Evidence map›Paper›PMID 29923827›Full record

ArticleeLife2018

Visualizing conformational dynamics of proteins in solution and at the cell membrane.

Sharona E Gordon, Mika Munari, William N Zagotta

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

32 citing papers in PubMed, 68 citations in OpenAlex.

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  9. Long-distance tmFRET using bipyridyl- and phenanthroline-based ligands.bioRxiv : the preprint server for biology · 2024
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Sharona E GordonDepartment of Physiology and Biophysics, University of Washington, Seattle, United States.ORCID 0000-0002-0914-3361
Mika MunariDepartment of Physiology and Biophysics, University of Washington, Seattle, United States.ORCID 0000-0003-3598-6116
William N ZagottaDepartment of Physiology and Biophysics, University of Washington, Seattle, United States.ORCID 0000-0002-7631-8168
University of Washington · US

Funding

Vector and Transgenic Mouse CoreP30DK017047 · NIDDK · UNIVERSITY OF WASHINGTON · PI Karin E Bornfeldt · 1986 to 2026
$41.4M
Vision Research CoreP30EY001730 · NEI · UNIVERSITY OF WASHINGTON · PI JAMES Bryant HURLEY · 1985 to 2026
$23.5M
GATING MECHANISMS OF RETINAL ROD CGMP-ACTIVATED CHANNELSR01EY010329 · NEI · UNIVERSITY OF WASHINGTON · PI ZAGOTTA, WILLIAM N · 1994 to 2023
$7.7M
Inflammatory hyperalgesia mediated by TRPV1, the pepper spray receptor in the corR01EY017564 · NEI · UNIVERSITY OF WASHINGTON · PI GORDON, SHARONA E · 2006 to 2022
$6.5M
Regulation of KCNH ion channelsR01MH102378 · NIMH · UNIVERSITY OF WASHINGTON · PI ZAGOTTA, WILLIAM N · 2014 to 2018
$1.9M
Supplement to Multimodal Gating Mechanisms of TRPV1 Ion ChannelsR01GM125351 · NIGMS · UNIVERSITY OF WASHINGTON · PI GORDON, SHARONA E · 2018 to 2021
$1.8M
Mechanisms of TRPV1 Channel RegulationR01GM100718 · NIGMS · UNIVERSITY OF WASHINGTON · PI GORDON, SHARONA E, ZAGOTTA, WILLIAM N · 2012 to 2015
$1.5M
Electrophysiology-Optical Workstation for Ion Channel BiophysicsS10RR025429 · NCRR · UNIVERSITY OF WASHINGTON · PI GORDON, SHARONA E · 2009 to 2009
$499k
NCRR NIH HHS S10 RR025429NEI NIH HHS P30 EY001730NEI NIH HHS P30EY001730NEI NIH HHS R01 EY010329NEI NIH HHS R01EY010329NEI NIH HHS R01 EY017564NEI NIH HHS R01EY017564NIDDK NIH HHS P30 DK017047NIDDK NIH HHS P30DK017047NIGMS NIH HHS R01 GM100718NIGMS NIH HHS R01GM100718NIGMS NIH HHS R01 GM125351NIGMS NIH HHS R01GM125351NIH HHS S10RR025429NIMH NIH HHS R01 MH102378NIMH NIH HHS R01MH102378
6 · The paper itself

Abstract

Conformational dynamics underlie enzyme function, yet are generally inaccessible via traditional structural approaches. FRET has the potential to measure conformational dynamics in vitro and in intact cells, but technical barriers have thus far limited its accuracy, particularly in membrane proteins. Here, we combine amber codon suppression to introduce a donor fluorescent noncanonical amino acid with a new, biocompatible approach for labeling proteins with acceptor transition metals in a method called ACCuRET (Anap Cyclen-Cu

Indexed as

Amino AcidsBinding SitesCations, DivalentCell MembraneCodon, TerminatorCoordination ComplexesCopperCyclamsFluorescence Resonance Energy TransferFluorescent DyesHEK293 CellsHeterocyclic CompoundsHumansMaltoseMaltose-Binding ProteinsMembrane ProteinsAmino AcidsCations, DivalentCodon, TerminatorCoordination ComplexesCopperCyclamscyclenFluorescent DyesHeterocyclic CompoundsMaltoseMaltose-Binding ProteinsMembrane ProteinsRecombinant Proteinsbiochemistrychemical biologyFRETMBPmembrane proteinmolecular biophysicsnoncanonical amino acidnoneprotein dynamicsstructural biologytransition metal

Identifiers

PMID29923827
PMCPMC6056233
OpenAlexW2949192428

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.