Evidence map›Paper›PMID 28835537›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

XFEL structures of the influenza M2 proton channel: Room temperature water networks and insights into proton conduction.

Jessica L Thomaston, Rahel A Woldeyes, Takanori Nakane, Ayumi Yamashita, Tomoyuki Tanaka, Kotaro Koiwai, Aaron S Brewster, Benjamin A Barad, Yujie Chen, Thomas Lemmin and 16 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Solid-State NMR of Virus Membrane Proteins.Accounts of chemical research · 2025
    Article
  6. The Role of Cholesterol in M2 Clustering and Viral Budding Explained.Journal of chemical theory and computation · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Antiviral Approaches against Influenza Virus.Clinical microbiology reviews · 2023
    Review
  11. Article
  12. Article
  13. Serial femtosecond crystallography.Nature reviews. Methods primers · 2022
    Article
  14. Article
  15. Spiers Memorial Lecture: Analysis andFaraday discussions · 2021
    Article
  16. Article
  17. Article
  18. Pore-Bound Water at the Key Residue Histidine 37 in Influenza A M2.Angewandte Chemie (International ed. in English) · 2021
    Article
  19. Article
  20. Review
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

26 authors.

Jessica L ThomastonDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA 94158.
Rahel A WoldeyesDepartment of Bioengineering and Therapeutic Sciences, University of California, San Francisco, CA 94158.ORCID 0000-0003-0737-8383
Takanori NakaneDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo 113-0033, Japan.ORCID 0000-0003-2697-2767
Ayumi YamashitaSPring-8 Angstrom Compact Free Electron Laser (SACLA) Science Research Group, RIKEN SPring-8 Center, Saitama 351-0198, Japan.
Tomoyuki TanakaSPring-8 Angstrom Compact Free Electron Laser (SACLA) Science Research Group, RIKEN SPring-8 Center, Saitama 351-0198, Japan.
Kotaro KoiwaiStructural Biology Research Center, High Energy Accelerator Research Organization (KEK), Ibaraki 305-0801, Japan.
Aaron S BrewsterMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.
Benjamin A BaradDepartment of Bioengineering and Therapeutic Sciences, University of California, San Francisco, CA 94158.
Yujie ChenSchool of Applied and Engineering Physics, Cornell University, Ithaca, NY 14853.
Thomas LemminDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA 94158.
Monarin UervirojnangkoornDepartment of Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305.
Toshi ArimaSPring-8 Angstrom Compact Free Electron Laser (SACLA) Science Research Group, RIKEN SPring-8 Center, Saitama 351-0198, Japan.
Jun KobayashiSPring-8 Angstrom Compact Free Electron Laser (SACLA) Science Research Group, RIKEN SPring-8 Center, Saitama 351-0198, Japan.
Tetsuya MasudaSPring-8 Angstrom Compact Free Electron Laser (SACLA) Science Research Group, RIKEN SPring-8 Center, Saitama 351-0198, Japan.
Mamoru SuzukiSPring-8 Angstrom Compact Free Electron Laser (SACLA) Science Research Group, RIKEN SPring-8 Center, Saitama 351-0198, Japan.
Michihiro SugaharaSPring-8 Angstrom Compact Free Electron Laser (SACLA) Science Research Group, RIKEN SPring-8 Center, Saitama 351-0198, Japan.
Nicholas K SauterMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.
Rie TanakaSPring-8 Angstrom Compact Free Electron Laser (SACLA) Science Research Group, RIKEN SPring-8 Center, Saitama 351-0198, Japan.
Osamu NurekiDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo 113-0033, Japan.
Kensuke TonoExperimental Instrumentation Team, Japan Synchrotron Radiation Research Institute, Hyogo 679-5198, Japan.
Yasumasa JotiExperimental Instrumentation Team, Japan Synchrotron Radiation Research Institute, Hyogo 679-5198, Japan.
Eriko NangoSPring-8 Angstrom Compact Free Electron Laser (SACLA) Science Research Group, RIKEN SPring-8 Center, Saitama 351-0198, Japan.
So IwataSPring-8 Angstrom Compact Free Electron Laser (SACLA) Science Research Group, RIKEN SPring-8 Center, Saitama 351-0198, Japan.
Fumiaki YumotoStructural Biology Research Center, High Energy Accelerator Research Organization (KEK), Ibaraki 305-0801, Japan.
James S FraserDepartment of Bioengineering and Therapeutic Sciences, University of California, San Francisco, CA 94158.ORCID 0000-0002-5080-2859
William F DeGradoDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA 94158; william.degrado@ucsf.edu.

Funding

STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008284 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KORTEMME, TANJA · 1988 to 2022
$10.1M
RESEARCH TRAINING IN CHEMISTRY AND CHEMICAL BIOLOGYT32GM064337 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CRAIK, CHARLES SCOTT · 2002 to 2021
$7.8M
Deciphering the relationship between structure, dynamics and function in helical bundle proteinsR35GM122603 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WILLIAM DEGRADO · 2017 to 2026
$7.1M
DIALS: New Computational Methods to Enable Challenging Crystallographic ExperimentsR01GM117126 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI SAUTER, NICHOLAS K · 2016 to 2023
$6.1M
The Impact of Mutation on the Conformations and Recognition of UbiquitinDP5OD009180 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FRASER, JAMES SOLOMON · 2011 to 2015
$1.8M
A Multiscale Model of Protein Mediated Changes in membrane MorphologyR01GM117593 · NIGMS · COLORADO STATE UNIVERSITY · PI ZHOU, YONGCHENG · 2015 to 2019
$1.8M
Model Comparison in Structural BiologyR21GM110580 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FRASER, JAMES SOLOMON · 2014 to 2015
$419k
Anachem Lipidic Cubic Phase Crystallization RobotS10RR027234 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 2010 to 2010
$175k
Howard Hughes Medical InstituteNCRR NIH HHS S10 RR027234NIGMS NIH HHS R01 GM117126NIGMS NIH HHS R01 GM117593NIGMS NIH HHS R21 GM110580NIGMS NIH HHS R35 GM122603NIGMS NIH HHS T32 GM008284NIGMS NIH HHS T32 GM064337NIH HHS DP5 OD009180
6 · The paper itself

Abstract

The M2 proton channel of influenza A is a drug target that is essential for the reproduction of the flu virus. It is also a model system for the study of selective, unidirectional proton transport across a membrane. Ordered water molecules arranged in "wires" inside the channel pore have been proposed to play a role in both the conduction of protons to the four gating His37 residues and the stabilization of multiple positive charges within the channel. To visualize the solvent in the pore of the channel at room temperature while minimizing the effects of radiation damage, data were collected to a resolution of 1.4 Å using an X-ray free-electron laser (XFEL) at three different pH conditions: pH 5.5, pH 6.5, and pH 8.0. Data were collected on the Inward

Indexed as

ProtonsAmino Acid MotifsHydrogen BondingIon Channel GatingMolecular Dynamics SimulationProtein DomainsStatic ElectricityTemperatureViral Matrix ProteinsViroporin ProteinsM2 protein, Influenza A virusProtonsViral Matrix ProteinsViroporin Proteinsinfluenzamembrane proteinproton channelXFEL

Identifiers

PMID28835537
PMCPMC5754760

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.