Evidence map›Paper›PMID 28374543›Full record

ArticleAngewandte Chemie (International ed. in English)2017

Activation pH and Gating Dynamics of Influenza A M2 Proton Channel Revealed by Single-Molecule Spectroscopy.

Chun-Wei Lin, Bruk Mensa, Marta Barniol-Xicota, William F DeGrado, Feng Gai

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
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  5. Review
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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.

Chun-Wei LinUltrafast Optical Processes Laboratory, Department of Chemistry, University of Pennsylvania, Philadelphia, 231 S. 34th Street, Philadelphia, PA, 19104, USA.
Bruk MensaDepartment of Pharmaceutical Chemistry, University of California San Francisco, 600 16th Street, San Francisco, CA, 94158-2517, USA.
Marta Barniol-XicotaDepartment of Pharmaceutical Chemistry, University of California San Francisco, 600 16th Street, San Francisco, CA, 94158-2517, USA.
William F DeGradoDepartment of Pharmaceutical Chemistry, University of California San Francisco, 600 16th Street, San Francisco, CA, 94158-2517, USA.
Feng GaiUltrafast Optical Processes Laboratory, Department of Chemistry, University of Pennsylvania, Philadelphia, 231 S. 34th Street, Philadelphia, PA, 19104, USA.

Funding

RESEARCH TRAINING IN CHEMISTRY AND CHEMICAL BIOLOGYT32GM064337 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CRAIK, CHARLES SCOTT · 2002 to 2021
$7.8M
ULTRAFAST OPTICAL PROCESSES LABORATORYP41GM104605 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GAI, FENG · 2012 to 2017
$5.6M
De novo design of alpha-helical bundlesR37GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2004 to 2013
$3.6M
DE NOVO DESIGN OF ALPHA HELICAL BUNDLESR01GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1996 to 2016
$2.4M
A Multiscale Model of Protein Mediated Changes in membrane MorphologyR01GM117593 · NIGMS · COLORADO STATE UNIVERSITY · PI ZHOU, YONGCHENG · 2015 to 2019
$1.8M
NIGMS NIH HHS P41 GM104605NIGMS NIH HHS R01 GM054616NIGMS NIH HHS R01 GM117593NIGMS NIH HHS R37 GM054616NIGMS NIH HHS T32 GM064337
6 · The paper itself

Abstract

Because of its importance in viral replication, the M2 proton channel of the influenza A virus has been the focus of many studies. Although we now know a great deal about the structural architecture underlying its proton conduction function, we know little about its conformational dynamics, especially those controlling the rate of this action. Herein, we employ a single-molecule fluorescence method to assess the dynamics of the inter-helical channel motion of both full-length M2 and the transmembrane domain of M2. The rate of this motion depends not only on the identity of the channel and membrane composition but also on the pH in a sigmoidal manner. For the full-length M2 channel, the rate is increased from approximately 190 μs

Indexed as

ThermodynamicsElectron TransportFluorescent DyesHydrogen-Ion ConcentrationPhotochemical ProcessesProtein ConformationSpectrometry, FluorescenceViral Matrix ProteinsViroporin ProteinsFluorescent DyesM2 protein, Influenza A virusViral Matrix ProteinsViroporin Proteinsconformational dynamicsfluorescence correlation spectroscopyM2 proton channelsphotoinduced electron transferpH titration

Identifiers

PMID28374543
PMCPMC5543805

What OpenQuestion holds

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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.