Evidence map›Paper›PMID 21359964›Full record

ArticleMolecular and cellular biochemistry2011

Expression and analysis of two novel rat organic cation transporter homologs, SLC22A17 and SLC22A23.

Katie M Bennett, Jun Liu, Courtney Hoelting, James Stoll

Abstract read
In one paragraph

Article in Molecular and cellular biochemistry, 2011. 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
0.6field-weighted citation impact, top 31% 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, 40 citations in OpenAlex.

  1. Pharmaceutics · 2026
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  4. Alzheimer's disease multi-ancestry genome-wide interaction and stratified study with smoking.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025
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  5. Review
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  10. Review
  11. Drug metabolism and disposition: the biological fate of chemicals · 2021
    Article
  12. Article
  13. Review
  14. Review
  15. Deorphaning a solute carrier 22 family member, SLC22A15, through functional genomic studies.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review
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

4 authors at 2 institutions in 1 country.

Katie M BennettDepartment of Biomedical Sciences, Texas Tech University Health Sciences Center, School of Pharmacy, Amarillo, TX 79106, USA.
Jun Liu
Courtney Hoelting
James Stoll
Texas Tech University · USTexas Tech University Health Sciences Center · US

Funding

Characterization of the ubiquitous choline transporterR15GM070578 · NIGMS · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI STOLL, JAMES · 2004 to 2004
$222k
NIGMS NIH HHS R15 GM070578
6 · The paper itself

Abstract

The organic cation transporter (OCT, SLC22) family is a family of polyspecific transmembrane proteins that are responsible for the uptake or excretion of many cationic drugs, toxins, and endogenous metabolites in a variety of tissues. Many of the OCTs have been previously characterized, but there are a number of orphan genes whose functions remain unknown. In this study, two novel rat SLC22 genes, SLC22A17 (BOCT1) and SLC22A23 (BOCT2), were cloned and characterized. Northern blot analysis showed that BOCT1 and BOCT2 mRNA was expressed in a wide variety of tissues. BOCT1 was strongly expressed in brain, primary neurons and brain endothelial cells, with highest expression in choroid plexus. BOCT2 was also abundantly expressed in brain, as well as in liver. To characterize the products of these genes, BOCT1 cDNA was isolated from a rat blood-brain barrier cDNA library, and BOCT2 cDNA was isolated from rat brain capillary and from cultured neurons using PCR techniques. Plasmids expressing BOCT1 and BOCT2 were transfected into HEK-293 cells, as were control cDNAs for OCT1 and OCTN2. Recombinant cell surface protein was verified by western blot and fluorescence microscopy. Transport activity of BOCT1 and BOCT2 was evaluated using radioisotope uptake assays. The OCT1- and OCTN2-expressing cells transported the canonical substrates, 1-methyl-4-phenyl-pyridinium (MPP(+)) and carnitine, respectively. However, BOCT1 and BOCT2-expressing cells did not show transport activity for these substrates or a number of other SLC22 substrates. These novel family members have a nonconserved amino terminus, relative to other OCTs, that may preclude typical SLC22 transport function.

Indexed as

Amino Acid SequenceAnimalsBase SequenceBlotting, WesternDNA, ComplementaryDNA PrimersMicroscopy, FluorescenceMolecular Sequence DataOrganic Cation Transport ProteinsRatsRNA, MessengerSequence Homology, Amino AcidDNA, ComplementaryDNA PrimersOrganic Cation Transport ProteinsRNA, Messenger

Identifiers

PMID21359964
PMCPMC3097276
OpenAlexW2032089093

What OpenQuestion holds

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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.