Evidence map›Paper›PMID 33712696›Full record

ArticleCommunications biology2021

Water orientation and dynamics in the closed and open influenza B virus M2 proton channels.

Martin D Gelenter, Venkata S Mandala, Michiel J M Niesen, Dina A Sharon, Aurelio J Dregni, Adam P Willard, Mei Hong

Open access · goldAbstract readComparative StudyVideo-Audio Media
In one paragraph

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

24 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. HInternational journal of molecular sciences · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Solid-State NMR of Virus Membrane Proteins.Accounts of chemical research · 2025
    Article
  8. Article
  9. Activation of the influenza B M2 proton channel (BM2).bioRxiv : the preprint server for biology · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Functional Regulation of Aquaporin Dynamics by Lipid Bilayer Composition.bioRxiv : the preprint server for biology · 2023
    Article
  19. Article
  20. 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

7 authors at 1 institution in 1 country.

Martin D Gelenter *Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.ORCID 0000-0002-6412-805X
Venkata S Mandala *Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.ORCID 0000-0002-6358-0642
Michiel J M Niesen *Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.ORCID 0000-0002-9255-6203
Dina A Sharon *Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.
Aurelio J DregniDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.
Adam P WillardDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.
Mei HongDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA. meihong@mit.edu.ORCID 0000-0001-5255-5858
Massachusetts Institute of Technology · US

Funding

Structures and Dynamics of Proton and Cation-Dependent Channels and TransportersR01GM088204 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI HONG, MEI · 2009 to 2024
$4.8M
Solid-state NMR studies of the dynamic interactions of the influenza A M2 membrane protein with water, antiviral drugs, and the M1 proteinF31AI133989 · NIAID · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GELENTER, MARTIN DAVID · 2018 to 2020
$128k
Investigation of Seeded Alzheimer's Disease Tau Fibrils with Solid-State NMRF31AG069418 · NIA · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI DREGNI, AURELIO JAMES · 2020 to 2021
$85k
NIAID NIH HHS F31 AI133989NIA NIH HHS F31 AG069418NIGMS NIH HHS R01 GM088204
6 · The paper itself

Abstract

The influenza B M2 protein forms a water-filled tetrameric channel to conduct protons across the lipid membrane. To understand how channel water mediates proton transport, we have investigated the water orientation and dynamics using solid-state NMR spectroscopy and molecular dynamics (MD) simulations.

Indexed as

Ion Channel GatingHistidineHydrogen BondingHydrogen-Ion ConcentrationInfluenza B virusIon ChannelsMolecular Dynamics SimulationProton Magnetic Resonance SpectroscopyProtonsViral ProteinsWaterHistidineIon ChannelsProtonsViral ProteinsWater

Identifiers

PMID33712696
PMCPMC7955094
OpenAlexW3134807046

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.