Evidence map›Paper›PMID 30413716›Full record

ArticleNature communications2018

Harnessing photoinduced electron transfer to optically determine protein sub-nanoscale atomic distances.

Antonios Pantazis, Karin Westerberg, Thorsten Althoff, Jeff Abramson, Riccardo Olcese

Abstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. A Historical Outline of Fluorescence Spectroscopy in Ion Channel Research.Advances in experimental medicine and biology · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
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  12. Article
  13. Review
  14. Review
  15. 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.

Antonios PantazisDivision of Molecular Medicine, Department of Anesthesiology & Perioperative Medicine, UCLA, Los Angeles, CA, 90095, USA. antonios.pantazis@liu.se.
Karin WesterbergAmgen, Thousand Oaks, CA, 91320, USA.
Thorsten AlthoffDepartment of Physiology, UCLA, Los Angeles, CA, 90095, USA.
Jeff AbramsonDepartment of Physiology, UCLA, Los Angeles, CA, 90095, USA.
Riccardo OlceseDivision of Molecular Medicine, Department of Anesthesiology & Perioperative Medicine, UCLA, Los Angeles, CA, 90095, USA. rolcese@ucla.edu.

Funding

Structures of sodium glucose transporters by cryo electron microscopyR01GM078844 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI ABRAMSON, JEFFREY S · 2006 to 2018
$5.3M
Structure/Function Studies on the Ca2+: Cation Antiporter family of transportersR21HL093278 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI ABRAMSON, JEFFREY S · 2009 to 2010
$424k
DRVCF, a new optical method for real-time, high resolution, intramolecular distance measurements in conducting ion channelsR21NS101734 · NINDS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI OLCESE, RICCARDO · 2017 to 2018
$399k
NHLBI NIH HHS R21 HL093278NIGMS NIH HHS R01 GM078844NINDS NIH HHS R21 NS101734
6 · The paper itself

Abstract

Proteins possess a complex and dynamic structure, which is influenced by external signals and may change as they perform their biological functions. We present an optical approach, distance-encoding photoinduced electron transfer (DEPET), capable of the simultaneous study of protein structure and function. An alternative to FRET-based methods, DEPET is based on the quenching of small conjugated fluorophores by photoinduced electron transfer: a reaction that requires contact of the excited fluorophore with a suitable electron donor. This property allows DEPET to exhibit exceptional spatial and temporal resolution capabilities in the range pertinent to protein conformational change. We report the first implementation of DEPET on human large-conductance K

Indexed as

ElectronsLightAnimalsAplysiaFluorescent DyesHumansIon Channel GatingLarge-Conductance Calcium-Activated Potassium ChannelsMembrane PotentialsOptics and PhotonicsPeptidesProteinsRhodaminesTryptophanFluorescent DyesLarge-Conductance Calcium-Activated Potassium ChannelsPeptidesProteinsRhodaminesTryptophan

Identifiers

PMID30413716
PMCPMC6226468

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.