Evidence map›Paper›PMID 39118325›Full record

ArticleBiophysical journal2024

FTIR study of light-induced proton transfer and Ca

Teppei Sugimoto, Kota Katayama, Hideki Kandori

Abstract read
In one paragraph

Article in Biophysical journal, 2024. 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
–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

3 citing papers in PubMed.

  1. Article
  2. Article
  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

3 authors.

Teppei SugimotoDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Nagoya, Japan.
Kota KatayamaDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Nagoya, Japan; OptoBioTechnology Research Center, Nagoya Institute of Technology, Nagoya, Japan.
Hideki KandoriDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Nagoya, Japan; OptoBioTechnology Research Center, Nagoya Institute of Technology, Nagoya, Japan. Electronic address: kandori@nitech.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proton transfer reactions play important functional roles in many proteins, such as enzymes and transporters, which is also the case in rhodopsins. In fact, functional expression of rhodopsins accompanies intramolecular proton transfer reactions in many cases. One of the exceptional cases can be seen in the protonated form of marine bacterial TAT rhodopsin, which isomerizes the retinal by light but returns to the original state within 10

Indexed as

CalciumLightMutationProtonsMutant ProteinsProtein BindingRhodopsinSchiff BasesSpectroscopy, Fourier Transform InfraredCalciumMutant ProteinsProtonsRhodopsinSchiff Bases

Identifiers

PMID39118325
PMCPMC11700351

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.