Evidence map›Paper›PMID 31647368›Full record

ArticleChannels (Austin, Tex.)2019

Voltage vs. Ligand I: Structural basis of the intrinsic flexibility of S3 segment and its significance in ion channel activation.

Daniel Balleza, Mario E Rosas, Sergio Romero-Romero

Abstract read
In one paragraph

Article in Channels (Austin, Tex.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed, 1 pooled it
–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

8 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. CNG channel structure, function, and gating: a tale of conformational flexibility.Pflugers Archiv : European journal of physiology · 2021
    Review
  7. 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

3 authors.

Daniel BallezaDepartamento de Química ICET, Universidad Autónoma de Guadalajara , Zapopan Jalisco , Mexico.ORCID 0000-0002-6848-9135
Mario E RosasDepartamento de Química ICET, Universidad Autónoma de Guadalajara , Zapopan Jalisco , Mexico.
Sergio Romero-RomeroFacultad de Medicina, Departamento de Bioquímica, Universidad Nacional Autónoma de México, 04510 Mexico City, Mexico. Current address: Department of Biochemistry, University of Bayreuth , Bayreuth , Germany.ORCID 0000-0003-2144-7912

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We systematically predict the internal flexibility of the S3 segment, one of the most mobile elements in the voltage-sensor domain. By analyzing the primary amino acid sequences of V-sensor containing proteins, including Hv1, TPC channels and the voltage-sensing phosphatases, we established correlations between the local flexibility and modes of activation for different members of the VGIC superfamily. Taking advantage of the structural information available, we also assessed structural aspects to understand the role played by the flexibility of S3 during the gating of the pore. We found that S3 flexibility is mainly determined by two specific regions: (1) a short NxxD motif in the N-half portion of the helix (S3a), and (2) a short sequence at the beginning of the so-called

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsEukaryotaIon Channel GatingIon ChannelsLigandsPhylogenyProtein ConformationSequence AlignmentIon ChannelsLigandschannel activationLocal flexibilityS3 segmentvoltage sensor

Identifiers

PMID31647368
PMCPMC6833973

What OpenQuestion holds

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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.