.

Junyi SongCollege of Liberal Arts Science, National University of Defense Technology, Changsha, China.
Chuanyang LiuCollege of Liberal Arts Science, National University of Defense Technology, Changsha, China.
Baoshan LiCollege of Liberal Arts Science, National University of Defense Technology, Changsha, China.
Liangcheng LiuCollege of Liberal Arts Science, National University of Defense Technology, Changsha, China.
Ling ZengCollege of Liberal Arts Science, National University of Defense Technology, Changsha, China.
Zonghuang YeCollege of Liberal Arts Science, National University of Defense Technology, Changsha, China.
Ting MaoLogistics Center, National University of Defense Technology, Changsha, China.
Wenjian WuCollege of Liberal Arts Science, National University of Defense Technology, Changsha, China.
Biru HuCollege of Liberal Arts Science, National University of Defense Technology, Changsha, China.
National University of Defense Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reflectin proteins are natural copolymers consisting of repeated canonical domains. They are located in a biophotonic system called Bragg lamellae and manipulate the dynamic structural coloration of iridocytes. Their biological functions are intriguing, but the underlying mechanism is not fully understood. Reflectin A1, A2, B1, and C were found to present distinguished cyto-/nucleoplasmic localization preferences in the work. Comparable intracellular localization was reproduced by truncated reflectin variants, suggesting a conceivable evolutionary order among reflectin proteins. The size-dependent access of reflectin variants into the nucleus demonstrated a potential model of how reflectins get into Bragg lamellae. Moreover, RfA1 was found to extensively interact with the cytoskeleton, including its binding to actin and enrichment at the microtubule organizing center. This implied that the cytoskeleton system plays a fundamental role during the organization and transportation of reflectin proteins. The findings presented here provide evidence to get an in-depth insight into the evolutionary processes and working mechanisms of reflectins, as well as novel molecular tools to achieve tunable intracellular transportation.

Indexed as

cytoskeleton interactionintracellular localizationmolecular evolutionreflectinstruncated peptides

Identifiers

PMID35813206
PMCPMC9259870
OpenAlexW4283317974

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.