Evidence map›Paper›PMID 39741807›Full record

ArticleACS omega2024

Structure-Function Relationships of the CMP-Sialic Acid Transporter through Analysis of a Pathogenic Variant in an Alternatively Spliced Functional Isoform.

Brenda I Velázquez-Dodge, Marco A Ramírez-Martínez, Nina Pastor, Iván Martínez-Duncker, Yobana Pérez-Cervera, Héctor M Mora-Montes, Blanca E Domínguez-Mendoza, Roberta Salinas-Marín

Abstract read
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In one paragraph

Article in ACS omega, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Frontiers in genetics · 2025
    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

8 authors.

Brenda I Velázquez-DodgeLaboratorio de Glicobiología y Diagnóstico Molecular, Centro de Investigación en Dinámica Celular, Universidad Autónoma del Estado de Morelos, Av. Universidad 1001, Col. Chamilpa, Cuernavaca 62209, Morelos, México.
Marco A Ramírez-MartínezLaboratorio de Dinámica de Proteínas, Centro de Investigación en Dinámica Celular, Universidad Autónoma del Estado de Morelos, Cuernavaca 62209, México.
Nina PastorLaboratorio de Dinámica de Proteínas, Centro de Investigación en Dinámica Celular, Universidad Autónoma del Estado de Morelos, Cuernavaca 62209, México.ORCID https://orcid.org/0000-0001-7755-2936
Iván Martínez-DunckerLaboratorio de Glicobiología y Diagnóstico Molecular, Centro de Investigación en Dinámica Celular, Universidad Autónoma del Estado de Morelos, Av. Universidad 1001, Col. Chamilpa, Cuernavaca 62209, Morelos, México.
Yobana Pérez-CerveraCentro de Estudios en Ciencias de la Salud y la Enfermedad, Facultad de Odontología, Universidad Autónoma Benito Juárez de Oaxaca, Avenida Universidad S/N, C.P. 68120, Oaxaca de Juárez 68110, Oaxaca, México.
Héctor M Mora-MontesDepartamento de Biología, División de Ciencias Naturales y Exactas, Campus Guanajuato, Universidad de Guanajuato, Noria Alta s/n, col. Noria Alta, C.P., Guanajuato Gto 36050, México.
Blanca E Domínguez-MendozaCentro de Investigaciones Químicas, IICBA, Universidad Autónoma Del Estado de Morelos, Cuernavaca 62209, Morelos, México.
Roberta Salinas-MarínLaboratorio de Glicobiología y Diagnóstico Molecular, Centro de Investigación en Dinámica Celular, Universidad Autónoma del Estado de Morelos, Av. Universidad 1001, Col. Chamilpa, Cuernavaca 62209, Morelos, México.ORCID https://orcid.org/0000-0003-0815-447X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human CMP-sialic acid transporter (hCST) is a mammalian highly conserved type III antiporter that translocates CMP-sialic acid into the Golgi lumen, supporting sialylation. Although different works have focused on elucidating structure-function relationships in the hCST, this is the first study to address them in an alternatively spliced isoform. We have previously reported the expression of a functional human del177 isoform that has skipping of exon 6, resulting in a loss of 59 amino acids, without change in the open reading frame and conserving its C-terminal region. To elucidate structure-function relationships, we interrogated this isoform with a known pathogenic variant c.303C>T (p.Q101H) for the

Identifiers

PMID39741807
PMCPMC11683650

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Registered trials

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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.