Side Chain Structures of the Proton-Selective Histidine and Gating Tryptophan in Influenza BM2 Reveal Both Conservation and Variation of the Proton Conduction Mechanism.

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Article in Biochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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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

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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.

Engineered Channel Asymmetry Extends Hydrogen-Bonding Networks for Proton Conduction.bioRxiv : the preprint server for biology · 2026
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

2 authors.

Yanina PankratovaDepartment of Chemistry, Massachusetts Institute of Technology, 170 Albany Street, Cambridge, Massachusetts 02139, United States.ORCID 0009-0003-8848-4213

Mei HongDepartment of Chemistry, Massachusetts Institute of Technology, 170 Albany Street, Cambridge, Massachusetts 02139, United States.ORCID 0000-0001-5255-5858

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

Structures and Dynamics of Proton- and Cation-Conducting ViroporinsR01GM159321 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI Mei Hong · 2025 to 2026

$824k

NIGMS NIH HHS R01 GM088204NIGMS NIH HHS R01 GM159321

6 · The paper itself

Abstract

Aromatic residues play important roles in protein structure and function, but are difficult to study at atomic resolution by NMR because of their low spectral sensitivity and resolution. The M2 proton channels of influenza A and B viruses use a histidine for proton selection and a tryptophan for gating. High-resolution structures and dynamics of His37 and Trp41 side chains in AM2 have provided detailed insights into the proton conduction mechanism of AM2. However, the side chain structures of the corresponding His19 and Trp23 in BM2 have not been established. Here, we directly determine the side chain conformations of His19 and Trp23 using

Indexed as

HistidineProtonsTryptophanViral Matrix ProteinsViral ProteinsInfluenza B virusIon Channel GatingModels, MolecularProtein ConformationBM2 polypeptide, influenza B virusHistidineProtonsTryptophanViral Matrix ProteinsViral Proteins

Identifiers

PMID40554716

DOI10.1021/acs.biochem.5c00242

PMCPMC12961958

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