Evidence map›Paper›PMID 27857596›Full record

ReviewBiophysics (Nagoya-shi, Japan)2011

Light-induced structural changes of the LOV2 domains in various phototropins revealed by FTIR spectroscopy.

Tatsuya Iwata, Satoru Tokutomi, Hideki Kandori

Open access · diamondAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Biophysics (Nagoya-shi, Japan), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 27% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. 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

3 authors at 2 institutions in 1 country.

Tatsuya IwataCenter for Fostering Young and Innovative Researchers, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan; Department of Frontier Materials, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan.
Satoru TokutomiGraduate School of Science, Osaka Prefecture University, Sakai, Osaka 599-8531, Japan.
Hideki KandoriDepartment of Frontier Materials, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan.
Nagoya Institute of Technology · JPOsaka Prefecture University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phototropin (Phot), a blue-light photoreceptor in plants, consists of two FMN-binding domains (named LOV1 and LOV2) and a serine/threonine (Ser/Thr) kinase domain. We have investigated light-induced structural changes of LOV domains, which lead to the activation of the kinase domain, by means of light-induced difference FTIR spectroscopy. FTIR spectroscopy revealed that the reactive cysteine is protonated in both unphotolyzed and triplet-excited states, which is difficult to detect by other methods such as X-ray crystallography. In this review, we describe the light-induced structural changes of hydrogen-bonding environment of FMN chromophore and protein backbone in

Indexed as

blue-light photoreceptorFMNFTIR spectroscopyLOV domainphototropin

Identifiers

PMID27857596
PMCPMC5036776
OpenAlexW2029968595

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.