Evidence map›Paper›PMID 37873407›Full record

ArticlebioRxiv : the preprint server for biology2024

Long-distance tmFRET using bipyridyl- and phenanthroline-based ligands.

Sharona E Gordon, Eric G B Evans, Shauna C Otto, Maxx H Tessmer, Kyle D Shaffer, Moshe T Gordon, E James Petersson, Stefan Stoll, William N Zagotta

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2024. 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
–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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Sharona E GordonDepartment of Physiology and Biophysics, University of Washington, Seattle, Washington 98195.
Eric G B EvansDepartment of Physiology and Biophysics, University of Washington, Seattle, Washington 98195.
Shauna C OttoDepartment of Physiology and Biophysics, University of Washington, Seattle, Washington 98195.
Maxx H TessmerDepartment of Chemistry, University of Washington, Seattle, Washington 98195.
Kyle D ShafferDepartment of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, PA 19104.
Moshe T GordonDepartment of Physiology and Biophysics, University of Washington, Seattle, Washington 98195.
E James PeterssonDepartment of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, PA 19104.
Stefan StollDepartment of Chemistry, University of Washington, Seattle, Washington 98195.
William N ZagottaDepartment of Physiology and Biophysics, University of Washington, Seattle, Washington 98195.ORCID 0000-0002-7631-8168
University of Washington · USUniversity of Pennsylvania · US

Funding

VISUAL SCIENCES TRAINING PROGRAMT32EY007031 · NEI · UNIVERSITY OF WASHINGTON · PI Wyeth Daniel Bair, Anitha Pasupathy · 1985 to 2026
$6.1M
Conformational Energetics and Heterogeneity to Reveal Gating Mechanisms of TRPV and TRPM Ion ChannelsR35GM145225 · NIGMS · UNIVERSITY OF WASHINGTON · PI Sharona E Gordon · 2022 to 2026
$3.4M
Structural energetics of voltage- and ligand-dependent gating in ion channelsR35GM148137 · NIGMS · UNIVERSITY OF WASHINGTON · PI William N Zagotta · 2023 to 2026
$2.0M
Equipment Supplement: Analysis tools for quantifying protein conformational landscapes using DEER spectroscopyR01GM125753 · NIGMS · UNIVERSITY OF WASHINGTON · PI STOLL, STEFAN · 2019 to 2022
$1.3M
Functional and structural dynamics of KCNH4 and KCNH8R03TR004135 · NCATS · UNIVERSITY OF WASHINGTON · PI ZAGOTTA, WILLIAM N · 2022 to 2022
$156k
NCATS NIH HHS R03 TR004135NEI NIH HHS T32 EY007031NIGMS NIH HHS R01 GM125753NIGMS NIH HHS R35 GM145225NIGMS NIH HHS R35 GM148137
6 · The paper itself

Abstract

With the great progress on determining protein structures over the last decade comes a renewed appreciation that structures must be combined with dynamics and energetics to understand function. Fluorescence spectroscopy, specifically Förster resonance energy transfer (FRET), provides a great window into dynamics and energetics due to its application at physiological temperatures and ability to measure dynamics on the ångström scale. We have recently advanced transition metal FRET (tmFRET) to study allosteric regulation of maltose binding protein and have reported measurements of maltose-dependent distance changes with an accuracy of ~1.5 Å. When paired with the noncanonical amino acid Acd as a donor, our previous tmFRET acceptors were useful over a working distance of 10 Å to 20 Å. Here, we use cysteine-reactive bipyridyl and phenanthroline compounds as chelators for Fe

Identifiers

PMID37873407
PMCPMC10592757
OpenAlexW4387568424

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.