Evidence map›Paper›PMID 19519772›Full record

ArticleJournal of neurochemistry2009

Interaction of catechol and non-catechol substrates with externally or internally facing dopamine transporters.

Ying-Jian Liang, Juan Zhen, Nianhang Chen, Maarten E A Reith

Open access · greenAbstract read
In one paragraph

Article in Journal of neurochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Hypocretin receptor 1 blockade early in abstinence prevents incubation of cocaine seeking and normalizes dopamine transmission.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Synaptic ZnTranslational psychiatry · 2021
    Article
  6. Dopamine transporter function fluctuates across sleep/wake state: potential impact for addiction.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

4 authors at 1 institution in 1 country.

Ying-Jian LiangDepartment of Psychiatry, New York University School of Medicine, Millhauser Labs, New York, New York 10016, USA.
Juan Zhen
Nianhang Chen
Maarten E A Reith
New York University · US

Funding

Dopamine Transporters: Mechanisms of Ligand InteractionR01DA019676 · NIDA · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI REITH, MAARTEN E · 2006 to 2016
$2.9M
The dopamine transporter and ions, substrates, blockersR01DA013261 · NIDA · UNIVERSITY OF ILLINOIS AT CHICAGO · PI REITH, MAARTEN E · 2000 to 2010
$2.4M
NIDA NIH HHS DA019676NIDA NIH HHS DA13261NIDA NIH HHS R01 DA013261NIDA NIH HHS R01 DA019676
6 · The paper itself

Abstract

Our previous work suggested that collapsing the Na(+) gradient and membrane potential converts the dopamine (DA) transporter (DAT) to an inward-facing conformation with a different substrate binding profile. Here, DAT expressing human embryonic kidney 293 cells were permeabilized with digitonin, disrupting ion/voltage gradients and allowing passage of DAT substrates. The potency of p-tyramine and other non-catechols (d-amphetamine, beta-phenethylamine, MPP(+)) in inhibiting cocaine analog binding to DAT in digitonin-treated cells was markedly weakened to a level similar to that observed in cell-free membranes. In contrast, the potency of DA and another catechol, norepinephrine, was not significantly changed by the same treatment, whereas epinephrine showed only a modest reduction. These findings suggest that catechol substrates interact symmetrically with both sides of DAT and non-catechol substrates, favoring binding to outward-facing transporter. In the cocaine analog binding assay, the mutant W84L displayed enhanced intrinsic binding affinity for substrates in interacting with both outward- and inward-facing states; D313N showed wild-type-like symmetric binding; but D267L and E428Q showed an apparent improvement in the permeation pathway from the external face towards the substrate site. Thus, the structure of both substrate and transporter play a role in the sidedness and mode of interaction between them.

Indexed as

Binding SitesCatecholsCell LineDigitoninDopamine Plasma Membrane Transport ProteinsHumansKineticsModels, MolecularMutationPermeabilityProtein BindingProtein ConformationSubstrate SpecificityZincCatecholsDigitoninDopamine Plasma Membrane Transport ProteinsZinc

Identifiers

PMID19519772
PMCPMC2696066
OpenAlexW1968292591

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.