Evidence map›Paper›PMID 25817866›Full record

ReviewVitamins and hormones2015

The sodium/multivitamin transporter: a multipotent system with therapeutic implications.

Matthias Quick, Lei Shi

Open access · greenAbstract readReview
In one paragraph

Review in Vitamins and hormones, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
6.7field-weighted citation impact, top 4% 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

26 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Lipoic acid attachment to proteins: stimulating new developments.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  8. Biotin Homeostasis and Human Disorders: Recent Findings and Perspectives.International journal of molecular sciences · 2024
    Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  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

2 authors at 2 institutions in 1 country.

Matthias QuickDepartment of Psychiatry, Division of Molecular Therapeutics, Columbia University College of Physicians and Surgeons, New York State Psychiatric Institute, New York, USA. Electronic address: mq2102@columbia.edu.
Lei ShiDepartment of Physiology and Biophysics, Institute for Computational Biomedicine, Weill Medical College of Cornell University, New York, USA.
Cornell University · USNew York Psychoanalytic Society and Institute · US

Funding

Structural basis for the functions of dopamine receptors, neurotransmitter transporters, and sigma 1 receptorZIADA000606 · NIDA · NATIONAL INSTITUTE ON DRUG ABUSE · PI SHI, LEI · 2015 to 2025
$20.5M
The Neurotransmitter: Sodium Symporter Permeation PathwayR00DA023694 · NIDA · WEILL MEDICAL COLL OF CORNELL UNIV · PI SHI, LEI · 2010 to 2012
$725k
The Neurotransmitter: Sodium Symporter Permeation PathwayK99DA023694 · NIDA · WEILL MEDICAL COLL OF CORNELL UNIV · PI SHI, LEI · 2008 to 2009
$180k
NIDA NIH HHS DA023694NIDA NIH HHS K99 DA023694NIDA NIH HHS R00 DA023694
6 · The paper itself

Abstract

The Na(+)/multivitamin transporter (SMVT) is a member of the solute:sodium symporter family that catalyzes the Na(+)-dependent uptake of the structurally diverse water-soluble vitamins pantothenic acid (vitamin B5) and biotin (vitamin H), α-lipoic acid-a vitamin-like substance with strong antioxidant properties-and iodide. The organic substrates of SMVT play central roles in the cellular metabolism and are, therefore, essential for normal human health and development. For example, biotin deficiency leads to growth retardation, dermatological disorders, and neurological disorders. Animal studies have shown that biotin deficiency during pregnancy is directly correlated to embryonic growth retardation, congenital malformation, and death of the embryo. This chapter focuses on the structural and functional features of the human isoform of SMVT (hSMVT); the discovery of which was greatly facilitated by the cloning and expression of hSMVT in tractable expression systems. Special emphasis will be given to mechanistic implications of the transport process of hSMVT that will inform our understanding of the molecular determinants of hSMVT-mediated transport in dynamic context to alleviate the development and optimization of hSMVT as a multipotent platform for drug delivery.

Indexed as

Biological TransportHumansMembrane Transport ProteinsProtein IsoformsSodiumSymportersVitaminsMembrane Transport ProteinsProtein IsoformsSodiumSymportersVitaminsBiotinLipoic acidNa(+)-coupled transportPantothenic acidSLC5Sodium/multivitamin transporterSolute:sodium symporter family

Identifiers

PMID25817866
PMCPMC5530880
OpenAlexW2208187841

What OpenQuestion holds

Textmetadata
LicenceTDM
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.